QCR7_HUMAN - dbPTM
QCR7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QCR7_HUMAN
UniProt AC P14927
Protein Name Cytochrome b-c1 complex subunit 7
Gene Name UQCRB
Organism Homo sapiens (Human).
Sequence Length 111
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 component is involved in redox-linked proton pumping..
Protein Sequence MAGKQAVSASGKWLDGIRKWYYNAAGFNKLGLMRDDTIYEDEDVKEAIRRLPENLYNDRMFRIKRALDLNLKHQILPKEQWTKYEEENFYLEPYLKEVIRERKEREEWAKK
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------MAGKQAVSA
------CCCCHHHCC
33.61-
4Acetylation----MAGKQAVSASG
----CCCCHHHCCCC
26.0820167786
4Ubiquitination----MAGKQAVSASG
----CCCCHHHCCCC
26.0833845483
8PhosphorylationMAGKQAVSASGKWLD
CCCCHHHCCCCCHHH
21.5221712546
10PhosphorylationGKQAVSASGKWLDGI
CCHHHCCCCCHHHHH
33.1421712546
12AcetylationQAVSASGKWLDGIRK
HHHCCCCCHHHHHHH
41.9323236377
12SuccinylationQAVSASGKWLDGIRK
HHHCCCCCHHHHHHH
41.93-
12UbiquitinationQAVSASGKWLDGIRK
HHHCCCCCHHHHHHH
41.9321890473
12UbiquitinationQAVSASGKWLDGIRK
HHHCCCCCHHHHHHH
41.9321890473
12SuccinylationQAVSASGKWLDGIRK
HHHCCCCCHHHHHHH
41.9321890473
13UbiquitinationAVSASGKWLDGIRKW
HHCCCCCHHHHHHHH
11.8322817900
19AcetylationKWLDGIRKWYYNAAG
CHHHHHHHHHHCCCC
37.3125825284
19SuccinylationKWLDGIRKWYYNAAG
CHHHHHHHHHHCCCC
37.3123954790
19MalonylationKWLDGIRKWYYNAAG
CHHHHHHHHHHCCCC
37.3126320211
21PhosphorylationLDGIRKWYYNAAGFN
HHHHHHHHHCCCCCH
7.00-
29UbiquitinationYNAAGFNKLGLMRDD
HCCCCCHHCCCCCCC
41.4921890473
29UbiquitinationYNAAGFNKLGLMRDD
HCCCCCHHCCCCCCC
41.4921906983
37PhosphorylationLGLMRDDTIYEDEDV
CCCCCCCCCCCCHHH
29.73-
39PhosphorylationLMRDDTIYEDEDVKE
CCCCCCCCCCHHHHH
21.3027642862
40UbiquitinationMRDDTIYEDEDVKEA
CCCCCCCCCHHHHHH
51.5823503661
45AcetylationIYEDEDVKEAIRRLP
CCCCHHHHHHHHHCC
54.4726822725
45UbiquitinationIYEDEDVKEAIRRLP
CCCCHHHHHHHHHCC
54.4721906983
452-HydroxyisobutyrylationIYEDEDVKEAIRRLP
CCCCHHHHHHHHHCC
54.47-
46AcetylationYEDEDVKEAIRRLPE
CCCHHHHHHHHHCCH
49.5319608861
46UbiquitinationYEDEDVKEAIRRLPE
CCCHHHHHHHHHCCH
49.5323503661
51UbiquitinationVKEAIRRLPENLYND
HHHHHHHCCHHHHCC
4.4823503661
56PhosphorylationRRLPENLYNDRMFRI
HHCCHHHHCCHHHHH
26.97-
59MethylationPENLYNDRMFRIKRA
CHHHHCCHHHHHHHH
23.62115919541
64UbiquitinationNDRMFRIKRALDLNL
CCHHHHHHHHHCCCC
27.6223503661
72UbiquitinationRALDLNLKHQILPKE
HHHCCCCCCCCCCHH
32.1823503661
72AcetylationRALDLNLKHQILPKE
HHHCCCCCCCCCCHH
32.1825825284
78AcetylationLKHQILPKEQWTKYE
CCCCCCCHHHHCCHH
60.1223954790
78SuccinylationLKHQILPKEQWTKYE
CCCCCCCHHHHCCHH
60.12-
78SuccinylationLKHQILPKEQWTKYE
CCCCCCCHHHHCCHH
60.1223954790
78UbiquitinationLKHQILPKEQWTKYE
CCCCCCCHHHHCCHH
60.1219608861
83UbiquitinationLPKEQWTKYEEENFY
CCHHHHCCHHHHCCC
47.9423503661
83AcetylationLPKEQWTKYEEENFY
CCHHHHCCHHHHCCC
47.9425038526
90PhosphorylationKYEEENFYLEPYLKE
CHHHHCCCHHHHHHH
23.0327642862
94PhosphorylationENFYLEPYLKEVIRE
HCCCHHHHHHHHHHH
22.49-
96UbiquitinationFYLEPYLKEVIRERK
CCHHHHHHHHHHHHH
44.0523503661
96AcetylationFYLEPYLKEVIRERK
CCHHHHHHHHHHHHH
44.0523236377
96SuccinylationFYLEPYLKEVIRERK
CCHHHHHHHHHHHHH
44.0523954790
110AcetylationKEREEWAKK------
HHHHHHHHC------
61.156572095
110SuccinylationKEREEWAKK------
HHHHHHHHC------
61.1523954790
111AcetylationEREEWAKK-------
HHHHHHHC-------
58.805643605

