MYPC1_HUMAN
ID MYPC1_HUMAN Reviewed; 1141 AA.
AC Q00872; B4DKR5; B7Z8G8; B7ZL02; B7ZL09; B7ZL10; E7ESM5; E7EWS6; G3XAE8;
AC Q15497; Q17RR7; Q569K7; Q86T48; Q86TC8; Q8N3L2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Myosin-binding protein C, slow-type;
DE Short=Slow MyBP-C;
DE AltName: Full=C-protein, skeletal muscle slow isoform;
GN Name=MYBPC1; Synonyms=MYBPCS;
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=Fetal skeletal muscle;
RX PubMed=1429890; DOI=10.1242/jcs.102.4.769;
RA Fuerst D.O., Vinkemeier U., Weber K.;
RT "Mammalian skeletal muscle C-protein: purification from bovine muscle,
RT binding to titin and the characterization of a full-length human cDNA.";
RL J. Cell Sci. 102:769-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7).
RC TISSUE=Hippocampus, Thymus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5; 6; 8; 9 AND 10).
RC TISSUE=Brain, and Pancreas;
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 [8]
RP INTERACTION WITH USP25.
RX PubMed=16501887; DOI=10.1007/s00018-005-5533-1;
RA Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.;
RT "The ubiquitin-specific protease USP25 interacts with three sarcomeric
RT proteins.";
RL Cell. Mol. Life Sci. 63:723-734(2006).
RN [9]
RP INVOLVEMENT IN LCCS4.
RX PubMed=22610851; DOI=10.1002/humu.22122;
RA Markus B., Narkis G., Landau D., Birk R.Z., Cohen I., Birk O.S.;
RT "Autosomal recessive lethal congenital contractural syndrome type 4 (LCCS4)
RT caused by a mutation in MYBPC1.";
RL Hum. Mutat. 33:1435-1438(2012).
RN [10]
RP STRUCTURE BY NMR OF 58-170 AND 342-431.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and third Ig-like domain of myosin-binding
RT protein C, slow-type.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [11]
RP VARIANTS DA1B ARG-211 AND HIS-849.
RX PubMed=20045868; DOI=10.1093/hmg/ddp587;
RA Gurnett C.A., Desruisseau D.M., McCall K., Choi R., Meyer Z.I.,
RA Talerico M., Miller S.E., Ju J.S., Pestronk A., Connolly A.M., Druley T.E.,
RA Weihl C.C., Dobbs M.B.;
RT "Myosin binding protein C1: a novel gene for autosomal dominant distal
RT arthrogryposis type 1.";
RL Hum. Mol. Genet. 19:1165-1173(2010).
RN [12]
RP VARIANT DA1B LYS-161.
RX PubMed=26661508; DOI=10.1111/cge.12707;
RA Ekhilevitch N., Kurolap A., Oz-Levi D., Mory A., Hershkovitz T., Ast G.,
RA Mandel H., Baris H.N.;
RT "Expanding the MYBPC1 phenotypic spectrum: a novel homozygous mutation
RT causes arthrogryposis multiplex congenita.";
RL Clin. Genet. 90:84-89(2016).
RN [13]
RP INVOLVEMENT IN MYOTREM, VARIANTS MYOTREM PRO-234 AND ARG-238, AND
RP CHARACTERIZATION OF VARIANTS MYOTREM PRO-234 AND ARG-238.
RX PubMed=31264822; DOI=10.1002/humu.23760;
RG Undiagnosed Diseases Network;
RA Shashi V., Geist J., Lee Y., Yoo Y., Shin U., Schoch K., Sullivan J.,
RA Stong N., Smith E., Jasien J., Kranz P., Lee Y., Shin Y.B., Wright N.T.,
RA Choi M., Kontrogianni-Konstantopoulos A.;
RT "Heterozygous variants in MYBPC1 are associated with an expanded
RT neuromuscular phenotype beyond arthrogryposis.";
RL Hum. Mutat. 40:1115-1126(2019).
RN [14]
RP INVOLVEMENT IN MYOTREM, VARIANTS MYOTREM HIS-222 AND LYS-223, AND
RP CHARACTERIZATION OF VARIANTS MYOTREM HIS-222 AND LYS-223.
