LOCUS       NP_005954               1939 aa            linear   PRI 12-JUN-2025
DEFINITION  myosin-1 [Homo sapiens].
ACCESSION   NP_005954
VERSION     NP_005954.3
DBSOURCE    REFSEQ: accession NM_005963.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1939)
  AUTHORS   Jung,J., Joo,S.Y., Min,H., Roh,J.W., Kim,K.A., Ma,J.H., Rim,J.H.,
            Kim,J.A., Kim,S.J., Jang,S.H., Koh,Y.I., Kim,H.Y., Lee,H.,
            Kim,B.C., Gee,H.Y., Bok,J., Choi,J.Y. and Seong,J.K.
  TITLE     MYH1 deficiency disrupts outer hair cell electromotility, resulting
            in hearing loss
  JOURNAL   Exp Mol Med 56 (11), 2423-2435 (2024)
   PUBMED   39482536
REFERENCE   2  (residues 1 to 1939)
  AUTHORS   Alsaif,H.S., Alshehri,A., Sulaiman,R.A., Al-Hindi,H.,
            Guzman-Vega,F.J., Arold,S.T. and Alkuraya,F.S.
  TITLE     MYH1 is a candidate gene for recurrent rhabdomyolysis in humans
  JOURNAL   Am J Med Genet A 185 (7), 2131-2135 (2021)
   PUBMED   33755318
  REMARK    GeneRIF: MYH1 is a candidate gene for recurrent rhabdomyolysis in
            humans.
REFERENCE   3  (residues 1 to 1939)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1939)
  AUTHORS   Qiu,X., Chen,D., Li,M., Gao,Y., Liu,F., Zheng,H. and Chen,S.
  TITLE     Transition of myosin heavy chain isoforms in human laryngeal
            abductors following denervation
  JOURNAL   Eur Arch Otorhinolaryngol 272 (10), 2915-2923 (2015)
   PUBMED   26059207
  REMARK    GeneRIF: Transcriptional levels of MHC-I, MHC-IIa, and MHC-IIb in
            denervation groups were significantly down-regulated compared with
            controls
REFERENCE   5  (residues 1 to 1939)
  AUTHORS   Miller,M.S., Bedrin,N.G., Ades,P.A., Palmer,B.M. and Toth,M.J.
  TITLE     Molecular determinants of force production in human skeletal muscle
            fibers: effects of myosin isoform expression and cross-sectional
            area
  JOURNAL   Am J Physiol Cell Physiol 308 (6), C473-C484 (2015)
   PUBMED   25567808
  REMARK    GeneRIF: Myosin isoforms impact single-fiber force generation and
            may lead to alterations in whole skeletal muscle performance.
REFERENCE   6  (residues 1 to 1939)
  AUTHORS   Weiss,A., McDonough,D., Wertman,B., Acakpo-Satchivi,L.,
            Montgomery,K., Kucherlapati,R., Leinwand,L. and Krauter,K.
  TITLE     Organization of human and mouse skeletal myosin heavy chain gene
            clusters is highly conserved
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2958-2963 (1999)
   PUBMED   10077619
REFERENCE   7  (residues 1 to 1939)
  AUTHORS   Smerdu,V., Karsch-Mizrachi,I., Campione,M., Leinwand,L. and
            Schiaffino,S.
  TITLE     Type IIx myosin heavy chain transcripts are expressed in type IIb
            fibers of human skeletal muscle
  JOURNAL   Am J Physiol 267 (6 Pt 1), C1723-C1728 (1994)
   PUBMED   7545970
REFERENCE   8  (residues 1 to 1939)
  AUTHORS   Yoon,S.J., Seiler,S.H., Kucherlapati,R. and Leinwand,L.
  TITLE     Organization of the human skeletal myosin heavy chain gene cluster
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12078-12082 (1992)
   PUBMED   1465443
REFERENCE   9  (residues 1 to 1939)
  AUTHORS   Saez,L. and Leinwand,L.A.
  TITLE     Characterization of diverse forms of myosin heavy chain expressed
            in adult human skeletal muscle
  JOURNAL   Nucleic Acids Res 14 (7), 2951-2969 (1986)
   PUBMED   2421254
REFERENCE   10 (residues 1 to 1939)
  AUTHORS   Leinwand,L.A., Saez,L., McNally,E. and Nadal-Ginard,B.
  TITLE     Isolation and characterization of human myosin heavy chain genes
  JOURNAL   Proc Natl Acad Sci U S A 80 (12), 3716-3720 (1983)
   PUBMED   6304733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA826478.1, BC114545.1,
            AF111785.1 and AJ573764.1.
            
            On Oct 4, 2006 this sequence version replaced NP_005954.2.
            
            Summary: Myosin is a major contractile protein which converts
            chemical energy into mechanical energy through the hydrolysis of
            ATP. Myosin is a hexameric protein composed of a pair of myosin
            heavy chains (MYH) and two pairs of nonidentical light chains.
