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Protein

Myosin light chain kinase, smooth muscle

Gene

Mylk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.9 Publications

Catalytic activityi

ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1515ATPPROSITE-ProRule annotation1
Active sitei1607Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1492 – 1500ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • myosin light chain kinase activity Source: MGI

GO - Biological processi

  • aorta smooth muscle tissue morphogenesis Source: MGI
  • bleb assembly Source: MGI
  • cellular hypotonic response Source: MGI
  • cellular response to calcium ion Source: MGI
  • cellular response to drug Source: MGI
  • cellular response to potassium ion Source: MGI
  • positive regulation of calcium ion transport Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of wound healing Source: MGI
  • smooth muscle contraction Source: UniProtKB
  • tonic smooth muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

Actin-binding, ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.18. 3474.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

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:
Gene namesi
Name:MylkImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:894806. Mylk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Mice lacking isoform 1 show a reduced flow-mediated dilation of small mesenteric arteries but no significant changes in main cardiovascular function. Increased survival from burn. Prevention of epithelial MLC phosphorylation, tight junction disruption, protein leak, and diarrhea following T-cell activation.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002339491 – 1941Myosin light chain kinase, smooth muscleAdd BLAST1941
ChainiPRO_00004037321 – 1934Myosin light chain kinase, smooth muscle, deglutamylated formAdd BLAST1934

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi177 ↔ 228PROSITE-ProRule annotation
Modified residuei226Phosphotyrosine; by ABL1By similarity1
Modified residuei295PhosphoserineBy similarity1
Modified residuei333PhosphoserineCombined sources1
Modified residuei355PhosphoserineCombined sources1
Disulfide bondi423 ↔ 475PROSITE-ProRule annotation
Modified residuei452Phosphotyrosine; by ABL1 and SRCBy similarity1
Disulfide bondi523 ↔ 571PROSITE-ProRule annotation
Disulfide bondi730 ↔ 793PROSITE-ProRule annotation
Modified residuei780Phosphotyrosine; by ABL1By similarity1
Modified residuei935PhosphoserineCombined sources1
Disulfide bondi1141 ↔ 1192PROSITE-ProRule annotation
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1471Phosphotyrosine; by ABL1By similarity1
Modified residuei1597Phosphotyrosine; by ABL1By similarity1
Modified residuei1657Phosphotyrosine; by ABL1By similarity1
Modified residuei1781PhosphoserineCombined sources1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1794PhosphoserineBy similarity1
Modified residuei1795PhosphoserineCombined sources1
Modified residuei1798PhosphoserineCombined sources1
Modified residuei1800PhosphothreonineCombined sources1
Modified residuei1801PhosphoserineCombined sources1
Disulfide bondi1852 ↔ 1904PROSITE-ProRule annotation

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-452 promotes CTTN binding (By similarity).By similarity
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 (PubMed:21074048).1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ6PDN3.
PeptideAtlasiQ6PDN3.
PRIDEiQ6PDN3.

PTM databases

iPTMnetiQ6PDN3.
PhosphoSitePlusiQ6PDN3.

Expressioni

Tissue specificityi

Smooth muscle isoform expressed in all tissues with highest levels in bladder, uterus, vas deferens, colon, ileum, and tracheae. Isoform 1 expressed in lung, bladder, and vas deferens. Telokin expressed in smooth muscle cells of uterus, vas deferens, bladder, colon, kidney, ureter, ovary and trachea.2 Publications

Developmental stagei

Isoform 1 ubiquitously expressed in E14.5 embryos with highest levels in some areas of the developing brain, the lower gastrointestinal tract as well as certain blood vessels. Primary cultures of endothelial cells lose high level expression of Smooth muscle isoform with increasing number of passages. Telokin expressed in embryonic gut from E11.5 with highest level in E15.5. Also expressed in developing bronchi from E13.5. High levels in E15.5 bladder, ureter, urethra and rectum. Telokin expression is induced in reproductive tract during postnatal development.2 Publications

Gene expression databases

CleanExiMM_MYLK.

