QCR6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: QCR6_HUMAN
• UniProt AC: P07919
• Protein Name: Cytochrome b-c1 complex subunit 6, mitochondrial
• Gene Name: UQCRH
• Organism: Homo sapiens (Human).
• Sequence Length: 91
• Subcellular Localization: Mitochondrion inner membrane .
• Protein Description: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1..
• Protein Sequence: MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK

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
11	Phosphorylation	EDEQKMLTESGDPEE HHHHHHHHCCCCHHH	25.30	28348404
13	Phosphorylation	EQKMLTESGDPEEEE HHHHHHCCCCHHHHH	43.17	26657352
42	Acetylation	EQCEQLEKCVKARER HHHHHHHHHHHHHHH	53.58	25825284
42	Ubiquitination	EQCEQLEKCVKARER HHHHHHHHHHHHHHH	53.58	-
42	2-Hydroxyisobutyrylation	EQCEQLEKCVKARER HHHHHHHHHHHHHHH	53.58	-
42	Succinylation	EQCEQLEKCVKARER HHHHHHHHHHHHHHH	53.58	27452117
53	Glutathionylation	ARERLELCDERVSSR HHHHHHHCCHHHHCC	3.59	22555962
58	Phosphorylation	ELCDERVSSRSHTEE HHCCHHHHCCCCCHH	26.67	26437602
59	Phosphorylation	LCDERVSSRSHTEED HCCHHHHCCCCCHHH	34.64	28450419
61	Phosphorylation	DERVSSRSHTEEDCT CHHHHCCCCCHHHHH	36.39	25159151
63	Phosphorylation	RVSSRSHTEEDCTEE HHHCCCCCHHHHHHH	42.17	21082442
67	Glutathionylation	RSHTEEDCTEELFDF CCCCHHHHHHHHHHH	6.12	22555962
68	Phosphorylation	SHTEEDCTEELFDFL CCCHHHHHHHHHHHH	44.83	30108239
85	Acetylation	RDHCVAHKLFNNLK- HHHHHHHHHHHHCC-	45.06	23954790
85	Ubiquitination	RDHCVAHKLFNNLK- HHHHHHHHHHHHCC-	45.06	19608861

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

Oops, there are no upstream regulatory protein records of QCR6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of QCR6_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 QCR6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL4_HUMAN	RPL4	physical	22939629
F189B_HUMAN	FAM189B	physical	25416956
RNF24_HUMAN	RNF24	physical	25416956
ARL8A_HUMAN	ARL8A	physical	25416956
NDUS4_HUMAN	NDUFS4	physical	26344197
COX7R_HUMAN	COX7A2L	physical	28514442
DOC11_HUMAN	DOCK11	physical	28514442
QCR7_HUMAN	UQCRB	physical	28514442
PEX19_HUMAN	PEX19	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
DCTN5_HUMAN	DCTN5	physical	28514442
CYB_HUMAN	CYTB	physical	28514442
CY1_HUMAN	CYC1	physical	28514442
DCTN6_HUMAN	DCTN6	physical	28514442
QCR8_HUMAN	UQCRQ	physical	28514442
TBB5_HUMAN	TUBB	physical	28514442
ACTY_HUMAN	ACTR1B	physical	28514442
DCTN3_HUMAN	DCTN3	physical	28514442
ILEU_HUMAN	SERPINB1	physical	28514442
QCR1_HUMAN	UQCRC1	physical	28514442
QCR2_HUMAN	UQCRC2	physical	28514442
DCTN2_HUMAN	DCTN2	physical	28514442
DCTN4_HUMAN	DCTN4	physical	28514442

Drug and Disease Associations

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

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-85, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASSSPECTROMETRY.
PubMed: 17081983