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Protein

Cytochrome b-c1 complex subunit 7

Gene

Uqcrb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 7
Alternative name(s):
Complex III subunit 7
Complex III subunit VII
Ubiquinol-cytochrome c reductase complex 14 kDa protein
Gene namesi
Name:Uqcrb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1914780. Uqcrb.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrial respiratory chain complex III Source: GO_Central
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 111110Cytochrome b-c1 complex subunit 7PRO_0000193525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei12 – 121N6-acetyllysine; alternateCombined sources
Modified residuei12 – 121N6-succinyllysine; alternateCombined sources
Modified residuei19 – 191N6-acetyllysineCombined sources
Modified residuei78 – 781N6-acetyllysine; alternateCombined sources
Modified residuei78 – 781N6-succinyllysine; alternateCombined sources
Modified residuei83 – 831N6-acetyllysineCombined sources
Modified residuei88 – 881N6-acetyllysine; alternateCombined sources
Modified residuei88 – 881N6-succinyllysine; alternateCombined sources
Modified residuei96 – 961N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D855.
MaxQBiQ9D855.
PaxDbiQ9D855.
PRIDEiQ9D855.
TopDownProteomicsiQ9D855.

PTM databases

iPTMnetiQ9D855.
PhosphoSiteiQ9D855.

Expressioni

Gene expression databases

CleanExiMM_UQCRB.

Interactioni

Subunit structurei

The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).By similarity

Protein-protein interaction databases

IntActiQ9D855. 2 interactions.
MINTiMINT-1859815.
STRINGi10090.ENSMUSP00000021993.

Structurei

3D structure databases

ProteinModelPortaliQ9D855.
SMRiQ9D855. Positions 13-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UQCRB/QCR7 family.Curated

Phylogenomic databases

eggNOGiKOG3440. Eukaryota.
ENOG4111V1G. LUCA.
HOGENOMiHOG000188221.
HOVERGENiHBG002984.
InParanoidiQ9D855.
PhylomeDBiQ9D855.

Family and domain databases

Gene3Di1.10.1090.10. 1 hit.
InterProiIPR003197. QCR7.
[Graphical view]
PANTHERiPTHR12022. PTHR12022. 1 hit.
PfamiPF02271. UCR_14kD. 1 hit.
[Graphical view]
PIRSFiPIRSF000022. Bc1_14K. 1 hit.
ProDomiPD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81524. SSF81524. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRSAVSAS SKWLDGFRKW YYNAAGFNKL GLMRDDTLHE TEDVKEAIRR
60 70 80 90 100
LPEDLYNDRM LRIKRALDLT MRHQILPKDQ WTKYEEDKFY LEPYLKEVIR
110
ERKEREEWAK K
Length:111
Mass (Da):13,527
Last modified:January 23, 2007 - v3
Checksum:iA4C9BEFA39CBE94A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71V → F in AAH31607 (PubMed:15489334).Curated
Sequence conflicti61 – 611L → F in AAH31607 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008455 mRNA. Translation: BAB25678.1.
BC031607 mRNA. Translation: AAH31607.1.
CCDSiCCDS26610.1.
UniGeneiMm.379136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008455 mRNA. Translation: BAB25678.1.
BC031607 mRNA. Translation: AAH31607.1.
CCDSiCCDS26610.1.
UniGeneiMm.379136.

3D structure databases

ProteinModelPortaliQ9D855.
SMRiQ9D855. Positions 13-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D855. 2 interactions.
MINTiMINT-1859815.
STRINGi10090.ENSMUSP00000021993.

PTM databases

iPTMnetiQ9D855.
PhosphoSiteiQ9D855.

Proteomic databases

EPDiQ9D855.
MaxQBiQ9D855.
PaxDbiQ9D855.
PRIDEiQ9D855.
TopDownProteomicsiQ9D855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1914780. Uqcrb.

Phylogenomic databases

eggNOGiKOG3440. Eukaryota.
ENOG4111V1G. LUCA.
HOGENOMiHOG000188221.
HOVERGENiHBG002984.
InParanoidiQ9D855.
PhylomeDBiQ9D855.

Miscellaneous databases

PROiQ9D855.
SOURCEiSearch...

Gene expression databases

CleanExiMM_UQCRB.

Family and domain databases

Gene3Di1.10.1090.10. 1 hit.
InterProiIPR003197. QCR7.
[Graphical view]
PANTHERiPTHR12022. PTHR12022. 1 hit.
PfamiPF02271. UCR_14kD. 1 hit.
[Graphical view]
PIRSFiPIRSF000022. Bc1_14K. 1 hit.
ProDomiPD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81524. SSF81524. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-45; 51-59; 66-72 AND 84-96, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-12; LYS-78 AND LYS-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12; LYS-19; LYS-78; LYS-83; LYS-88 AND LYS-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiQCR7_MOUSE
AccessioniPrimary (citable) accession number: Q9D855
Secondary accession number(s): Q8K2E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.