QCR1_HUMAN - dbPTM
QCR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QCR1_HUMAN
UniProt AC P31930
Protein Name Cytochrome b-c1 complex subunit 1, mitochondrial
Gene Name UQCRC1
Organism Homo sapiens (Human).
Sequence Length 480
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 MAASVVCRAATAGAQVLLRARRSPALLRTPALRSTATFAQALQFVPETQVSLLDNGLRVASEQSSQPTCTVGVWIDVGSRFETEKNNGAGYFLEHLAFKGTKNRPGSALEKEVESMGAHLNAYSTREHTAYYIKALSKDLPKAVELLGDIVQNCSLEDSQIEKERDVILREMQENDASMRDVVFNYLHATAFQGTPLAQAVEGPSENVRKLSRADLTEYLSTHYKAPRMVLAAAGGVEHQQLLDLAQKHLGGIPWTYAEDAVPTLTPCRFTGSEIRHRDDALPFAHVAIAVEGPGWASPDNVALQVANAIIGHYDCTYGGGVHLSSPLASGAVANKLCQSFQTFSICYAETGLLGAHFVCDRMKIDDMMFVLQGQWMRLCTSATESEVARGKNILRNALVSHLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIAEVDASVVREICSKYIYDQCPAVAGYGPIEQLPDYNRIRSGMFWLRF
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
85AcetylationGSRFETEKNNGAGYF
CCCEEEECCCCCCHH		64.2325953088
85UbiquitinationGSRFETEKNNGAGYF
CCCEEEECCCCCCHH		64.2323503661
91PhosphorylationEKNNGAGYFLEHLAF
ECCCCCCHHHHHHHC		12.40-
99SuccinylationFLEHLAFKGTKNRPG
HHHHHHCCCCCCCCC		61.1323954790
99UbiquitinationFLEHLAFKGTKNRPG
HHHHHHCCCCCCCCC		61.1323503661
101PhosphorylationEHLAFKGTKNRPGSA
HHHHCCCCCCCCCCH		26.24-
102UbiquitinationHLAFKGTKNRPGSAL
HHHCCCCCCCCCCHH		60.6823503661
102SuccinylationHLAFKGTKNRPGSAL
HHHCCCCCCCCCCHH		60.6827452117
107PhosphorylationGTKNRPGSALEKEVE
CCCCCCCCHHHHHHH		32.1523401153
111MalonylationRPGSALEKEVESMGA
CCCCHHHHHHHHCCC		68.8326320211
111UbiquitinationRPGSALEKEVESMGA
CCCCHHHHHHHHCCC		68.8319608861
111AcetylationRPGSALEKEVESMGA
CCCCHHHHHHHHCCC		68.8319608861
111SuccinylationRPGSALEKEVESMGA
CCCCHHHHHHHHCCC		68.8323954790
115PhosphorylationALEKEVESMGAHLNA
HHHHHHHHCCCCCCH		27.9122210691
116SulfoxidationLEKEVESMGAHLNAY
HHHHHHHCCCCCCHH		3.3028183972
123PhosphorylationMGAHLNAYSTREHTA
CCCCCCHHCCCHHHH		14.97-
124PhosphorylationGAHLNAYSTREHTAY
CCCCCHHCCCHHHHH		20.6922210691
125PhosphorylationAHLNAYSTREHTAYY
CCCCHHCCCHHHHHH		27.6622210691
129PhosphorylationAYSTREHTAYYIKAL
HHCCCHHHHHHHHHH		16.1728152594
131PhosphorylationSTREHTAYYIKALSK
CCCHHHHHHHHHHHC		13.5928152594
132PhosphorylationTREHTAYYIKALSKD
CCHHHHHHHHHHHCC		8.0928152594
134AcetylationEHTAYYIKALSKDLP
HHHHHHHHHHHCCHH		27.4426051181
134UbiquitinationEHTAYYIKALSKDLP
HHHHHHHHHHHCCHH		27.4423503661
138MalonylationYYIKALSKDLPKAVE
HHHHHHHCCHHHHHH		65.2226320211
138SuccinylationYYIKALSKDLPKAVE
HHHHHHHCCHHHHHH		65.2227452117
138AcetylationYYIKALSKDLPKAVE
HHHHHHHCCHHHHHH		65.22-
138UbiquitinationYYIKALSKDLPKAVE
HHHHHHHCCHHHHHH		65.2223503661
142UbiquitinationALSKDLPKAVELLGD
HHHCCHHHHHHHHHH		72.8123503661
142AcetylationALSKDLPKAVELLGD
HHHCCHHHHHHHHHH		72.8125825284
155PhosphorylationGDIVQNCSLEDSQIE
HHHHHHCCCCHHHHH		42.2027251275
159PhosphorylationQNCSLEDSQIEKERD
