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Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac-MyBP-C-associated Ca/CaM kinase) (Cardiac-MLCK)

 MYLK3_HUMAN             Reviewed;         819 AA.
Q32MK0; B5BUL9; B7Z5U8; Q32MK1; Q96DV1;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
12-SEP-2018, entry version 108.
RecName: Full=Myosin light chain kinase 3;
EC=2.7.11.18;
AltName: Full=Cardiac-MyBP-C-associated Ca/CaM kinase;
Short=Cardiac-MLCK;
Name=MYLK3; Synonyms=MLCK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-180.
TISSUE=Cardiac myocyte;
Mues A., Seidel R., Gautel M.;
"The cardiac-MyBP-C associated Ca/CaM kinase is a novel MLCK with
cardiac-specific domains.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-180.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=17885681; DOI=10.1172/JCI30804;
Seguchi O., Takashima S., Yamazaki S., Asakura M., Asano Y.,
Shintani Y., Wakeno M., Minamino T., Kondo H., Furukawa H.,
Nakamaru K., Naito A., Takahashi T., Ohtsuka T., Kawakami K.,
Isomura T., Kitamura S., Tomoike H., Mochizuki N., Kitakaze M.;
"A cardiac myosin light chain kinase regulates sarcomere assembly in
the vertebrate heart.";
J. Clin. Invest. 117:2812-2824(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-408, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
VARIANT [LARGE SCALE ANALYSIS] ARG-390.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Kinase that phosphorylates MYL2 in vitro. Promotes
sarcomere formation in cardiomyocytes and increases cardiomyocyte
contractility (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + [myosin light-chain] = ADP + [myosin
light-chain] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q32MK0-3; Sequence=Displayed;
Name=2;
IsoId=Q32MK0-4; Sequence=VSP_044312;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Restricted to heart.
{ECO:0000269|PubMed:17885681}.
-!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI09098.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC42766.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AJ247087; CAC42766.1; ALT_INIT; mRNA.
EMBL; AK299443; BAH13034.1; -; mRNA.
EMBL; AB451455; BAG70269.1; -; mRNA.
EMBL; AC007225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC109097; AAI09098.2; ALT_INIT; mRNA.
CCDS; CCDS10723.2; -. [Q32MK0-3]
CCDS; CCDS76861.1; -. [Q32MK0-4]
RefSeq; NP_001295230.1; NM_001308301.1. [Q32MK0-4]
RefSeq; NP_872299.2; NM_182493.2. [Q32MK0-3]
RefSeq; XP_006721397.1; XM_006721334.3. [Q32MK0-4]
UniGene; Hs.130465; -.
ProteinModelPortal; Q32MK0; -.
SMR; Q32MK0; -.
BioGrid; 124881; 7.
IntAct; Q32MK0; 2.
STRING; 9606.ENSP00000378288; -.
BindingDB; Q32MK0; -.
ChEMBL; CHEMBL4627; -.
iPTMnet; Q32MK0; -.
PhosphoSitePlus; Q32MK0; -.
BioMuta; MYLK3; -.
DMDM; 254763411; -.
MaxQB; Q32MK0; -.
PaxDb; Q32MK0; -.
PeptideAtlas; Q32MK0; -.
PRIDE; Q32MK0; -.
ProteomicsDB; 61603; -.
Ensembl; ENST00000394809; ENSP00000378288; ENSG00000140795. [Q32MK0-3]
Ensembl; ENST00000536476; ENSP00000439297; ENSG00000140795. [Q32MK0-4]
GeneID; 91807; -.
KEGG; hsa:91807; -.
UCSC; uc002eei.5; human. [Q32MK0-3]
CTD; 91807; -.
DisGeNET; 91807; -.
EuPathDB; HostDB:ENSG00000140795.12; -.
GeneCards; MYLK3; -.
HGNC; HGNC:29826; MYLK3.
HPA; HPA073447; -.
MIM; 612147; gene.
neXtProt; NX_Q32MK0; -.
OpenTargets; ENSG00000140795; -.
PharmGKB; PA162396375; -.
eggNOG; KOG0032; Eukaryota.
eggNOG; ENOG410XRMJ; LUCA.
GeneTree; ENSGT00760000118877; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG080416; -.
InParanoid; Q32MK0; -.
KO; K00907; -.
OMA; CLTTMDK; -.
OrthoDB; EOG091G005W; -.
PhylomeDB; Q32MK0; -.
TreeFam; TF314166; -.
SignaLink; Q32MK0; -.
ChiTaRS; MYLK3; human.
GeneWiki; MYLK3; -.
GenomeRNAi; 91807; -.
PRO; PR:Q32MK0; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140795; Expressed in 147 organ(s), highest expression level in cardiac muscle of right atrium.
CleanEx; HS_MYLK3; -.
Genevisible; Q32MK0; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:BHF-UCL.
GO; GO:0004687; F:myosin light chain kinase activity; ISS:BHF-UCL.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:BHF-UCL.
GO; GO:0071347; P:cellular response to interleukin-1; IMP:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0060298; P:positive regulation of sarcomere organization; ISS:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; ISS:BHF-UCL.
GO; GO:0002528; P:regulation of vascular permeability involved in acute inflammatory response; IMP:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; ISS:BHF-UCL.
GO; GO:0048769; P:sarcomerogenesis; ISS:BHF-UCL.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Magnesium; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 819 Myosin light chain kinase 3.
/FTId=PRO_0000272200.
DOMAIN 515 770 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 521 529 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 636 636 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 544 544 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:E9PT87}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:E9PT87}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 341 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044312.
VARIANT 70 70 S -> T (in dbSNP:rs9923813).
/FTId=VAR_058335.
VARIANT 180 180 V -> L (in dbSNP:rs28407821).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1}.
/FTId=VAR_058336.
VARIANT 390 390 G -> R (in a colorectal cancer sample;
somatic mutation; dbSNP:rs141602742).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035630.
CONFLICT 149 149 R -> G (in Ref. 2; BAG70269).
{ECO:0000305}.
CONFLICT 199 199 G -> R (in Ref. 1; CAC42766).
{ECO:0000305}.
SEQUENCE 819 AA; 88393 MW; 21148BBACB0FF0D9 CRC64;
MSGTSKESLG HGGLPGLGKT CLTTMDTKLN MLNEKVDQLL HFQEDVTEKL QSMCRDMGHL
ERGLHRLEAS RAPGPGGADG VPHIDTQAGW PEVLELVRAM QQDAAQHGAR LEALFRMVAA
VDRAIALVGA TFQKSKVADF LMQGRVPWRR GSPGDSPEEN KERVEEEGGK PKHVLSTSGV
QSDAREPGEE SQKADVLEGT AERLPPIRAS GLGADPAQAV VSPGQGDGVP GPAQAFPGHL
PLPTKVEAKA PETPSENLRT GLELAPAPGR VNVVSPSLEV APGAGQGASS SRPDPEPLEE
GTRLTPGPGP QCPGPPGLPA QARATHSGGE TPPRISIHIQ EMDTPGEMLM TGRGSLGPTL
TTEAPAAAQP GKQGPPGTGR CLQAPGTEPG EQTPEGAREL SPLQESSSPG GVKAEEEQRA
GAEPGTRPSL ARSDDNDHEV GALGLQQGKS PGAGNPEPEQ DCAARAPVRA EAVRRMPPGA
EAGSVVLDDS PAPPAPFEHR VVSVKETSIS AGYEVCQHEV LGGGRFGQVH RCTEKSTGLP
LAAKIIKVKS AKDREDVKNE INIMNQLSHV NLIQLYDAFE SKHSCTLVME YVDGGELFDR
ITDEKYHLTE LDVVLFTRQI CEGVHYLHQH YILHLDLKPE NILCVNQTGH QIKIIDFGLA
RRYKPREKLK VNFGTPEFLA PEVVNYEFVS FPTDMWSVGV ITYMLLSGLS PFLGETDAET
MNFIVNCSWD FDADTFEGLS EEAKDFVSRL LVKEKSCRMS ATQCLKHEWL NNLPAKASRS
KTRLKSQLLL QKYIAQRKWK KHFYVVTAAN RLRKFPTSP


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