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Overview

Uniprot IDQ00872
Protein NameMyosin-binding protein C, slow-type
Gene NameMYBPC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1021 SEDATMTKESAVIAR
108 DLASKAGKHLQLKET

Function

Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. Slow skeletal protein that binds to both myosin and actin (PubMed:31025394, PubMed:31264822). In vitro, binds to native thin filaments and modifies the activity of actin-activated myosin ATPase. May modulate muscle contraction or may play a more structural role

Protein Sequence

10 MPEPTKKEEN 20 EVPAPAPPPE 30 EPSKEKEAGT 40 TPAKDWTLVE 50 TPPGEEQAKQ 60 NANSQLSILF 70 IEKPQGGTVK 80 VGEDITFIAK 90 VKAEDLLRKP 100 TIKWFKGKWM 110 DLASKAGKHL 120 QLKETFERHS 130 RVYTFEMQII 140 KAKDNFAGNY 150 RCEVTYKDKF 160 DSCSFDLEVH 170 ESTGTTPNID 180 IRSAFKRSGE 190 GQEDAGELDF 200 SGLLKRREVK 210 QQEEEPQVDV 220 WELLKNAKPS 230 EYEKIAFQYG 240 ITDLRGMLKR 250 LKRMRREEKK 260 SAAFAKILDP 270 AYQVDKGGRV 280 RFVVELADPK 290 LEVKWYKNGQ 300 EIRPSTKYIF 310 EHKGCQRILF 320 INNCQMTDDS 330 EYYVTAGDEK 340 CSTELFVREP 350 PIMVTKQLED 360 TTAYCGERVE 370 LECEVSEDDA 380 NVKWFKNGEE 390 IIPGPKSRYR 400 IRVEGKKHIL 410 IIEGATKADA 420 AEYSVMTTGG 430 QSSAKLSVDL 440 KPLKILTPLT 450 DQTVNLGKEI 460 CLKCEISENI 470 PGKWTKNGLP 480 VQESDRLKVV 490 HKGRIHKLVI 500 ANALTEDEGD 510 YVFAPDAYNV 520 TLPAKVHVID 530 PPKIILDGLD 540 ADNTVTVIAG 550 NKLRLEIPIS 560 GEPPPKAMWS 570 RGDKAIMEGS 580 GRIRTESYPD 590 SSTLVIDIAE 600 RDDSGVYHIN 610 LKNEAGEAHA 620 SIKVKVVDFP 630 DPPVAPTVTE 640 VGDDWCIMNW 650 EPPAYDGGSP 660 ILGYFIERKK 670 KQSSRWMRLN 680 FDLCKETTFE 690 PKKMIEGVAY 700 EVRIFAVNAI 710 GISKPSMPSR 720 PFVPLAVTSP 730 PTLLTVDSVT 740 DTTVTMRWRP 750 PDHIGAAGLD 760 GYVLEYCFEG 770 STSAKQSDEN 780 GEAAYDLPAE 790 DWIVANKDLI 800 DKTKFTITGL 810 PTDAKIFVRV 820 KAVNAAGASE 830 PKYYSQPILV 840 KEIIEPPKIR 850 IPRHLKQTYI 860 RRVGEAVNLV 870 IPFQGKPRPE 880 LTWKKDGAEI 890 DKNQINIRNS 900 ETDTIIFIRK 910 AERSHSGKYD 920 LQVKVDKFVE 930 TASIDIQIID 940 RPGPPQIVKI 950 EDVWGENVAL 960 TWTPPKDDGN 970 AAITGYTIQK 980 ADKKSMEWFT 990 VIEHYHRTSA 1000 TITELVIGNE 1010 YYFRVFSENM 1020 CGLSEDATMT 1030 KESAVIARDG 1040 KIYKNPVYED 1050 FDFSEAPMFT 1060 QPLVNTYAIA 1070 GYNATLNCSV 1080 RGNPKPKITW 1090 MKNKVAIVDD 1100 PRYRMFSNQG 1110 VCTLEIRKPS 1120 PYDGGTYCCK 1130 AVNDLGTVEI 1140 ECKLEVKVIA Q

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0031430 M band
Cellular Component GO:0030016 myofibril
Cellular Component GO:0032982 myosin filament
Molecular Function GO:0003779 actin binding
Molecular Function GO:0017022 myosin binding
Molecular Function GO:0008307 structural constituent of muscle
Molecular Function GO:0031432 titin binding
Biological Process GO:0007155 cell adhesion
Biological Process GO:0045214 sarcomere organization

Reference

[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.