MYH4_HUMAN
ID MYH4_HUMAN Reviewed; 1939 AA.
AC Q9Y623;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Myosin-4;
DE AltName: Full=Myosin heavy chain 2b;
DE Short=MyHC-2b;
DE AltName: Full=Myosin heavy chain 4;
DE AltName: Full=Myosin heavy chain IIb;
DE Short=MyHC-IIb;
DE AltName: Full=Myosin heavy chain, skeletal muscle, fetal;
GN Name=MYH4;
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 [MRNA], AND VARIANTS MET-1106; LYS-1209; GLY-1802 AND
RP GLU-1911.
RC TISSUE=Skeletal muscle;
RX PubMed=10388558; DOI=10.1006/jmbi.1999.2865;
RA Weiss A., Schiaffino S., Leinwand L.A.;
RT "Comparative sequence analysis of the complete human sarcomeric myosin
RT heavy chain family: implications for functional diversity.";
RL J. Mol. Biol. 290:61-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
CC -!- FUNCTION: Muscle contraction.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-4 (MYO4). {ECO:0000305}.
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DR EMBL; AF111783; AAD29949.1; -; mRNA.
DR EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11154.1; -.
DR RefSeq; NP_060003.2; NM_017533.2.
DR RefSeq; XP_016880165.1; XM_017024676.1.
DR AlphaFoldDB; Q9Y623; -.
DR SMR; Q9Y623; -.
DR BioGRID; 110707; 81.
DR IntAct; Q9Y623; 19.
DR MINT; Q9Y623; -.
DR STRING; 9606.ENSP00000255381; -.
DR iPTMnet; Q9Y623; -.
DR PhosphoSitePlus; Q9Y623; -.
DR BioMuta; MYH4; -.
DR DMDM; 224471840; -.
DR UCD-2DPAGE; Q9Y623; -.
DR EPD; Q9Y623; -.
DR jPOST; Q9Y623; -.
DR MassIVE; Q9Y623; -.
DR MaxQB; Q9Y623; -.
DR PaxDb; Q9Y623; -.
DR PeptideAtlas; Q9Y623; -.
DR PRIDE; Q9Y623; -.
DR ProteomicsDB; 86589; -.
DR Antibodypedia; 62478; 144 antibodies from 23 providers.
DR DNASU; 4622; -.
DR Ensembl; ENST00000255381.2; ENSP00000255381.2; ENSG00000264424.1.
DR GeneID; 4622; -.
DR KEGG; hsa:4622; -.
DR MANE-Select; ENST00000255381.2; ENSP00000255381.2; NM_017533.2; NP_060003.2.
DR UCSC; uc002gmn.4; human.
DR CTD; 4622; -.
DR DisGeNET; 4622; -.
DR GeneCards; MYH4; -.
DR HGNC; HGNC:7574; MYH4.
DR HPA; ENSG00000264424; Tissue enriched (skeletal).
DR MIM; 160742; gene.
DR neXtProt; NX_Q9Y623; -.
DR OpenTargets; ENSG00000264424; -.
DR PharmGKB; PA31371; -.
DR VEuPathDB; HostDB:ENSG00000264424; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000163211; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; Q9Y623; -.
DR OMA; APTGKMQ; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q9Y623; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; Q9Y623; -.
DR SignaLink; Q9Y623; -.
DR BioGRID-ORCS; 4622; 20 hits in 1069 CRISPR screens.
DR GeneWiki; MYH4; -.
DR GenomeRNAi; 4622; -.
DR Pharos; Q9Y623; Tbio.
DR PRO; PR:Q9Y623; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y623; protein.
DR Bgee; ENSG00000264424; Expressed in skeletal muscle tissue of rectus abdominis and 23 other tissues.
DR Genevisible; Q9Y623; HS.
DR GO; GO:0005859; C:muscle myosin complex; NAS:BHF-UCL.
DR GO; GO:0030016; C:myofibril; IDA:BHF-UCL.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; NAS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; NAS:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; IDA:BHF-UCL.
