UniProtKB - Q15746 (MYLK_HUMAN)
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- BLAST>sp|Q15746|MYLK_HUMAN Myosin light chain kinase, smooth muscle OS=Homo sapiens OX=9606 GN=MYLK PE=1 SV=4 MGDVKLVASSHISKTSLSVDPSRVDSMPLTEAPAFILPPRNLCIKEGATAKFEGRVRGYP EPQVTWHRNGQPITSGGRFLLDCGIRGTFSLVIHAVHEEDRGKYTCEATNGSGARQVTVE LTVEGSFAKQLGQPVVSKTLGDRFSAPAVETRPSIWGECPPKFATKLGRVVVKEGQMGRF SCKITGRPQPQVTWLKGNVPLQPSARVSVSEKNGMQVLEIHGVNQDDVGVYTCLVVNGSG KASMSAELSIQGLDSANRSFVRETKATNSDVRKEVTNVISKESKLDSLEAAAKSKNCSSP QRGGSPPWAANSQPQPPRESKLESCKDSPRTAPQTPVLQKTSSSITLQAARVQPEPRAPG LGVLSPSGEERKRPAPPRPATFPTRQPGLGSQDVVSKAANRRIPMEGQRDSAFPKFESKP QSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTR DSGTYSCTASNAQGQLSCSWTLQVERLAVMEVAPSFSSVLKDCAVIEGQDFVLQCSVRGT PVPRITWLLNGQPIQYARSTCEAGVAELHIQDALPEDHGTYTCLAENALGQVSCSAWVTV HEKKSSRKSEYLLPVAPSKPTAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHNG NEIQESEDFHFEQRGTQHSLCIQEVFPEDTGTYTCEAWNSAGEVRTQAVLTVQEPHDGTQ PWFISKPRSVTASLGQSVLISCAIAGDPFPTVHWLRDGKALCKDTGHFEVLQNEDVFTLV LKKVQPWHAGQYEILLKNRVGECSCQVSLMLQNSSARALPRGREPASCEDLCGGGVGADG GGSDRYGSLRPGWPARGQGWLEEEDGEDVRGVLKRRVETRQHTEEAIRQQEVEQLDFRDL LGKKVSTKTLSEDDLKEIPAEQMDFRANLQRQVKPKTVSEEERKVHSPQQVDFRSVLAKK GTSKTPVPEKVPPPKPATPDFRSVLGGKKKLPAENGSSSAETLNAKAVESSKPLSNAQPS GPLKPVGNAKPAETLKPMGNAKPAETLKPMGNAKPDENLKSASKEELKKDVKNDVNCKRG HAGTTDNEKRSESQGTAPAFKQKLQDVHVAEGKKLLLQCQVSSDPPATIIWTLNGKTLKT TKFIILSQEGSLCSVSIEKALPEDRGLYKCVAKNDAGQAECSCQVTVDDAPASENTKAPE MKSRRPKSSLPPVLGTESDATVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGK VTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQ AQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYSIEIWDSANKTWKE LATCRSTSFNVQDLLPDHEYKFRVRAINVYGTSEPSQESELTTVGEKPEEPKDEVEVSDD DEKEPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSA KEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTER ECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKV LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDF DDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYM ARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAV AEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYD EDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGEEEEE
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Protein
Myosin light chain kinase, smooth muscle
Gene
MYLK
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca2+ entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.13 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract] - Ref.7"The N-terminus of the long MLCK induces a disruption in normal spindle morphology and metaphase arrest."
Dulyaninova N.G., Patskovsky Y.V., Bresnick A.R.
J. Cell Sci. 117:1481-1493(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CELL CYCLE, SUBCELLULAR LOCATION. - Ref.15"Myosin light chain kinase modulates hypotonicity-induced Ca2+ entry and Cl- channel activity in human cervical cancer cells."
Shen M.-R., Furla P., Chou C.-Y., Ellory J.C.
Pflugers Arch. 444:276-285(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN HYPOTONICITY RESPONSE, ENZYME REGULATION. - Ref.17"Distinct temporal-spatial roles for rho kinase and myosin light chain kinase in epithelial purse-string wound closure."
Russo J.M., Florian P., Shen L., Graham W.V., Tretiakova M.S., Gitter A.H., Mrsny R.J., Turner J.R.
Gastroenterology 128:987-1001(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN WOUND HEALING. - Ref.19"Myosin light chain kinase plays a role in the regulation of epithelial cell survival."
Connell L.E., Helfman D.M.
J. Cell Sci. 119:2269-2281(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EPITHELIAL CELL SURVIVAL, ENZYME REGULATION. - Ref.20"Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN TRPC5 REGULATION, ENZYME REGULATION. - Ref.21"Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2."
Zhou X., Liu Y., You J., Zhang H., Zhang X., Ye L.
Cancer Lett. 270:312-327(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION. - Ref.23"Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins."
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.
Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS PTK2B/PYK2 KINASE, INTERACTION WITH PTK2B/PYK2. - Ref.27"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BY NAA10/ARD1, INTERACTION WITH NAA10/ARD1, MUTAGENESIS OF LYS-608. - Ref.28"Myosin light chain kinase is responsible for high proliferative ability of breast cancer cells via anti-apoptosis involving p38 pathway."
Cui W.-J., Liu Y., Zhou X.-L., Wang F.-Z., Zhang X.-D., Ye L.-H.
Acta Pharmacol. Sin. 31:725-732(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN BREAST CANCER. - Ref.29"Modulation of factors affecting optic nerve head astrocyte migration."
Miao H., Crabb A.W., Hernandez M.R., Lukas T.J.
Invest. Ophthalmol. Vis. Sci. 51:4096-4103(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN OPTIC NERVE HEAD ASTROCYTE MIGRATION. - Ref.32"The angiotensin II type 1 receptor induces membrane blebbing by coupling to Rho A, Rho kinase, and myosin light chain kinase."
Godin C.M., Ferguson S.S.G.
Mol. Pharmacol. 77:903-911(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN MEMBRANE BLEBBING. - Ref.33"Non-muscle myosin light chain kinase isoform is a viable molecular target in acute inflammatory lung injury."
Mirzapoiazova T., Moitra J., Moreno-Vinasco L., Sammani S., Turner J.R., Chiang E.T., Evenoski C., Wang T., Singleton P.A., Huang Y., Lussier Y.A., Watterson D.M., Dudek S.M., Garcia J.G.N.
Am. J. Respir. Cell Mol. Biol. 44:40-52(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
Miscellaneous
In asthmatic patients, overexpression promotes actin filament propulsion, thus contributing to airway hyperresponsiveness. Some MYLK variants may contribute to acute lung injury (ALI) susceptibility. Potential therapeutic target in the treatment of burn edema.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
Isoform 1 is activated by phosphorylation on Tyr-464 and Tyr-471. Isoforms which lack these tyrosine residues are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation. Repressed by organometallic pyridylnaphthalimide complexes, wortmannin, ML-7 (a synthetic naphthalenesulphonyl derivative that inhibits the binding of ATP to MLCK) and ML-9.6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract] - Ref.15"Myosin light chain kinase modulates hypotonicity-induced Ca2+ entry and Cl- channel activity in human cervical cancer cells."
Shen M.-R., Furla P., Chou C.-Y., Ellory J.C.
Pflugers Arch. 444:276-285(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN HYPOTONICITY RESPONSE, ENZYME REGULATION. - Ref.16"Quantitative measurements of Ca(2+)/calmodulin binding and activation of myosin light chain kinase in cells."
Geguchadze R., Zhi G., Lau K.S., Isotani E., Persechini A., Kamm K.E., Stull J.T.
FEBS Lett. 557:121-124(2004) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION BY CALCIUM. - Ref.19"Myosin light chain kinase plays a role in the regulation of epithelial cell survival."
Connell L.E., Helfman D.M.
J. Cell Sci. 119:2269-2281(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EPITHELIAL CELL SURVIVAL, ENZYME REGULATION. - Ref.20"Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN TRPC5 REGULATION, ENZYME REGULATION. - Ref.34"Organometallic pyridylnaphthalimide complexes as protein kinase inhibitors."
Blanck S., Cruchter T., Vultur A., Riedel R., Harms K., Herlyn M., Meggers E.
Organometallics 30:4598-4606(2011) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=6.5 µM for MLC (isoform 1 at 22 degrees Celsius)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract]
- KM=7.2 µM for MLC (isoform 2 at 22 degrees Celsius)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract]
- Vmax=11.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract]
- Vmax=10.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract]
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 1493 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 1585 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 1470 – 1478 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 9 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin binding Source: UniProtKB-KW
- ATP binding Source: UniProtKB-KW
- calmodulin binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- myosin light chain kinase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- aorta smooth muscle tissue morphogenesis Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- bleb assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular hypotonic response Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- muscle contraction Source: Reactome
- positive regulation of calcium ion transport Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of cell migration Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of wound healing Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein phosphorylation Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- smooth muscle contraction Source: UniProtKB
- tonic smooth muscle contraction Source: UniProtKB
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Actin-binding, Calmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase |
| Ligand | ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.11.18 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-445355 Smooth Muscle Contraction R-HSA-5627123 RHO GTPases activate PAKs |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q15746 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q15746 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q15746 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Myosin light chain kinase, smooth muscle (EC:2.7.11.18)Short name: MLCK Short name: smMLCK Alternative name(s): Kinase-related protein Short name: KRP Telokin Cleaved into the following chain: |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:MYLK Synonyms:MLCK, MLCK1, MYLK1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000065534.18 |
Human Gene Nomenclature Database More...HGNCi | HGNC:7590 MYLK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600922 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15746 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytoskeleton
Other locations
Note: Localized to stress fibers during interphase and to the cleavage furrow during mitosis.
Cytoskeleton
- actin cytoskeleton Source: HPA
- stress fiber Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Cytosol
- cytosol Source: Reactome
Plasma Membrane
- cleavage furrow Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: HPA
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lamellipodium Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell projection, Cytoplasm, Cytoskeleton<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Aortic aneurysm, familial thoracic 7 (AAT7)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.42"Mutations in myosin light chain kinase cause familial aortic dissections."
Wang L., Guo D.C., Cao J., Gong L., Kamm K.E., Regalado E., Li L., Shete S., He W.Q., Zhu M.S., Offermanns S., Gilchrist D., Elefteriades J., Stull J.T., Milewicz D.M.
Am. J. Hum. Genet. 87:701-707(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS AAT7 MET-1213; THR-1754 AND PRO-1759, VARIANTS VAL-128; HIS-133; ARG-160; CYS-656; ALA-1085 AND LYS-1399, CHARACTERIZATION OF VARIANTS AAT7 THR-1754 AND PRO-1759.
Ref.42
"Mutations in myosin light chain kinase cause familial aortic dissections."
Wang L., Guo D.C., Cao J., Gong L., Kamm K.E., Regalado E., Li L., Shete S., He W.Q., Zhu M.S., Offermanns S., Gilchrist D., Elefteriades J., Stull J.T., Milewicz D.M.
Am. J. Hum. Genet. 87:701-707(2010) [PubMed] [Europe PMC] [Abstract]
Wang L., Guo D.C., Cao J., Gong L., Kamm K.E., Regalado E., Li L., Shete S., He W.Q., Zhu M.S., Offermanns S., Gilchrist D., Elefteriades J., Stull J.T., Milewicz D.M.
Am. J. Hum. Genet. 87:701-707(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AAT7 MET-1213; THR-1754 AND PRO-1759, VARIANTS VAL-128; HIS-133; ARG-160; CYS-656; ALA-1085 AND LYS-1399, CHARACTERIZATION OF VARIANTS AAT7 THR-1754 AND PRO-1759.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
See also OMIM:613780| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065574 | 1213 | V → M in AAT7; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065576 | 1754 | A → T in AAT7; 4-fold reduced affinity for calmodulin; decreased kinase activity compared to wild-type protein. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065577 | 1759 | S → P in AAT7; 7-fold reduced affinity for calmodulin; 6-fold decreased Vmax. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 608 | K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Aortic aneurysm, Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 4638 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | MYLK |
MalaCards human disease database More...MalaCardsi | MYLK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613780 phenotype |
Open Targets More...OpenTargetsi | ENSG00000065534 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 91387 Familial thoracic aortic aneurysm and aortic dissection |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31388 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2428 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1552 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MYLK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 300669714 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000024354 | 1 – 1914 | Myosin light chain kinase, smooth muscleAdd BLAST | 1914 | ||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000403731 | 1 – 1910 | Myosin light chain kinase, smooth muscle, deglutamylated formBy similarityAdd BLAST | 1910 | ||
| Isoform 6 (identifier: Q15746-8) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||||
| Isoform 8 (identifier: Q15746-10) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||||
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 182 ↔ 233 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 231 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 305 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 343 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 365 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 435 ↔ 487 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 464 | Phosphotyrosine; by ABL1 and SRC3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 471 | Phosphotyrosine; by SRC2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 535 ↔ 583 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 556 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 608 | N6-acetyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 611 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 742 ↔ 805 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 792 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 846 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 947 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 1119 ↔ 1170 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1438 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1449 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1575 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1635 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1759 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1760 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1772 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1773 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1776 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1778 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1779 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 1830 ↔ 1882 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | |||
| Isoform 6 (identifier: Q15746-8) | |||||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Isoform 8 (identifier: Q15746-10) | |||||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-464 and Tyr-471 promotes CTTN binding.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)."
Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N.
J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract] - Ref.14"Novel interaction of cortactin with endothelial cell myosin light chain kinase."
Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.
Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CTTN, PHOSPHORYLATION AT TYR-464 AND TYR-471 BY SRC. - Ref.31"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-231; TYR-464; TYR-556; TYR-611; TYR-792; TYR-846; TYR-1449; TYR-1575 AND TYR-1635 BY ABL1, INTERACTION WITH CTTN AND ABL1.
The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (By similarity).By similarity
Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BY NAA10/ARD1, INTERACTION WITH NAA10/ARD1, MUTAGENESIS OF LYS-608.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Disulfide bond, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15746 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q15746 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q15746 |
PeptideAtlas More...PeptideAtlasi | Q15746 |
PRoteomics IDEntifications database More...PRIDEi | Q15746 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 60733 60734 [Q15746-2] 60735 [Q15746-3] 60736 [Q15746-4] 60737 [Q15746-5] 60738 [Q15746-6] 60739 [Q15746-7] 60740 [Q15746-8] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15746 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15746 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. Telokin has been found in a wide variety of adult and fetal tissues. Accumulates in well differentiated enterocytes of the intestinal epithelium in response to tumor necrosis factor (TNF).4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21."
