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Myosin-binding protein C, fast-type (Fast MyBP-C) (C-protein, skeletal muscle fast isoform)

 MYPC2_HUMAN             Reviewed;        1141 AA.
Q14324; A1L4G9;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
28-FEB-2018, entry version 163.
RecName: Full=Myosin-binding protein C, fast-type;
Short=Fast MyBP-C;
AltName: Full=C-protein, skeletal muscle fast isoform;
Name=MYBPC2; Synonyms=MYBPCF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal skeletal muscle;
PubMed=8375400; DOI=10.1111/j.1432-1033.1993.tb18186.x;
Weber F.E., Vaughan K.T., Reinach F.C., Fischman D.A.;
"Complete sequence of human fast-type and slow-type muscle myosin-
binding-protein C (MyBP-C). Differential expression, conserved domain
structure and chromosome assignment.";
Eur. J. Biochem. 216:661-669(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
STRUCTURE BY NMR OF 44-157; 345-438 AND 825-935.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first, third and 6th Ig-like domains from
human myosin-binding protein c, fast-type.";
Submitted (AUG-2007) to the PDB data bank.
-!- FUNCTION: Thick filament-associated protein located in the
crossbridge region of vertebrate striated muscle a bands. In vitro
it binds MHC, F-actin and native thin filaments, and modifies the
activity of actin-activated myosin ATPase. It may modulate muscle
contraction or may play a more structural role.
-!- INTERACTION:
Q00872:MYBPC1; NbExp=3; IntAct=EBI-5653200, EBI-5652924;
Q8WZ42:TTN; NbExp=14; IntAct=EBI-5653200, EBI-681210;
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X73113; CAA51544.1; -; mRNA.
EMBL; AC020909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW71866.1; -; Genomic_DNA.
EMBL; BC130536; AAI30537.1; -; mRNA.
EMBL; BC136389; AAI36390.1; -; mRNA.
CCDS; CCDS46152.1; -.
PIR; S36845; S36845.
RefSeq; NP_004524.3; NM_004533.3.
UniGene; Hs.85937; -.
PDB; 2E7C; NMR; -; A=824-934.
PDB; 2EDK; NMR; -; A=345-438.
PDB; 2EDN; NMR; -; A=47-157.
PDBsum; 2E7C; -.
PDBsum; 2EDK; -.
PDBsum; 2EDN; -.
ProteinModelPortal; Q14324; -.
SMR; Q14324; -.
BioGrid; 110691; 2.
IntAct; Q14324; 30.
MINT; Q14324; -.
STRING; 9606.ENSP00000350332; -.
CarbonylDB; Q14324; -.
iPTMnet; Q14324; -.
PhosphoSitePlus; Q14324; -.
BioMuta; MYBPC2; -.
DMDM; 296439237; -.
REPRODUCTION-2DPAGE; IPI00030104; -.
PaxDb; Q14324; -.
PeptideAtlas; Q14324; -.
PRIDE; Q14324; -.
DNASU; 4606; -.
Ensembl; ENST00000357701; ENSP00000350332; ENSG00000086967.
GeneID; 4606; -.
KEGG; hsa:4606; -.
UCSC; uc002psf.3; human.
CTD; 4606; -.
DisGeNET; 4606; -.
EuPathDB; HostDB:ENSG00000086967.9; -.
GeneCards; MYBPC2; -.
H-InvDB; HIX0040195; -.
HGNC; HGNC:7550; MYBPC2.
HPA; HPA042991; -.
HPA; HPA046745; -.
MIM; 160793; gene.
neXtProt; NX_Q14324; -.
OpenTargets; ENSG00000086967; -.
PharmGKB; PA31350; -.
eggNOG; ENOG410IFCI; Eukaryota.
eggNOG; ENOG4110AYI; LUCA.
GeneTree; ENSGT00860000133685; -.
HOGENOM; HOG000220906; -.
HOVERGEN; HBG052560; -.
InParanoid; Q14324; -.
KO; K12558; -.
OMA; KVEYVPK; -.
OrthoDB; EOG091G00ND; -.
PhylomeDB; Q14324; -.
TreeFam; TF351819; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
ChiTaRS; MYBPC2; human.
EvolutionaryTrace; Q14324; -.
GenomeRNAi; 4606; -.
PRO; PR:Q14324; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000086967; -.
CleanEx; HS_MYBPC2; -.
ExpressionAtlas; Q14324; baseline and differential.
Genevisible; Q14324; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031430; C:M band; IBA:GO_Central.
GO; GO:0005859; C:muscle myosin complex; IBA:GO_Central.
GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
GO; GO:0097493; F:structural molecule activity conferring elasticity; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
GO; GO:0006941; P:striated muscle contraction; IBA:GO_Central.
GO; GO:0071688; P:striated muscle myosin thick filament assembly; IBA:GO_Central.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 7.
SMART; SM00060; FN3; 3.
SMART; SM00409; IG; 7.
SMART; SM00408; IGc2; 4.
SUPFAM; SSF48726; SSF48726; 7.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell adhesion; Complete proteome;
Immunoglobulin domain; Muscle protein; Polymorphism;
Reference proteome; Repeat; Thick filament.
CHAIN 1 1141 Myosin-binding protein C, fast-type.
/FTId=PRO_0000072691.
DOMAIN 50 153 Ig-like C2-type 1.
DOMAIN 255 344 Ig-like C2-type 2.
DOMAIN 345 437 Ig-like C2-type 3.
DOMAIN 438 538 Ig-like C2-type 4.
DOMAIN 539 638 Ig-like C2-type 5.
DOMAIN 641 737 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 739 834 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 838 932 Ig-like C2-type 6.
DOMAIN 935 1030 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1048 1141 Ig-like C2-type 7.
VARIANT 29 29 E -> K (in dbSNP:rs57092106).
/FTId=VAR_061321.
VARIANT 52 52 G -> S (in dbSNP:rs25669).
/FTId=VAR_014657.
VARIANT 282 282 D -> N (in dbSNP:rs35951152).
/FTId=VAR_056060.
VARIANT 341 341 V -> I (in dbSNP:rs58511181).
/FTId=VAR_061322.
VARIANT 514 514 G -> S (in dbSNP:rs8104931).
/FTId=VAR_056061.
VARIANT 624 624 V -> I (in dbSNP:rs25665).
/FTId=VAR_014658.
VARIANT 1089 1089 R -> H (in dbSNP:rs25667).
/FTId=VAR_014659.
CONFLICT 517 517 L -> LG (in Ref. 1; CAA51544).
{ECO:0000305}.
CONFLICT 820 820 S -> T (in Ref. 1; CAA51544).
{ECO:0000305}.
STRAND 51 53 {ECO:0000244|PDB:2EDN}.
STRAND 62 64 {ECO:0000244|PDB:2EDN}.
STRAND 73 76 {ECO:0000244|PDB:2EDN}.
TURN 77 79 {ECO:0000244|PDB:2EDN}.
STRAND 80 82 {ECO:0000244|PDB:2EDN}.
STRAND 87 90 {ECO:0000244|PDB:2EDN}.
TURN 91 93 {ECO:0000244|PDB:2EDN}.
STRAND 105 110 {ECO:0000244|PDB:2EDN}.
STRAND 112 114 {ECO:0000244|PDB:2EDN}.
STRAND 116 125 {ECO:0000244|PDB:2EDN}.
TURN 128 130 {ECO:0000244|PDB:2EDN}.
STRAND 134 139 {ECO:0000244|PDB:2EDN}.
STRAND 144 149 {ECO:0000244|PDB:2EDN}.
STRAND 152 154 {ECO:0000244|PDB:2EDN}.
STRAND 348 350 {ECO:0000244|PDB:2EDK}.
STRAND 355 360 {ECO:0000244|PDB:2EDK}.
STRAND 367 370 {ECO:0000244|PDB:2EDK}.
STRAND 377 382 {ECO:0000244|PDB:2EDK}.
STRAND 396 399 {ECO:0000244|PDB:2EDK}.
STRAND 401 407 {ECO:0000244|PDB:2EDK}.
HELIX 413 415 {ECO:0000244|PDB:2EDK}.
STRAND 417 422 {ECO:0000244|PDB:2EDK}.
STRAND 431 435 {ECO:0000244|PDB:2EDK}.
STRAND 835 840 {ECO:0000244|PDB:2E7C}.
TURN 844 846 {ECO:0000244|PDB:2E7C}.
STRAND 850 856 {ECO:0000244|PDB:2E7C}.
STRAND 858 868 {ECO:0000244|PDB:2E7C}.
STRAND 871 876 {ECO:0000244|PDB:2E7C}.
STRAND 887 890 {ECO:0000244|PDB:2E7C}.
STRAND 892 901 {ECO:0000244|PDB:2E7C}.
TURN 904 906 {ECO:0000244|PDB:2E7C}.
STRAND 908 915 {ECO:0000244|PDB:2E7C}.
STRAND 924 930 {ECO:0000244|PDB:2E7C}.
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


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