RX PubMed=31025394; DOI=10.1002/ana.25494;
RA Stavusis J., Lace B., Schaefer J., Geist J., Inashkina I., Kidere D.,
RA Pajusalu S., Wright N.T., Saak A., Weinhold M., Haubenberger D.,
RA Jackson S., Kontrogianni-Konstantopoulos A., Boennemann C.G.;
RT "Novel mutations in MYBPC1 are associated with myogenic tremor and mild
RT myopathy.";
RL Ann. Neurol. 86:129-142(2019).
CC -!- FUNCTION: Thick filament-associated protein located in the crossbridge
CC region of vertebrate striated muscle a bands. Slow skeletal protein
CC that binds to both myosin and actin (PubMed:31264822, PubMed:31025394).
CC In vitro, binds to native thin filaments and modifies the activity of
CC actin-activated myosin ATPase. May modulate muscle contraction or may
CC play a more structural role. {ECO:0000269|PubMed:31025394,
CC ECO:0000269|PubMed:31264822}.
CC -!- SUBUNIT: Interacts with USP25 (isoform USP25m only); the interaction
CC prevents proteasomal degradation of MYBPC1.
CC {ECO:0000269|PubMed:16501887}.
CC -!- INTERACTION:
CC Q00872; O75923: DYSF; NbExp=4; IntAct=EBI-5652924, EBI-2799016;
CC Q00872; Q14324: MYBPC2; NbExp=3; IntAct=EBI-5652924, EBI-5653200;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=Q00872-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00872-2; Sequence=VSP_039105, VSP_039106;
CC Name=3;
CC IsoId=Q00872-3; Sequence=VSP_039106;
CC Name=4;
CC IsoId=Q00872-4; Sequence=VSP_039105, VSP_039106, VSP_045241;
CC Name=5;
CC IsoId=Q00872-5; Sequence=VSP_046736, VSP_039106, VSP_045241;
CC Name=6;
CC IsoId=Q00872-6; Sequence=VSP_046740;
CC Name=7;
CC IsoId=Q00872-7; Sequence=VSP_046737, VSP_039106, VSP_046739;
CC Name=8;
CC IsoId=Q00872-8; Sequence=VSP_046735, VSP_039106, VSP_045241;
CC Name=9;
CC IsoId=Q00872-9; Sequence=VSP_046738, VSP_039106, VSP_045241;
CC Name=10;
CC IsoId=Q00872-10; Sequence=VSP_039106, VSP_045241;
CC -!- DISEASE: Arthrogryposis, distal, 1B (DA1B) [MIM:614335]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. Distal
CC arthrogryposis type 1 is characterized largely by camptodactyly and
CC clubfoot. Hypoplasia and/or absence of some interphalangeal creases is
CC common. The shoulders and hips are less frequently affected.
CC {ECO:0000269|PubMed:20045868, ECO:0000269|PubMed:26661508}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Lethal congenital contracture syndrome 4 (LCCS4) [MIM:614915]:
CC A form of lethal congenital contracture syndrome, an autosomal
CC recessive disorder characterized by degeneration of anterior horn
CC neurons, extreme skeletal muscle atrophy and congenital non-progressive
CC joint contractures. The contractures can involve the upper or lower
CC limbs and/or the vertebral column, leading to various degrees of
CC flexion or extension limitations evident at birth.
CC {ECO:0000269|PubMed:22610851}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myopathy, congenital, with tremor (MYOTREM) [MIM:618524]: An
CC autosomal dominant muscular disorder characterized by muscle weakness,
CC hypotonia associated with high-frequency postural tremor of the limbs,
CC mildly delayed walking, and steppage gait. Additional features include
CC skeletal deformities such as scoliosis, thoracic asymmetry and spinal
CC rigidity. Some patients show mild facial dysmorphic features. Cognitive
CC functions are normal. {ECO:0000269|PubMed:31025394,
CC ECO:0000269|PubMed:31264822}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000305}.
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DR EMBL; X66276; CAA46987.1; -; mRNA.
DR EMBL; X73114; CAA51545.1; -; mRNA.
DR EMBL; AK295727; BAG58568.1; -; mRNA.
DR EMBL; AK296681; BAG59277.1; -; mRNA.