Potier M.-C., Chelot E., Pekarsky Y., Gardiner K., Rossier J., Turnell W.G.
Genomics 29:562-570(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), TISSUE SPECIFICITY. - Ref.5"Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing and polymorphic marker."
Watterson D.M., Schavocky J.P., Guo L., Weiss C., Chlenski A., Shrinsky V.P., Van Eldik L.J., Haiech J.
J. Cell. Biochem. 75:481-491(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1614-1914 (ISOFORM 9/DEL-1790), TISSUE SPECIFICITY. - Ref.18"Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter."
Graham W.V., Wang F., Clayburgh D.R., Cheng J.X., Yoon B., Wang Y., Lin A., Turner J.R.
J. Biol. Chem. 281:26205-26215(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY TNF, TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE (ISOFORMS 1/2/3A/3B/4/DEL-1790). - Ref.30"Quantitative distribution and colocalization of non-muscle myosin light chain kinase isoforms and cortactin in human lung endothelium."
Brown M., Adyshev D., Bindokas V., Moitra J., Garcia J.G.N., Dudek S.M.
Microvasc. Res. 80:75-88(2010) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INTERACTION WITH CTTN, SUBCELLULAR LOCATION.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Accumulates in individuals with asthma (at protein levels). Induced by tumor necrosis factor (TNF). Repressed by androgens (e.g. R1881).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter."
Graham W.V., Wang F., Clayburgh D.R., Cheng J.X., Yoon B., Wang Y., Lin A., Turner J.R.
J. Biol. Chem. 281:26205-26215(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY TNF, TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE (ISOFORMS 1/2/3A/3B/4/DEL-1790). - Ref.26"Androgens down-regulate myosin light chain kinase in human prostate cancer cells."
Leveille N., Fournier A., Labrie C.
J. Steroid Biochem. Mol. Biol. 114:174-179(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY ANDROGENS. - Ref.35"Myosin, transgelin, and myosin light chain kinase: expression and function in asthma."
Leguillette R., Laviolette M., Bergeron C., Zitouni N., Kogut P., Solway J., Kachmar L., Hamid Q., Lauzon A.-M.
Am. J. Respir. Crit. Care Med. 179:194-204(2009) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON ASTHMA, INDUCTION BY ASTHMA.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000065534 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15746 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15746 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB020789 HPA031677 HPA048055 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
All isoforms including Telokin bind calmodulin. Interacts with SVIL (By similarity). Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 and PTK2B/PYK2.By similarity6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Novel interaction of cortactin with endothelial cell myosin light chain kinase."
Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.
Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CTTN, PHOSPHORYLATION AT TYR-464 AND TYR-471 BY SRC. - Ref.23"Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins."
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.
Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS PTK2B/PYK2 KINASE, INTERACTION WITH PTK2B/PYK2. - Ref.27"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase."
Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W.
PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BY NAA10/ARD1, INTERACTION WITH NAA10/ARD1, MUTAGENESIS OF LYS-608. - Ref.30"Quantitative distribution and colocalization of non-muscle myosin light chain kinase isoforms and cortactin in human lung endothelium."
Brown M., Adyshev D., Bindokas V., Moitra J., Garcia J.G.N., Dudek S.M.
Microvasc. Res. 80:75-88(2010) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INTERACTION WITH CTTN, SUBCELLULAR LOCATION. - Ref.31"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-231; TYR-464; TYR-556; TYR-611; TYR-792; TYR-846; TYR-1449; TYR-1575 AND TYR-1635 BY ABL1, INTERACTION WITH CTTN AND ABL1. - Ref.40"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction."
Gsponer J., Christodoulou J., Cavalli A., Bui J.M., Richter B., Dobson C.M., Vendruscolo M.
Structure 16:736-746(2008) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 1742-1760 IN COMPLEX WITH CALMODULIN.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GOPC | Q9HD26 | 3 | EBI-968482,EBI-349832 | |
| NCK1 | P16333 | 2 | EBI-968482,EBI-389883 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin binding Source: UniProtKB-KW
- calmodulin binding Source: UniProtKB-KW
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110722, 17 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q15746 |
Protein interaction database and analysis system More...IntActi | Q15746, 23 interactors |
Molecular INTeraction database More...MINTi | Q15746 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353452 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q15746 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 512 – 518 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 523 – 526 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 531 – 534 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 536 – 541 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 546 – 553 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 560 – 562 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 565 – 570 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 581 – 586 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 591 – 595 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 598 – 601 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1239 – 1241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1246 – 1250 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1255 – 1266 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1268 – 1277 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1281 – 1288 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1290 – 1297 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1302 – 1304 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1306 – 1313 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1318 – 1320 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1323 – 1328 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1743 – 1760 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15746 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15746 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q15746 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 33 – 122 | Ig-like C2-type 1Add BLAST | 90 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 161 – 249 | Ig-like C2-type 2Add BLAST | 89 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 414 – 503 | Ig-like C2-type 3Add BLAST | 90 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 514 – 599 | Ig-like C2-type 4Add BLAST | 86 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 620 – 711 | Ig-like C2-type 5Add BLAST | 92 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 721 – 821 | Ig-like C2-type 6Add BLAST | 101 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 868 – 895 | 1-1Add BLAST | 28 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 896 – 923 | 1-2Add BLAST | 28 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 924 – 951 | 1-3Add BLAST | 28 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 952 – 979 | 1-4Add BLAST | 28 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 980 – 998 | 1-5; truncatedAdd BLAST | 19 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 999 – 1003 | 2-1; truncated | 5 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 