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Protein

Myosin-binding protein C, cardiac-type

Gene

Mybpc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi206 – 2061ZincBy similarity
Metal bindingi208 – 2081ZincBy similarity
Metal bindingi221 – 2211ZincBy similarity
Metal bindingi223 – 2231ZincBy similarity

GO - Molecular functioni

  • identical protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • myosin binding Source: MGI
  • myosin heavy chain binding Source: MGI
  • structural constituent of cytoskeleton Source: MGI
  • structural constituent of muscle Source: MGI

GO - Biological processi

  • cardiac muscle contraction Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • heart morphogenesis Source: MGI
  • muscle contraction Source: MGI
  • myosin filament assembly Source: MGI
  • regulation of heart contraction Source: MGI
  • regulation of heart rate Source: MGI
  • sarcomere organization Source: MGI
  • ventricular cardiac muscle tissue morphogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-binding protein C, cardiac-type
Short name:
Cardiac MyBP-C
Alternative name(s):
C-protein, cardiac muscle isoform
Gene namesi
Name:Mybpc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:102844. Mybpc3.

Subcellular locationi

GO - Cellular componenti

  • A band Source: MGI
  • cytoskeleton Source: MGI
  • myofibril Source: MGI
  • sarcomere Source: MGI
  • striated muscle myosin thick filament Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12701270Myosin-binding protein C, cardiac-typePRO_0000072694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei273 – 2731Phosphoserine; by PKA and PKC1 Publication
Modified residuei282 – 2821Phosphoserine; by PKA and PKC1 Publication
Modified residuei302 – 3021Phosphoserine; by PKA and PKC1 Publication
Modified residuei307 – 3071PhosphoserineCombined sources
Modified residuei423 – 4231PhosphoserineCombined sources
Disulfide bondi432 ↔ 439PROSITE-ProRule annotation
Modified residuei455 – 4551PhosphoserineCombined sources
Modified residuei546 – 5461PhosphoserineCombined sources
Modified residuei603 – 6031PhosphothreonineBy similarity

Post-translational modificationi

Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity).By similarity
Polyubiquitinated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO70468.
PaxDbiO70468.
PRIDEiO70468.

PTM databases

iPTMnetiO70468.
PhosphoSiteiO70468.

Expressioni

Gene expression databases

CleanExiMM_MYBPC3.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Actc1P680333EBI-8347074,EBI-352284
Myh6Q025663EBI-8347074,EBI-299157

GO - Molecular functioni

  • identical protein binding Source: MGI
  • myosin binding Source: MGI
  • myosin heavy chain binding Source: MGI

Protein-protein interaction databases

DIPiDIP-48624N.
IntActiO70468. 3 interactions.
MINTiMINT-4102925.
STRINGi10090.ENSMUSP00000127070.

