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P11799

- MYLK_CHICK

UniProt

P11799 - MYLK_CHICK

Protein

Myosin light chain kinase, smooth muscle

Gene

Mylk

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity
    Calcium.By similarity

    Enzyme regulationi

    Activated by phosphorylation on Tyr-478. Isoforms which lack this tyrosine residue are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1482 – 14821ATPPROSITE-ProRule annotation
    Active sitei1574 – 15741Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1459 – 14679ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. myosin light chain kinase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.18. 1306.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin light chain kinase, smooth muscle (EC:2.7.11.18)
    Short name:
    MLCK
    Alternative name(s):
    Telokin
    Cleaved into the following chain:
    Gene namesi
    Name:Mylk
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Membrane 1 Publication
    Note: Telokin is cytosolic and can translocate to the membrane upon stimulation.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1762 – 17621S → A: Decreases membrane translocation. 1 Publication
    Mutagenesisi1768 – 17681S → A: Decreases membrane translocation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19061906Myosin light chain kinase, smooth musclePRO_0000024361Add
    BLAST
    Chaini1 – 19011901Myosin light chain kinase, smooth muscle, deglutamylated formPRO_0000424867Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei478 – 4781Phosphotyrosine1 Publication
    Modified residuei1748 – 17481Phosphoserine1 Publication
    Modified residuei1762 – 17621Phosphoserine; by PKG2 Publications
    Modified residuei1768 – 17681Phosphoserine; by MAPK2 Publications

    Post-translational modificationi

    The C-terminus is deglutamylated, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The C-terminus is variable, with one to five C-terminal glutamyl residues being removed producing five forms differring in their number of C-terminal glutamyl residues.
    Acetylated.1 Publication
    Phosphorylation of telokin by PKG has no significant effect on its myosin binding activity, but promotes translocation to the membrane.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP11799.
    PRIDEiP11799.

    Expressioni

    Tissue specificityi

    Isoform telokin is expressed in gizzard, heart, lung, intestine, and skeletal muscle although the levels of the expression in the latter were much less than that in the gizzard.

    Interactioni

    Subunit structurei

    All isoforms including Telokin bind calmodulin.1 Publication

    Protein-protein interaction databases

    BioGridi676694. 1 interaction.
    IntActiP11799. 3 interactions.

    Structurei

    Secondary structure

    1
    1906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1731 – 174717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CDLX-ray2.00E/F/G/H1730-1749[»]
    1QS7X-ray1.80B/D1731-1749[»]
    1QTXX-ray1.65B1731-1749[»]
    1VRKX-ray1.90B1731-1749[»]
    2O5GX-ray1.08B1730-1748[»]
    3EVUX-ray1.75A1731-1749[»]
    3EVVX-ray2.60A1731-1749[»]
    3O77X-ray2.35A1730-1749[»]
    3O78X-ray2.60A/B1730-1749[»]
    ProteinModelPortaliP11799.
    SMRiP11799. Positions 525-614, 1221-1325, 1448-1716, 1785-1887.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11799.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 11790Ig-like C2-type 1Add
    BLAST
    Domaini156 – 24489Ig-like C2-type 2Add
    BLAST
    Domaini429 – 51789Ig-like C2-type 3Add
    BLAST
    Domaini521 – 61393Ig-like C2-type 4Add
    BLAST
    Domaini637 – 72589Ig-like C2-type 5Add
    BLAST
    Repeati660 – 67617IIA-1Add
    BLAST
    Repeati693 – 70816IIB-1Add
    BLAST
    Domaini735 – 83096Ig-like C2-type 6Add
    BLAST
    Repeati758 – 77417IIA-2Add
    BLAST
    Repeati791 – 80717IIB-2Add
    BLAST
    Repeati970 – 98718III-1Add
    BLAST
    Repeati999 – 101618III-2Add
    BLAST
    Repeati1061 – 107818III-3Add
    BLAST
    Domaini1084 – 117289Ig-like C2-type 7Add
    BLAST
    Repeati1107 – 112317IIA-3Add
    BLAST
    Repeati1140 – 115617IIB-3Add
    BLAST
    Repeati1209 – 122618III-4Add
    BLAST
    Domaini1225 – 131389Ig-like C2-type 8Add
    BLAST
    Repeati1281 – 129717IIB-4Add
    BLAST
    Domaini1321 – 141494Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1453 – 1708256Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1794 – 188592Ig-like C2-type 9Add
    BLAST
    Repeati1817 – 183317IIA-4Add
    BLAST
    Repeati1851 – 186616IIB-5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni660 – 183311744 X repeats, motif IIAAdd
    BLAST
    Regioni693 – 186611745 X repeats, motif IIBAdd
    BLAST
    Regioni970 – 12262574 X repeats, motif IIIAdd
    BLAST
    Regioni1317 – 136448Motif IAAdd
    BLAST
    Regioni1385 – 140218Motif IBAdd
    BLAST
    Regioni1700 – 176364Calmodulin-bindingAdd
    BLAST
    Regioni1716 – 172813Calmodulin autoinhibition (AM13) regionSequence AnalysisAdd
    BLAST
    Regioni1730 – 174920Calmodulin recognition (RS20) regionSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1896 – 190611Poly-GluAdd
    BLAST

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049287.
    HOVERGENiHBG052551.
    InParanoidiP11799.
    KOiK00907.
    PhylomeDBiP11799.

    Family and domain databases

    Gene3Di2.60.40.10. 10 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR015725. Telokin/Myosin_light_ch_kin.
    [Graphical view]
    PANTHERiPTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF44. PTHR22964:SF44. 1 hit.
    PfamiPF00041. fn3. 1 hit.
    PF07679. I-set. 9 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 8 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. 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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative initiation. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P11799-1) [UniParc]FASTAAdd to Basket

    Also known as: MLCK-108, Smooth-muscle

    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

    MGDVKLVTST RVSKTSLTLS PSVPAEAPAF TLPPRNIRVQ LGATARFEGK     50
    VRGYPEPQIT WYRNGHPLPE GDHYVVDHSI RGIFSLVIKG VQEGDSGKYT 100
    CEAANDGGVR QVTVELTVEG NSLKKYSLPS SAKTPGGRLS VPPVEHRPSI 150
    WGESPPKFAT KPNRVVVREG QTGRFSCKIT GRPQPQVTWT KGDIHLQQNE 200
    RFNMFEKTGI QYLEIQNVQL ADAGIYTCTV VNSAGKASVS AELTVQGPDK 250
    TDTHAQPLCM PPKPTTLATK AIENSDFKQA TSNGIAKELK STSTELMVET 300
    KDRLSAKKET FYTSREAKDG KQGQNQEANA VPLQESRGTK GPQVLQKTSS 350
    TITLQAVKAQ PEPKAEPQTT FIRQAEDRKR TVQPLMTTTT QENPSLTGQV 400
    SPRSRETENR AGVRKSVKEE KREPLGIPPQ FESRPQSLEA SEGQEIKFKS 450
    KVSGKPKPDV EWFKEGVPIK TGEGIQIYEE DGTHCLWLKK ACLGDSGSYS 500
    CAAFNPRGQT STSWLLTVKR PKVEEVAPCF SSVLKGCTVS EGQDFVLQCY 550
    VGGVPVPEIT WLLNEQPIQY AHSTFEAGVA KLTVQDALPE DDGIYTCLAE 600
    NNAGRASCSA QVTVKEKKSS KKAEGTQAAK LNKTFAPIFL KGLTDLKVMD 650
    GSQVIMTVEV SANPCPEIIW LHNGKEIQET EDFHFEKKGN EYSLYIQEVF 700
    PEDTGKYTCE AWNELGETQT QATLTVQEPQ DGIQPWFISK PRSVTAAAGQ 750
    NVLISCAIAG DPFPTVHWFK DGQEITPGTG CEILQNEDIF TLILRNVQSR 800
    HAGQYEIQLR NQVGECSCQV SLMLRESSAS RAEMLRDGRE SASSGERRDG 850
    GNYGALTFGR TSGFKKSSSE TRAAEEEQED VRGVLKRRVE TREHTEESLR 900
    QQEAEQLDFR DILGKKVSTK SFSEEDLKEI PAEQMDFRAN LQRQVKPKTL 950
    SEEERKVHAP QQVDFRSVLA KKGTPKTPLP EKVPPPKPAV TDFRSVLGAK 1000
    KKPPAENGSA STPAPNARAG SEAQNATPNS EAPAPKPVVK KEEKNDRKCE 1050
    HGCAVVDGGI IGKKAENKPA ASKPTPPPSK GTAPSFTEKL QDAKVADGEK 1100
    LVLQCRISSD PPASVSWTLD SKAIKSSKSI VISQEGTLCS LTIEKVMPED 1150
    GGEYKCIAEN AAGKAECACK VLVEDTSSTK AAKPAEKKTK KPKTTLPPVL 1200
    STESSEATVK KKPAPKTPPK AATPPQITQF PEDRKVRAGE SVELFAKVVG 1250
    TAPITCTWMK FRKQIQENEY IKIENAENSS KLTISSTKQE HCGCYTLVVE 1300
    NKLGSRQAQV NLTVVDKPDP PAGTPCASDI RSSSLTLSWY GSSYDGGSAV 1350
    QSYTVEIWNS VDNKWTDLTT CRSTSFNVQD LQADREYKFR VRAANVYGIS 1400
    EPSQESEVVK VGEKQEEELK EEEAELSDDE GKETEVNYRT VTINTEQKVS 1450
    DVYNIEERLG SGKFGQVFRL VEKKTGKVWA GKFFKAYSAK EKENIRDEIS 1500
    IMNCLHHPKL VQCVDAFEEK ANIVMVLEMV SGGELFERII DEDFELTERE 1550
    CIKYMRQISE GVEYIHKQGI VHLDLKPENI MCVNKTGTSI KLIDFGLARR 1600
    LESAGSLKVL FGTPEFVAPE VINYEPIGYE TDMWSIGVIC YILVSGLSPF 1650
    MGDNDNETLA NVTSATWDFD DEAFDEISDD AKDFISNLLK KDMKSRLNCT 1700
    QCLQHPWLQK DTKNMEAKKL SKDRMKKYMA RRKWQKTGHA VRAIGRLSSM 1750
    AMISGMSGRK ASGSSPTSPI NADKVENEDA FLEEVAEEKP HVKPYFTKTI 1800
    LDMEVVEGSA ARFDCKIEGY PDPEVMWYKD DQPVKESRHF QIDYDEEGNC 1850
    SLTISEVCGD DDAKYTCKAV NSLGEATCTA ELLVETMGKE GEGEGEGEED 1900
    EEEEEE 1906
    Length:1,906
    Mass (Da):210,446
    Last modified:July 15, 1998 - v2
    Checksum:iAD7D8A3B69EE3363
    GO
    Isoform 2 (identifier: P11799-2) [UniParc]FASTAAdd to Basket

    Also known as: MLCK-210, Non-muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         1-934: Missing.

    Show »
    Length:972
    Mass (Da):107,547
    Checksum:i375ED3627731EFFE
    GO
    Isoform 3 (identifier: P11799-3) [UniParc]FASTAAdd to Basket

    Also known as: Telokin

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1749: Missing.

    Show »
    Length:157
    Mass (Da):17,337
    Checksum:i557E7CD96C672E7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1439 – 14391R → Q in AAA49069. (PubMed:3030394)Curated
    Sequence conflicti1439 – 14391R → Q in AAA69964. (PubMed:3030394)Curated
    Sequence conflicti1776 – 17761E → D AA sequence (PubMed:9283094)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17491749Missing in isoform 3. 2 PublicationsVSP_018852Add
    BLAST
    Alternative sequencei1 – 934934Missing in isoform 2. 1 PublicationVSP_018851Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52876 mRNA. Translation: CAA37056.1.
    X52876 mRNA. Translation: CAA37057.1.
    X52876 mRNA. Translation: CAA37058.1.
    M31048 mRNA. Translation: AAA49069.1.
    M14953 mRNA. Translation: AAA69964.1.
    AF045285
    , AF045255, AF045256, AF045257, AF045260, AF045259, AF045258, AF045261, AF045263, AF045265, AF045274, AF045273, AF045272, AF045271, AF045270, AF045269, AF045268, AF045267, AF045266, AF045283, AF045282, AF045281, AF045280, AF045279, AF045278, AF045277, AF045276, AF045275, AF045284, AF045264, AF045262 Genomic DNA. Translation: AAC29031.1.
    M96655 mRNA. Translation: AAA49083.1.
    M88283 mRNA. Translation: AAA48647.1.
    M88284 Genomic DNA. Translation: AAB53768.1.
    PIRiS68235.
    RefSeqiNP_990790.1. NM_205459.2. [P11799-1]
    UniGeneiGga.4091.

    Genome annotation databases

    GeneIDi396445.
    KEGGigga:396445.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52876 mRNA. Translation: CAA37056.1 .
    X52876 mRNA. Translation: CAA37057.1 .
    X52876 mRNA. Translation: CAA37058.1 .
    M31048 mRNA. Translation: AAA49069.1 .
    M14953 mRNA. Translation: AAA69964.1 .
    AF045285
    , AF045255 , AF045256 , AF045257 , AF045260 , AF045259 , AF045258 , AF045261 , AF045263 , AF045265 , AF045274 , AF045273 , AF045272 , AF045271 , AF045270 , AF045269 , AF045268 , AF045267 , AF045266 , AF045283 , AF045282 , AF045281 , AF045280 , AF045279 , AF045278 , AF045277 , AF045276 , AF045275 , AF045284 , AF045264 , AF045262 Genomic DNA. Translation: AAC29031.1 .
    M96655 mRNA. Translation: AAA49083.1 .
    M88283 mRNA. Translation: AAA48647.1 .
    M88284 Genomic DNA. Translation: AAB53768.1 .
    PIRi S68235.
    RefSeqi NP_990790.1. NM_205459.2. [P11799-1 ]
    UniGenei Gga.4091.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CDL X-ray 2.00 E/F/G/H 1730-1749 [» ]
    1QS7 X-ray 1.80 B/D 1731-1749 [» ]
    1QTX X-ray 1.65 B 1731-1749 [» ]
    1VRK X-ray 1.90 B 1731-1749 [» ]
    2O5G X-ray 1.08 B 1730-1748 [» ]
    3EVU X-ray 1.75 A 1731-1749 [» ]
    3EVV X-ray 2.60 A 1731-1749 [» ]
    3O77 X-ray 2.35 A 1730-1749 [» ]
    3O78 X-ray 2.60 A/B 1730-1749 [» ]
    ProteinModelPortali P11799.
    SMRi P11799. Positions 525-614, 1221-1325, 1448-1716, 1785-1887.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676694. 1 interaction.
    IntActi P11799. 3 interactions.

    Chemistry

    BindingDBi P11799.
    ChEMBLi CHEMBL3062.

    Proteomic databases

    PaxDbi P11799.
    PRIDEi P11799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396445.
    KEGGi gga:396445.

    Organism-specific databases

    CTDi 4638.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049287.
    HOVERGENi HBG052551.
    InParanoidi P11799.
    KOi K00907.
    PhylomeDBi P11799.

    Enzyme and pathway databases

    BRENDAi 2.7.11.18. 1306.

    Miscellaneous databases

    EvolutionaryTracei P11799.
    NextBioi 20816486.
    PROi P11799.

    Family and domain databases

    Gene3Di 2.60.40.10. 10 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR020675. Myosin_light_ch_kinase-rel.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR015725. Telokin/Myosin_light_ch_kin.
    [Graphical view ]
    PANTHERi PTHR22964. PTHR22964. 1 hit.
    PTHR22964:SF44. PTHR22964:SF44. 1 hit.
    Pfami PF00041. fn3. 1 hit.
    PF07679. I-set. 9 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 8 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple gene products are produced from a novel protein kinase transcription region."
      Watterson D.M., Collinge M., Lukas T.J., van Eldik L.J., Birukov K.G., Stepanova O.V., Shirinsky V.P.
      FEBS Lett. 373:217-220(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Regulatory and structural motifs of chicken gizzard myosin light chain kinase."
      Olson N.J., Pearson R.B., Needleman D.S., Hurwitz M.J., Kemp B.E., Means A.R.
      Proc. Natl. Acad. Sci. U.S.A. 87:2284-2288(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The organization of the genetic locus for chicken myosin light chain kinase is complex: multiple proteins are encoded and exhibit differential expression and localization."
      Birukov K.G., Schavocky J.P., Shirinsky V.P., Van Eldik L.J., Watterson D.M.
      J. Cell. Biochem. 70:402-413(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    4. "Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity."
      Shoemaker M.O., Lau W., Shattuck R.L., Kwiatkowski A.P., Matrisian P.E., Guerra-Santos L., Wilson E., Lukas T.J., van Eldik L.J., Watterson D.M.
      J. Cell Biol. 111:1107-1125(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 649-1906, PARTIAL PROTEIN SEQUENCE.
      Tissue: Fibroblast.
    5. "Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA."
      Guerriero V. Jr., Russo M.A., Olson N.J., Putkey J.A., Means A.R.
      Biochemistry 25:8372-8381(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1906.
      Tissue: Gizzard.
    6. "Molecular cloning of the chicken gizzard telokin gene and cDNA."
      Yoshikai S., Ikebe M.
      Arch. Biochem. Biophys. 299:242-247(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1906 (ISOFORM 3).
      Tissue: Gizzard.
    7. "Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene."
      Collinge M., Matrisian P.E., Zimmer W.E., Shattuck R.L., Lukas T.J., van Eldik L.J., Watterson D.M.
      Mol. Cell. Biol. 12:2359-2371(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1750-1906 (ISOFORM 3).
    8. "Characterization of the chicken telokin heterogeneity by time-of-flight mass spectrometry."
      Rusconi F., Potier M.C., Le Caer J.P., Schmitter J.M., Rossier J.
      Biochemistry 36:11021-11026(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1775-1789, ACETYLATION, DEGLUTAMYLATION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Translocation of telokin by cGMP signaling in smooth muscle cells."
      Komatsu S., Miyazaki K., Tuft R.A., Ikebe M.
      Am. J. Physiol. 283:C752-C761(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1762 AND SER-1768, MUTAGENESIS OF SER-1762 AND SER-1768.
    10. "Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties."
      Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F., Watterson D.M.
      Biochemistry 38:3936-3947(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1731-1749 IN COMPLEX WITH CALM1 AND CALCIUM.

    Entry informationi

    Entry nameiMYLK_CHICK
    AccessioniPrimary (citable) accession number: P11799
    Secondary accession number(s): P19038, Q549S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3