MYL6_HUMAN
ID MYL6_HUMAN Reviewed; 151 AA.
AC P60660; P16475; P24572; P24573; Q12790; Q561V9; Q6IAZ0; Q6IPY5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Myosin light polypeptide 6;
DE AltName: Full=17 kDa myosin light chain;
DE Short=LC17;
DE AltName: Full=Myosin light chain 3;
DE Short=MLC-3;
DE AltName: Full=Myosin light chain alkali 3;
DE Short=Myosin light chain A3;
DE AltName: Full=Smooth muscle and nonmuscle myosin light chain alkali 6;
GN Name=MYL6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS NON-MUSCLE AND SMOOTH
RP MUSCLE).
RX PubMed=2722814; DOI=10.1016/s0021-9258(18)81895-6;
RA Lenz S., Lohse P., Seidel U., Arnold H.H.;
RT "The alkali light chains of human smooth and nonmuscle myosins are encoded
RT by a single gene. Tissue-specific expression by alternative splicing
RT pathways.";
RL J. Biol. Chem. 264:9009-9015(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NON-MUSCLE).
RX PubMed=2304459; DOI=10.1128/mcb.10.3.1095-1104.1990;
RA Hailstones D.L., Gunning P.W.;
RT "Characterization of human myosin light chains 1sa and 3nm: implications
RT for isoform evolution and function.";
RL Mol. Cell. Biol. 10:1095-1104(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NON-MUSCLE).
RC TISSUE=Eye;
RX PubMed=8188229; DOI=10.1006/geno.1994.1041;
RA Bora P.S., Bora N.S., Wu X., Kaplan H.J., Lange L.G.;
RT "Molecular cloning, sequencing, and characterization of smooth muscle
RT myosin alkali light chain from human eye cDNA: homology with myocardial
RT fatty acid ethyl ester synthase-III cDNA.";
RL Genomics 19:186-188(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NON-MUSCLE).
RX PubMed=11436981; DOI=10.1540/jsmr.37.25;
RA Watanabe M., Kohri M., Takaishi M., Horie R., Higashihara M.;
RT "Molecular cloning and sequencing of myosin light chains in human
RT megakaryoblastic leukemia cells.";
RL J. Smooth Muscle Res. 37:25-38(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-MUSCLE).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS NON-MUSCLE AND SMOOTH
RP MUSCLE).
RC TISSUE=Brain, Duodenum, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 14-21; 38-50; 64-94 AND 111-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM SMOOTH MUSCLE),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Regulatory light chain of myosin. Does not bind calcium.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC Interacts with SPATA6. {ECO:0000250|UniProtKB:Q60605}.
CC -!- INTERACTION:
CC P60660; P58397: ADAMTS12; NbExp=4; IntAct=EBI-300817, EBI-9028051;
CC P60660; O95994: AGR2; NbExp=3; IntAct=EBI-300817, EBI-712648;
CC P60660; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-300817, EBI-742054;
CC P60660; P03372: ESR1; NbExp=3; IntAct=EBI-300817, EBI-78473;
CC P60660; Q86XJ1: GAS2L3; NbExp=3; IntAct=EBI-300817, EBI-9248152;
CC P60660; O43809: NUDT21; NbExp=5; IntAct=EBI-300817, EBI-355720;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Non-muscle; Synonyms=MLC3nm, LC17A, LC17-nm;
CC IsoId=P60660-1, P16475-1;
CC Sequence=Displayed;
CC Name=Smooth muscle; Synonyms=MLC3sm, LC17B, LC17-sm;
CC IsoId=P60660-2, P24572-2;
CC Sequence=VSP_009735;
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DR EMBL; M22918; AAA36347.1; -; mRNA.
DR EMBL; M22919; AAA59892.1; -; Genomic_DNA.
DR EMBL; M22919; AAA59893.1; -; Genomic_DNA.
DR EMBL; M22920; AAA36348.1; -; mRNA.
DR EMBL; M31212; AAA59853.1; -; mRNA.
DR EMBL; U02629; AAA20643.1; -; mRNA.
DR EMBL; AB046613; BAB62402.1; -; mRNA.
DR EMBL; CR457014; CAG33295.1; -; mRNA.
DR EMBL; BC006781; AAH06781.2; -; mRNA.
DR EMBL; BC017455; AAH17455.1; -; mRNA.
DR EMBL; BC071661; AAH71661.1; -; mRNA.
DR EMBL; BC093066; AAH93066.1; -; mRNA.
DR CCDS; CCDS31834.1; -. [P60660-2]
DR CCDS; CCDS8906.1; -.
DR PIR; A33709; MOHU6N.
DR PIR; A49620; MOHU6E.
DR PIR; B33709; MOHU6M.
DR RefSeq; NP_066299.2; NM_021019.4. [P60660-1]
DR RefSeq; NP_524147.2; NM_079423.3. [P60660-2]
DR AlphaFoldDB; P60660; -.
