Hmdb loader
Identification
HMDB Protein ID HMDBP08257
Secondary Accession Numbers
  • 13969
Name Protein SCO2 homolog, mitochondrial
Synonyms Not Available
Gene Name SCO2
Protein Type Unknown
Biological Properties
General Function Involved in copper ion binding
Specific Function Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2)
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
organelle membrane
organelle inner membrane
mitochondrial inner membrane
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
copper ion binding
Process
copper ion transport
establishment of localization
cellular process
transport
cellular component organization or biogenesis
biological regulation
cellular component organization
cellular component assembly
macromolecular complex assembly
cellular protein complex assembly
respiratory chain complex iv assembly
cellular copper ion homeostasis
protein complex assembly
cellular homeostasis
cell redox homeostasis
ion transport
cation transport
metal ion transport
transition metal ion transport
regulation of biological quality
homeostatic process
chemical homeostasis
ion homeostasis
cellular ion homeostasis
cellular cation homeostasis
cellular di-, tri-valent inorganic cation homeostasis
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location Chromosome:2
Locus 22q13.33
SNPs SCO2
Gene Sequence
>801 bp
ATGCTGCTGCTGACTCGGAGCCCCACAGCTTGGCACAGGCTCTCTCAGCTCAAGCCTCGG
GTCCTCCCTGGGACCCTGGGAGGCCAGGCCCTGCATCTGAGGTCCTGGCTTTTGTCAAGG
CAGGGCCCTGCAGAGACAGGTGGGCAGGGCCAGCCCCAGGGCCCTGGGCTTCGAACCCGG
CTGCTGATCACAGGCCTGTTCGGGGCTGGACTCGGTGGGGCCTGGCTGGCCCTGAGGGCT
GAGAAGGAGAGGCTGCAGCAGCAAAAGCGAACAGAAGCCCTGCGCCAGGCAGCTGTGGGC
CAGGGCGACTTCCACCTGCTGGATCACAGAGGCCGGGCTCGCTGCAAGGCTGACTTCCGG
GGCCAGTGGGTGCTGATGTACTTTGGCTTCACTCACTGCCCTGACATCTGCCCAGACGAG
CTGGAGAAGCTGGTGCAGGTGGTGCGGCAGCTGGAAGCAGAGCCTGGTTTGCCTCCAGTG
CAGCCTGTCTTCATCACTGTGGACCCCGAGCGGGACGACGTTGAAGCCATGGCCCGCTAC
GTCCAGGACTTCCACCCAAGACTGTTGGGTCTGACCGGCTCCACCAAACAGGTTGCCCAG
GCTAGTCACAGTTACCGCGTGTACTACAATGCAGGCCCCAAGGATGAGGACCAGGACTAC
ATCGTGGACCACTCCATTGCCATCTACCTGCTCAACCCTGACGGCCTCTTCACGGATTAC
TACGGCCGGAGCAGATCGGCTGAGCAGATCTCAGACAGTGTGCGGCGGCACATGGCGGCT
TTCCGCAGTGTCCTGTCTTGA
Protein Properties
Number of Residues 266
Molecular Weight 29809.7
Theoretical pI 9.07
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Protein SCO2 homolog, mitochondrial
MLLLTRSPTAWHRLSQLKPRVLPGTLGGQALHLRSWLLSRQGPAETGGQGQPQGPGLRTR
LLITGLFGAGLGGAWLALRAEKERLQQQKRTEALRQAAVGQGDFHLLDHRGRARCKADFR
GQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGLPPVQPVFITVDPERDDVEAMARY
VQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDEDQDYIVDHSIAIYLLNPDGLFTDY
YGRSRSAEQISDSVRRHMAAFRSVLS
GenBank ID Protein 6175867
UniProtKB/Swiss-Prot ID O43819
UniProtKB/Swiss-Prot Entry Name SCO2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF177385
GeneCard ID SCO2
GenAtlas ID SCO2
HGNC ID HGNC:10604
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed:15461802 ]
  3. Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [PubMed:12529303 ]
  4. Papadopoulou LC, Sue CM, Davidson MM, Tanji K, Nishino I, Sadlock JE, Krishna S, Walker W, Selby J, Glerum DM, Coster RV, Lyon G, Scalais E, Lebel R, Kaplan P, Shanske S, De Vivo DC, Bonilla E, Hirano M, DiMauro S, Schon EA: Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene. Nat Genet. 1999 Nov;23(3):333-7. [PubMed:10545952 ]
  5. Banci L, Bertini I, Ciofi-Baffoni S, Gerothanassis IP, Leontari I, Martinelli M, Wang S: A structural characterization of human SCO2. Structure. 2007 Sep;15(9):1132-40. [PubMed:17850752 ]
  6. Jaksch M, Ogilvie I, Yao J, Kortenhaus G, Bresser HG, Gerbitz KD, Shoubridge EA: Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency. Hum Mol Genet. 2000 Mar 22;9(5):795-801. [PubMed:10749987 ]
  7. Jaksch M, Horvath R, Horn N, Auer DP, Macmillan C, Peters J, Gerbitz KD, Kraegeloh-Mann I, Muntau A, Karcagi V, Kalmanchey R, Lochmuller H, Shoubridge EA, Freisinger P: Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy. Neurology. 2001 Oct 23;57(8):1440-6. [PubMed:11673586 ]