DR EMBL; AK303401; BAH13954.1; -; mRNA.
DR EMBL; AL831993; CAD89907.1; -; mRNA.
DR EMBL; AL832000; CAD91144.1; -; mRNA.
DR EMBL; AL834249; CAD38925.1; -; mRNA.
DR EMBL; AC010205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97665.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97669.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97672.1; -; Genomic_DNA.
DR EMBL; BC092418; AAH92418.1; -; mRNA.
DR EMBL; BC117217; AAI17218.1; -; mRNA.
DR EMBL; BC143495; AAI43496.1; -; mRNA.
DR EMBL; BC143502; AAI43503.1; -; mRNA.
DR EMBL; BC143503; AAI43504.1; -; mRNA.
DR EMBL; BC143504; AAI43505.1; -; mRNA.
DR CCDS; CCDS55877.1; -. [Q00872-3]
DR CCDS; CCDS58268.1; -. [Q00872-6]
DR CCDS; CCDS58269.1; -. [Q00872-10]
DR CCDS; CCDS58270.1; -. [Q00872-9]
DR CCDS; CCDS58271.1; -. [Q00872-8]
DR CCDS; CCDS58272.1; -. [Q00872-7]
DR CCDS; CCDS58273.1; -. [Q00872-5]
DR CCDS; CCDS9083.1; -. [Q00872-4]
DR CCDS; CCDS9084.1; -. [Q00872-2]
DR CCDS; CCDS9085.1; -. [Q00872-1]
DR PIR; S24614; S24614.
DR PIR; S36846; S36846.
DR RefSeq; NP_001241647.1; NM_001254718.1. [Q00872-6]
DR RefSeq; NP_001241648.1; NM_001254719.1. [Q00872-10]
DR RefSeq; NP_001241649.1; NM_001254720.1. [Q00872-8]
DR RefSeq; NP_001241650.1; NM_001254721.1. [Q00872-9]
DR RefSeq; NP_001241651.1; NM_001254722.1. [Q00872-5]
DR RefSeq; NP_001241652.1; NM_001254723.1. [Q00872-7]
DR RefSeq; NP_002456.2; NM_002465.3. [Q00872-4]
DR RefSeq; NP_996555.1; NM_206819.2. [Q00872-2]
DR RefSeq; NP_996556.1; NM_206820.2. [Q00872-1]
DR RefSeq; NP_996557.1; NM_206821.2. [Q00872-3]
DR PDB; 1X44; NMR; -; A=342-431.
DR PDB; 2DAV; NMR; -; A=58-170.
DR PDB; 2YUV; NMR; -; A=252-338.
DR PDB; 2YUW; NMR; -; A=718-832.
DR PDB; 2YUX; NMR; -; A=922-1034.
DR PDB; 2YUZ; NMR; -; A=433-519.
DR PDB; 2YXM; X-ray; 1.51 A; A=252-338.
DR PDBsum; 1X44; -.
DR PDBsum; 2DAV; -.
DR PDBsum; 2YUV; -.
DR PDBsum; 2YUW; -.
DR PDBsum; 2YUX; -.
DR PDBsum; 2YUZ; -.
DR PDBsum; 2YXM; -.
DR AlphaFoldDB; Q00872; -.
DR BMRB; Q00872; -.
DR SMR; Q00872; -.
DR BioGRID; 110689; 33.
DR IntAct; Q00872; 19.
DR STRING; 9606.ENSP00000400908; -.
DR iPTMnet; Q00872; -.
DR PhosphoSitePlus; Q00872; -.
DR BioMuta; MYBPC1; -.
DR DMDM; 6166597; -.
DR MassIVE; Q00872; -.
DR PaxDb; Q00872; -.
DR PeptideAtlas; Q00872; -.
DR PRIDE; Q00872; -.
DR ProteomicsDB; 18023; -.
DR ProteomicsDB; 18903; -.
DR ProteomicsDB; 33729; -.
DR ProteomicsDB; 57876; -. [Q00872-1]
DR ProteomicsDB; 57877; -. [Q00872-2]
DR ProteomicsDB; 57878; -. [Q00872-3]
DR ProteomicsDB; 61165; -.
DR ProteomicsDB; 7205; -.
