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P31930 (QCR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b-c1 complex subunit 1, mitochondrial
Alternative name(s):
Complex III subunit 1
Core protein I
Ubiquinol-cytochrome-c reductase complex core protein 1
Gene names
Name:UQCRC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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).

Subcellular location

Mitochondrion inner membrane.

Sequence similarities

Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.

Caution

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

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic respiration

Traceable author statement Ref.1. Source: ProtInc

cellular metabolic process

Traceable author statement. Source: Reactome

hydrogen ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

mitochondrial electron transport, ubiquinol to cytochrome c

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Traceable author statement Ref.1. Source: ProtInc

oxidative phosphorylation

Traceable author statement Ref.1. Source: ProtInc

respiratory electron transport chain

Traceable author statement. Source: Reactome

response to activity

Inferred from electronic annotation. Source: Ensembl

response to alkaloid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial respiratory chain

Traceable author statement Ref.1. Source: ProtInc

mitochondrial respiratory chain complex III

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

ubiquinol-cytochrome-c reductase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.8
Chain35 – 480446Cytochrome b-c1 complex subunit 1, mitochondrial
PRO_0000026786

Amino acid modifications

Modified residue1111N6-acetyllysine Ref.11
Modified residue1381N6-acetyllysine By similarity
Modified residue1631N6-acetyllysine; alternate By similarity
Modified residue1631N6-succinyllysine; alternate By similarity
Modified residue2481N6-acetyllysine By similarity

Natural variations

Natural variant2151D → H.
Corresponds to variant rs17080284 [ dbSNP | Ensembl ].
VAR_034581
Natural variant3011N → S. Ref.1 Ref.13
Corresponds to variant rs144710790 [ dbSNP | Ensembl ].
VAR_013629

Sequences

Sequence LengthMass (Da)Tools
P31930 [UniParc].

Last modified April 4, 2006. Version 3.
Checksum: E76B082166CAF48F

FASTA48052,646
        10         20         30         40         50         60 
MAASVVCRAA TAGAQVLLRA RRSPALLRTP ALRSTATFAQ ALQFVPETQV SLLDNGLRVA 

        70         80         90        100        110        120 
SEQSSQPTCT VGVWIDVGSR FETEKNNGAG YFLEHLAFKG TKNRPGSALE KEVESMGAHL 

       130        140        150        160        170        180 
NAYSTREHTA YYIKALSKDL PKAVELLGDI VQNCSLEDSQ IEKERDVILR EMQENDASMR 

       190        200        210        220        230        240 
DVVFNYLHAT AFQGTPLAQA VEGPSENVRK LSRADLTEYL STHYKAPRMV LAAAGGVEHQ 

       250        260        270        280        290        300 
QLLDLAQKHL GGIPWTYAED AVPTLTPCRF TGSEIRHRDD ALPFAHVAIA VEGPGWASPD 

       310        320        330        340        350        360 
NVALQVANAI IGHYDCTYGG GVHLSSPLAS GAVANKLCQS FQTFSICYAE TGLLGAHFVC 

       370        380        390        400        410        420 
DRMKIDDMMF VLQGQWMRLC TSATESEVAR GKNILRNALV SHLDGTTPVC EDIGRSLLTY 

       430        440        450        460        470        480 
GRRIPLAEWE SRIAEVDASV VREICSKYIY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF 

« Hide

References

« Hide 'large scale' references
[1]"Complete coding sequence, intron/exon organization, and chromosomal location of the gene for the core I protein of human ubiquinol-cytochrome c reductase."
Hoffman G.G., Lee S., Christiano A.M., Chung-Honet L.C., Cheng W., Katchman S., Uitto J., Greenspan D.S.
J. Biol. Chem. 268:21113-21119(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-301.
Tissue: Placenta.
[2]"A complete cDNA sequence for core I protein subunit of human ubiquinol-cytochrome c reductase."
Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.
Biochem. Mol. Biol. Int. 32:797-805(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[3]Erratum
Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.
Biochem. Mol. Biol. Int. 33:410-410(1994) [PubMed] [Europe PMC] [Abstract]
[4]Erratum
Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.
Biochem. Mol. Biol. Int. 33:815-815(1994) [PubMed] [Europe PMC] [Abstract]
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Subthalamic nucleus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Bone marrow.
[8]"Human liver protein map: update 1993."
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.
Electrophoresis 14:1216-1222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-45.
Tissue: Liver.
[9]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 86-99; 214-225; 229-248; 397-415; 424-442; 448-470 AND 473-479, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 143-165; 181-209 AND 397-415.
Tissue: Adipocyte.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"A mitochondrial cytochrome b mutation but no mutations of nuclearly encoded subunits in ubiquinol cytochrome c reductase (complex III) deficiency."
Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B., Munnich A., Kachaner J., Rustin P., Roetig A.
Hum. Genet. 104:460-466(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-301.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16842 mRNA. Translation: AAA20046.1.
D26485 mRNA. Translation: BAA05495.1.
AK313090 mRNA. Translation: BAG35915.1.
CH471055 Genomic DNA. Translation: EAW64898.1.
BC009586 mRNA. Translation: AAH09586.1.
CCDSCCDS2774.1.
PIRA48043.
RefSeqNP_003356.2. NM_003365.2.
UniGeneHs.119251.

3D structure databases

ProteinModelPortalP31930.
SMRP31930. Positions 35-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113230. 30 interactions.
IntActP31930. 10 interactions.
MINTMINT-3012677.
STRING9606.ENSP00000203407.

Chemistry

DrugBankDB01117. Atovaquone.

Protein family/group databases

MEROPSM16.973.

PTM databases

PhosphoSiteP31930.

Polymorphism databases

DMDM92090651.

2D gel databases

OGPP31930.
REPRODUCTION-2DPAGEIPI00013847.
SWISS-2DPAGEP31930.
UCD-2DPAGEP31930.

Proteomic databases

MaxQBP31930.
PaxDbP31930.
PeptideAtlasP31930.
PRIDEP31930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000203407; ENSP00000203407; ENSG00000010256.
GeneID7384.
KEGGhsa:7384.
UCSCuc003cub.1. human.

Organism-specific databases

CTD7384.
GeneCardsGC03M048636.
HGNCHGNC:12585. UQCRC1.
HPACAB033782.
HPA002815.
HPA003525.
MIM191328. gene.
neXtProtNX_P31930.
PharmGKBPA37216.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0612.
HOGENOMHOG000242450.
HOVERGENHBG006393.
InParanoidP31930.
KOK00414.
OMAFFLQGQW.
OrthoDBEOG74R1QJ.
PhylomeDBP31930.
TreeFamTF105032.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SignaLinkP31930.

Gene expression databases

ArrayExpressP31930.
BgeeP31930.
CleanExHS_UQCRC1.
GenevestigatorP31930.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 2 hits.
ProtoNetSearch...

Other

ChiTaRSUQCRC1. human.
GeneWikiUQCRC1.
GenomeRNAi7384.
NextBio28912.
PROP31930.
SOURCESearch...

Entry information

Entry nameQCR1_HUMAN
AccessionPrimary (citable) accession number: P31930
Secondary accession number(s): B2R7R8, Q96DD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM