COX5B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COX5B_HUMAN
• UniProt AC: P10606
• Protein Name: Cytochrome c oxidase subunit 5B, mitochondrial
• Gene Name: COX5B
• Organism: Homo sapiens (Human).
• Sequence Length: 129
• Subcellular Localization: Mitochondrion inner membrane.
• Protein Description: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport..
• Protein Sequence: MASRLLRGAGTLAAQALRARGPSGAAAMRSMASGGGVPTDEEQATGLEREIMLAAKKGLDPYNVLAPKGASGTREDPNLVPSISNKRIVGCICEEDNTSVVWFWLHKGEAQRCPRCGAHYKLVPQQLAH

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
3	Phosphorylation	-----MASRLLRGAG -----CHHHHHHHHH	23.35	20860994
30	Phosphorylation	SGAAAMRSMASGGGV CHHHHHHHHHCCCCC	12.96	20068231
33	Phosphorylation	AAMRSMASGGGVPTD HHHHHHHCCCCCCCC	29.36	22210691
39	Phosphorylation	ASGGGVPTDEEQATG HCCCCCCCCHHHHHC	54.35	20068231
45	Phosphorylation	PTDEEQATGLEREIM CCCHHHHHCCHHHHH	41.83	20068231
56	Acetylation	REIMLAAKKGLDPYN HHHHHHHHCCCCCCC	41.59	25953088
56	Succinylation	REIMLAAKKGLDPYN HHHHHHHHCCCCCCC	41.59	27452117
56	Malonylation	REIMLAAKKGLDPYN HHHHHHHHCCCCCCC	41.59	26320211
56	2-Hydroxyisobutyrylation	REIMLAAKKGLDPYN HHHHHHHHCCCCCCC	41.59	-
56	Ubiquitination	REIMLAAKKGLDPYN HHHHHHHHCCCCCCC	41.59	-
57	Ubiquitination	EIMLAAKKGLDPYNV HHHHHHHCCCCCCCC	61.04	21890473
57	Acetylation	EIMLAAKKGLDPYNV HHHHHHHCCCCCCCC	61.04	25038526
57	Ubiquitination	EIMLAAKKGLDPYNV HHHHHHHCCCCCCCC	61.04	21890473
57	Malonylation	EIMLAAKKGLDPYNV HHHHHHHCCCCCCCC	61.04	26320211
62	Phosphorylation	AKKGLDPYNVLAPKG HHCCCCCCCCCCCCC	19.98	28152594
68	Ubiquitination	PYNVLAPKGASGTRE CCCCCCCCCCCCCCC	62.59	21890473
68	Ubiquitination	PYNVLAPKGASGTRE CCCCCCCCCCCCCCC	62.59	21890473
68	Acetylation	PYNVLAPKGASGTRE CCCCCCCCCCCCCCC	62.59	30584465
68	Malonylation	PYNVLAPKGASGTRE CCCCCCCCCCCCCCC	62.59	26320211
71	Phosphorylation	VLAPKGASGTREDPN CCCCCCCCCCCCCCC	49.74	17349628
73	Phosphorylation	APKGASGTREDPNLV CCCCCCCCCCCCCCC	28.52	26437602
84	Phosphorylation	PNLVPSISNKRIVGC CCCCCCCCCCEEEEE	40.41	26437602
86	2-Hydroxyisobutyrylation	LVPSISNKRIVGCIC CCCCCCCCEEEEEEE	36.39	-
86	Ubiquitination	LVPSISNKRIVGCIC CCCCCCCCEEEEEEE	36.39	21890473
86	Acetylation	LVPSISNKRIVGCIC CCCCCCCCEEEEEEE	36.39	25953088
86	Ubiquitination	LVPSISNKRIVGCIC CCCCCCCCEEEEEEE	36.39	21890473
107	Acetylation	VVWFWLHKGEAQRCP EEEEEEECCCHHCCC	57.17	25825284
121	Acetylation	PRCGAHYKLVPQQLA CCCCCCEEECHHHHC	32.89	19608861

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

Oops, there are no upstream regulatory protein records of COX5B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COX5B_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 COX5B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ODP2_HUMAN	DLAT	physical	22939629
K1C15_HUMAN	KRT15	physical	25416956
K1H1_HUMAN	KRT31	physical	25416956
TRAF1_HUMAN	TRAF1	physical	25416956
BHE40_HUMAN	BHLHE40	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
TFP11_HUMAN	TFIP11	physical	25416956
IHO1_HUMAN	CCDC36	physical	25416956
COX2_HUMAN	COX2	physical	26344197
PPIL3_HUMAN	PPIL3	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
IHO1_HUMAN	CCDC36	physical	21516116
TRI23_HUMAN	TRIM23	physical	21516116
F208B_HUMAN	FAM208B	physical	21516116

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB02659: Cholic Acid

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND MASS SPECTROMETRY.
PubMed: 19608861