CYC_RAT - dbPTM
CYC_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYC_RAT
UniProt AC P62898
Protein Name Cytochrome c, somatic
Gene Name Cycs
Organism Rattus norvegicus (Rat).
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 MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
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
47.90191069
6Acetylation--MGDVEKGKKIFVQ
--CCCHHHCCEEEEE
75.7222902405
8AcetylationMGDVEKGKKIFVQKC
CCCHHHCCEEEEEEC
54.4822902405
9AcetylationGDVEKGKKIFVQKCA
CCHHHCCEEEEEECC
50.4722902405
28AcetylationVEKGGKHKTGPNLHG
ECCCCCCCCCCCCCH
59.6722902405
29PhosphorylationEKGGKHKTGPNLHGL
CCCCCCCCCCCCCHH
58.5523991683
40SuccinylationLHGLFGRKTGQAAGF
CCHHCCCCCCCCCCC
58.3426843850
41PhosphorylationHGLFGRKTGQAAGFS
CHHCCCCCCCCCCCE
32.9228689409
48PhosphorylationTGQAAGFSYTDANKN
CCCCCCCEEECCCCC
26.6329779826
49PhosphorylationGQAAGFSYTDANKNK
CCCCCCEEECCCCCC
13.3320586425
50PhosphorylationQAAGFSYTDANKNKG
CCCCCEEECCCCCCC
27.6923991683
56SuccinylationYTDANKNKGITWGED
EECCCCCCCCCCCHH
53.98-
56AcetylationYTDANKNKGITWGED
EECCCCCCCCCCCHH
53.9822902405
56SuccinylationYTDANKNKGITWGED
EECCCCCCCCCCCHH
53.98-
59PhosphorylationANKNKGITWGEDTLM
CCCCCCCCCCHHHHH
35.7723991683
64PhosphorylationGITWGEDTLMEYLEN
CCCCCHHHHHHHHHC
24.5723991683
68PhosphorylationGEDTLMEYLENPKKY
CHHHHHHHHHCHHHC
12.8323991683
73SuccinylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.5526843850
73SuccinylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.55-
73AcetylationMEYLENPKKYIPGTK
HHHHHCHHHCCCCCC
70.5523923745
74AcetylationEYLENPKKYIPGTKM
HHHHCHHHCCCCCCE
50.0623923753
80AcetylationKKYIPGTKMIFAGIK
HHCCCCCCEEEEEEC
35.5923923765
88AcetylationMIFAGIKKKGERADL
EEEEEECCCCCHHHH
65.1822902405
89AcetylationIFAGIKKKGERADLI
EEEEECCCCCHHHHH
62.0922902405
98PhosphorylationERADLIAYLKKATNE
CHHHHHHHHHHHHCC
16.4423991683
100AcetylationADLIAYLKKATNE--
HHHHHHHHHHHCC--
27.90-

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

Oops, there are no upstream regulatory protein records of CYC_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_RAT !!

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

Oops, there are no PPI records of CYC_RAT !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Primary structure of mouse, rat, and guinea pig cytochrome c.";
Carlson S.S., Mross G.A., Wilson A.C., Mead R.T., Wolin L.D.,Bowers S.F., Foley N.T., Muijsers A.O., Margoliash E.;
Biochemistry 16:1437-1442(1977).
Cited for: PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.

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