ID   MYH2_HUMAN              Reviewed;        1941 AA.
AC   Q9UKX2; A0AVL4; Q14322; Q16229; Q567P6; Q86T56;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Myosin-2;
DE   AltName: Full=Myosin heavy chain 2;
DE   AltName: Full=Myosin heavy chain 2a;
DE            Short=MyHC-2a;
DE   AltName: Full=Myosin heavy chain IIa;
DE            Short=MyHC-IIa;
DE   AltName: Full=Myosin heavy chain, skeletal muscle, adult 2;
GN   Name=MYH2; Synonyms=MYHSA2;
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] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cerebellum;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1711-1941 (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
RX   PubMed=7545970; DOI=10.1152/ajpcell.1994.267.6.c1723;
RA   Smerdu V., Karsch-Mizrachi I., Campione M., Leinwand L., Schiaffino S.;
RT   "Type IIx myosin heavy chain transcripts are expressed in type IIb fibers
RT   of human skeletal muscle.";
RL   Am. J. Physiol. 267:C1723-C1728(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1823-1941 (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
RX   PubMed=7751403; DOI=10.1007/bf00125308;
RA   Ennion S., Sant'ana Pereira J., Sargeant T., Young A., Goldspink G.;
RT   "Characterization of human skeletal muscle fibres according to the myosin
RT   heavy chains they express.";
RL   J. Muscle Res. Cell Motil. 16:35-43(1995).
RN   [7]
RP   INTERACTION WITH GCSAM.
RX   PubMed=17823310; DOI=10.1182/blood-2007-04-087775;
RA   Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M., Lossos I.S.;
RT   "HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and
RT   mediates the effects of IL-6 on cell migration.";
RL   Blood 110:4268-4277(2007).
RN   [8]
RP   VARIANT CMYP6 LYS-706.
RX   PubMed=11114175; DOI=10.1073/pnas.250289597;
RA   Martinsson T., Oldfors A., Darin N., Berg K., Tajsharghi H., Kyllerman M.,
RA   Wahlstroem J.;
RT   "Autosomal dominant myopathy: missense mutation (Glu-706 --> Lys) in the
RT   myosin heavy chain IIa gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14614-14619(2000).
RN   [9]
RP   VARIANTS ILE-970 AND VAL-1061.
RX   PubMed=15741996; DOI=10.1038/sj.ejhg.5201375;
RA   Tajsharghi H., Darin N., Rekabdar E., Kyllerman M., Wahlstroem J.,
RA   Martinsson T., Oldfors A.;
RT   "Mutations and sequence variation in the human myosin heavy chain IIa gene
RT   (MYH2).";
RL   Eur. J. Hum. Genet. 13:617-622(2005).
CC   -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization
CC       (By similarity). {ECO:0000250}.
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 GCSAM.
CC       {ECO:0000269|PubMed:17823310}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC       myofibrils.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UKX2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UKX2-2; Sequence=VSP_056291;
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   -!- DISEASE: Congenital myopathy 6 with ophthalmoplegia (CMYP6)
CC       [MIM:605637]: A muscular disorder characterized by mild-to-moderate
CC       muscle weakness, ophthalmoplegia, and contractures at birth in some
CC       patients. Muscle biopsies from patients show predominance of type 1
CC       fibers and small or absent type 2A fibers. The disease is non-
CC       progressive or it progresses very slowly. Inheritance is autosomal
CC       dominant or recessive. {ECO:0000269|PubMed:11114175}. Note=The disease
CC       is caused by variants affecting the gene represented in this entry.
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-2 (MYO2). {ECO:0000305}.
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DR   EMBL; AF111784; AAD29950.1; -; mRNA.
DR   EMBL; BX510904; CAD91136.1; -; mRNA.
DR   EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093082; AAH93082.1; -; mRNA.
DR   EMBL; BC126409; AAI26410.1; -; mRNA.
DR   EMBL; S73840; AAC13916.1; -; mRNA.
DR   EMBL; Z32858; CAA83687.1; -; mRNA.
DR   CCDS; CCDS11156.1; -. [Q9UKX2-1]
DR   PIR; I51912; I51912.
DR   RefSeq; NP_001093582.1; NM_001100112.1. [Q9UKX2-1]
DR   RefSeq; NP_060004.3; NM_017534.5. [Q9UKX2-1]
DR   AlphaFoldDB; Q9UKX2; -.
DR   SMR; Q9UKX2; -.
DR   BioGRID; 110705; 50.
DR   IntAct; Q9UKX2; 20.
DR   MINT; Q9UKX2; -.
DR   STRING; 9606.ENSP00000380367; -.
DR   BindingDB; Q9UKX2; -.