DR GO; GO:0030049; P:muscle filament sliding; NAS:BHF-UCL.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN 1..1939
FT /note="Myosin-4"
FT /id="PRO_0000123398"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 785..814
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 761..775
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 843..1939
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 757
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 776
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1464
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1736
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT VARIANT 594
FT /note="A -> T (in dbSNP:rs12949680)"
FT /id="VAR_030198"
FT VARIANT 883
FT /note="T -> M (in dbSNP:rs3744558)"
FT /id="VAR_022110"
FT VARIANT 1106
FT /note="I -> M (in dbSNP:rs917361)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_030199"
FT VARIANT 1117
FT /note="A -> D (in dbSNP:rs16943441)"
FT /id="VAR_030200"
FT VARIANT 1209
FT /note="E -> K (in dbSNP:rs11651295)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_030201"
FT VARIANT 1802
FT /note="D -> G (in dbSNP:rs2277649)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_030202"
FT VARIANT 1862
FT /note="R -> C (in dbSNP:rs34260986)"
FT /id="VAR_056175"
FT VARIANT 1911
FT /note="K -> E (in dbSNP:rs3744554)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_024542"
FT CONFLICT 1167
FT /note="M -> L (in Ref. 1; AAD29949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1939 AA; 223071 MW; 023D6F73C476B19B CRC64;
MSSDSEMAIF GEAAPFLRKS EKERIEAQNK PFDAKTSVFV VDPKESYVKA IVQSREGGKV
TAKTEAGATV TVKEDQVFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP ASGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QILSNKKPEL
IEMLLITTNP YDFAFVSQGE ITVPSIDDQE ELMATDSAVD ILGFTADEKV AIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL TSLNSADLLK SLCYPRVKVG NEFVTKGQTV
QQVYNAVGAL AKAIYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKPEAHF SLVHYAGTVD YNIAGWLDKN
KDPLNETVVG LYQKSAMKTL AFLFSGAQTA EAEGGGGKKG GKKKGSSFQT VSALFRENLN
KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIEIDHTQY KFGHTKVFFK AGLLGTLEEM
RDEKLAQLIT RTQAICRGFL MRVEFRKMME RRESIFCIQY NIRAFMNVKH WPWMKLYFKI
KPLLKSAETE KEMANMKEEF EKTKEELAKT EAKRKELEEK MVTLMQEKND LQLQVQAEAD
ALADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQMEEDK
VNTLTKAKTK LEQQVDDLEG SLEQEKKLCM DLERAKRKLE GDLKLAQEST MDTENDKQQL
NEKLKKKEFE MSNLQGKIED EQALAIQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEESTLQHE ATAAALRKKH
ADSVAELGEQ IDSLQRVKQK LEKEKSELKM EINDLASNME TVSKAKANFE KMCRTLEDQL
SEIKTKEEEQ QRLINELSAQ KARLHTESGE FSRQLDEKDA MVSQLSRGKQ AFTQQIEELK
RQLEEETKAK STLAHALQSA RHDCDLLREQ YEEEQEAKAE LQRGMSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNSKCASLEK TKQRLQNEVE DLMIDVERSN
AACIALDKKQ RNFDKVLAEW KQKYEETQAE LEASQKESRS LSTELFKVKN AYEESLDHLE
TLKRENKNLQ QEISDLTEQI AEGGKHIHEL EKVKKQLDHE KSELQTSLEE AEASLEHEEG
KILRIQLELN QVKSEIDRKI AEKDEELDQL KRNHLRVVES MQSTLDAEIR SRNDALRIKK
KMEGDLNEME IQLNHANRQA AEALRNLRNT QGILKDTQLH LDDAIRGQDD LKEQLAMVER
RANLMQAEVE ELRASLERTE RGRKMAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
IQGEMEDIVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQLR
LDEAEQLALK GGKKQIQKLE ARVRELESEV ESEQKHNVEA VKGLRKHERR VKELTYQTEE
DRKNILRLQD LVDKLQTKVK AYKRQAEEAE EQSNVNLAKF RKLQHELEEA KERADIAESQ
VNKLRVKSRE VHTKVISEE
