ID MYH1_HUMAN Reviewed; 1939 AA. AC P12882; Q14CA4; Q9Y622; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 3. DT 04-NOV-2026, entry version 227. DE RecName: Full=Myosin-1; DE AltName: Full=Myosin heavy chain 1 {ECO:0000303|PubMed:39482536}; DE AltName: Full=Myosin heavy chain 2x; DE Short=MyHC-2x; DE AltName: Full=Myosin heavy chain IIx/d; DE Short=MyHC-IIx/d; DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 1; GN Name=MYH1 {ECO:0000312|HGNC:HGNC:7567}; 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]. 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). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1064-1939. RX PubMed=2421254; DOI=10.1093/nar/14.7.2951; RA Saez L., Leinwand L.A.; RT "Characterization of diverse forms of myosin heavy chain expressed in adult RT human skeletal muscle."; RL Nucleic Acids Res. 14:2951-2969(1986). RN [5] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-1306; THR-1445 AND MET-1598. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [6] RP VARIANT [LARGE SCALE ANALYSIS] SER-640. RX PubMed=18987736; DOI=10.1038/nature07485; RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., RA DiPersio J.F., Wilson R.K.; RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia RT genome."; RL Nature 456:66-72(2008). RN [7] RP VARIANT LYS-1566. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). RN [8] RP INTERACTION WITH SLC26A5, AND VARIANTS HIS-194; THR-460; THR-744; VAL-813; RP ARG-832; VAL-993; HIS-1539 AND LYS-1806. RX PubMed=39482536; DOI=10.1038/s12276-024-01338-4; RA Jung J., Joo S.Y., Min H., Roh J.W., Kim K.A., Ma J.H., Rim J.H., Kim J.A., RA Kim S.J., Jang S.H., Koh Y.I., Kim H.Y., Lee H., Kim B.C., Gee H.Y., RA Bok J., Choi J.Y., Seong J.K.; RT "MYH1 deficiency disrupts outer hair cell electromotility, resulting in RT hearing loss."; RL Exp. Mol. Med. 56:2423-2435(2024). CC -!- FUNCTION: Required for normal hearing. It plays a role in cochlear CC amplification of auditory stimuli, likely through the positive CC regulation of prestin (SLC26A5) activity and outer hair cell (OHC) CC electromotility. {ECO:0000250|UniProtKB:Q5SX40}. 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). Interacts with SLC26A5 CC (PubMed:39482536). {ECO:0000269|PubMed:39482536}. CC -!- INTERACTION: CC P12882; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-366238, EBI-11977221; CC P12882; A1A4E9: KRT13; NbExp=3; IntAct=EBI-366238, EBI-10171552; 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-1 (MYO1). {ECO:0000305}. 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; AF111785; AAD29951.1; -; mRNA. DR EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC114545; AAI14546.1; -; mRNA. DR EMBL; X03740; CAA27380.1; -; mRNA. DR CCDS; CCDS11155.1; -. DR PIR; A23767; A23767. DR RefSeq; NP_005954.3; NM_005963.4. DR RefSeq; XP_016880164.1; XM_017024675.2. DR AlphaFoldDB; P12882; -. DR SMR; P12882; -. DR BioGRID; 110704; 79. DR ComplexPortal; CPX-26732; Myosin class II complex, MYL1-MYL2-MYH1 variant. DR FunCoup; P12882; 546. DR IntAct; P12882; 53. DR STRING; 9606.ENSP00000226207; -. DR BindingDB; P12882; -. DR CarbonylDB; P12882; -. DR GlyCosmos; P12882; 2 sites, 1 glycan. DR GlyGen; P12882; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P12882; -. DR PhosphoSitePlus; P12882; -. DR BioMuta; MYH1; -. DR DMDM; 226694176; -. DR jPOST; P12882; -. DR MassIVE; P12882; -. DR PaxDb; 9606-ENSP00000226207; -. DR PeptideAtlas; P12882; -. DR ProteomicsDB; 52882; -. DR Pumba; P12882; -. DR Antibodypedia; 4383; 236 antibodies from 31 providers. DR DNASU; 4619; -. DR Ensembl; ENST00000226207.6; ENSP00000226207.5; ENSG00000109061.11. DR Ensembl; ENST00000958695.1; ENSP00000628754.1; ENSG00000109061.11. DR Ensembl; ENST00000958696.1; ENSP00000628755.1; ENSG00000109061.11. DR Ensembl; ENST00000958697.1; ENSP00000628756.1; ENSG00000109061.11. DR Ensembl; ENST00000958699.1; ENSP00000628758.1; ENSG00000109061.11. DR Ensembl; ENST00000958702.1; ENSP00000628761.1; ENSG00000109061.11. DR Ensembl; ENST00000958704.1; ENSP00000628763.1; ENSG00000109061.11. DR GeneID; 4619; -. DR KEGG; hsa:4619; -. DR MANE-Select; ENST00000226207.6; ENSP00000226207.5; NM_005963.4; NP_005954.3. DR UCSC; uc002gmo.4; human. DR AGR; HGNC:7567; -. DR ClinPGx; PA31365; -. DR CTD; 4619; -. DR DisGeNET; 4619; -. DR GeneCards; MYH1; -. DR HGNC; HGNC:7567; MYH1. DR HPA; ENSG00000109061; Tissue enriched (skeletal). DR MalaCards; MYH1; -. DR MIM; 160730; gene. DR OpenTargets; ENSG00000109061; -. DR VEuPathDB; HostDB:ENSG00000109061; -. DR eggNOG; KOG0161; Eukaryota. DR