DR   ChEMBL; CHEMBL4295980; -.
DR   iPTMnet; Q9UKX2; -.
DR   PhosphoSitePlus; Q9UKX2; -.
DR   BioMuta; MYH2; -.
DR   DMDM; 13431716; -.
DR   EPD; Q9UKX2; -.
DR   jPOST; Q9UKX2; -.
DR   MassIVE; Q9UKX2; -.
DR   MaxQB; Q9UKX2; -.
DR   PaxDb; 9606-ENSP00000245503; -.
DR   PeptideAtlas; Q9UKX2; -.
DR   ProteomicsDB; 62563; -.
DR   ProteomicsDB; 84903; -. [Q9UKX2-1]
DR   Pumba; Q9UKX2; -.
DR   ABCD; Q9UKX2; 2 sequenced antibodies.
DR   Antibodypedia; 4384; 171 antibodies from 25 providers.
DR   DNASU; 4620; -.
DR   Ensembl; ENST00000245503.10; ENSP00000245503.5; ENSG00000125414.19. [Q9UKX2-1]
DR   Ensembl; ENST00000397183.6; ENSP00000380367.2; ENSG00000125414.19. [Q9UKX2-1]
DR   Ensembl; ENST00000532183.6; ENSP00000433944.1; ENSG00000125414.19. [Q9UKX2-2]
DR   Ensembl; ENST00000622564.4; ENSP00000482463.1; ENSG00000125414.19. [Q9UKX2-2]
DR   GeneID; 4620; -.
DR   KEGG; hsa:4620; -.
DR   MANE-Select; ENST00000245503.10; ENSP00000245503.5; NM_017534.6; NP_060004.3.
DR   UCSC; uc002gmp.5; human. [Q9UKX2-1]
DR   AGR; HGNC:7572; -.
DR   CTD; 4620; -.
DR   DisGeNET; 4620; -.
DR   GeneCards; MYH2; -.
DR   HGNC; HGNC:7572; MYH2.
DR   HPA; ENSG00000125414; Group enriched (skeletal muscle, tongue).
DR   MalaCards; MYH2; -.
DR   MIM; 160740; gene.
DR   MIM; 605637; phenotype.
DR   neXtProt; NX_Q9UKX2; -.
DR   OpenTargets; ENSG00000125414; -.
DR   Orphanet; 363677; Childhood-onset autosomal recessive myopathy with external ophthalmoplegia.
DR   Orphanet; 79091; Hereditary inclusion body myopathy-joint contractures-ophthalmoplegia syndrome.
DR   PharmGKB; PA31369; -.
DR   VEuPathDB; HostDB:ENSG00000125414; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000161336; -.
DR   HOGENOM; CLU_000192_7_5_1; -.
DR   InParanoid; Q9UKX2; -.
DR   OMA; TARSWAN; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; Q9UKX2; -.
DR   TreeFam; TF314375; -.
DR   PathwayCommons; Q9UKX2; -.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   SignaLink; Q9UKX2; -.
DR   SIGNOR; Q9UKX2; -.
DR   BioGRID-ORCS; 4620; 13 hits in 1146 CRISPR screens.
DR   ChiTaRS; MYH2; human.
DR   GeneWiki; MYH2; -.
DR   GenomeRNAi; 4620; -.
DR   Pharos; Q9UKX2; Tbio.
DR   PRO; PR:Q9UKX2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9UKX2; Protein.
DR   Bgee; ENSG00000125414; Expressed in skeletal muscle tissue of rectus abdominis and 105 other cell types or tissues.
DR   ExpressionAtlas; Q9UKX2; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005859; C:muscle myosin complex; TAS:UniProtKB.
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:0032991; C:protein-containing complex; IDA:LIFEdb.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IDA:BHF-UCL.
DR   GO; GO:0030049; P:muscle filament sliding; NAS:BHF-UCL.
DR   CDD; cd14912; MYSc_Myh2_mammals; 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.
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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF39; MYOSIN-2; 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.
DR   UCD-2DPAGE; Q9UKX2; -.
DR   Genevisible; Q9UKX2; HS.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Coiled coil; Cytoplasm; Disease variant; Methylation; Motor protein;
KW   Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Thick filament.