DR ProteomicsDB; 7206; -.
DR ProteomicsDB; 7207; -.
DR Antibodypedia; 17936; 309 antibodies from 31 providers.
DR DNASU; 4604; -.
DR Ensembl; ENST00000361466.7; ENSP00000354849.2; ENSG00000196091.15. [Q00872-4]
DR Ensembl; ENST00000361685.6; ENSP00000354845.2; ENSG00000196091.15. [Q00872-2]
DR Ensembl; ENST00000392934.7; ENSP00000376665.3; ENSG00000196091.15. [Q00872-7]
DR Ensembl; ENST00000452455.6; ENSP00000400908.2; ENSG00000196091.15. [Q00872-6]
DR Ensembl; ENST00000536007.5; ENSP00000446128.1; ENSG00000196091.15. [Q00872-9]
DR Ensembl; ENST00000541119.5; ENSP00000442847.1; ENSG00000196091.15. [Q00872-8]
DR Ensembl; ENST00000545503.6; ENSP00000440034.2; ENSG00000196091.15. [Q00872-10]
DR Ensembl; ENST00000547405.5; ENSP00000448175.1; ENSG00000196091.15. [Q00872-5]
DR Ensembl; ENST00000550270.1; ENSP00000449702.1; ENSG00000196091.15. [Q00872-1]
DR Ensembl; ENST00000553190.5; ENSP00000447900.1; ENSG00000196091.15. [Q00872-3]
DR GeneID; 4604; -.
DR KEGG; hsa:4604; -.
DR MANE-Select; ENST00000361466.7; ENSP00000354849.2; NM_002465.4; NP_002456.2. [Q00872-4]
DR UCSC; uc001tig.4; human. [Q00872-1]
DR CTD; 4604; -.
DR DisGeNET; 4604; -.
DR GeneCards; MYBPC1; -.
DR HGNC; HGNC:7549; MYBPC1.
DR HPA; ENSG00000196091; Group enriched (skeletal muscle, tongue).
DR MalaCards; MYBPC1; -.
DR MIM; 160794; gene.
DR MIM; 614335; phenotype.
DR MIM; 614915; phenotype.
DR MIM; 618524; phenotype.
DR neXtProt; NX_Q00872; -.
DR OpenTargets; ENSG00000196091; -.
DR Orphanet; 1146; Distal arthrogryposis type 1.
DR Orphanet; 137783; Lethal congenital contracture syndrome type 3.
DR Orphanet; 498693; MYBPC1-related autosomal recessive non-lethal arthrogryposis multiplex congenita syndrome.
DR PharmGKB; PA31349; -.
DR VEuPathDB; HostDB:ENSG00000196091; -.
DR eggNOG; ENOG502QPYI; Eukaryota.
DR GeneTree; ENSGT00940000158254; -.
DR InParanoid; Q00872; -.
DR OMA; SDVGDDW; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; Q00872; -.
DR TreeFam; TF351819; -.
DR PathwayCommons; Q00872; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; Q00872; -.
DR BioGRID-ORCS; 4604; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; MYBPC1; human.
DR EvolutionaryTrace; Q00872; -.
DR GeneWiki; MYBPC1; -.
DR GenomeRNAi; 4604; -.
DR Pharos; Q00872; Tbio.
DR PRO; PR:Q00872; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q00872; protein.
DR Bgee; ENSG00000196091; Expressed in skeletal muscle tissue of rectus abdominis and 153 other tissues.
DR ExpressionAtlas; Q00872; baseline and differential.
DR Genevisible; Q00872; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IDA:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0031432; F:titin binding; ISS:BHF-UCL.
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; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
KW Disease variant; Immunoglobulin domain; Muscle protein; Phosphoprotein;
KW Reference proteome; Repeat; Thick filament.