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 QCR7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QCR7_HUMAN !!

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 QCR7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UCRI_HUMANUQCRFS1physical
22939629
RS10_HUMANRPS10physical
22939629
RL9_HUMANRPL9physical
22939629
RL23_HUMANRPL23physical
22939629
RL11_HUMANRPL11physical
22939629
TIM10_HUMANTIMM10physical
22939629
RL14_HUMANRPL14physical
22939629
RS2_HUMANRPS2physical
22939629
THIL_HUMANACAT1physical
22939629
RS16_HUMANRPS16physical
22939629
RL6_HUMANRPL6physical
22939629
1A1L1_HUMANACCSphysical
25416956
QCR2_HUMANUQCRC2physical
26186194
COX7R_HUMANCOX7A2Lphysical
26186194
MY18A_HUMANMYO18Aphysical
26186194
UHRF1_HUMANUHRF1physical
26186194
S10AA_HUMANS100A10physical
26186194
KPCA_HUMANPRKCAphysical
26186194
QCR1_HUMANUQCRC1physical
26186194
CYB_HUMANCYTBphysical
26186194
RABL6_HUMANRABL6physical
26186194
QCR9_HUMANUQCR10physical
26186194
QCR6_HUMANUQCRHphysical
26186194
COX1_HUMANCOX1physical
26186194
CX6B1_HUMANCOX6B1physical
26186194
QCR8_HUMANUQCRQphysical
26186194
COX5A_HUMANCOX5Aphysical
26344197
OST48_HUMANDDOSTphysical
26344197
NDUAC_HUMANNDUFA12physical
26344197
NDUA8_HUMANNDUFA8physical
26344197
NDUS4_HUMANNDUFS4physical
26344197
NDUV1_HUMANNDUFV1physical
26344197
VDAC1_HUMANVDAC1physical
26344197
CYB_HUMANCYTBphysical
28514442
COX7R_HUMANCOX7A2Lphysical
28514442
MY18A_HUMANMYO18Aphysical
28514442
QCR1_HUMANUQCRC1physical
28514442
UHRF1_HUMANUHRF1physical
28514442
QCR2_HUMANUQCRC2physical
28514442
S10AA_HUMANS100A10physical
28514442
ACTBL_HUMANACTBL2physical
28514442
COX1_HUMANCOX1physical
28514442
ZO1_HUMANTJP1physical
28514442
ACTB_HUMANACTBphysical
28514442

Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
OMIM Disease
615158Mitochondrial complex III deficiency, nuclear 3 (MC3DN3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QCR7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-78, AND MASS SPECTROMETRY.

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