FT   CHAIN           1..1941
FT                   /note="Myosin-2"
FT                   /id="PRO_0000123393"
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..784
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          787..816
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          763..777
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1128..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          845..1941
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         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         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         759
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28641"
FT   MOD_RES         1094
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1098
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1243
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1257
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1288
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1469
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1494
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1503
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1516
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1519
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1728
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1732
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1738
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1741
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   VAR_SEQ         659..1891
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056291"
FT   VARIANT         706
FT                   /note="E -> K (in CMYP6; dbSNP:rs121434589)"
FT                   /evidence="ECO:0000269|PubMed:11114175"
FT                   /id="VAR_032630"
FT   VARIANT         970
FT                   /note="V -> I (in one patient with familial myopathy;
FT                   uncertain significance; dbSNP:rs143872329)"
FT                   /evidence="ECO:0000269|PubMed:15741996"
FT                   /id="VAR_032631"
FT   VARIANT         1061
FT                   /note="L -> V (in dbSNP:rs142586585)"
FT                   /evidence="ECO:0000269|PubMed:15741996"
FT                   /id="VAR_032632"
FT   VARIANT         1927
FT                   /note="R -> Q (in dbSNP:rs34161789)"
FT                   /id="VAR_032633"
FT   CONFLICT        150
FT                   /note="E -> G (in Ref. 2; CAD91136)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1844
FT                   /note="K -> R (in Ref. 6; CAA83687)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1941 AA;  223044 MW;  681E866F83AEA83F CRC64;
     MSSDSELAVF GEAAPFLRKS ERERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSREGGKV
     TVKTEGGATL TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYKPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGEKKKEEI TSGKIQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVVFQL KAERSYHIFY QITSNKKPEL
     IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELMATDSAID ILGFTNEEKV SIYKLTGAVM
     HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
     EQVSNAVGAL AKAVYEKMFL WMVARINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYDQHL GKSANFQKPK VVKGKAEAHF ALIHYAGVVD YNITGWLEKN
     KDPLNETVVG LYQKSAMKTL AQLFSGAQTA EGEGAGGGAK KGGKKKGSSF QTVSALFREN
     LNKLMTNLRS THPHFVRCII PNETKTPGAM EHELVLHQLR CNGVLEGIRI CRKGFPSRIL
     YADFKQRYKV LNASAIPEGQ FIDSKKASEK LLASIDIDHT QYKFGHTKVF FKAGLLGLLE
     EMRDDKLAQL ITRTQARCRG FLARVEYQRM VERREAIFCI QYNIRSFMNV KHWPWMKLFF
     KIKPLLKSAE TEKEMATMKE EFQKIKDELA KSEAKRKELE EKMVTLLKEK NDLQLQVQAE
     AEGLADAEER CDQLIKTKIQ LEAKIKEVTE RAEDEEEINA ELTAKKRKLE DECSELKKDI
     DDLELTLAKV EKEKHATENK VKNLTEEMAG LDETIAKLTK EKKALQEAHQ QTLDDLQAEE
     DKVNTLTKAK IKLEQQVDDL EGSLEQEKKL RMDLERAKRK LEGDLKLAQE SIMDIENEKQ
     QLDEKLKKKE FEISNLQSKI EDEQALGIQL QKKIKELQAR IEELEEEIEA ERASRAKAEK
     QRSDLSRELE EISERLEEAG GATSAQIEMN KKREAEFQKM RRDLEEATLQ HEATAATLRK
     KHADSVAELG EQIDNLQRVK QKLEKEKSEM KMEIDDLASN VETVSKAKGN LEKMCRTLED
     QLSELKSKEE EQQRLINDLT AQRGRLQTES GEFSRQLDEK EALVSQLSRG KQAFTQQIEE
     LKRQLEEEIK AKNALAHALQ SSRHDCDLLR EQYEEEQESK AELQRALSKA NTEVAQWRTK
     YETDAIQRTE ELEEAKKKLA QRLQAAEEHV EAVNAKCASL EKTKQRLQNE VEDLMLDVER
     TNAACAALDK KQRNFDKILA EWKQKCEETH AELEASQKEA RSLGTELFKI KNAYEESLDQ
     LETLKRENKN LQQEISDLTE QIAEGGKRIH ELEKIKKQVE QEKCELQAAL EEAEASLEHE
     EGKILRIQLE LNQVKSEVDR KIAEKDEEID QLKRNHIRIV ESMQSTLDAE IRSRNDAIRL
     KKKMEGDLNE MEIQLNHANR MAAEALRNYR NTQGILKDTQ IHLDDALRSQ EDLKEQLAMV
     ERRANLLQAE IEELRATLEQ TERSRKIAEQ ELLDASERVQ LLHTQNTSLI NTKKKLETDI
     SQMQGEMEDI LQEARNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NMEQTVKDLQ
     LRLDEAEQLA LKGGKKQIQK LEARVRELEG EVESEQKRNA EAVKGLRKHE RRVKELTYQT
     EEDRKNILRL QDLVDKLQAK VKSYKRQAEE AEEQSNTNLA KFRKLQHELE EAEERADIAE
     SQVNKLRVKS REVHTKVISE E
//