MYPC2_HUMAN
ID MYPC2_HUMAN Reviewed; 1141 AA.
AC Q14324; A1L4G9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Myosin-binding protein C, fast-type;
DE Short=Fast MyBP-C;
DE AltName: Full=C-protein, skeletal muscle fast isoform;
GN Name=MYBPC2; Synonyms=MYBPCF;
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=Fetal skeletal muscle;
RX PubMed=8375400; DOI=10.1111/j.1432-1033.1993.tb18186.x;
RA Weber F.E., Vaughan K.T., Reinach F.C., Fischman D.A.;
RT "Complete sequence of human fast-type and slow-type muscle myosin-binding-
RT protein C (MyBP-C). Differential expression, conserved domain structure and
RT chromosome assignment.";
RL Eur. J. Biochem. 216:661-669(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP STRUCTURE BY NMR OF 44-157; 345-438 AND 825-935.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first, third and 6th Ig-like domains from human
RT myosin-binding protein c, fast-type.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Thick filament-associated protein located in the crossbridge
CC region of vertebrate striated muscle a bands. In vitro it binds MHC, F-
CC actin and native thin filaments, and modifies the activity of actin-
CC activated myosin ATPase. It may modulate muscle contraction or may play
CC a more structural role.
CC -!- INTERACTION:
CC Q14324; Q00872: MYBPC1; NbExp=3; IntAct=EBI-5653200, EBI-5652924;
CC Q14324; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-5653200, EBI-6503765;
CC Q14324; Q8WZ42: TTN; NbExp=14; IntAct=EBI-5653200, EBI-681210;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000305}.
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DR EMBL; X73113; CAA51544.1; -; mRNA.
DR EMBL; AC020909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW71866.1; -; Genomic_DNA.
DR EMBL; BC130536; AAI30537.1; -; mRNA.
DR EMBL; BC136389; AAI36390.1; -; mRNA.
DR CCDS; CCDS46152.1; -.
DR PIR; S36845; S36845.
DR RefSeq; NP_004524.3; NM_004533.3.
DR PDB; 2E7C; NMR; -; A=824-934.
DR PDB; 2EDK; NMR; -; A=345-438.
DR PDB; 2EDN; NMR; -; A=47-157.
DR PDBsum; 2E7C; -.
DR PDBsum; 2EDK; -.
DR PDBsum; 2EDN; -.
DR AlphaFoldDB; Q14324; -.
DR SMR; Q14324; -.
DR BioGRID; 110691; 40.
DR IntAct; Q14324; 33.
DR MINT; Q14324; -.
DR STRING; 9606.ENSP00000350332; -.
DR CarbonylDB; Q14324; -.
DR iPTMnet; Q14324; -.
DR PhosphoSitePlus; Q14324; -.
DR BioMuta; MYBPC2; -.
DR DMDM; 296439237; -.
DR REPRODUCTION-2DPAGE; IPI00030104; -.
DR EPD; Q14324; -.
DR MassIVE; Q14324; -.
DR PaxDb; Q14324; -.
DR PeptideAtlas; Q14324; -.
DR PRIDE; Q14324; -.
DR ProteomicsDB; 59965; -.
DR Antibodypedia; 32323; 186 antibodies from 32 providers.
DR DNASU; 4606; -.
DR Ensembl; ENST00000357701.6; ENSP00000350332.4; ENSG00000086967.10.
DR GeneID; 4606; -.
DR KEGG; hsa:4606; -.
DR MANE-Select; ENST00000357701.6; ENSP00000350332.4; NM_004533.4; NP_004524.3.
DR UCSC; uc002psf.3; human.
DR CTD; 4606; -.
DR DisGeNET; 4606; -.
DR GeneCards; MYBPC2; -.
DR HGNC; HGNC:7550; MYBPC2.
DR HPA; ENSG00000086967; Group enriched (skeletal muscle, tongue).
DR MIM; 160793; gene.
DR neXtProt; NX_Q14324; -.
DR OpenTargets; ENSG00000086967; -.
DR PharmGKB; PA31350; -.
DR VEuPathDB; HostDB:ENSG00000086967; -.
DR eggNOG; ENOG502QW17; Eukaryota.
DR GeneTree; ENSGT00940000160092; -.
DR HOGENOM; CLU_006405_1_1_1; -.
DR InParanoid; Q14324; -.
DR OMA; CSFNIDV; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; Q14324; -.
DR TreeFam; TF351819; -.
DR PathwayCommons; Q14324; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; Q14324; -.
DR BioGRID-ORCS; 4606; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; MYBPC2; human.
DR EvolutionaryTrace; Q14324; -.
DR GenomeRNAi; 4606; -.
DR Pharos; Q14324; Tbio.
DR PRO; PR:Q14324; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14324; protein.
DR Bgee; ENSG00000086967; Expressed in vastus lateralis and 113 other tissues.
DR ExpressionAtlas; Q14324; baseline and differential.
DR Genevisible; Q14324; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR040849; MyBP-C_THB.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF18362; THB; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell adhesion; Immunoglobulin domain;
KW Muscle protein; Reference proteome; Repeat; Thick filament.