            Myosin heavy chains are encoded by a multigene family. In mammals
            at least 10 different myosin heavy chain (MYH) isoforms have been
            described from striated, smooth, and nonmuscle cells. These
            isoforms show expression that is spatially and temporally regulated
            during development. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF111785.1, EU794637.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968540,
                                    SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226207.6/ ENSP00000226207.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1939
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1939
                     /product="myosin-1"
                     /note="myosin heavy chain IIx/d; myosin, heavy polypeptide
                     1, skeletal muscle, adult; myHC-IIx/d; myosin heavy chain
                     2x; myosin heavy chain, skeletal muscle, adult 1;
                     epididymis luminal protein 71; myosin, heavy chain 1,
                     skeletal muscle, adult"
                     /calculated_mol_wt=223015
     Region          33..77
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Region          100..770
                     /region_name="MYSc_Myh1_mammals"
                     /note="class II myosin heavy chain 1, motor domain;
                     cd14910"
                     /db_xref="CDD:276875"
     Site            order(127..135,179..186,236..246,464..469)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276875"
     Site            127..135
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276875"
     Site            130
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P12882.3)"
     Site            179..186
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276875"
     Site            236..246
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276875"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            464..469
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276875"
     Site            order(493..504,507..516)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276875"
     Region          659..681
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P12882.3)"
     Site            701..710
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276875"
     Site            order(713..729,735..770)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276875"
     Site            757
                     /site_type="methylation"
                     /note="Pros-methylhistidine.
                     /evidence=ECO:0000250|UniProtKB:Q28641; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Region          761..775
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P12882.3)"
     Region          850..1927
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Site            1092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1096
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1265
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1467
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1492
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1501
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1517
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1603
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1730
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1736
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RW1; propagated from
                     UniProtKB/Swiss-Prot (P12882.3)"
     CDS             1..1939
                     /gene="MYH1"
                     /gene_synonym="HEL71; MYHa; MyHC-2x; MyHC-2X/D; MYHSA1"
                     /coded_by="NM_005963.4:95..5914"
                     /db_xref="CCDS:CCDS11155.1"
                     /db_xref="GeneID:4619"
                     /db_xref="HGNC:HGNC:7567"
                     /db_xref="MIM:160730"
ORIGIN      
        1 mssdsemaif geaapflrks ererieaqnk pfdaktsvfv vdpkesfvka tvqsreggkv
       61 takteagatv tvkddqvfpm nppkydkied mammthlhep avlynlkery aawmiytysg
      121 lfcvtvnpyk wlpvynaevv tayrgkkrqe apphifsisd nayqfmltdr enqsilitge
      181 sgagktvntk rviqyfatia vtgekkkeev tsgkmqgtle dqiisanpll eafgnaktvr
      241 ndnssrfgkf irihfgttgk lasadietyl leksrvtfql kaersyhify qimsnkkpdl
      301 iemllittnp ydyafvsqge itvpsiddqe elmatdsaie ilgftsderv siykltgavm
      361 hygnmkfkqk qreeqaepdg tevadkaayl qnlnsadllk alcyprvkvg neyvtkgqtv
      421 qqvynavgal akavydkmfl wmvtrinqql dtkqprqyfi gvldiagfei fdfnsleqlc
      481 inftneklqq ffnhhmfvle qeeykkegie wtfidfgmdl aacieliekp mgifsileee
      541 cmfpkatdts fknklyeqhl gksnnfqkpk pakgkpeahf slihyagtvd yniagwldkn
      601 kdplnetvvg lyqksamktl allfvgatga eaeagggkkg gkkkgssfqt vsalfrenln
      661 klmtnlrsth phfvrciipn etktpgameh elvlhqlrcn gvlegiricr kgfpsrilya
      721 dfkqrykvln asaipegqfi dskkasekll gsididhtqy kfghtkvffk agllglleem
      781 rdeklaqlit rtqamcrgfl arveyqkmve rresifciqy nvrafmnvkh wpwmklyfki
      841 kpllksaete kemanmkeef ektkeelakt eakrkeleek mvtlmqeknd lqlqvqaead
      901 sladaeercd qliktkiqle akikevtera edeeeinael takkrklede cselkkdidd
      961 leltlakvek ekhatenkvk nlteemagld etiakltkek kalqeahqqt lddlqaeedk
     1021 vntltkakik leqqvddleg sleqekkirm dlerakrkle gdlklaqest mdiendkqql
     1081 deklkkkefe msglqskied eqalgmqlqk kikelqarie eleeeieaer asrakaekqr
     1141 sdlsreleei serleeagga tsaqiemnkk reaefqkmrr dleeatlqhe ataatlrkkh
     1201 adsvaelgeq idnlqrvkqk lekeksemkm eiddlasnme tvskakgnle kmcraledql
     1261 seiktkeeeq qrlindltaq rarlqtesge ysrqldekdt lvsqlsrgkq aftqqieelk
     1321 rqleeeikak salahalqss rhdcdllreq yeeeqeakae lqramskans evaqwrtkye
     1381 tdaiqrteel eeakkklaqr lqdaeehvea vnakcaslek tkqrlqneve dlmidvertn
     1441 aacaaldkkq rnfdkilaew kqkceethae leasqkesrs lstelfkikn ayeesldqle
     1501 tlkrenknlq qeisdlteqi aeggkrihel ekikkqveqe kselqaalee aeasleheeg
     1561 kilriqleln qvksevdrki aekdeeidqm krnhirives mqstldaeir srndairlkk
     1621 kmegdlneme iqlnhanrma aealrnyrnt qailkdtqlh lddalrsqed lkeqlamver
     1681 ranllqaeie elratleqte rsrkiaeqel ldaservqll htqntslint kkkletdisq
     1741 iqgemediiq earnaeekak kaitdaamma eelkkeqdts ahlermkknl eqtvkdlqhr
     1801 ldeaeqlalk ggkkqiqkle arvrelegev eseqkrnvea vkglrkherk vkeltyqtee
     1861 drknilrlqd lvdklqakvk sykrqaeeae eqsnvnlskf rriqheleea eeradiaesq
     1921 vnklrvksre vhtkiisee
//
