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Protein

Cytochrome b-c1 complex subunit 2, mitochondrial

Gene

Uqcrc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. The core protein 2 is required for the assembly of the complex (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Protein family/group databases

MEROPSiM16.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 2, mitochondrial
Alternative name(s):
Complex III subunit 2
Core protein II
Ubiquinol-cytochrome-c reductase complex core protein 2
Gene namesi
Name:Uqcrc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914253. Uqcrc2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial respiratory chain complex III Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1414MitochondrionBy similarityAdd
BLAST
Chaini15 – 453439Cytochrome b-c1 complex subunit 2, mitochondrialPRO_0000026792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysineCombined sources
Modified residuei199 – 1991N6-acetyllysineCombined sources
Modified residuei250 – 2501N6-acetyllysineCombined sources
Modified residuei368 – 3681PhosphoserineBy similarity

Post-translational modificationi

Acetylation of Lys-159 and Lys-250 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DB77.
MaxQBiQ9DB77.
PaxDbiQ9DB77.
PRIDEiQ9DB77.
TopDownProteomicsiQ9DB77.

PTM databases

iPTMnetiQ9DB77.
PhosphoSiteiQ9DB77.
SwissPalmiQ9DB77.

Expressioni

Gene expression databases

BgeeiQ9DB77.
CleanExiMM_UQCRC2.
GenevisibleiQ9DB77. MM.

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

BioGridi211868. 3 interactions.
IntActiQ9DB77. 10 interactions.
MINTiMINT-1842572.
STRINGi10090.ENSMUSP00000033176.

Structurei

3D structure databases

ProteinModelPortaliQ9DB77.
SMRiQ9DB77. Positions 35-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2583. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000046923.
HOVERGENiHBG055236.
InParanoidiQ9DB77.
KOiK00415.
OMAiVESSECF.
OrthoDBiEOG79CXZF.
PhylomeDBiQ9DB77.
TreeFamiTF105033.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 3 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DB77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSRAGSF SRFYSLKVAP KVKTSAAPGG VPLQPQDLEF TKLPNGLVIA
60 70 80 90 100
SLENYAPLSR IGLFVKAGSR YEDSNNLGTS HLLRLASSLT TKGASSFKIT
110 120 130 140 150
RGIEAVGGKL SVTATRENMA YTVEGIRSDI EILMEFLLNV TTAPEFRRWE
160 170 180 190 200
VAALRSQLKI DKAVAFQNSQ TRIIENLHDV AYKNALANPL YCPDYRMGKI
210 220 230 240 250
TSEELHYFVQ NHFTSARMAL VGLGVSHSVL KQVAEQFLNM RGGLGLAGAK
260 270 280 290 300
AKYRGGEIRE QNGDNLVHAA IVAESAAIGN AEANAFSVLQ HLLGAGPHIK
310 320 330 340 350
RGNNTTSLLS QSVAKGSHQP FDVSAFNASY SDSGLFGIYT ISQAAAAGEV
360 370 380 390 400
INAAYNQVKA VAQGNLSSAD VQAAKNKLKA GYLMSVETSE GFLSEIGSQA
410 420 430 440 450
LAAGSYMPPS TVLQQIDSVA DADVVKAAKK FVSGKKSMAA SGNLGHTPFL

DEL
Length:453
Mass (Da):48,235
Last modified:June 1, 2001 - v1
Checksum:i24A2BDDDA657867E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361Q → L in BAB25176 (PubMed:16141072).Curated
Sequence conflicti319 – 3191Q → R in BAC36876 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005151 mRNA. Translation: BAB23845.1.
AK007669 mRNA. Translation: BAB25176.1.
AK077583 mRNA. Translation: BAC36876.1.
AK088103 mRNA. Translation: BAC40146.1.
BC003423 mRNA. Translation: AAH03423.1.
CCDSiCCDS21795.1.
PIRiPC7073.
RefSeqiNP_080175.1. NM_025899.2.
UniGeneiMm.334206.

Genome annotation databases

EnsembliENSMUST00000033176; ENSMUSP00000033176; ENSMUSG00000030884.
GeneIDi67003.
KEGGimmu:67003.
UCSCiuc009jms.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005151 mRNA. Translation: BAB23845.1.
AK007669 mRNA. Translation: BAB25176.1.
AK077583 mRNA. Translation: BAC36876.1.
AK088103 mRNA. Translation: BAC40146.1.
BC003423 mRNA. Translation: AAH03423.1.
CCDSiCCDS21795.1.
PIRiPC7073.
RefSeqiNP_080175.1. NM_025899.2.
UniGeneiMm.334206.

3D structure databases

ProteinModelPortaliQ9DB77.
SMRiQ9DB77. Positions 35-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211868. 3 interactions.
IntActiQ9DB77. 10 interactions.
MINTiMINT-1842572.
STRINGi10090.ENSMUSP00000033176.

Protein family/group databases

MEROPSiM16.974.

PTM databases

iPTMnetiQ9DB77.
PhosphoSiteiQ9DB77.
SwissPalmiQ9DB77.

Proteomic databases

EPDiQ9DB77.
MaxQBiQ9DB77.
PaxDbiQ9DB77.
PRIDEiQ9DB77.
TopDownProteomicsiQ9DB77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033176; ENSMUSP00000033176; ENSMUSG00000030884.
GeneIDi67003.
KEGGimmu:67003.
UCSCiuc009jms.1. mouse.

Organism-specific databases

CTDi7385.
MGIiMGI:1914253. Uqcrc2.

Phylogenomic databases

eggNOGiKOG2583. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000046923.
HOVERGENiHBG055236.
InParanoidiQ9DB77.
KOiK00415.
OMAiVESSECF.
OrthoDBiEOG79CXZF.
PhylomeDBiQ9DB77.
TreeFamiTF105033.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Miscellaneous databases

ChiTaRSiUqcrc2. mouse.
PROiQ9DB77.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB77.
CleanExiMM_UQCRC2.
GenevisibleiQ9DB77. MM.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 3 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
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: Cerebellum, Pancreas and Thymus.
  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].
  3. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 24-60; 71-85; 117-147; 163-196; 200-241; 301-315; 360-375 AND 436-453, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "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-66; LYS-199 AND LYS-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiQCR2_MOUSE
AccessioniPrimary (citable) accession number: Q9DB77
Secondary accession number(s): Q8BK11, Q9CVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.Curated

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. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.