FT CHAIN 1..1141
FT /note="Myosin-binding protein C, slow-type"
FT /id="PRO_0000072689"
FT DOMAIN 72..144
FT /note="Ig-like C2-type 1"
FT DOMAIN 251..340
FT /note="Ig-like C2-type 2"
FT DOMAIN 341..431
FT /note="Ig-like C2-type 3"
FT DOMAIN 432..520
FT /note="Ig-like C2-type 4"
FT DOMAIN 522..619
FT /note="Ig-like C2-type 5"
FT DOMAIN 622..721
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 722..833
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 837..931
FT /note="Ig-like C2-type 6"
FT DOMAIN 934..1029
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1047..1141
FT /note="Ig-like C2-type 7"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63518"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63518"
FT MOD_RES 798
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63518"
FT MOD_RES 823
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63518"
FT VAR_SEQ 8..19
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046735"
FT VAR_SEQ 9..34
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_046736"
FT VAR_SEQ 9..34
FT /note="ENEVPAPAPPPEEPSKEKEAGTTPAK -> DEEEVSPPSALPP (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046737"
FT VAR_SEQ 34
FT /note="K -> KDEEEVSPPSALPPGLGSRALERKDS (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039105"
FT VAR_SEQ 176..194
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046738"
FT VAR_SEQ 761..779
FT /note="STSAKQSDENGEAAYDLPA -> T (in isoform 2, isoform 3,
FT isoform 4, isoform 5, isoform 7, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:8375400"
FT /id="VSP_039106"
FT VAR_SEQ 1138..1141
FT /note="VIAQ -> GGLSFCRLLLQGVPPNIIDSYLRDLHSSNPEEY (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046739"
FT VAR_SEQ 1140..1141
FT /note="AQ -> YQGVNTPGQPVFLEGQQQSLHNKDF (in isoform 4,
FT isoform 5, isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_045241"
FT VAR_SEQ 1140..1141
FT /note="AQ -> YQGVNTPGQPVFLEGQQQVGSPSADSSCKAYLQT (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_046740"
FT VARIANT 161
FT /note="E -> K (in DA1B; may affect splicing;
FT dbSNP:rs1370563966)"
FT /evidence="ECO:0000269|PubMed:26661508"
FT /id="VAR_075219"
FT VARIANT 211
FT /note="W -> R (in DA1B; dbSNP:rs387906657)"
FT /evidence="ECO:0000269|PubMed:20045868"
FT /id="VAR_067045"
FT VARIANT 222
FT /note="Y -> H (in MYOTREM; changes in electrostatic
FT interactions resulting in increased myosin binding; no
FT effect on actin binding; dbSNP:rs1593846841)"
FT /evidence="ECO:0000269|PubMed:31025394"
FT /id="VAR_083207"
FT VARIANT 223
FT /note="E -> K (in MYOTREM; changes in electrostatic
FT interactions resulting in increased myosin binding; no
FT effect on actin binding; dbSNP:rs564856283)"
FT /evidence="ECO:0000269|PubMed:31025394"
FT /id="VAR_083208"
FT VARIANT 234
FT /note="L -> P (in MYOTREM; no effects on myosin or actin
FT binding; reduced helicity of certain domains;
FT dbSNP:rs1421405659)"
FT /evidence="ECO:0000269|PubMed:31264822"
FT /id="VAR_083209"
FT VARIANT 238
FT /note="L -> R (in MYOTREM; decreased binding to myosin; no
FT effect on actin binding; dbSNP:rs1565943228)"
FT /evidence="ECO:0000269|PubMed:31264822"
FT /id="VAR_083210"
FT VARIANT 481
FT /note="H -> Q (in dbSNP:rs3817552)"
FT /id="VAR_021923"
FT VARIANT 849
FT /note="Y -> H (in DA1B; dbSNP:rs387906658)"
FT /evidence="ECO:0000269|PubMed:20045868"
FT /id="VAR_067046"
FT CONFLICT 87..88
FT /note="LR -> SE (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..97
FT /note="KWFKG -> NGSR (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="Y -> H (in Ref. 3; BAG59277)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> T (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..235
FT /note="GITDLR -> ESPTCS (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..245
FT /note="MR -> SI (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> V (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="Y -> N (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="I -> L (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..312