Structurei

Secondary structure

1
1270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi155 – 1573Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi186 – 1916Combined sources
Turni192 – 1943Combined sources
Helixi197 – 2004Combined sources
Beta strandi205 – 2128Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 2248Combined sources
Helixi229 – 2313Combined sources
Beta strandi233 – 2408Combined sources
Beta strandi245 – 25511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EDQX-ray1.64A/B149-269[»]
ProteinModelPortaliO70468.
SMRiO70468. Positions 2-96, 104-262, 315-349, 354-447, 449-632, 637-766, 1056-1164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini151 – 254104Ig-like C2-type 1Add
BLAST
Domaini358 – 44891Ig-like C2-type 2Add
BLAST
Domaini449 – 53991Ig-like C2-type 3Add
BLAST
Domaini540 – 62990Ig-like C2-type 4Add
BLAST
Domaini641 – 767127Ig-like C2-type 5Add
BLAST
Domaini770 – 86697Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini868 – 96396Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini967 – 106195Ig-like C2-type 6Add
BLAST
Domaini1064 – 115996Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1177 – 127094Ig-like C2-type 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi100 – 15051Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. MyBP family.Curated
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiENOG410IFCI. Eukaryota.
ENOG4110AYI. LUCA.
HOVERGENiHBG052560.
InParanoidiO70468.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 8 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 8 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPGKKPVS AFNKKPRSAE VTAGSAAVFE AETERSGVMV RWQRDGSDIT
60 70 80 90 100
ANDKYGLAAE GKRHTLTVRD ASPDDQGSYA VIAGSSKVKF DLKVTEPAPP
110 120 130 140 150
EKAESEVAPG APEEVPAPAT ELEESVSSPE GSVSVTQDGS AAEHQGAPDD
160 170 180 190 200
PIGLFLMRPQ DGEVTVGGSI VFSARVAGAS LLKPPVVKWF KGKWVDLSSK
210 220 230 240 250
VGQHLQLHDS YDRASKVYLF ELHITDAQTT SAGGYRCEVS TKDKFDSCNF
260 270 280 290 300
NLTVHEAIGS GDLDLRSAFR RTSLAGAGRR TSDSHEDAGT PDFSSLLKKR
310 320 330 340 350
DSFRRDSKLE APAEEDVWEI LRQAPPSEYE RIAFQHGVEA CHRPLKRLKG
360 370 380 390 400
MKQDEKKSTA FQKKLEPAYQ VNKGHKIRLT VELADPDAEV KWLKNGQEIQ
410 420 430 440 450
MSGSKYIFES VGAKRTLTIS QCSLADDAAY QCVVGGEKCS TELFVKEPPV
460 470 480 490 500
LITRSLEDQL VMVGQRVEFE CEVSEEGAQV KWLKDGVELT REETFKYRFK
510 520 530 540 550
KDGRKHHLII NEATLEDAGH YAVRTSGGQS LAELIVQEKK LEVYQSIADL
560 570 580 590 600
AVGAKDQAVF KCEVSDENVR GVWLKNGKEL VPDNRIKVSH IGRVHKLTID
610 620 630 640 650
DVTPADEADY SFVPEGFACN LSAKLHFMEV KIDFVPRQEP PKIHLDCPGS
660 670 680 690 700
TPDTIVVVTG NKLRLDVPIS GDPAPTVVWQ KTVTQGKKAS AGPHPDAPED
710 720 730 740 750
AGADEEWVFD KKLLCETEGR VRVETTKDRS VFTVEGAEKE DEGVYTVTVK
760 770 780 790 800
NPVGEDQVNL TVKVIDVPDA PAAPKISNVG EDSCTVQWEP PAYDGGQPVL
810 820 830 840 850
GYILERKKKK SYRWMRLNFD LLRELSHEAR RMIEGVAYEM RVYAVNAVGM
860 870 880 890 900
SRPSPASQPF MPIGPPGEPT HLAVEDVSDT TVSLKWRPPE RVGAGGLDGY
910 920 930 940 950
SVEYCQEGCS EWTPALQGLT ERRSMLVKDL PTGARLLFRV RAHNVAGPGG
960 970 980 990 1000
PIVTKEPVTV QEILQRPRLQ LPRHLRQTIQ KKVGEPVNLL IPFQGKPRPQ
1010 1020 1030 1040 1050
VTWTKEGQPL AGEEVSIRNS PTDTILFIRA ARRTHSGTYQ VTVRIENMED
1060 1070 1080 1090 1100
KATLILQIVD KPSPPQDIRI VETWGFNVAL EWKPPQDDGN TEIWGYTVQK
1110 1120 1130 1140 1150
ADKKTMEWFT VLEHYRRTHC VVSELIIGNG YYFRVFSHNM VGSSDKAAAT
1160 1170 1180 1190 1200
KEPVFIPRPG ITYEPPKYKA LDFSEAPSFT QPLANRSIIA GYNAILCCAV
1210 1220 1230 1240 1250
RGSPKPKISW FKNGLDLGED ARFRMFCKQG VLTLEIRKPC PYDGGVYVCR
1260 1270
ATNLQGEAQC ECRLEVRVPQ
Length:1,270
Mass (Da):140,632
Last modified:August 1, 1998 - v1
Checksum:i699947C3C9B58931
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321E → G in AAC64202 (Ref. 2) Curated
Sequence conflicti39 – 391M → K in AAC64202 (Ref. 2) Curated
Sequence conflicti113 – 1131E → K in AAC64202 (Ref. 2) Curated
Sequence conflicti249 – 2491N → S in AAC64202 (Ref. 2) Curated
Sequence conflicti291 – 2911P → L in AAC64202 (Ref. 2) Curated
Sequence conflicti339 – 3446EACHRP → TDLRGM in AAC64202 (Ref. 2) Curated
Sequence conflicti659 – 6591T → A in AAC64202 (Ref. 2) Curated
Sequence conflicti691 – 6911A → T in AAC64202 (Ref. 2) Curated
Sequence conflicti738 – 7381E → G in AAC64202 (Ref. 2) Curated
Sequence conflicti923 – 9231R → T in AAC64202 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059576 mRNA. Translation: AAC14570.1.
AF097333 mRNA. Translation: AAC64202.1.
UniGeneiMm.10728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059576 mRNA. Translation: AAC14570.1.
AF097333 mRNA. Translation: AAC64202.1.
UniGeneiMm.10728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EDQX-ray1.64A/B149-269[»]
ProteinModelPortaliO70468.
SMRiO70468. Positions 2-96, 104-262, 315-349, 354-447, 449-632, 637-766, 1056-1164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48624N.
IntActiO70468. 3 interactions.
MINTiMINT-4102925.
STRINGi10090.ENSMUSP00000127070.

PTM databases

iPTMnetiO70468.
PhosphoSiteiO70468.

Proteomic databases

MaxQBiO70468.
PaxDbiO70468.
PRIDEiO70468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:102844. Mybpc3.

Phylogenomic databases

eggNOGiENOG410IFCI. Eukaryota.
ENOG4110AYI. LUCA.
HOVERGENiHBG052560.
InParanoidiO70468.

Miscellaneous databases

ChiTaRSiMybpc3. mouse.
PROiO70468.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MYBPC3.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 8 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 8 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "In vivo modeling of myosin binding protein C familial hypertrophic cardiomyopathy."
    Yang Q., Sanbe A., Osinska H., Hewett T.E., Klevitsky R., Robbins J.
    Circ. Res. 85:841-847(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/NJ.
    Tissue: Heart muscle.
  2. "Sequence of the cardiac isoform of murine myosin binding protein-C (MyBP-C) cDNA."
    McDonald K.S., Hollander M.S., Moss R.L.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart muscle.
  3. "Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state."
    Ge Y., Rybakova I.N., Xu Q., Moss R.L.
    Proc. Natl. Acad. Sci. U.S.A. 106:12658-12663(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-273; SER-282 AND SER-302.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-72; SER-307; SER-423; SER-455 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart and Lung.

Entry informationi

Entry nameiMYPC3_MOUSE
AccessioniPrimary (citable) accession number: O70468
Secondary accession number(s): O88997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.