1004 – 1015 | 2-2Add BLAST | 12 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 1016 – 1027 | 2-3Add BLAST | 12 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 1028 – 1039 | 2-4Add BLAST | 12 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 1040 – 1051 | 2-5Add BLAST | 12 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 1052 – 1063 | 2-6Add BLAST | 12 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1098 – 1186 | Ig-like C2-type 7Add BLAST | 89 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1238 – 1326 | Ig-like C2-type 8Add BLAST | 89 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1334 – 1426 | Fibronectin type-IIIPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 93 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1464 – 1719 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 256 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1809 – 1898 | Ig-like C2-type 9Add BLAST | 90 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 868 – 998 | 5 X 28 AA approximate tandem repeatsAdd BLAST | 131 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 923 – 963 | Actin-binding (calcium/calmodulin-sensitive)By similarityAdd BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 948 – 963 | Calmodulin-bindingBy similarityAdd BLAST | 16 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 999 – 1063 | 6 X 12 AA approximate tandem repeatsAdd BLAST | 65 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1061 – 1460 | Actin-binding (calcium/calmodulin-insensitive)By similarityAdd BLAST | 400 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1711 – 1774 | Calmodulin-bindingAdd BLAST | 64 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1906 – 1914 | Poly-Glu | 9 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Immunoglobulin domain, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0613 Eukaryota ENOG410XQFD LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118877 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000049287 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052551 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15746 |
KEGG Orthology (KO) More...KOi | K00907 |
Identification of Orthologs from Complete Genome Data More...OMAi | KFIILSQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G005W |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15746 |
TreeFam database of animal gene trees More...TreeFami | TF314166 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00063 FN3, 1 hit cd14191 STKc_MLCK1, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.10, 10 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003961 FN3_dom IPR036116 FN3_sf IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR013098 Ig_I-set IPR003599 Ig_sub IPR003598 Ig_sub2 IPR011009 Kinase-like_dom_sf IPR015725 MLCK1_kinase_dom IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00041 fn3, 1 hit PF07679 I-set, 9 hits PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00060 FN3, 1 hit SM00409 IG, 9 hits SM00408 IGc2, 9 hits SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48726 SSF48726, 9 hits SSF49265 SSF49265, 1 hit SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50853 FN3, 1 hit PS50835 IG_LIKE, 9 hits PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (11)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 11 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: Q15746-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Non-muscle isozyme
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
1510 1520 1530 1540 1550
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
1560 1570 1580 1590 1600
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
1610 1620 1630 1640 1650
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
1660 1670 1680 1690 1700
CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL
1710 1720 1730 1740 1750
KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN
1760 1770 1780 1790 1800
AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV
1810 1820 1830 1840 1850
AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR
1860 1870 1880 1890 1900
ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE
1910
TMEEGEGEGE EEEE
Length:1,914
Mass (Da):210,715
Last modified:July 13, 2010 - v4
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i2D094E161CE2D4BA
Isoform 2 (identifier: Q15746-2) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEGLAV MEVAPSFSSV
460 470 480 490 500
LKDCAVIEGQ DFVLQCSVRG TPVPRITWLL NGQPIQYARS TCEAGVAELH
510 520 530 540 550
IQDALPEDHG TYTCLAENAL GQVSCSAWVT VHEKKSSRKS EYLLPVAPSK
560 570 580 590 600
PTAPIFLQGL SDLKVMDGSQ VTMTVQVSGN PPPEVIWLHN GNEIQESEDF
610 620 630 640 650
HFEQRGTQHS LCIQEVFPED TGTYTCEAWN SAGEVRTQAV LTVQEPHDGT
660 670 680 690 700
QPWFISKPRS VTASLGQSVL ISCAIAGDPF PTVHWLRDGK ALCKDTGHFE
710 720 730 740 750
VLQNEDVFTL VLKKVQPWHA GQYEILLKNR VGECSCQVSL MLQNSSARAL
760 770 780 790 800
PRGREPASCE DLCGGGVGAD GGGSDRYGSL RPGWPARGQG WLEEEDGEDV
810 820 830 840 850
RGVLKRRVET RQHTEEAIRQ QEVEQLDFRD LLGKKVSTKT LSEDDLKEIP
860 870 880 890 900
AEQMDFRANL QRQVKPKTVS EEERKVHSPQ QVDFRSVLAK KGTSKTPVPE
910 920 930 940 950
KVPPPKPATP DFRSVLGGKK KLPAENGSSS AETLNAKAVE SSKPLSNAQP
960 970 980 990 1000
SGPLKPVGNA KPAETLKPMG NAKPAETLKP MGNAKPDENL KSASKEELKK
1010 1020 1030 1040 1050
DVKNDVNCKR GHAGTTDNEK RSESQGTAPA FKQKLQDVHV AEGKKLLLQC
1060 1070 1080 1090 1100
QVSSDPPATI IWTLNGKTLK TTKFIILSQE GSLCSVSIEK ALPEDRGLYK
1110 1120 1130 1140 1150
CVAKNDAGQA ECSCQVTVDD APASENTKAP EMKSRRPKSS LPPVLGTESD
1160 1170 1180 1190 1200
ATVKKKPAPK TPPKAAMPPQ IIQFPEDQKV RAGESVELFG KVTGTQPITC
1210 1220 1230 1240 1250
TWMKFRKQIQ ESEHMKVENS ENGSKLTILA ARQEHCGCYT LLVENKLGSR
1260 1270 1280 1290 1300
QAQVNLTVVD KPDPPAGTPC ASDIRSSSLT LSWYGSSYDG GSAVQSYSIE
1310 1320 1330 1340 1350
IWDSANKTWK ELATCRSTSF NVQDLLPDHE YKFRVRAINV YGTSEPSQES
1360 1370 1380 1390 1400
ELTTVGEKPE EPKDEVEVSD DDEKEPEVDY RTVTINTEQK VSDFYDIEER
1410 1420 1430 1440 1450
LGSGKFGQVF RLVEKKTRKV WAGKFFKAYS AKEKENIRQE ISIMNCLHHP
1460 1470 1480 1490 1500
KLVQCVDAFE EKANIVMVLE IVSGGELFER IIDEDFELTE RECIKYMRQI
1510 1520 1530 1540 1550
SEGVEYIHKQ GIVHLDLKPE NIMCVNKTGT RIKLIDFGLA RRLENAGSLK
1560 1570 1580 1590 1600
VLFGTPEFVA PEVINYEPIG YATDMWSIGV ICYILVSGLS PFMGDNDNET
1610 1620 1630 1640 1650
LANVTSATWD FDDEAFDEIS DDAKDFISNL LKKDMKNRLD CTQCLQHPWL
1660 1670 1680 1690 1700
MKDTKNMEAK KLSKDRMKKY MARRKWQKTG NAVRAIGRLS SMAMISGLSG
1710 1720 1730 1740 1750
RKSSTGSPTS PLNAEKLESE EDVSQAFLEA VAEEKPHVKP YFSKTIRDLE
1760 1770 1780 1790 1800
VVEGSAARFD CKIEGYPDPE VVWFKDDQSI RESRHFQIDY DEDGNCSLII
1810 1820 1830 1840
SDVCGDDDAK YTCKAVNSLG EATCTAELIV ETMEEGEGEG EEEEE
Length:1,845
Mass (Da):203,055
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0111D4C5A88349AB
Isoform 3A (identifier: Q15746-3) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
1655-1705: Missing.
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
1510 1520 1530 1540 1550
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
1560 1570 1580 1590 1600
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
1610 1620 1630 1640 1650
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
1660 1670 1680 1690 1700
CYILNRLDCT QCLQHPWLMK DTKNMEAKKL SKDRMKKYMA RRKWQKTGNA
1710 1720 1730 1740 1750
VRAIGRLSSM AMISGLSGRK SSTGSPTSPL NAEKLESEED VSQAFLEAVA
1760 1770 1780 1790 1800
EEKPHVKPYF SKTIRDLEVV EGSAARFDCK IEGYPDPEVV WFKDDQSIRE
1810 1820 1830 1840 1850
SRHFQIDYDE DGNCSLIISD VCGDDDAKYT CKAVNSLGEA TCTAELIVET
1860
MEEGEGEGEE EEE
Length:1,863
Mass (Da):205,059
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iA526210F1B9E546C
Isoform 3B (identifier: Q15746-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
1655-1705: Missing.