Interactioni

Subunit structurei

All isoforms including Telokin bind calmodulin. 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 (By similarity). Interacts with SVIL and PTK2B/PYK2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Patz1Q9JMG93EBI-647412,EBI-647451

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ6PDN3. 21 interactors.
MINTiMINT-1849579.
STRINGi10090.ENSMUSP00000023538.

Structurei

3D structure databases

ProteinModelPortaliQ6PDN3.
SMRiQ6PDN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 122Ig-like C2-type 1Sequence analysisAdd BLAST90
Domaini156 – 244Ig-like C2-type 2Sequence analysisAdd BLAST89
Domaini402 – 485Ig-like C2-type 3Sequence analysisAdd BLAST84
Domaini502 – 587Ig-like C2-type 4Sequence analysisAdd BLAST86
Domaini611 – 699Ig-like C2-type 5Sequence analysisAdd BLAST89
Domaini709 – 809Ig-like C2-type 6Sequence analysisAdd BLAST101
Repeati856 – 8831-1By similarityAdd BLAST28
Repeati884 – 9111-2By similarityAdd BLAST28
Repeati912 – 9391-3By similarityAdd BLAST28
Repeati940 – 9661-4By similarityAdd BLAST27
Repeati967 – 9851-5; truncatedAdd BLAST19
Repeati990 – 10022-1By similarityAdd BLAST13
Repeati1003 – 10142-2By similarityAdd BLAST12
Repeati1015 – 10262-3By similarityAdd BLAST12
Repeati1027 – 10382-4By similarityAdd BLAST12
Repeati1039 – 10492-5By similarityAdd BLAST11
Domaini1120 – 1208Ig-like C2-type 7Sequence analysisAdd BLAST89
Domaini1260 – 1348Ig-like C2-type 8Sequence analysisAdd BLAST89
Domaini1356 – 1449Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST94
Domaini1486 – 1741Protein kinasePROSITE-ProRule annotationAdd BLAST256
Domaini1831 – 1920Ig-like C2-type 9Sequence analysisAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni856 – 9855 X 28 AA approximate tandem repeatsAdd BLAST130
Regioni911 – 951Actin-binding (calcium/calmodulin-sensitive)By similarityAdd BLAST41
Regioni936 – 951Calmodulin-bindingBy similarityAdd BLAST16
Regioni990 – 10495 X 12 AA approximate tandem repeatsAdd BLAST60
Regioni1048 – 1482Actin-binding (calcium/calmodulin-insensitive)By similarityAdd BLAST435
Regioni1733 – 1796Calmodulin-bindingBy similarityAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1918 – 1941Glu-richSequence analysisAdd BLAST24

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 9 Ig-like C2-type (immunoglobulin-like) domains.Sequence analysis
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
HOVERGENiHBG052551.
InParanoidiQ6PDN3.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. 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.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. AlignAdd to basket

Isoform 11 Publication (identifier: Q6PDN3-1) [UniParc]FASTAAdd to basket
Also known as: Non muscle isozyme1 Publication

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.

