CYC_BOVIN - dbPTM
CYC_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYC_BOVIN
UniProt AC P62894
Protein Name Cytochrome c
Gene Name CYCS
Organism Bos taurus (Bovine).
Sequence Length 105
Subcellular Localization Mitochondrion intermembrane space. Loosely associated with the inner membrane.
Protein Description Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity)..
Protein Sequence MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MGDVEKGKK
------CCCHHHCCE
47.905933874
6Acetylation--MGDVEKGKKIFVQ
--CCCHHHCCEEEEE
75.723937105
8AcetylationMGDVEKGKKIFVQKC
CCCHHHCCEEEEEEC
54.483937113
9AcetylationGDVEKGKKIFVQKCA
CCHHHCCEEEEEECC
50.47127017
14AcetylationGKKIFVQKCAQCHTV
CCEEEEEECCCCCEE
26.663937117
23AcetylationAQCHTVEKGGKHKTG
CCCCEECCCCCCCCC
69.493937103
26AcetylationHTVEKGGKHKTGPNL
CEECCCCCCCCCCCC
51.073937119
28AcetylationVEKGGKHKTGPNLHG
ECCCCCCCCCCCCCH
59.672374837
40AcetylationLHGLFGRKTGQAPGF
CCHHCCCCCCCCCCC
58.343937109
48PhosphorylationTGQAPGFSYTDANKN
CCCCCCCCCCCCCCC
32.7929541418
49PhosphorylationGQAPGFSYTDANKNK
CCCCCCCCCCCCCCC
13.3316866357
54AcetylationFSYTDANKNKGITWG
CCCCCCCCCCCCCCC
62.853937115
56SuccinylationYTDANKNKGITWGEE
CCCCCCCCCCCCCHH
53.98-
56SuccinylationYTDANKNKGITWGEE
CCCCCCCCCCCCCHH
53.98-
56AcetylationYTDANKNKGITWGEE
CCCCCCCCCCCCCHH
53.983937121
73AcetylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.55165127
73SuccinylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.55-
73SuccinylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.55-
74AcetylationEYLENPKKYIPGTKM
HHHHCHHHCCCCCCE
50.062374841
80AcetylationKKYIPGTKMIFAGIK
HHCCCCCCEEEEEEC
35.593937107
87AcetylationKMIFAGIKKKGERED
CEEEEEECCCCCHHH
47.732374845
88AcetylationMIFAGIKKKGEREDL
EEEEEECCCCCHHHH
65.183937111
89AcetylationIFAGIKKKGEREDLI
EEEEECCCCCHHHHH
62.093937123
98PhosphorylationEREDLIAYLKKATNE
CHHHHHHHHHHHHCC
16.4418471988
100AcetylationEDLIAYLKKATNE--
HHHHHHHHHHHCC--
27.902381201
101AcetylationDLIAYLKKATNE---
HHHHHHHHHHCC---
58.823937097

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
29TPhosphorylationKinasePRKAA1Q13131
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYC_BOVIN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CYC_BOVIN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CYC_BOVIN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYC_BOVIN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The amino acid sequence of bovine heart cytochrome c.";
Nakashima T., Higa H., Matsubara H., Benson A.M., Yasunobu K.T.;
J. Biol. Chem. 241:1166-1177(1966).
Cited for: PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo,inhibiting mitochondrial respiration.";
Yu H., Lee I., Salomon A.R., Yu K., Huttemann M.;
Biochim. Biophys. Acta 1777:1066-1071(2008).
Cited for: PHOSPHORYLATION AT TYR-98.
"New prospects for an old enzyme: mammalian cytochrome c is tyrosine-phosphorylated in vivo.";
Lee I., Salomon A.R., Yu K., Doan J.W., Grossman L.I., Huttemann M.;
Biochemistry 45:9121-9128(2006).
Cited for: PHOSPHORYLATION AT TYR-49.

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