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEGLAV MEVAPSFSSV
460 470 480 490 500
LKDCAVIEGQ DFVLQCSVRG TPVPRITWLL NGQPIQYARS TCEAGVAELH
510 520 530 540 550
IQDALPEDHG TYTCLAENAL GQVSCSAWVT VHEKKSSRKS EYLLPVAPSK
560 570 580 590 600
PTAPIFLQGL SDLKVMDGSQ VTMTVQVSGN PPPEVIWLHN GNEIQESEDF
610 620 630 640 650
HFEQRGTQHS LCIQEVFPED TGTYTCEAWN SAGEVRTQAV LTVQEPHDGT
660 670 680 690 700
QPWFISKPRS VTASLGQSVL ISCAIAGDPF PTVHWLRDGK ALCKDTGHFE
710 720 730 740 750
VLQNEDVFTL VLKKVQPWHA GQYEILLKNR VGECSCQVSL MLQNSSARAL
760 770 780 790 800
PRGREPASCE DLCGGGVGAD GGGSDRYGSL RPGWPARGQG WLEEEDGEDV
810 820 830 840 850
RGVLKRRVET RQHTEEAIRQ QEVEQLDFRD LLGKKVSTKT LSEDDLKEIP
860 870 880 890 900
AEQMDFRANL QRQVKPKTVS EEERKVHSPQ QVDFRSVLAK KGTSKTPVPE
910 920 930 940 950
KVPPPKPATP DFRSVLGGKK KLPAENGSSS AETLNAKAVE SSKPLSNAQP
960 970 980 990 1000
SGPLKPVGNA KPAETLKPMG NAKPAETLKP MGNAKPDENL KSASKEELKK
1010 1020 1030 1040 1050
DVKNDVNCKR GHAGTTDNEK RSESQGTAPA FKQKLQDVHV AEGKKLLLQC
1060 1070 1080 1090 1100
QVSSDPPATI IWTLNGKTLK TTKFIILSQE GSLCSVSIEK ALPEDRGLYK
1110 1120 1130 1140 1150
CVAKNDAGQA ECSCQVTVDD APASENTKAP EMKSRRPKSS LPPVLGTESD
1160 1170 1180 1190 1200
ATVKKKPAPK TPPKAAMPPQ IIQFPEDQKV RAGESVELFG KVTGTQPITC
1210 1220 1230 1240 1250
TWMKFRKQIQ ESEHMKVENS ENGSKLTILA ARQEHCGCYT LLVENKLGSR
1260 1270 1280 1290 1300
QAQVNLTVVD KPDPPAGTPC ASDIRSSSLT LSWYGSSYDG GSAVQSYSIE
1310 1320 1330 1340 1350
IWDSANKTWK ELATCRSTSF NVQDLLPDHE YKFRVRAINV YGTSEPSQES
1360 1370 1380 1390 1400
ELTTVGEKPE EPKDEVEVSD DDEKEPEVDY RTVTINTEQK VSDFYDIEER
1410 1420 1430 1440 1450
LGSGKFGQVF RLVEKKTRKV WAGKFFKAYS AKEKENIRQE ISIMNCLHHP
1460 1470 1480 1490 1500
KLVQCVDAFE EKANIVMVLE IVSGGELFER IIDEDFELTE RECIKYMRQI
1510 1520 1530 1540 1550
SEGVEYIHKQ GIVHLDLKPE NIMCVNKTGT RIKLIDFGLA RRLENAGSLK
1560 1570 1580 1590 1600
VLFGTPEFVA PEVINYEPIG YATDMWSIGV ICYILNRLDC TQCLQHPWLM
1610 1620 1630 1640 1650
KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN AVRAIGRLSS MAMISGLSGR
1660 1670 1680 1690 1700
KSSTGSPTSP LNAEKLESEE DVSQAFLEAV AEEKPHVKPY FSKTIRDLEV
1710 1720 1730 1740 1750
VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD EDGNCSLIIS
1760 1770 1780 1790
DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE
Length:1,794
Mass (Da):197,399
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i9EE35F5BADBB0D9A
Isoform 4 (identifier: Q15746-5) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
1473-1545: Missing.
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSLFERIIDE DFELTERECI KYMRQISEGV
1510 1520 1530 1540 1550
EYIHKQGIVH LDLKPENIMC VNKTGTRIKL IDFGLARRLE NAGSLKVLFG
1560 1570 1580 1590 1600
TPEFVAPEVI NYEPIGYATD MWSIGVICYI LVSGLSPFMG DNDNETLANV
1610 1620 1630 1640 1650
TSATWDFDDE AFDEISDDAK DFISNLLKKD MKNRLDCTQC LQHPWLMKDT
1660 1670 1680 1690 1700
KNMEAKKLSK DRMKKYMARR KWQKTGNAVR AIGRLSSMAM ISGLSGRKSS
1710 1720 1730 1740 1750
TGSPTSPLNA EKLESEEDVS QAFLEAVAEE KPHVKPYFSK TIRDLEVVEG
1760 1770 1780 1790 1800
SAARFDCKIE GYPDPEVVWF KDDQSIRESR HFQIDYDEDG NCSLIISDVC
1810 1820 1830 1840
GDDDAKYTCK AVNSLGEATC TAELIVETME EGEGEGEEEE E
Length:1,841
Mass (Da):202,350
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i23EDB48D1A11DE70
Isoform Del-1790 (identifier: Q15746-6) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
1790-1790: Missing.
10 20 30 40 50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
1510 1520 1530 1540 1550
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
1560 1570 1580 1590 1600
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
1610 1620 1630 1640 1650
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
1660 1670 1680 1690 1700
CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL
1710 1720 1730 1740 1750
KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN
1760 1770 1780 1790 1800
AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESED VSQAFLEAVA
1810 1820 1830 1840 1850
EEKPHVKPYF SKTIRDLEVV EGSAARFDCK IEGYPDPEVV WFKDDQSIRE
1860 1870 1880 1890 1900
SRHFQIDYDE DGNCSLIISD VCGDDDAKYT CKAVNSLGEA TCTAELIVET
1910
MEEGEGEGEE EEE
Length:1,913
Mass (Da):210,586
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i6D3029D5CCA13B41
Isoform 5 (identifier: Q15746-7) [UniParc]FASTAAdd to basketAdded to basket
Also known as: Smooth-muscle isozyme
The sequence of this isoform differs from the canonical sequence as follows:
1-922: Missing.
