QCR2_MOUSE - dbPTM
QCR2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QCR2_MOUSE
UniProt AC Q9DB77
Protein Name Cytochrome b-c1 complex subunit 2, mitochondrial
Gene Name Uqcrc2
Organism Mus musculus (Mouse).
Sequence Length 453
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side.
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. The core protein 2 is required for the assembly of the complex (By similarity)..
Protein Sequence MKLLSRAGSFSRFYSLKVAPKVKTSAAPGGVPLQPQDLEFTKLPNGLVIASLENYAPLSRIGLFVKAGSRYEDSNNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVTATRENMAYTVEGIRSDIEILMEFLLNVTTAPEFRRWEVAALRSQLKIDKAVAFQNSQTRIIENLHDVAYKNALANPLYCPDYRMGKITSEELHYFVQNHFTSARMALVGLGVSHSVLKQVAEQFLNMRGGLGLAGAKAKYRGGEIREQNGDNLVHAAIVAESAAIGNAEANAFSVLQHLLGAGPHIKRGNNTTSLLSQSVAKGSHQPFDVSAFNASYSDSGLFGIYTISQAAAAGEVINAAYNQVKAVAQGNLSSADVQAAKNKLKAGYLMSVETSEGFLSEIGSQALAAGSYMPPSTVLQQIDSVADADVVKAAKKFVSGKKSMAASGNLGHTPFLDEL
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
9PhosphorylationKLLSRAGSFSRFYSL
CCHHCCCCCHHEEEE		21.0424719451
17SuccinylationFSRFYSLKVAPKVKT
CHHEEEEEECCCCCC		30.3424315375
24PhosphorylationKVAPKVKTSAAPGGV
EECCCCCCCCCCCCC		26.9627742792
25PhosphorylationVAPKVKTSAAPGGVP
ECCCCCCCCCCCCCC		19.4027742792
42AcetylationPQDLEFTKLPNGLVI
CCCCCEEECCCCEEE		68.2323864654
42SuccinylationPQDLEFTKLPNGLVI
CCCCCEEECCCCEEE		68.2323954790
66AcetylationSRIGLFVKAGSRYED
HHEEEEEECCCCCCC		39.4323576753
66SuccinylationSRIGLFVKAGSRYED
HHEEEEEECCCCCCC		39.4323806337
74PhosphorylationAGSRYEDSNNLGTSH
CCCCCCCCCCCCHHH		18.7123737553
80PhosphorylationDSNNLGTSHLLRLAS
CCCCCCHHHHHHHHH		15.4424899341
92AcetylationLASSLTTKGASSFKI
HHHHCCCCCCCCCEE		47.4423806337
92UbiquitinationLASSLTTKGASSFKI
HHHHCCCCCCCCCEE		47.44-
92SuccinylationLASSLTTKGASSFKI
HHHHCCCCCCCCCEE		47.44-
92MalonylationLASSLTTKGASSFKI
HHHHCCCCCCCCCEE		47.4426320211
98UbiquitinationTKGASSFKITRGIEA
CCCCCCCEEECCEEE		45.1527667366
98SuccinylationTKGASSFKITRGIEA
CCCCCCCEEECCEEE		45.1526388266
98AcetylationTKGASSFKITRGIEA
CCCCCCCEEECCEEE		45.1523864654
98MalonylationTKGASSFKITRGIEA
CCCCCCCEEECCEEE		45.1526320211
109SuccinylationGIEAVGGKLSVTATR
CEEEECCEEEEEEEE		31.4923954790
156PhosphorylationWEVAALRSQLKIDKA
HHHHHHHHHCCCCHH		40.49-
159SuccinylationAALRSQLKIDKAVAF
HHHHHHCCCCHHHHC		41.0224315375
159AcetylationAALRSQLKIDKAVAF
HHHHHHCCCCHHHHC		41.0223864654
162AcetylationRSQLKIDKAVAFQNS
HHHCCCCHHHHCCCC		48.5124062335
169PhosphorylationKAVAFQNSQTRIIEN
HHHHCCCCCHHHHHH		23.3423737553
171PhosphorylationVAFQNSQTRIIENLH
HHCCCCCHHHHHHHH		24.5323737553
192S-nitrosocysteineALANPLYCPDYRMGK
CCCCCCCCCCCCCCC		2.45-
192S-palmitoylationALANPLYCPDYRMGK
CCCCCCCCCCCCCCC		2.4528526873
192S-nitrosylationALANPLYCPDYRMGK
CCCCCCCCCCCCCCC		2.4524895380
199AcetylationCPDYRMGKITSEELH
CCCCCCCCCCHHHHH		33.2123576753
199SuccinylationCPDYRMGKITSEELH
CCCCCCCCCCHHHHH		33.2123806337
202PhosphorylationYRMGKITSEELHYFV
CCCCCCCHHHHHHHH		32.3322817900
207PhosphorylationITSEELHYFVQNHFT
CCHHHHHHHHHHCCC		20.3317242355
226PhosphorylationALVGLGVSHSVLKQV
HHHHCCCCHHHHHHH		14.3022817900
228PhosphorylationVGLGVSHSVLKQVAE
HHCCCCHHHHHHHHH		22.9519060867
231AcetylationGVSHSVLKQVAEQFL
CCCHHHHHHHHHHHH		40.3424062335
250MalonylationGLGLAGAKAKYRGGE
CCCCCCCCCHHCCCC		44.4826320211
250AcetylationGLGLAGAKAKYRGGE
CCCCCCCCCHHCCCC		44.4823576753
250GlutarylationGLGLAGAKAKYRGGE
CCCCCCCCCHHCCCC		44.4824703693
250SuccinylationGLGLAGAKAKYRGGE
CCCCCCCCCHHCCCC		44.4823806337
305PhosphorylationHIKRGNNTTSLLSQS
CCCCCCCHHHHHHHH		23.05-
310PhosphorylationNNTTSLLSQSVAKGS
CCHHHHHHHHHHCCC		26.2122802335
312PhosphorylationTTSLLSQSVAKGSHQ
HHHHHHHHHHCCCCC		22.2125890499
315AcetylationLLSQSVAKGSHQPFD
HHHHHHHCCCCCCCC		59.8123864654
367PhosphorylationAVAQGNLSSADVQAA
HHHCCCCCHHHHHHH		27.7229899451
368PhosphorylationVAQGNLSSADVQAAK
HHCCCCCHHHHHHHH		31.4925521595
375SuccinylationSADVQAAKNKLKAGY
HHHHHHHHHHCCCCE		58.6026388266
375UbiquitinationSADVQAAKNKLKAGY
HHHHHHHHHHCCCCE		58.60-
435AcetylationAKKFVSGKKSMAASG
HHHHHCCCCHHHCCC		33.8823864654
436SuccinylationKKFVSGKKSMAASGN
HHHHCCCCHHHCCCC		49.3326388266
437PhosphorylationKFVSGKKSMAASGNL
HHHCCCCHHHCCCCC		19.6920495213
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 QCR2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
159KAcetylation

-
250KAcetylation

23576753
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 QCR2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of QCR2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of QCR2_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-159 AND LYS-250, AND MASSSPECTROMETRY.

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