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 12-APR-2017, entry version 141. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS NON-MUSCLE AND RP SMOOTH MUSCLE). RX PubMed=2722814; RA Lenz S., Lohse P., Seidel U., Arnold H.H.; RT "The alkali light chains of human smooth and nonmuscle myosins are RT encoded by a single gene. Tissue-specific expression by alternative RT splicing 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; RA Hailstones D.L., Gunning P.W.; RT "Characterization of human myosin light chains 1sa and 3nm: RT implications 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 RT myocardial 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 RT project: 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 RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM SMOOTH RP MUSCLE), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [11] 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., RA Buerckstuemmer T., 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION RP BY 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., 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 P58397:ADAMTS12; NbExp=3; IntAct=EBI-300817, EBI-9028051; CC P03372:ESR1; NbExp=3; IntAct=EBI-300817, EBI-78473; CC O43809:NUDT21; NbExp=3; 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; CC Note=Contains a phosphoserine at position 135. CC {ECO:0000244|PubMed:18669648}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.632717; -. DR ProteinModelPortal; P60660; -. DR SMR; P60660; -. DR BioGrid; 110721; 66. DR IntAct; P60660; 43. DR MINT; MINT-1131667; -. DR STRING; 9606.ENSP00000446714; -. DR iPTMnet; 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 MaxQB; P60660; -. DR PaxDb; P60660; -. DR PeptideAtlas; P60660; -. DR PRIDE; P60660; -. DR TopDownProteomics; P60660-1; -. [P60660-1] DR TopDownProteomics; P60660-2; -. [P60660-2] DR DNASU; 4637; -. DR Ensembl; ENST00000547649; ENSP00000446714; ENSG00000092841. [P60660-2] DR Ensembl; ENST00000548293; ENSP00000448101; ENSG00000092841. [P60660-1] DR Ensembl; ENST00000550697; ENSP00000446955; ENSG00000092841. [P60660-1] DR GeneID; 4637; -. DR KEGG; hsa:4637; -. DR UCSC; uc001sjw.3; human. DR CTD; 4637; -. DR GeneCards; MYL6; -. DR HGNC; HGNC:7587; MYL6. DR HPA; HPA046859; -. DR HPA; HPA063034; -. DR MIM; 609931; gene. DR neXtProt; NX_P60660; -. DR OpenTargets; ENSG00000092841; -. DR PharmGKB; PA31384; -. DR eggNOG; KOG0030; Eukaryota. DR eggNOG; COG5126; LUCA. DR GeneTree; ENSGT00590000082921; -. DR HOVERGEN; HBG012180; -. DR InParanoid; P60660; -. DR KO; K12751; -. DR PhylomeDB; P60660; -. DR TreeFam; TF351553; -. 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 ChiTaRS; MYL6; human. DR GeneWiki; MYL6; -. DR GenomeRNAi; 4637; -. DR PRO; PR:P60660; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000092841; -. DR CleanEx; HS_MYL6; -. 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; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0016459; C:myosin complex; TAS:HGNC. DR GO; GO:0016461; C:unconventional myosin complex; TAS:BHF-UCL. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0030898; F:actin-dependent ATPase activity; ISS:HGNC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0003774; F:motor activity; TAS:HGNC. DR GO; GO:0008307; F:structural constituent of muscle; IDA:HGNC. DR GO; GO:0006936; P:muscle contraction; TAS:HGNC. DR GO; GO:0030049; P:muscle filament sliding; TAS:HGNC. DR GO; GO:0007519; P:skeletal muscle tissue development; TAS:UniProtKB. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.238.10; -; 4. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR002048; EF_hand_dom. DR Pfam; PF13405; EF-hand_6; 1. 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; Complete proteome; KW Direct protein sequencing; Motor protein; Muscle protein; Myosin; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000244|PubMed:25944712}. FT CHAIN 2 151 Myosin light polypeptide 6. FT /FTId=PRO_0000198690. FT DOMAIN 7 42 EF-hand 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 84 119 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 119 151 EF-hand 3. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT MOD_RES 2 2 N-acetylcysteine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000244|PubMed:25944712}. FT MOD_RES 57 57 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 81 81 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT VAR_SEQ 143 151 AFVRHILSG -> ELVRMVLNG (in isoform Smooth FT muscle). {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:2722814}. FT /FTId=VSP_009735. FT VARIANT 85 85 T -> I (in dbSNP:rs11553509). FT /FTId=VAR_050457. FT VARIANT 103 103 T -> P (in dbSNP:rs1050470). FT /FTId=VAR_034118. FT CONFLICT 10 10 A -> ADLIPST (in Ref. 3; AAA20643). FT {ECO:0000305}. FT CONFLICT 45 45 N -> D (in Ref. 2; AAA59853). FT {ECO:0000305}. FT CONFLICT 76 76 T -> R (in Ref. 3; AAA20643). FT {ECO:0000305}. SQ SEQUENCE 151 AA; 16930 MW; A2B7B4F41179523D CRC64; MCDFTEDQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEM NVKVLDFEHF LPMLQTVAKN KDQGTYEDYV EGLRVFDKEG NGTVMGAEIR HVLVTLGEKM TEEEVEMLVA GHEDSNGCIN YEAFVRHILS G //