DR SMR; P60660; -.
DR BioGRID; 110721; 189.
DR CORUM; P60660; -.
DR IntAct; P60660; 80.
DR MINT; P60660; -.
DR STRING; 9606.ENSP00000446955; -.
DR GlyGen; P60660; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P60660; -.
DR MetOSite; P60660; -.
DR PhosphoSitePlus; P60660; -.
DR SwissPalm; P60660; -.
DR BioMuta; MYL6; -.
DR DMDM; 47606436; -.
DR DOSAC-COBS-2DPAGE; P60660; -.
DR SWISS-2DPAGE; P60660; -.
DR EPD; P60660; -.
DR jPOST; P60660; -.
DR MassIVE; P60660; -.
DR MaxQB; P60660; -.
DR PaxDb; P60660; -.
DR PeptideAtlas; P60660; -.
DR PRIDE; P60660; -.
DR ProteomicsDB; 57221; -.
DR ProteomicsDB; 57222; -. [P60660-2]
DR TopDownProteomics; P60660-1; -. [P60660-1]
DR TopDownProteomics; P60660-2; -. [P60660-2]
DR Antibodypedia; 27997; 350 antibodies from 29 providers.
DR DNASU; 4637; -.
DR Ensembl; ENST00000547649.5; ENSP00000446714.1; ENSG00000092841.19. [P60660-2]
DR Ensembl; ENST00000548293.5; ENSP00000448101.1; ENSG00000092841.19. [P60660-1]
DR Ensembl; ENST00000550697.6; ENSP00000446955.2; ENSG00000092841.19. [P60660-1]
DR GeneID; 4637; -.
DR KEGG; hsa:4637; -.
DR MANE-Select; ENST00000550697.6; ENSP00000446955.2; NM_021019.5; NP_066299.2.
DR UCSC; uc001sjw.3; human.
DR CTD; 4637; -.
DR GeneCards; MYL6; -.
DR HGNC; HGNC:7587; MYL6.
DR HPA; ENSG00000092841; Low tissue specificity.
DR MIM; 609931; gene.
DR neXtProt; NX_P60660; -.
DR OpenTargets; ENSG00000092841; -.
DR PharmGKB; PA31384; -.
DR VEuPathDB; HostDB:ENSG00000092841; -.
DR eggNOG; KOG0030; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR InParanoid; P60660; -.
DR OrthoDB; 1470794at2759; -.
DR PhylomeDB; P60660; -.
DR TreeFam; TF351553; -.
DR PathwayCommons; P60660; -.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR SignaLink; P60660; -.
DR BioGRID-ORCS; 4637; 28 hits in 1074 CRISPR screens.
DR ChiTaRS; MYL6; human.
DR GeneWiki; MYL6; -.
DR GenomeRNAi; 4637; -.
DR Pharos; P60660; Tbio.
DR PRO; PR:P60660; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P60660; protein.
DR Bgee; ENSG00000092841; Expressed in muscle layer of sigmoid colon and 204 other tissues.
DR ExpressionAtlas; P60660; baseline and differential.
DR Genevisible; P60660; HS.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; TAS:HGNC-UCL.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0016461; C:unconventional myosin complex; TAS:BHF-UCL.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:HGNC-UCL.
DR GO; GO:0000146; F:microfilament motor activity; ISS:HGNC-UCL.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:HGNC-UCL.
DR GO; GO:0006936; P:muscle contraction; TAS:HGNC-UCL.
DR GO; GO:0030049; P:muscle filament sliding; TAS:HGNC-UCL.
DR GO; GO:0007519; P:skeletal muscle tissue development; TAS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Motor protein; Muscle protein; Myosin; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..151
FT /note="Myosin light polypeptide 6"
FT /id="PRO_0000198690"
FT DOMAIN 7..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 84..119
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..151
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 143..151
FT /note="AFVRHILSG -> ELVRMVLNG (in isoform Smooth muscle)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2722814"
FT /id="VSP_009735"
FT VARIANT 85
FT /note="T -> I (in dbSNP:rs11553509)"
FT /id="VAR_050457"
FT VARIANT 103
FT /note="T -> P (in dbSNP:rs1050470)"
FT /id="VAR_034118"
FT CONFLICT 10
FT /note="A -> ADLIPST (in Ref. 3; AAA20643)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="N -> D (in Ref. 2; AAA59853)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="T -> R (in Ref. 3; AAA20643)"
FT /evidence="ECO:0000305"
FT MOD_RES P60660-2:135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 151 AA; 16930 MW; A2B7B4F41179523D CRC64;
MCDFTEDQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEM
NVKVLDFEHF LPMLQTVAKN KDQGTYEDYV EGLRVFDKEG NGTVMGAEIR HVLVTLGEKM
TEEEVEMLVA GHEDSNGCIN YEAFVRHILS G
