CYC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYC_HUMAN
• UniProt AC: P99999
• Protein Name: Cytochrome c
• Gene Name: CYCS
• Organism: Homo sapiens (Human).
• 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: MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE

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 ------CCCHHCCCE	47.90	13933734
9	Acetylation	GDVEKGKKIFIMKCS CCHHCCCEEEEEECC	52.06	25825284
9	Ubiquitination	GDVEKGKKIFIMKCS CCHHCCCEEEEEECC	52.06	-
14	Succinylation	GKKIFIMKCSQCHTV CCEEEEEECCCCCEE	26.39	27452117
14	Malonylation	GKKIFIMKCSQCHTV CCEEEEEECCCCCEE	26.39	26320211
15	S-palmitoylation	KKIFIMKCSQCHTVE CEEEEEECCCCCEEE	1.56	21044946
18	S-palmitoylation	FIMKCSQCHTVEKGG EEEECCCCCEEECCC	1.34	21044946
28	Succinylation	VEKGGKHKTGPNLHG EECCCCCCCCCCCCC	59.67	23954790
28	Malonylation	VEKGGKHKTGPNLHG EECCCCCCCCCCCCC	59.67	26320211
28	Ubiquitination	VEKGGKHKTGPNLHG EECCCCCCCCCCCCC	59.67	-
28	Sumoylation	VEKGGKHKTGPNLHG EECCCCCCCCCCCCC	59.67	-
29	Phosphorylation	EKGGKHKTGPNLHGL ECCCCCCCCCCCCCC	58.55	28348404
40	Ubiquitination	LHGLFGRKTGQAPGY CCCCCCCCCCCCCCC	58.34	-
40	Succinylation	LHGLFGRKTGQAPGY CCCCCCCCCCCCCCC	58.34	27452117
40	Acetylation	LHGLFGRKTGQAPGY CCCCCCCCCCCCCCC	58.34	26051181
40	2-Hydroxyisobutyrylation	LHGLFGRKTGQAPGY CCCCCCCCCCCCCCC	58.34	-
41	Phosphorylation	HGLFGRKTGQAPGYS CCCCCCCCCCCCCCE	32.92	20068231
47	Nitration	KTGQAPGYSYTAANK CCCCCCCCEEECCCC	9.46	-
47	Phosphorylation	KTGQAPGYSYTAANK CCCCCCCCEEECCCC	9.46	28152594
48	Phosphorylation	TGQAPGYSYTAANKN CCCCCCCEEECCCCC	23.17	25159151
49	Nitration	GQAPGYSYTAANKNK CCCCCCEEECCCCCC	7.60	-
49	Phosphorylation	GQAPGYSYTAANKNK CCCCCCEEECCCCCC	7.60	21712546
50	Phosphorylation	QAPGYSYTAANKNKG CCCCCEEECCCCCCC	17.22	28152594
54	Succinylation	YSYTAANKNKGIIWG CEEECCCCCCCEEEC	56.14	27452117
54	Acetylation	YSYTAANKNKGIIWG CEEECCCCCCCEEEC	56.14	26051181
54	Ubiquitination	YSYTAANKNKGIIWG CEEECCCCCCCEEEC	56.14	-
54	2-Hydroxyisobutyrylation	YSYTAANKNKGIIWG CEEECCCCCCCEEEC	56.14	-
56	Succinylation	YTAANKNKGIIWGED EECCCCCCCEEECCH	53.77	-
56	Ubiquitination	YTAANKNKGIIWGED EECCCCCCCEEECCH	53.77	-
56	Succinylation	YTAANKNKGIIWGED EECCCCCCCEEECCH	53.77	-
68	Phosphorylation	GEDTLMEYLENPKKY CCHHHHHHHHCHHHC	12.83	-
68	Nitration	GEDTLMEYLENPKKY CCHHHHHHHHCHHHC	12.83	-
73	Ubiquitination	MEYLENPKKYIPGTK HHHHHCHHHCCCCCE	70.55	-
73	Acetylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCE	70.55	23236377
73	Succinylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCE	70.55	-
73	Succinylation	MEYLENPKKYIPGTK HHHHHCHHHCCCCCE	70.55	23954790
74	Malonylation	EYLENPKKYIPGTKM HHHHCHHHCCCCCEE	50.06	26320211
74	Acetylation	EYLENPKKYIPGTKM HHHHCHHHCCCCCEE	50.06	2374843
74	Ubiquitination	EYLENPKKYIPGTKM HHHHCHHHCCCCCEE	50.06	-
75	Nitration	YLENPKKYIPGTKMI HHHCHHHCCCCCEEE	20.62	-
75	Phosphorylation	YLENPKKYIPGTKMI HHHCHHHCCCCCEEE	20.62	-
79	Phosphorylation	PKKYIPGTKMIFVGI HHHCCCCCEEEEEEE	16.46	-
80	Ubiquitination	KKYIPGTKMIFVGIK HHCCCCCEEEEEEEC	35.59	21906983
87	Malonylation	KMIFVGIKKKEERAD EEEEEEECCHHHHHH	52.44	26320211
87	2-Hydroxyisobutyrylation	KMIFVGIKKKEERAD EEEEEEECCHHHHHH	52.44	-
87	Acetylation	KMIFVGIKKKEERAD EEEEEEECCHHHHHH	52.44	25953088
87	Ubiquitination	KMIFVGIKKKEERAD EEEEEEECCHHHHHH	52.44	21890473
88	Acetylation	MIFVGIKKKEERADL EEEEEECCHHHHHHH	64.59	20167786
89	Acetylation	IFVGIKKKEERADLI EEEEECCHHHHHHHH	60.86	20167786
98	Nitration	ERADLIAYLKKATNE HHHHHHHHHHHHHCC	16.44	-
98	Phosphorylation	ERADLIAYLKKATNE HHHHHHHHHHHHHCC	16.44	28152594
100	Malonylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	26320211
100	Ubiquitination	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	21890473
100	Acetylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	23236377
100	Methylation	ADLIAYLKKATNE-- HHHHHHHHHHHCC--	27.90	19608861
101	Methylation	DLIAYLKKATNE--- HHHHHHHHHHCC---	58.82	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2CL1_HUMAN	BCL2L1	physical	9192670
CY1_HUMAN	CYC1	physical	6262312
APAF_HUMAN	APAF1	physical	9267021
HSP7C_HUMAN	HSPA8	physical	8663341
CYB5_HUMAN	CYB5A	physical	199233
NDOR1_HUMAN	NDOR1	physical	10625700
PRDX2_HUMAN	PRDX2	physical	22939629
K1C40_HUMAN	KRT40	physical	25416956
THIL_HUMAN	ACAT1	physical	26344197
GLRX2_HUMAN	GLRX2	physical	26344197
IMPA1_HUMAN	IMPA1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
NLE1_HUMAN	NLE1	physical	26344197
TRAF6_HUMAN	TRAF6	physical	25241761
CASP9_HUMAN	CASP9	physical	25241761
B2CL1_HUMAN	BCL2L1	physical	25241761

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612004: Thrombocytopenia 4 (THC4)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB01017: Minocycline

Related Literatures of Post-Translational Modification

Acetylation

"The amino acid sequence of human heart cytochrome c.";
Matsubara H., Smith E.L.;
J. Biol. Chem. 237:3575-3576(1962).
Cited for: PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
PubMed: 13933734