FT /note="HKGCQRILFIN -> DTRCQSILNID (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="F -> L (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="A -> D (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="N -> Q (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..387
FT /note="PGPKS -> LVQT (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="E -> D (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="Q -> L (in Ref. 4; CAD91144)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..492
FT /note="AN -> DH (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="Y -> C (in Ref. 4; CAD89907)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="Y -> H (in Ref. 4; CAD38925)"
FT /evidence="ECO:0000305"
FT CONFLICT 840..843
FT /note="RIPR -> HSPK (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 855..858
FT /note="EAVN -> DRVI (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="D -> G (in Ref. 3; BAH13954)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="Q -> R (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="E -> R (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 979..980
FT /note="FT -> LR (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 985..992
FT /note="YHRTSATI -> IIEPVPH (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056..1063
FT /note="TYAIAGYN -> RLCHSGYM (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 1099
FT /note="Q -> L (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT CONFLICT 1107
FT /note="R -> G (in Ref. 1; CAA46987)"
FT /evidence="ECO:0000305"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2DAV"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:2DAV"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2DAV"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:2YXM"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:2YXM"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:1X44"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:1X44"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 483..492
FT /evidence="ECO:0007829|PDB:2YUZ"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 499..508
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:2YUZ"
FT STRAND 722..729
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 734..739
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 749..758
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 780..784
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 805..814
FT /evidence="ECO:0007829|PDB:2YUW"
FT STRAND 938..944
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 947..952
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 968..972
FT /evidence="ECO:0007829|PDB:2YUX"
FT TURN 973..975
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 979..984
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 997..1005
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:2YUX"
FT STRAND 1024..1026
FT /evidence="ECO:0007829|PDB:2YUX"
SQ SEQUENCE 1141 AA; 128294 MW; 8B3A91422CA9F2B2 CRC64;
MPEPTKKEEN EVPAPAPPPE EPSKEKEAGT TPAKDWTLVE TPPGEEQAKQ NANSQLSILF
IEKPQGGTVK VGEDITFIAK VKAEDLLRKP TIKWFKGKWM DLASKAGKHL QLKETFERHS
RVYTFEMQII KAKDNFAGNY RCEVTYKDKF DSCSFDLEVH ESTGTTPNID IRSAFKRSGE
GQEDAGELDF SGLLKRREVK QQEEEPQVDV WELLKNAKPS EYEKIAFQYG ITDLRGMLKR
LKRMRREEKK SAAFAKILDP AYQVDKGGRV RFVVELADPK LEVKWYKNGQ EIRPSTKYIF
EHKGCQRILF INNCQMTDDS EYYVTAGDEK CSTELFVREP PIMVTKQLED TTAYCGERVE
LECEVSEDDA NVKWFKNGEE IIPGPKSRYR IRVEGKKHIL IIEGATKADA AEYSVMTTGG
QSSAKLSVDL KPLKILTPLT DQTVNLGKEI CLKCEISENI PGKWTKNGLP VQESDRLKVV
HKGRIHKLVI ANALTEDEGD YVFAPDAYNV TLPAKVHVID PPKIILDGLD ADNTVTVIAG
NKLRLEIPIS GEPPPKAMWS RGDKAIMEGS GRIRTESYPD SSTLVIDIAE RDDSGVYHIN
LKNEAGEAHA SIKVKVVDFP DPPVAPTVTE VGDDWCIMNW EPPAYDGGSP ILGYFIERKK
KQSSRWMRLN FDLCKETTFE PKKMIEGVAY EVRIFAVNAI GISKPSMPSR PFVPLAVTSP
PTLLTVDSVT DTTVTMRWRP PDHIGAAGLD GYVLEYCFEG STSAKQSDEN GEAAYDLPAE
DWIVANKDLI DKTKFTITGL PTDAKIFVRV KAVNAAGASE PKYYSQPILV KEIIEPPKIR
IPRHLKQTYI RRVGEAVNLV IPFQGKPRPE LTWKKDGAEI DKNQINIRNS ETDTIIFIRK
AERSHSGKYD LQVKVDKFVE TASIDIQIID RPGPPQIVKI EDVWGENVAL TWTPPKDDGN
AAITGYTIQK ADKKSMEWFT VIEHYHRTSA TITELVIGNE YYFRVFSENM CGLSEDATMT
KESAVIARDG KIYKNPVYED FDFSEAPMFT QPLVNTYAIA GYNATLNCSV RGNPKPKITW
MKNKVAIVDD PRYRMFSNQG VCTLEIRKPS PYDGGTYCCK AVNDLGTVEI ECKLEVKVIA
Q
