Hmdb loader
Identification
HMDB Protein ID HMDBP00987
Secondary Accession Numbers
  • 6275
Name Cytochrome b-c1 complex subunit 1, mitochondrial
Synonyms
  1. Complex III subunit 1
  2. Core protein I
  3. Ubiquinol-cytochrome-c reductase complex core protein 1
Gene Name UQCRC1
Protein Type Unknown
Biological Properties
General Function Involved in catalytic activity
Specific 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
Pathways
  • Oxidative phosphorylation
Reactions Not Available
GO Classification
Function
endopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
metalloendopeptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:3
Locus 3p21.3
SNPs UQCRC1
Gene Sequence
>1443 bp
ATGGCGGCGTCCGTGGTCTGTCGGGCCGCTACCGCCGGGGCACAAGTGCTATTGCGCGCC
CGCCGCTCGCCGGCCCTGCTGCGGACGCCAGCCTTGCGGAGTACGGCAACCTTCGCTCAG
GCGCTCCAGTTCGTGCCGGAGACGCAGGTTAGCCTGCTGGACAACGGCCTGCGTGTGGCC
TCCGAGCAGTCCTCTCAGCCCACTTGCACGGTGGGAGTGTGGATTGATGTTGGCAGCCGT
TTTGAGACTGAGAAGAATAATGGGGCAGGCTACTTTTTGGAGCATCTGGCTTTCAAGGGA
ACAAAGAATCGGCCTGGCAGTGCCCTGGAGAAGGAGGTGGAGAGCATGGGGGCCCATCTT
AATGCCTACAGCACCCGGGAGCACACAGCTTACTACATCAAGGCGCTGTCCAAGGATCTG
CCGAAAGCTGTGGAGCTCCTGGGTGACATTGTGCAGAACTGTAGTCTGGAAGACTCACAG
ATTGAGAAGGAACGTGATGTGATCCTGCGGGAGATGCAGGAGAATGATGCATCTATGCGA
GATGTGGTCTTTAACTACCTGCATGCCACAGCATTCCAGGGCACACCTCTAGCCCAGGCT
GTGGAGGGGCCCAGTGAGAATGTCAGGAAGCTGTCTCGTGCAGACTTGACCGAGTACCTC
AGCACACATTACAAGGCCCCTCGAATGGTGCTGGCAGCAGCTGGAGGAGTGGAGCACCAG
CAACTGTTAGACCTCGCCCAGAAGCACCTCGGTGGCATCCCATGGACATATGCAGAGGAC
GCTGTGCCCACTCTTACTCCATGCCGCTTCACTGGCAGTGAGATCCGCCACCGTGATGAT
GCTCTACCTTTTGCCCACGTGGCCATTGCAGTAGAGGGTCCTGGCTGGGCCAGCCCGGAC
AATGTGGCCTTGCAAGTGGCCAATGCCATCATCGGCCACTATGACTGCACTTATGGTGGT
GGCGTGCACCTGTCCAGCCCACTGGCTTCAGGTGCTGTGGCCAACAAGCTATGCCAGAGT
TTCCAGACCTTCAGCATCTGCTATGCAGAGACGGGCTTGCTGGGTGCACACTTTGTCTGT
GACCGAATGAAAATCGATGACATGATGTTCGTCCTGCAAGGGCAGTGGATGCGCCTGTGT
ACCAGTGCCACGGAGAGTGAGGTGGCCCGGGGCAAAAACATCCTCAGAAATGCCCTGGTA
TCTCATCTAGATGGCACTACTCCTGTGTGTGAGGACATCGGACGCAGCCTCCTGACCTAT
GGCCGCCGCATCCCCCTGGCTGAATGGGAAAGCCGGATTGCGGAGGTGGATGCCAGTGTG
GTACGTGAGATCTGCTCCAAGTACATCTATGACCAGTGCCCAGCAGTGGCTGGATATGGC
CCCATTGAGCAGCTCCCAGACTACAACCGGATCCGTAGCGGCATGTTCTGGCTGCGCTTC
TAG
Protein Properties
Number of Residues 480
Molecular Weight 52645.3
Theoretical pI 6.32
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Cytochrome b-c1 complex subunit 1, mitochondrial
MAASVVCRAATAGAQVLLRARRSPALLRTPALRSTATFAQALQFVPETQVSLLDNGLRVA
SEQSSQPTCTVGVWIDVGSRFETEKNNGAGYFLEHLAFKGTKNRPGSALEKEVESMGAHL
NAYSTREHTAYYIKALSKDLPKAVELLGDIVQNCSLEDSQIEKERDVILREMQENDASMR
DVVFNYLHATAFQGTPLAQAVEGPSENVRKLSRADLTEYLSTHYKAPRMVLAAAGGVEHQ
QLLDLAQKHLGGIPWTYAEDAVPTLTPCRFTGSEIRHRDDALPFAHVAIAVEGPGWASPD
NVALQVANAIIGHYDCTYGGGVHLSSPLASGAVANKLCQSFQTFSICYAETGLLGAHFVC
DRMKIDDMMFVLQGQWMRLCTSATESEVARGKNILRNALVSHLDGTTPVCEDIGRSLLTY
GRRIPLAEWESRIAEVDASVVREICSKYIYDQCPAVAGYGPIEQLPDYNRIRSGMFWLRF
GenBank ID Protein 189053663
UniProtKB/Swiss-Prot ID P31930
UniProtKB/Swiss-Prot Entry Name QCR1_HUMAN
PDB IDs Not Available
GenBank Gene ID AK313090
GeneCard ID UQCRC1
GenAtlas ID UQCRC1
HGNC ID HGNC:12585
References
General References
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  3. Hughes GJ, Frutiger S, Paquet N, Pasquali C, Sanchez JC, Tissot JD, Bairoch A, Appel RD, Hochstrasser DF: Human liver protein map: update 1993. Electrophoresis. 1993 Nov;14(11):1216-22. [PubMed:8313870 ]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  6. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed:15242332 ]
  7. Hoffman GG, Lee S, Christiano AM, Chung-Honet LC, Cheng W, Katchman S, Uitto J, Greenspan DS: Complete coding sequence, intron/exon organization, and chromosomal location of the gene for the core I protein of human ubiquinol-cytochrome c reductase. J Biol Chem. 1993 Oct 5;268(28):21113-9. [PubMed:8407948 ]
  8. Islam MM, Tanaka M, Suzuki H, Torii K, Hattori N, Ozawa T: A complete cDNA sequence for core I protein subunit of human ubiquinol-cytochrome c reductase. Biochem Mol Biol Int. 1994 Apr;32(5):797-805. [PubMed:8069229 ]
  9. Islam MM, Tanaka M, Suzuki H, Torii K, Hattori N, Ozawa T: A complete cDNA sequence for core I protein subunit of human ubiquinol-cytochrome c reductase. Biochem Mol Biol Int. 1994 May;33(2):410. [PubMed:7951059 ]
  10. Islam MM, Tanaka M, Suzuki H, Torii K, Hattori N, Ozawa T: A complete cDNA sequence for core I protein subunit of human ubiquinol-cytochrome c reductase. Biochem Mol Biol Int. 1994 Jul;33(4):815. [PubMed:7981668 ]
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