MYLK4_MOUSE
ID MYLK4_MOUSE Reviewed; 386 AA.
AC Q5SUV5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Myosin light chain kinase family member 4;
DE EC=2.7.11.1;
DE AltName: Full=Sugen kinase 85;
DE Short=SgK085;
GN Name=Mylk4; Synonyms=Sgk085;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AL645808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q5SUV5; -.
DR SMR; Q5SUV5; -.
DR STRING; 10090.ENSMUSP00000060149; -.
DR iPTMnet; Q5SUV5; -.
DR PhosphoSitePlus; Q5SUV5; -.
DR MaxQB; Q5SUV5; -.
DR PaxDb; Q5SUV5; -.
DR PRIDE; Q5SUV5; -.
DR ProteomicsDB; 287658; -.
DR MGI; MGI:3643758; Mylk4.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; Q5SUV5; -.
DR PhylomeDB; Q5SUV5; -.
DR ChiTaRS; Mylk4; mouse.
DR PRO; PR:Q5SUV5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5SUV5; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..386
FT /note="Myosin light chain kinase family member 4"
FT /id="PRO_0000261031"
FT DOMAIN 107..361
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 386 AA; 43905 MW; 6BD8AAEC2A86D2C7 CRC64;
MLKVKRLEEI SSCHSSNPLE KVAFFQCMEE VEKVKCFLEE NSGDLDLQSG DNEAEENVWS
NRALDERIIV KGGRTSALTD DIPAPAAPFD HRMVMAKHAS VDNLYTVSKS EILGGGRFGQ
VHKCEEKATG LKLAAKIIKT RGAKDKEDVK NEISVMNQLD HVNLIQLYDA FESKHDIILV
MDVEGGELFD RIIDENCNLT ELDTILFMKQ ICEGIRYMHQ MYILHLDLKP ENILCVNRDA
KQIKIIDFGL ARRYKPREKL KVNFGTPEFL APEVVNYDFV SFSTDMWSVG VITYMLLSGL
SPFLGDNDAE TLTNILACRW DLEDEEFQDI SEEAKEFISK LLIKEKSWRI SASEALKHPW
LSDHKLHSRL SAQKNCNSGV LNLTTK