FT CHAIN 1..1141
FT /note="Myosin-binding protein C, fast-type"
FT /id="PRO_0000072691"
FT DOMAIN 50..153
FT /note="Ig-like C2-type 1"
FT DOMAIN 255..344
FT /note="Ig-like C2-type 2"
FT DOMAIN 345..437
FT /note="Ig-like C2-type 3"
FT DOMAIN 438..538
FT /note="Ig-like C2-type 4"
FT DOMAIN 539..638
FT /note="Ig-like C2-type 5"
FT DOMAIN 641..737
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 739..834
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 838..932
FT /note="Ig-like C2-type 6"
FT DOMAIN 935..1030
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1048..1141
FT /note="Ig-like C2-type 7"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 29
FT /note="E -> K (in dbSNP:rs57092106)"
FT /id="VAR_061321"
FT VARIANT 52
FT /note="G -> S (in dbSNP:rs25669)"
FT /id="VAR_014657"
FT VARIANT 282
FT /note="D -> N (in dbSNP:rs35951152)"
FT /id="VAR_056060"
FT VARIANT 341
FT /note="V -> I (in dbSNP:rs58511181)"
FT /id="VAR_061322"
FT VARIANT 514
FT /note="G -> S (in dbSNP:rs8104931)"
FT /id="VAR_056061"
FT VARIANT 624
FT /note="V -> I (in dbSNP:rs25665)"
FT /id="VAR_014658"
FT VARIANT 1089
FT /note="R -> H (in dbSNP:rs25667)"
FT /id="VAR_014659"
FT CONFLICT 517
FT /note="L -> LG (in Ref. 1; CAA51544)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="S -> T (in Ref. 1; CAA51544)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2EDN"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2EDN"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:2EDN"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2EDN"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:2EDK"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:2EDK"
FT STRAND 835..840
FT /evidence="ECO:0007829|PDB:2E7C"
FT TURN 844..846
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 850..856
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 858..868
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 871..876
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 892..901
FT /evidence="ECO:0007829|PDB:2E7C"
FT TURN 904..906
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 908..915
FT /evidence="ECO:0007829|PDB:2E7C"
FT STRAND 924..930
FT /evidence="ECO:0007829|PDB:2E7C"
SQ SEQUENCE 1141 AA; 128072 MW; 91F4B18C4367743A CRC64;
MPEAKPAAKK APKGKDAPKG APKEAPPKEA PAEAPKEAPP EDQSPTAEEP TGVFLKKPDS
VSVETGKDAV VVAKVNGKEL PDKPTIKWFK GKWLELGSKS GARFSFKESH NSASNVYTVE
LHIGKVVLGD RGYYRLEVKA KDTCDSCGFN IDVEAPRQDA SGQSLESFKR TSEKKSDTAG
ELDFSGLLKK REVVEEEKKK KKKDDDDLGI PPEIWELLKG AKKSEYEKIA FQYGITDLRG
MLKRLKKAKV EVKKSAAFTK KLDPAYQVDR GNKIKLMVEI SDPDLTLKWF KNGQEIKPSS
KYVFENVGKK RILTINKCTL ADDAAYEVAV KDEKCFTELF VKEPPVLIVT PLEDQQVFVG
DRVEMAVEVS EEGAQVMWMK DGVELTREDS FKARYRFKKD GKRHILIFSD VVQEDRGRYQ
VITNGGQCEA ELIVEEKQLE VLQDIADLTV KASEQAVFKC EVSDEKVTGK WYKNGVEVRP
SKRITISHVG RFHKLVIDDV RPEDEGDYTF VPDGYALSLS AKLNFLEIKV EYVPKQEPPK
IHLDCSGKTS ENAIVVVAGN KLRLDVSITG EPPPVATWLK GDEVFTTTEG RTRIEKRVDC
SSFVIESAQR EDEGRYTIKV TNPVGEDVAS IFLQVVDVPD PPEAVRITSV GEDWAILVWE
PPMYDGGKPV TGYLVERKKK GSQRWMKLNF EVFTETTYES TKMIEGILYE MRVFAVNAIG
VSQPSMNTKP FMPIAPTSEP LHLIVEDVTD TTTTLKWRPP NRIGAGGIDG YLVEYCLEGS
EEWVPANTEP VERCGFTVKN LPTGARILFR VVGVNIAGRS EPATLAQPVT IREIAEPPKI
RLPRHLRQTY IRKVGEQLNL VVPFQGKPRP QVVWTKGGAP LDTSRVHVRT SDFDTVFFVR
QAARSDSGEY ELSVQIENMK DTATIRIRVV EKAGPPINVM VKEVWGTNAL VEWQAPKDDG
NSEIMGYFVQ KADKKTMEWF NVYERNRHTS CTVSDLIVGN EYYFRVYTEN ICGLSDSPGV
SKNTARILKT GITFKPFEYK EHDFRMAPKF LTPLIDRVVV AGYSAALNCA VRGHPKPKVV
WMKNKMEIRE DPKFLITNYQ GVLTLNIRRP SPFDAGTYTC RAVNELGEAL AECKLEVRVP
Q
