CYC_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYC_MOUSE
• UniProt AC: P62897
• Protein Name: Cytochrome c, somatic
• Gene Name: Cycs
• Organism: Mus musculus (Mouse).
• 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..
• 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
2	Acetylation	------MGDVEKGKK ------CCCHHHCCE	47.90	191069
6	Acetylation	--MGDVEKGKKIFVQ --CCCHHHCCEEEEE	75.72	23576753
9	Acetylation	GDVEKGKKIFVQKCA CCHHHCCEEEEEECC	50.47	92087
9	Malonylation	GDVEKGKKIFVQKCA CCHHHCCEEEEEECC	50.47	26073543
14	Malonylation	GKKIFVQKCAQCHTV CCEEEEEECCCCCEE	26.66	26320211
15	S-palmitoylation	KKIFVQKCAQCHTVE CEEEEEECCCCCEEC	1.44	26165157
15	S-nitrosylation	KKIFVQKCAQCHTVE CEEEEEECCCCCEEC	1.44	22178444
18	S-nitrosylation	FVQKCAQCHTVEKGG EEEECCCCCEECCCC	1.22	22178444
28	Acetylation	VEKGGKHKTGPNLHG ECCCCCCCCCCCCCH	59.67	24062335
28	Ubiquitination	VEKGGKHKTGPNLHG ECCCCCCCCCCCCCH	59.67	-
28	Malonylation	VEKGGKHKTGPNLHG ECCCCCCCCCCCCCH	59.67	26320211
29	Phosphorylation	EKGGKHKTGPNLHGL CCCCCCCCCCCCCHH	58.55	25521595
40	Malonylation	LHGLFGRKTGQAAGF CCHHCCCCCCCCCCC	58.34	26320211
40	Ubiquitination	LHGLFGRKTGQAAGF CCHHCCCCCCCCCCC	58.34	-
41	Phosphorylation	HGLFGRKTGQAAGFS CHHCCCCCCCCCCCE	32.92	30635358
48	Phosphorylation	TGQAAGFSYTDANKN CCCCCCCEEECCCCC	26.63	25521595
49	Phosphorylation	GQAAGFSYTDANKNK CCCCCCEEECCCCCC	13.33	19060867
50	Phosphorylation	QAAGFSYTDANKNKG CCCCCEEECCCCCCC	27.69	26745281
54	Ubiquitination	FSYTDANKNKGITWG CEEECCCCCCCCCCC	62.85	-
54	Malonylation	FSYTDANKNKGITWG CEEECCCCCCCCCCC	62.85	26320211
56	Succinylation	YTDANKNKGITWGED EECCCCCCCCCCCHH	53.98	-
56	Acetylation	YTDANKNKGITWGED EECCCCCCCCCCCHH	53.98	23806337
56	Succinylation	YTDANKNKGITWGED EECCCCCCCCCCCHH	53.98	23806337
59	Phosphorylation	ANKNKGITWGEDTLM CCCCCCCCCCHHHHH	35.77	23737553
64	Phosphorylation	GITWGEDTLMEYLEN CCCCCHHHHHHHHHC	24.57	29899451
73	Acetylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCC	70.55	23576753
73	Succinylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCC	70.55	23806337
73	Succinylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCC	70.55	-
73	Malonylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCC	70.55	26073543
73	Ubiquitination	MEYLENPKKYIPGTK HHHHHCHHHCCCCCC	70.55	-
74	Malonylation	EYLENPKKYIPGTKM HHHHCHHHCCCCCCE	50.06	26073543
74	Succinylation	EYLENPKKYIPGTKM HHHHCHHHCCCCCCE	50.06	26388266
74	Acetylation	EYLENPKKYIPGTKM HHHHCHHHCCCCCCE	50.06	2373211
74	Ubiquitination	EYLENPKKYIPGTKM HHHHCHHHCCCCCCE	50.06	-
80	Ubiquitination	KKYIPGTKMIFAGIK HHCCCCCCEEEEEEC	35.59	-
81	Sulfoxidation	KYIPGTKMIFAGIKK HCCCCCCEEEEEECC	2.82	21406390
87	Malonylation	KMIFAGIKKKGERAD CEEEEEECCCCCHHH	47.73	26320211
87	Acetylation	KMIFAGIKKKGERAD CEEEEEECCCCCHHH	47.73	23864654
87	Ubiquitination	KMIFAGIKKKGERAD CEEEEEECCCCCHHH	47.73	-
87	Succinylation	KMIFAGIKKKGERAD CEEEEEECCCCCHHH	47.73	23954790
88	Malonylation	MIFAGIKKKGERADL EEEEEECCCCCHHHH	65.18	25418362
98	Phosphorylation	ERADLIAYLKKATNE CHHHHHHHHHHHHCC	16.44	25521595
100	Acetylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	23576753
100	Malonylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	26320211
100	Succinylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	26388266
100	Ubiquitination	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	-
101	Succinylation	DLIAYLKKATNE--- HHHHHHHHHHCC---	58.82	24315375

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
29	T	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EP15R_MOUSE	Eps15l1	physical	20697350
PP1G_MOUSE	Ppp1cc	physical	20697350

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 191069