« Hide

        10         20         30         40         50
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED
110 120 130 140 150
KGKYTCEASN GSGARQVTVE LTVEGNSMKK RDQPVLSKAS GFPGETRPSI
160 170 180 190 200
WGECPPKFAT KLGRAVVKEG QMWRFSCKIT GRPPPQVTWL KGNVPLQPSA
210 220 230 240 250
RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS AELSIPGLDN
260 270 280 290 300
ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
310 320 330 340 350
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA
360 370 380 390 400
IGSFSPGEDR KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST
410 420 430 440 450
FPRFESQPQS QEVTEGQTVK FICEVSGIPK PDVGWFLEGI PVRRREGITE
460 470 480 490 500
VYEDGVSHHL CLLRARTRDS RKYSCTASNS LGQVSCSWSL LVDRPNLAQT
510 520 530 540 550
APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ PIQFAHSICE
560 570 580 590 600
AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
610 620 630 640 650
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE
660 670 680 690 700
IQESEDFHFE QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV
710 720 730 740 750
QEPHDGTQPW FISKPRSVTA TLGQSVLISC AIAGDPFPTV HWLRDGRALS
760 770 780 790 800
KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY EILLKNRVGE CSCQVSLMLH
810 820 830 840 850
NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC WPARGQGWPE
860 870 880 890 900
EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
910 920 930 940 950
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT
960 970 980 990 1000
PKTPVPEKAP PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP
1010 1020 1030 1040 1050
AGDAQAIGAL KPVGNAKPAE TPKPIGNAKP TETLKPVGNT KPAETLKPIA
1060 1070 1080 1090 1100
NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE TSKPAGKEEV KEVKNDVNCK
1110 1120 1130 1140 1150
KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ CQVISDPPAT
1160 1170 1180 1190 1200
VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
1210 1220 1230 1240 1250
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP
1260 1270 1280 1290 1300
KTPTKAAMPP QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI
1310 1320 1330 1340 1350
QESEHIKVEN GESGSKLTIL AARQEHCGCY TLVVENKLGS RQAQVNLTVV
1360 1370 1380 1390 1400
DKPDPPAGTP CASDIRSSSL TLSWYGSSYD GGSAVQSYNV EIWDTEDKVW
1410 1420 1430 1440 1450
KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE SELTAVGEKP
1460 1470 1480 1490 1500
EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
1510 1520 1530 1540 1550
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF
1560 1570 1580 1590 1600
EEKANIVMVL EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK
1610 1620 1630 1640 1650
QGIVHLDLKP ENIMCVNKTG TRIKLIDFGL ARRLENAGSL KVLFGTPEFV
1660 1670 1680 1690 1700
APEVINYEPI GYATDMWSIG VICYILVSGL SPFMGDNDNE TLANVTSATW
1710 1720 1730 1740 1750
DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW LMKDTKNMEA
1760 1770 1780 1790 1800
KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
1810 1820 1830 1840 1850
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF
1860 1870 1880 1890 1900
DCKIEGYPDP EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA
1910 1920 1930 1940
KYTCKAVNSL GEATCTAELI VETMEEGEGE EGGEEEEEEE E
Length:1,941
Mass (Da):212,925
Last modified:May 2, 2006 - v3
Checksum:i7FF12C60F1BDFFDD
GO
Isoform 21 Publication (identifier: Q6PDN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1254: Missing.
     1255-1256: KA → MQ

Note: Produced by alternative promoter usage and alternative splicing. No experimental confirmation available.
Show »
Length:687
Mass (Da):77,433
Checksum:iDCCF826A8ABA42B5
GO
Isoform 3 (identifier: Q6PDN3-3) [UniParc]FASTAAdd to basket
Also known as: Smooth muscle isozyme

The sequence of this isoform differs from the canonical sequence as follows:
     1-910: Missing.

Note: Produced by alternative initiation at Met-911 of isoform 1.
Show »
Length:1,031
Mass (Da):113,703
Checksum:iD9435CF18C0E4337
GO
Isoform 4 (identifier: Q6PDN3-4) [UniParc]FASTAAdd to basket
Also known as: Telokin

The sequence of this isoform differs from the canonical sequence as follows:
     1-1782: Missing.