10 20 30 40 50
MDFRANLQRQ VKPKTVSEEE RKVHSPQQVD FRSVLAKKGT SKTPVPEKVP
60 70 80 90 100
PPKPATPDFR SVLGGKKKLP AENGSSSAET LNAKAVESSK PLSNAQPSGP
110 120 130 140 150
LKPVGNAKPA ETLKPMGNAK PAETLKPMGN AKPDENLKSA SKEELKKDVK
160 170 180 190 200
NDVNCKRGHA GTTDNEKRSE SQGTAPAFKQ KLQDVHVAEG KKLLLQCQVS
210 220 230 240 250
SDPPATIIWT LNGKTLKTTK FIILSQEGSL CSVSIEKALP EDRGLYKCVA
260 270 280 290 300
KNDAGQAECS CQVTVDDAPA SENTKAPEMK SRRPKSSLPP VLGTESDATV
310 320 330 340 350
KKKPAPKTPP KAAMPPQIIQ FPEDQKVRAG ESVELFGKVT GTQPITCTWM
360 370 380 390 400
KFRKQIQESE HMKVENSENG SKLTILAARQ EHCGCYTLLV ENKLGSRQAQ
410 420 430 440 450
VNLTVVDKPD PPAGTPCASD IRSSSLTLSW YGSSYDGGSA VQSYSIEIWD
460 470 480 490 500
SANKTWKELA TCRSTSFNVQ DLLPDHEYKF RVRAINVYGT SEPSQESELT
510 520 530 540 550
TVGEKPEEPK DEVEVSDDDE KEPEVDYRTV TINTEQKVSD FYDIEERLGS
560 570 580 590 600
GKFGQVFRLV EKKTRKVWAG KFFKAYSAKE KENIRQEISI MNCLHHPKLV
610 620 630 640 650
QCVDAFEEKA NIVMVLEIVS GGELFERIID EDFELTEREC IKYMRQISEG
660 670 680 690 700
VEYIHKQGIV HLDLKPENIM CVNKTGTRIK LIDFGLARRL ENAGSLKVLF
710 720 730 740 750
GTPEFVAPEV INYEPIGYAT DMWSIGVICY ILVSGLSPFM GDNDNETLAN
760 770 780 790 800
VTSATWDFDD EAFDEISDDA KDFISNLLKK DMKNRLDCTQ CLQHPWLMKD
810 820 830 840 850
TKNMEAKKLS KDRMKKYMAR RKWQKTGNAV RAIGRLSSMA MISGLSGRKS
860 870 880 890 900
STGSPTSPLN AEKLESEEDV SQAFLEAVAE EKPHVKPYFS KTIRDLEVVE
910 920 930 940 950
GSAARFDCKI EGYPDPEVVW FKDDQSIRES RHFQIDYDED GNCSLIISDV
960 970 980 990
CGDDDAKYTC KAVNSLGEAT CTAELIVETM EEGEGEGEEE EE
Note: Transcribed from an alternative promoter resulting in the usage of Met-923 as initiator codon.1 Publication
Show »<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.36"An intronic MYLK variant associated with inflammatory lung disease regulates promoter activity of the smooth muscle myosin light chain kinase isoform."
Han Y.J., Ma S.F., Wade M.S., Flores C., Garcia J.G.
J. Mol. Med. 90:299-308(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORMS 5/9).
Length:992
Mass (Da):110,205
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i27288359F94FE260
Isoform 6 (identifier: Q15746-8) [UniParc]FASTAAdd to basketAdded to basket
Also known as: Telokin
The sequence of this isoform differs from the canonical sequence as follows:
1-1760: Missing.
10 20 30 40 50
MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV AEEKPHVKPY
60 70 80 90 100
FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD
110 120 130 140 150
EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE
EEEE
Note: Transcribed from an alternative promoter resulting in the usage of Met-1761 as initiator codon. Has no catalytic activity. Initiator Met is removed.Combined sources
Show »<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
- Ref.37"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 6 AND 8), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 6), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Length:154
Mass (Da):16,970
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0E3B6CAD36C563EE
Isoform 7 (identifier: Q15746-9) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-1200: Missing.
10 20 30 40 50
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
60 70 80 90 100
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
110 120 130 140 150
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
160 170 180 190 200
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
210 220 230 240 250
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
260 270 280 290 300
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
310 320 330 340 350
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
360 370 380 390 400
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
410 420 430 440 450
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
460 470 480 490 500
CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL
510 520 530 540 550
KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN
560 570 580 590 600
AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV
610 620 630 640 650
AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR
660 670 680 690 700
ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE
710
TMEEGEGEGE EEEE
Note: No experimental confirmation available.
Show »Length:714
Mass (Da):80,410
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i5C3E8AD06D8B855D
Isoform 8 (identifier: Q15746-10) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-1760: Missing.
1790-1790: Missing.
10 20 30 40 50
MAMISGLSGR KSSTGSPTSP LNAEKLESED VSQAFLEAVA EEKPHVKPYF
60 70 80 90 100
SKTIRDLEVV EGSAARFDCK IEGYPDPEVV WFKDDQSIRE SRHFQIDYDE
110 120 130 140 150
DGNCSLIISD VCGDDDAKYT CKAVNSLGEA TCTAELIVET MEEGEGEGEE
EEE
Note: Transcribed from an alternative promoter resulting in the usage of Met-1761 as initiator codon. Initiator Met is removed.Combined sources
Show »<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
- Ref.37"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 6 AND 8), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 6), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Length:153
Mass (Da):16,840
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iBF1292FFEB166F7B
Isoform 9 (identifier: Q15746-11) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-922: Missing.
1790-1790: Missing.
10 20 30 40 50
MDFRANLQRQ VKPKTVSEEE RKVHSPQQVD FRSVLAKKGT SKTPVPEKVP
60 70 80 90 100
PPKPATPDFR SVLGGKKKLP AENGSSSAET LNAKAVESSK PLSNAQPSGP
110 120 130 140 150
LKPVGNAKPA ETLKPMGNAK PAETLKPMGN AKPDENLKSA SKEELKKDVK
160 170 180 190 200
NDVNCKRGHA GTTDNEKRSE SQGTAPAFKQ KLQDVHVAEG KKLLLQCQVS
210 220 230 240 250
SDPPATIIWT LNGKTLKTTK FIILSQEGSL CSVSIEKALP EDRGLYKCVA
260 270 280 290 300
KNDAGQAECS CQVTVDDAPA SENTKAPEMK SRRPKSSLPP VLGTESDATV
310 320 330 340 350
KKKPAPKTPP KAAMPPQIIQ FPEDQKVRAG ESVELFGKVT GTQPITCTWM
360 370 380 390 400
KFRKQIQESE HMKVENSENG SKLTILAARQ EHCGCYTLLV ENKLGSRQAQ
410 420 430 440 450
VNLTVVDKPD PPAGTPCASD IRSSSLTLSW YGSSYDGGSA VQSYSIEIWD
460 470 480 490 500
SANKTWKELA TCRSTSFNVQ DLLPDHEYKF RVRAINVYGT SEPSQESELT
510 520 530 540 550
TVGEKPEEPK DEVEVSDDDE KEPEVDYRTV TINTEQKVSD FYDIEERLGS
560 570 580 590 600
GKFGQVFRLV EKKTRKVWAG KFFKAYSAKE KENIRQEISI MNCLHHPKLV
610 620 630 640 650
QCVDAFEEKA NIVMVLEIVS GGELFERIID EDFELTEREC IKYMRQISEG
660 670 680 690 700
VEYIHKQGIV HLDLKPENIM CVNKTGTRIK LIDFGLARRL ENAGSLKVLF
710 720 730 740 750
GTPEFVAPEV INYEPIGYAT DMWSIGVICY ILVSGLSPFM GDNDNETLAN
760 770 780 790 800
VTSATWDFDD EAFDEISDDA KDFISNLLKK DMKNRLDCTQ CLQHPWLMKD
810 820 830 840 850
TKNMEAKKLS KDRMKKYMAR RKWQKTGNAV RAIGRLSSMA MISGLSGRKS
860 870 880 890 900
STGSPTSPLN AEKLESEDVS QAFLEAVAEE KPHVKPYFSK TIRDLEVVEG
910 920 930 940 950
SAARFDCKIE GYPDPEVVWF KDDQSIRESR HFQIDYDEDG NCSLIISDVC
960 970 980 990
GDDDAKYTCK AVNSLGEATC TAELIVETME EGEGEGEEEE E
Note: Transcribed from an alternative promoter resulting in the usage of Met-923 as initiator codon.1 Publication
Show »<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.36"An intronic MYLK variant associated with inflammatory lung disease regulates promoter activity of the smooth muscle myosin light chain kinase isoform."