GeneTree; ENSGT00940000154760; -. DR HOGENOM; CLU_000192_8_1_1; -. DR InParanoid; P12882; -. DR OMA; ACFTQIE; -. DR OrthoDB; 312459at2759; -. DR PAN-GO; P12882; 6 GO annotations based on evolutionary models. DR PhylomeDB; P12882; -. DR BRENDA; 5.6.1.8; 2681. DR PathwayCommons; P12882; -. DR SignaLink; P12882; -. DR SIGNOR; P12882; -. DR Agora; ENSG00000109061; -. DR BioGRID-ORCS; 4619; 9 hits in 1152 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR GeneWiki; MYH1; -. DR GenomeRNAi; 4619; -. DR Pharos; P12882; Tbio. DR PRO; PR:P12882; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P12882; protein. DR Bgee; ENSG00000109061; Expressed in skeletal muscle tissue of rectus abdominis and 97 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL. DR GO; GO:0005859; C:muscle myosin complex; IDA:MGI. 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:ComplexPortal. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central. DR GO; GO:0030048; P:actin filament-based movement; NAS:ComplexPortal. DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR CDD; cd14910; MYSc_Myh1_mammals; 1. DR FunFam; 1.20.5.340:FF:000002; Myosin heavy chain; 1. DR FunFam; 1.20.5.340:FF:000003; Myosin heavy chain; 1. DR FunFam; 1.20.5.340:FF:000004; Myosin heavy chain; 1. DR FunFam; 1.20.5.340:FF:000006; Myosin heavy chain; 1. DR FunFam; 1.20.5.340:FF:000013; Myosin heavy chain; 1. DR FunFam; 1.20.5.370:FF:000001; Myosin heavy chain; 1. DR FunFam; 1.20.5.370:FF:000002; Myosin heavy chain; 1. DR FunFam; 1.20.5.370:FF:000003; Myosin heavy chain; 1. DR FunFam; 1.20.5.370:FF:000007; Myosin heavy chain; 1. DR FunFam; 1.20.5.370:FF:000008; Myosin heavy chain; 1. DR FunFam; 1.20.5.4820:FF:000001; Myosin heavy chain; 1. DR FunFam; 1.20.58.530:FF:000001; Myosin heavy chain; 1. DR FunFam; 2.30.30.360:FF:000001; Myosin heavy chain; 1. DR FunFam; 3.40.850.10:FF:000024; Myosin heavy chain, isoform J; 1. DR FunFam; 1.20.120.720:FF:000001; Myosin heavy chain, muscle; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.340; -; 5. DR Gene3D; 1.20.5.370; -; 4. DR Gene3D; 1.20.5.4820; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 6.10.250.2420; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom-like. DR InterPro; IPR008989; Myosin_S1_N. DR InterPro; IPR002928; Myosin_tail. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004009; SH3_Myosin. DR InterPro; IPR014751; XRCC4-like_C. DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1. DR PANTHER; PTHR45615:SF2; MYOSIN-1; 1. 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; SM00015; IQ; 1. DR SMART; SM00242; MYSc; 1. DR SUPFAM; SSF90257; Myosin rod fragments; 5. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51844; SH3_LIKE; 1. PE 1: Evidence at protein level; KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm; KW Hearing; Methylation; Motor protein; Muscle protein; Myosin; KW Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Thick filament. FT CHAIN 1..1939 FT /note="Myosin-1" FT /id="PRO_0000123391" 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 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 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 757 FT /note="Pros-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:Q28641" FT MOD_RES 1092 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q29RW1" FT MOD_RES 1096 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 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 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 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 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 194 FT /note="Q -> H (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs776053827)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090483" FT VARIANT 460 FT /note="I -> T (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs201061123)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090484" FT VARIANT 640 FT /note="G -> S (in dbSNP:rs150346984)" FT /evidence="ECO:0000269|PubMed:18987736" FT /id="VAR_054159" FT VARIANT 744 FT /note="K -> T (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs183833836)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090485" FT VARIANT 813 FT /note="E -> V (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs191339081)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090486" FT VARIANT 832 FT /note="P -> R (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs534110923)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090487" FT VARIANT 993 FT /note="I -> V (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs150191104)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090488" FT VARIANT 1306 FT /note="S -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs752643679)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036003" FT VARIANT 1341 FT /note="R -> C (in dbSNP:rs3744564)" FT /id="VAR_030193" FT VARIANT 1445 FT /note="A -> T (in a breast cancer sample; somatic mutation; FT dbSNP:rs139860229)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036004" FT VARIANT 1539 FT /note="Q -> H (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs3764850)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_030194" FT VARIANT 1566 FT /note="Q -> K (found in a renal cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064735" FT VARIANT 1598 FT /note="V -> M (in a breast cancer sample; somatic mutation; FT dbSNP:rs150456818)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036005" FT VARIANT 1716 FT /note="R -> C (in dbSNP:rs1077841)" FT /id="VAR_030195" FT VARIANT 1806 FT /note="Q -> K (found in autosomal recessive deafness; FT uncertain significance; dbSNP:rs140873918)" FT /evidence="ECO:0000269|PubMed:39482536" FT /id="VAR_090489" FT CONFLICT 1070 FT /note="T -> A (in Ref. 1; AAD29951 and 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1131 FT /note="A -> T (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1139 FT /note="Q -> L (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1158 FT /note="G -> V (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1163 FT /note="A -> T (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1286..1289 FT /note="TESG -> QNQV (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1302..1303 FT /note="VS -> ET (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1451 FT /note="R -> T (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1470 FT /note="E -> V (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1473..1474 FT /note="AS -> SF (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1531 FT /note="E -> K (in Ref. 3; AAI14546)" FT /evidence="ECO:0000305" FT CONFLICT 1569 FT /note="L -> V (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1598 FT /note="V -> E (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1606 FT /note="D -> N (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1643 FT /note="A -> D (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1648 FT /note="R -> Q (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1750 FT /note="Q -> K (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1822 FT /note="R -> K (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" FT CONFLICT 1845 FT /note="R -> H (in Ref. 4; CAA27380)" FT /evidence="ECO:0000305" SQ SEQUENCE 1939 AA; 223145 MW; D2B6F28C2C63CBDF CRC64; MSSDSEMAIF GEAAPFLRKS ERERIEAQNK PFDAKTSVFV VDPKESFVKA TVQSREGGKV TAKTEAGATV TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE SGAGKTVNTK RVIQYFATIA VTGEKKKEEV TSGKMQGTLE DQIISANPLL EAFGNAKTVR NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAIE ILGFTSDERV SIYKLTGAVM HYGNMKFKQK QREEQAEPDG TEVADKAAYL QNLNSADLLK ALCYPRVKVG NEYVTKGQTV QQVYNAVGAL AKAVYDKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKPEAHF SLIHYAGTVD YNIAGWLDKN KDPLNETVVG LYQKSAMKTL ALLFVGATGA EAEAGGGKKG GKKKGSSFQT VSALFRENLN KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIDIDHTQY KFGHTKVFFK AGLLGLLEEM RDEKLAQLIT RTQAMCRGFL ARVEYQKMVE RRESIFCIQY NVRAFMNVKH WPWMKLYFKI KPLLKSAETE KEMANMKEEF EKTKEELAKT EAKRKELEEK MVTLMQEKND LQLQVQAEAD SLADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK VNTLTKAKIK LEQQVDDLEG SLEQEKKIRM DLERAKRKLE GDLKLAQEST MDIENDKQQL DEKLKKKEFE MSGLQSKIED EQALGMQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKH ADSVAELGEQ IDNLQRVKQK LEKEKSEMKM EIDDLASNME TVSKAKGNLE KMCRALEDQL SEIKTKEEEQ QRLINDLTAQ RARLQTESGE YSRQLDEKDT LVSQLSRGKQ AFTQQIEELK RQLEEEIKAK SALAHALQSS RHDCDLLREQ YEEEQEAKAE LQRAMSKANS EVAQWRTKYE TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNAKCASLEK TKQRLQNEVE DLMIDVERTN AACAALDKKQ RNFDKILAEW KQKCEETHAE LEASQKESRS LSTELFKIKN AYEESLDQLE TLKRENKNLQ QEISDLTEQI AEGGKRIHEL EKIKKQVEQE KSELQAALEE AEASLEHEEG KILRIQLELN QVKSEVDRKI AEKDEEIDQM KRNHIRIVES MQSTLDAEIR SRNDAIRLKK KMEGDLNEME IQLNHANRMA AEALRNYRNT QAILKDTQLH LDDALRSQED LKEQLAMVER RANLLQAEIE ELRATLEQTE RSRKIAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ IQGEMEDIIQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EQTVKDLQHR LDEAEQLALK GGKKQIQKLE ARVRELEGEV ESEQKRNVEA VKGLRKHERK VKELTYQTEE DRKNILRLQD LVDKLQAKVK SYKRQAEEAE EQSNVNLSKF RRIQHELEEA EERADIAESQ VNKLRVKSRE VHTKIISEE //