Note: Produced by alternative initiation at Met-1783 of isoform 1.
Show »
Length:159
Mass (Da):17,529
Checksum:i7EFDC75F450F3B6D
GO

Sequence cautioni

The sequence AAH58610 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO85807 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173W → G (PubMed:11832329).Curated1
Sequence conflicti173W → G (PubMed:11472067).Curated1
Sequence conflicti252S → A in AAK53241 (PubMed:11472067).Curated1
Sequence conflicti471 – 472RK → GR (PubMed:11832329).Curated2
Sequence conflicti471 – 472RK → GR (PubMed:11472067).Curated2
Sequence conflicti478S → T in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti482G → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti666 – 667HS → TP in AAO85807 (PubMed:11832329).Curated2
Sequence conflicti677D → S in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti749 – 750LS → SP in AAO85807 (PubMed:11832329).Curated2
Sequence conflicti1004A → G in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1038G → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1106A → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1174 – 1181RFSVSIEK → TFLCLHRE in AAO85807 (PubMed:11832329).Curated8
Sequence conflicti1210D → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1289I → T in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1340Missing in BAE36678 (PubMed:16141072).Curated1
Sequence conflicti1409T → H in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1657Y → H in AAH58610 (PubMed:15489334).Curated1
Sequence conflicti1661G → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1678S → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1706A → E in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1732 – 1735CTQC → STHG in AAO85807 (PubMed:11832329).Curated4
Sequence conflicti1825E → K in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1888S → T in AAG34169 (PubMed:11121372).Curated1
Sequence conflicti1941Missing in AAH58610 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188481 – 1782Missing in isoform 4. 1 PublicationAdd BLAST1782
Alternative sequenceiVSP_0520021 – 1254Missing in isoform 2. 1 PublicationAdd BLAST1254
Alternative sequenceiVSP_0188471 – 910Missing in isoform 3. 1 PublicationAdd BLAST910
Alternative sequenceiVSP_0520031255 – 1256KA → MQ in isoform 2. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237727 mRNA. Translation: AAO85808.1.
AF314149 mRNA. Translation: AAG34169.1.
AY237726 mRNA. Translation: AAO85807.1. Different initiation.
AK162008 mRNA. Translation: BAE36678.1.
BC034209 mRNA. Translation: AAH34209.1.
BC045197 mRNA. Translation: AAH45197.1.
BC058610 mRNA. Translation: AAH58610.2. Different initiation.
AF335470 Genomic DNA. Translation: AAK53241.1.
UniGeneiMm.33360.

Genome annotation databases

UCSCiuc007zbe.1. mouse. [Q6PDN3-1]
uc007zbh.1. mouse. [Q6PDN3-4]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237727 mRNA. Translation: AAO85808.1.
AF314149 mRNA. Translation: AAG34169.1.
AY237726 mRNA. Translation: AAO85807.1. Different initiation.
AK162008 mRNA. Translation: BAE36678.1.
BC034209 mRNA. Translation: AAH34209.1.
BC045197 mRNA. Translation: AAH45197.1.
BC058610 mRNA. Translation: AAH58610.2. Different initiation.
AF335470 Genomic DNA. Translation: AAK53241.1.
UniGeneiMm.33360.

3D structure databases

ProteinModelPortaliQ6PDN3.
SMRiQ6PDN3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6PDN3. 21 interactors.
MINTiMINT-1849579.
STRINGi10090.ENSMUSP00000023538.

Protein family/group databases

MEROPSiI43.001.

PTM databases

iPTMnetiQ6PDN3.
PhosphoSitePlusiQ6PDN3.

Proteomic databases

PaxDbiQ6PDN3.
PeptideAtlasiQ6PDN3.
PRIDEiQ6PDN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc007zbe.1. mouse. [Q6PDN3-1]
uc007zbh.1. mouse. [Q6PDN3-4]

Organism-specific databases

MGIiMGI:894806. Mylk.

Phylogenomic databases

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
HOVERGENiHBG052551.
InParanoidiQ6PDN3.

Enzyme and pathway databases

BRENDAi2.7.11.18. 3474.

Miscellaneous databases

ChiTaRSiMylk. mouse.
PROiQ6PDN3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MYLK.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. 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.
[Graphical view]
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Entry informationi

Entry nameiMYLK_MOUSE
AccessioniPrimary (citable) accession number: Q6PDN3
Secondary accession number(s): Q3TSJ7
, Q80UX0, Q80YN7, Q80YN8, Q8K026, Q924D2, Q9ERD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: November 30, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.