HHCCCCHHHHHHHHH		24.5530266825
163SuccinylationLEDSQIEKERDVILR
CCHHHHHHHHHHHHH		60.73-
163SuccinylationLEDSQIEKERDVILR
CCHHHHHHHHHHHHH		60.73-
163UbiquitinationLEDSQIEKERDVILR
CCHHHHHHHHHHHHH		60.7321963094
163AcetylationLEDSQIEKERDVILR
CCHHHHHHHHHHHHH		60.7325038526
195PhosphorylationHATAFQGTPLAQAVE
HHHHCCCCCHHHHHC		12.35-
212PhosphorylationSENVRKLSRADLTEY
CHHHHHHCHHHHHHH		28.5825849741
217PhosphorylationKLSRADLTEYLSTHY
HHCHHHHHHHHHHHC		24.1123403867
219PhosphorylationSRADLTEYLSTHYKA
CHHHHHHHHHHHCCC		10.75-
221PhosphorylationADLTEYLSTHYKAPR
HHHHHHHHHHCCCCH		16.55-
222PhosphorylationDLTEYLSTHYKAPRM
HHHHHHHHHCCCCHH		26.99-
224PhosphorylationTEYLSTHYKAPRMVL
HHHHHHHCCCCHHHH		14.66-
225UbiquitinationEYLSTHYKAPRMVLA
HHHHHHCCCCHHHHH		44.2927667366
225UbiquitinationEYLSTHYKAPRMVLA
HHHHHHCCCCHHHHH		44.2921890473
225AcetylationEYLSTHYKAPRMVLA
HHHHHHCCCCHHHHH		44.2925953088
248AcetylationQLLDLAQKHLGGIPW
HHHHHHHHHHCCCCC		34.8892375
381PhosphorylationGQWMRLCTSATESEV
HHHHHHHCCCCHHHH		26.4517924679
386PhosphorylationLCTSATESEVARGKN
HHCCCCHHHHHHCHH		32.7728857561
401PhosphorylationILRNALVSHLDGTTP
HHHHHHHHHCCCCCC		21.12-
402MethylationLRNALVSHLDGTTPV
HHHHHHHHCCCCCCC		22.064204243
410GlutathionylationLDGTTPVCEDIGRSL
CCCCCCCCHHHHHHH		4.0222555962
416PhosphorylationVCEDIGRSLLTYGRR
CCHHHHHHHHHHCCC		23.6323911959
419PhosphorylationDIGRSLLTYGRRIPL
HHHHHHHHHCCCCCH		29.2623684312
420PhosphorylationIGRSLLTYGRRIPLA
HHHHHHHHCCCCCHH		14.4923684312
447AcetylationVVREICSKYIYDQCP
HHHHHHHHHHHHHCC		31.1225038526
447UbiquitinationVVREICSKYIYDQCP
HHHHHHHHHHHHHCC		31.1221963094
448PhosphorylationVREICSKYIYDQCPA
HHHHHHHHHHHHCCC		6.6022817900
450PhosphorylationEICSKYIYDQCPAVA
HHHHHHHHHHCCCCC		9.2528064214
459PhosphorylationQCPAVAGYGPIEQLP
HCCCCCCCCCHHHCC		15.2522817900
468PhosphorylationPIEQLPDYNRIRSGM
CHHHCCCCCCCCCCC		12.3722817900
473PhosphorylationPDYNRIRSGMFWLRF
CCCCCCCCCCCEECC		32.0424719451
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 QCR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QCR1_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 QCR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_HUMANRUVBL2physical
17353931
QCR2_HUMANUQCRC2physical
17353931
RUXF_HUMANSNRPFphysical
17353931
SRPRB_HUMANSRPRBphysical
17353931
DNJA1_HUMANDNAJA1physical
17353931
RTN4_HUMANRTN4physical
12067236
CYC_HUMANCYCSphysical
6251869
SURF1_HUMANSURF1physical
22939629
STOM_HUMANSTOMphysical
27173435
SOAT1_HUMANSOAT1physical
27173435
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
There are no disease associations of PTM sites.
Regulatory Network of QCR1_HUMAN

loading...

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-111, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-381, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory