QCR6_MOUSE - dbPTM
QCR6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QCR6_MOUSE
UniProt AC P99028
Protein Name Cytochrome b-c1 complex subunit 6, mitochondrial
Gene Name Uqcrh
Organism Mus musculus (Mouse).
Sequence Length 89
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 (By similarity)..
Protein Sequence MGLEDERKMLTGSGDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLELCDNRVSSRSQTEEDCTEELFDFLHARDHCVAHKLFKNLK
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
11PhosphorylationEDERKMLTGSGDPKE
HHHHHHHCCCCCCHH
26.2922817900
13PhosphorylationERKMLTGSGDPKEEE
HHHHHCCCCCCHHHH
34.4822817900
29PhosphorylationEELVDPLTTVREHCE
HHHCCHHHHHHHHHH
28.74-
30PhosphorylationELVDPLTTVREHCEQ
HHCCHHHHHHHHHHH
25.83-
35S-nitrosocysteineLTTVREHCEQLEKCV
HHHHHHHHHHHHHHH
2.82-
35S-nitrosylationLTTVREHCEQLEKCV
HHHHHHHHHHHHHHH
2.8221278135
40AcetylationEHCEQLEKCVKARER
HHHHHHHHHHHHHHH
53.5823576753
40MalonylationEHCEQLEKCVKARER
HHHHHHHHHHHHHHH
53.5826320211
51S-palmitoylationARERLELCDNRVSSR
HHHHHHHCCCCCCCC
2.9626165157
51S-nitrosylationARERLELCDNRVSSR
HHHHHHHCCCCCCCC
2.9621278135
51GlutathionylationARERLELCDNRVSSR
HHHHHHHCCCCCCCC
2.9624333276
51S-nitrosocysteineARERLELCDNRVSSR
HHHHHHHCCCCCCCC
2.96-
56PhosphorylationELCDNRVSSRSQTEE
HHCCCCCCCCCCCHH
19.4526643407
57PhosphorylationLCDNRVSSRSQTEED
HCCCCCCCCCCCHHH
32.8526643407
59PhosphorylationDNRVSSRSQTEEDCT
CCCCCCCCCCHHHHH
43.3221082442
61PhosphorylationRVSSRSQTEEDCTEE
CCCCCCCCHHHHHHH
42.4621082442
65S-nitrosocysteineRSQTEEDCTEELFDF
CCCCHHHHHHHHHHH
6.12-
65GlutathionylationRSQTEEDCTEELFDF
CCCCHHHHHHHHHHH
6.1224333276
65S-nitrosylationRSQTEEDCTEELFDF
CCCCHHHHHHHHHHH
6.1224895380
66PhosphorylationSQTEEDCTEELFDFL
CCCHHHHHHHHHHHH
44.8323140645
83AcetylationRDHCVAHKLFKNLK-
HHHHHHHHHHHHCC-
45.9723576753
83PhosphoglycerylationRDHCVAHKLFKNLK-
HHHHHHHHHHHHCC-
45.97-
83MalonylationRDHCVAHKLFKNLK-
HHHHHHHHHHHHCC-
45.9726320211
83SuccinylationRDHCVAHKLFKNLK-
HHHHHHHHHHHHCC-
45.9724315375
86AcetylationCVAHKLFKNLK----
HHHHHHHHHCC----
72.3323864654
86UbiquitinationCVAHKLFKNLK----
HHHHHHHHHCC----
72.3327667366
86MalonylationCVAHKLFKNLK----
HHHHHHHHHCC----
72.3326073543

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 QCR6_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QCR6_MOUSE !!

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 QCR6_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of QCR6_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QCR6_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND MASSSPECTROMETRY.

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