Han Y.J., Ma S.F., Wade M.S., Flores C., Garcia J.G.
J. Mol. Med. 90:299-308(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORMS 5/9).
Length:991
Mass (Da):110,076
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iBCFD66306197E14C
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Isoform 3A : The sequence AAD15922 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated
Isoform 3B : The sequence AAD15923 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated
Isoform 4 : The sequence AAD15924 differs from that shown. Reason: Frameshift at positions 1433 and 1439.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in AAC18423 (PubMed:9160829).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in AAQ02673 (PubMed:15020676).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in EAW79438 (Ref. 11) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | P → S in EAW79440 (Ref. 11) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 466 | D → N in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 496 | L → V in AAC18423 (PubMed:9160829).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 496 | L → V in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 496 | L → V in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 496 | L → V in AAQ02673 (PubMed:15020676).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 681 | C → W in AAC18423 (PubMed:9160829).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 681 | C → W in AAD15921 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 681 | C → W in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 681 | C → W in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 933 | V → M in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 963 | S → P in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1022 | P → A in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1048 – 1050 | KPM → EAH in CAA59685 (PubMed:8575746).Curated | 3 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1048 – 1050 | KPM → EAH in BAB21504 (Ref. 8) Curated | 3 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1162 | P → L in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1162 | P → L in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1210 | L → P in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1280 | E → D in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1280 | E → D in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1284 | M → I in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1284 | M → I in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1284 | M → I in AAD15924 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1300 | A → G in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1316 | L → S in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1326 | T → S in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1478 | V → C in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1511 | S → T in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1511 | S → T in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1518 | H → P in AAR29061 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1518 | H → P in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1563 | I → T in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1609 | A → P in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1634 | N → I in AAR29061 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1634 | N → I in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1639 – 1640 | GY → D in AAD15922 (PubMed:10198165).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1639 – 1640 | GY → D in AAD15923 (PubMed:10198165).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1639 – 1640 | GY → D in AAD15924 (PubMed:10198165).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1639 | G → R in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1648 | G → R in CAA59685 (PubMed:8575746).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1658 – 1659 | LS → PF in CAA59685 (PubMed:8575746).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1676 | A → P in AAR29061 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1676 | A → P in AAR29062 (PubMed:15507455).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1710 – 1711 | CT → LA in CAA59685 (PubMed:8575746).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1897 | L → H in AAD15922 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1897 | L → H in AAD15923 (PubMed:10198165).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1897 | L → H in AAD15924 (PubMed:10198165).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057106 | 21 | P → H. Corresponds to variant dbSNP:rs28497577EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065570 | 128 | A → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065571 | 133 | Q → H1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065572 | 160 | P → R1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040847 | 261 | V → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040848 | 276 | T → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057107 | 336 | P → L. Corresponds to variant dbSNP:rs35912339EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040849 | 378 | R → H1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040850 | 405 | M → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040851 | 443 | P → S1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040852 | 607 | R → G1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040853 | 652 | P → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040854 | 656 | W → C2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040855 | 692 | T → M1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040856 | 701 | A → T1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040857 | 709 | V → M1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057108 | 845 | R → C. Corresponds to variant dbSNP:rs3732485EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019986 | 861 | L → P. Corresponds to variant dbSNP:rs3732486EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057109 | 877 | V → M. Corresponds to variant dbSNP:rs34542174EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019987 | 914 | D → E. Corresponds to variant dbSNP:rs3732487EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065573 | 1085 | T → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065574 | 1213 | V → M in AAT7; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065575 | 1399 | E → K1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040858 | 1527 | A → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040859 | 1588 | P → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065576 | 1754 | A → T in AAT7; 4-fold reduced affinity for calmodulin; decreased kinase activity compared to wild-type protein. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065577 | 1759 | S → P in AAT7; 7-fold reduced affinity for calmodulin; 6-fold decreased Vmax. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_018846 | 1 – 1760 | Missing in isoform 6 and isoform 8. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1760 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_053791 | 1 – 1200 | Missing in isoform 7. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1200 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_018845 | 1 – 922 | Missing in isoform 5 and isoform 9. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 922 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004791 | 437 – 506 | VSGIP…LQVER → G in isoform 2 and isoform 3B. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 70 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004793 | 1473 – 1545 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 73 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004794 | 1655 – 1705 | Missing in isoform 3A and isoform 3B. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 51 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004795 | 1790 | Missing in isoform Del-1790, isoform 8 and isoform 9. 4 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 |
Sequence databases
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000346322; ENSP00000320622; ENSG00000065534 [Q15746-2] ENST00000354792; ENSP00000346846; ENSG00000065534 [Q15746-2] ENST00000359169; ENSP00000352088; ENSG00000065534 [Q15746-3] ENST00000360304; ENSP00000353452; ENSG00000065534 [Q15746-1] ENST00000360772; ENSP00000354004; ENSG00000065534 [Q15746-3] ENST00000418370; ENSP00000428967; ENSG00000065534 [Q15746-8] ENST00000475616; ENSP00000418335; ENSG00000065534 [Q15746-1] ENST00000578202; ENSP00000463691; ENSG00000065534 [Q15746-10] ENST00000583087; ENSP00000462118; ENSG00000065534 [Q15746-8] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4638 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4638 |
UCSC genome browser More...UCSCi | uc003egl.4 human [Q15746-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative promoter usage, Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q15746 | UPI000387C10C | 1924 | |||
| UPI0005D00DC7 | 1738 | ||||
| Q15746-9 | 714 | ||||
| Q15746-7 | 992 | ||||
| Long myosin light chain kinase (Fragment) | 76 | ||||
| Q15746-6 | UPI0003EAF632 | 1923 | |||
| UPI0007DC522C | 713 | ||||
| Q15746-11 | 991 | ||||
| Q15746-8 | MYLK isoform 5 | 154 | |||
| MYLK isoform 18 | 154 | ||||
| Myosin light chain kinase | 154 | ||||
| Myosin light chain kinase | 154 | ||||
| Myosin light chain kinase | 154 | ||||
| +12 | |||||
| Q15746-10 | MYLK isoform 6 | 153 | |||
| MYLK isoform 21 | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| UPI000653070F | 2675 | ||||
| Q15746-11 | UPI0003EAF632 | 1923 | |||
| Q15746-6 | 1913 | ||||
| UPI0007DC522C | 713 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q15746 | UPI000387C10C | 1924 | |||
| Myosin light chain kinase | 1934 | ||||
| MYLK isoform 10 | 1924 | ||||
| UPI00045D8E9B | 1923 | ||||
| UPI0004D07498 | 1922 | ||||
| +58 | |||||
| Q15746-2 | UPI000387DE20 | 1855 | |||
| UPI000B537FAA | 1860 | ||||
| UPI0004D05378 | 1853 | ||||
| MYLK isoform 2 | 1845 | ||||
| Myosin light chain kinase | 1845 | ||||
| +9 | |||||
| Q15746-3 | UPI000B52BF68 | 1878 | |||
| UPI0004D05922 | 1871 | ||||
| MYLK isoform 1 | 1863 | ||||
| MYLK isoform 1 | 1863 | ||||
| Myosin light chain kinase | 1863 | ||||
| +6 | |||||
| Q15746-8 | MYLK isoform 6 | 153 | |||
| MYLK isoform 21 | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| UPI000653070F | 2675 | ||||
| +18 | |||||
| Q15746-10 | MYLK isoform 6 | 153 | |||
| MYLK isoform 21 | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| Myosin light chain kinase | 153 | ||||
| UPI000653070F | 2675 | ||||
| +18 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q15746 | UPI000387C10C | 1924 | |||
| Myosin light chain kinase | 1934 | ||||
| MYLK isoform 10 | 1924 | ||||
| UPI00045D8E9B | 1923 | ||||
| UPI0004D07498 | 1922 | ||||
| +117 | |||||
| Q15746-2 | UPI000B5335DE | 1878 | |||
| UPI0004D05922 | 1871 | ||||
| Myosin light chain kinase | 1863 | ||||
| Myosin light chain kinase | 1863 | ||||
| MYLK isoform 1 | 1863 | ||||
| +38 | |||||
| Q15746-3 | UPI000B5335DE | 1878 | |||
| UPI0004D05922 | 1871 | ||||
| Myosin light chain kinase | 1863 | ||||
| Myosin light chain kinase | 1863 | ||||
| MYLK isoform 1 | 1863 | ||||
| +38 | |||||
| Q15746-4 | UPI000B5332F7 | 1809 | |||
| UPI0004D040C2 | 1802 | ||||
| UPI0005F3FDC2 | 1794 | ||||
| UPI00083C10CC | 1687 | ||||
| UPI00062A5633 | 1716 | ||||
| +250 | |||||
| Q15746-8 | Myosin light chain kinase, smooth muscle | 1176 | |||
| UPI00042CE525 | 2162 | ||||
| Myosin light chain kinase (Fragment) | 120 | ||||
| UPI000951EE12 | 255 | ||||
| UPI0003C133A9 | 156 | ||||
| +37 | |||||
| Q15746-10 | Myosin light chain kinase, smooth muscle | 1176 | |||
| UPI00042CE525 | 2162 | ||||
| Myosin light chain kinase (Fragment) | 120 | ||||
| UPI000951EE12 | 255 | ||||
| UPI0003C133A9 | 156 | ||||
| +37 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Myosin light-chain kinase entry |
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2CQV | NMR | - | A | 1238-1338 | [»] | |
| 2K0F | NMR | - | B | 1742-1760 | [»] | |
| 2YR3 | NMR | - | A | 510-601 | [»] | |
| 5JQA | X-ray | 1.80 | B | 1742-1761 | [»] | |
| 5JTH | X-ray | 1.84 | B | 1742-1761 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q15746 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q15746 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110722, 17 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q15746 |
Protein interaction database and analysis system More...IntActi | Q15746, 23 interactors |
Molecular INTeraction database More...MINTi | Q15746 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353452 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q15746 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2428 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1552 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q15746 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q15746 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MYLK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 300669714 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q15746 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q15746 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q15746 |
PeptideAtlas More...PeptideAtlasi | Q15746 |
PRoteomics IDEntifications database More...PRIDEi | Q15746 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 60733 60734 [Q15746-2] 60735 [Q15746-3] 60736 [Q15746-4] 60737 [Q15746-5] 60738 [Q15746-6] 60739 [Q15746-7] 60740 [Q15746-8] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4638 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000346322; ENSP00000320622; ENSG00000065534 [Q15746-2] ENST00000354792; ENSP00000346846; ENSG00000065534 [Q15746-2] ENST00000359169; ENSP00000352088; ENSG00000065534 [Q15746-3] ENST00000360304; ENSP00000353452; ENSG00000065534 [Q15746-1] ENST00000360772; ENSP00000354004; ENSG00000065534 [Q15746-3] ENST00000418370; ENSP00000428967; ENSG00000065534 [Q15746-8] ENST00000475616; ENSP00000418335; ENSG00000065534 [Q15746-1] ENST00000578202; ENSP00000463691; ENSG00000065534 [Q15746-10] ENST00000583087; ENSP00000462118; ENSG00000065534 [Q15746-8] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4638 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4638 |
UCSC genome browser More...UCSCi | uc003egl.4 human [Q15746-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4638 |
DisGeNET More...DisGeNETi | 4638 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000065534.18 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MYLK |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | MYLK |
Human Gene Nomenclature Database More...HGNCi | HGNC:7590 MYLK |
Human Protein Atlas More...HPAi | CAB020789 HPA031677 HPA048055 |
MalaCards human disease database More...MalaCardsi | MYLK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600922 gene 613780 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q15746 |
Open Targets More...OpenTargetsi | ENSG00000065534 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 91387 Familial thoracic aortic aneurysm and aortic dissection |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31388 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0613 Eukaryota ENOG410XQFD LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118877 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000049287 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052551 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q15746 |
KEGG Orthology (KO) More...KOi | K00907 |
Identification of Orthologs from Complete Genome Data More...OMAi | KFIILSQ |
Database of Orthologous Groups More...OrthoDBi | EOG091G005W |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q15746 |
TreeFam database of animal gene trees More...TreeFami | TF314166 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.11.18 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-445355 Smooth Muscle Contraction R-HSA-5627123 RHO GTPases activate PAKs |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q15746 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q15746 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q15746 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MYLK human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q15746 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MYLK |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4638 |
Protein Ontology More...PROi | PR:Q15746 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000065534 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q15746 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q15746 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00063 FN3, 1 hit cd14191 STKc_MLCK1, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.10, 10 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003961 FN3_dom IPR036116 FN3_sf IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR013098 Ig_I-set IPR003599 Ig_sub IPR003598 Ig_sub2 IPR011009 Kinase-like_dom_sf IPR015725 MLCK1_kinase_dom IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00041 fn3, 1 hit PF07679 I-set, 9 hits PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00060 FN3, 1 hit SM00409 IG, 9 hits SM00408 IGc2, 9 hits SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48726 SSF48726, 9 hits SSF49265 SSF49265, 1 hit SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50853 FN3, 1 hit PS50835 IG_LIKE, 9 hits PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MYLK_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q15746Primary (citable) accession number: Q15746 Secondary accession number(s): B4DUE3 , D3DN97, O95796, O95797, O95798, O95799, Q14844, Q16794, Q17S15, Q3ZCP9, Q5MY99, Q5MYA0, Q6P2N0, Q7Z4J0, Q9C0L5, Q9UBG5, Q9UBY6, Q9UIT9 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
| Last sequence update: | July 13, 2010 | |
| Last modified: | July 18, 2018 | |
| This is version 200 of the entry and version 4 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families - UniProtKB entry view manual
User manual for the UniProtKB entry view
