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Protein

Protein SCO2 homolog, mitochondrial

Gene

SCO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Copper1 Publication
Metal bindingi137 – 1371Copper1 Publication
Metal bindingi224 – 2241Copper1 Publication

GO - Molecular functioni

  • copper ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-611105. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SCO2 homolog, mitochondrial
Gene namesi
Name:SCO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:10604. SCO2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: InterPro
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
  • myofibril Source: MGI
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency 1 (CEMCOX1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by hypotonia, developmental delay, hypertrophic cardiomyopathy, lactic acidosis, gliosis, neuronal loss in basal ganglia, brainstem and spinal cord, and cytochrome c oxidase deficiency.
See also OMIM:604377
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331C → Y in CEMCOX1. 1 Publication
VAR_070054
Natural varianti140 – 1401E → K in CEMCOX1 and MYP6. 5 Publications
VAR_008874
Natural varianti171 – 1711R → W in CEMCOX1; renders the protein unstable. 2 Publications
Corresponds to variant rs28937598 [ dbSNP | Ensembl ].
VAR_013238
Natural varianti225 – 2251S → F in CEMCOX1. 1 Publication
VAR_008875
Myopia 6 (MYP6)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.
See also OMIM:608908
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → W in MYP6; unknown pathological significance. 1 Publication
VAR_074010
Natural varianti114 – 1141R → H in MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%. 2 Publications
VAR_070053
Natural varianti120 – 1201R → W in MYP6; unknown pathological significance. 1 Publication
VAR_074011
Natural varianti140 – 1401E → K in CEMCOX1 and MYP6. 5 Publications
VAR_008874
Natural varianti259 – 2591A → V in MYP6. 1 Publication
Corresponds to variant rs8139305 [ dbSNP | Ensembl ].
VAR_051912

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MalaCardsiSCO2.
MIMi604377. phenotype.
608908. phenotype.
Orphaneti1561. Fatal infantile cytochrome C oxidase deficiency.
70474. Leigh syndrome with cardiomyopathy.
98619. Rare isolated myopia.
PharmGKBiPA35013.

Polymorphism and mutation databases

BioMutaiSCO2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence analysisAdd
BLAST
Chaini42 – 266225Protein SCO2 homolog, mitochondrialPRO_0000031922Add
BLAST

Proteomic databases

EPDiO43819.
MaxQBiO43819.
PaxDbiO43819.
PRIDEiO43819.

PTM databases

iPTMnetiO43819.
PhosphoSiteiO43819.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO43819.
CleanExiHS_SCO2.
ExpressionAtlasiO43819. baseline and differential.
GenevisibleiO43819. HS.

Organism-specific databases

HPAiHPA056254.

Interactioni

Subunit structurei

Interacts with COA6.1 Publication

Protein-protein interaction databases

BioGridi115317. 38 interactions.
DIPiDIP-46088N.
IntActiO43819. 9 interactions.
MINTiMINT-1161273.
STRINGi9606.ENSP00000252785.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1084Combined sources
Beta strandi113 – 1153Combined sources
Turni116 – 1216Combined sources
Beta strandi122 – 1298Combined sources
Beta strandi134 – 1363Combined sources
Helixi137 – 15317Combined sources
Beta strandi160 – 1678Combined sources
Helixi174 – 1829Combined sources
Beta strandi190 – 1923Combined sources
Helixi195 – 20410Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi237 – 2448Combined sources
Helixi247 – 26115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RLINMR-A100-266[»]
ProteinModelPortaliO43819.
SMRiO43819. Positions 100-266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43819.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 259175ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SCO1/2 family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2792. Eukaryota.
COG1999. LUCA.
GeneTreeiENSGT00390000004323.
HOGENOMiHOG000258140.
HOVERGENiHBG000428.
InParanoidiO43819.
KOiK07152.
OMAiHSYRVYY.
OrthoDBiEOG7W41C7.
PhylomeDBiO43819.
TreeFamiTF313752.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR003782. SCO1/SenC.
IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR12151. PTHR12151. 1 hit.
PfamiPF02630. SCO1-SenC. 1 hit.
[Graphical view]
PIRSFiPIRSF037736. SCO1. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O43819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLTRSPTA WHRLSQLKPR VLPGTLGGQA LHLRSWLLSR QGPAETGGQG
60 70 80 90 100
QPQGPGLRTR LLITGLFGAG LGGAWLALRA EKERLQQQKR TEALRQAAVG
110 120 130 140 150
QGDFHLLDHR GRARCKADFR GQWVLMYFGF THCPDICPDE LEKLVQVVRQ
160 170 180 190 200
LEAEPGLPPV QPVFITVDPE RDDVEAMARY VQDFHPRLLG LTGSTKQVAQ
210 220 230 240 250
ASHSYRVYYN AGPKDEDQDY IVDHSIAIYL LNPDGLFTDY YGRSRSAEQI
260
SDSVRRHMAA FRSVLS
Length:266
Mass (Da):29,810
Last modified:May 30, 2000 - v3
Checksum:iBC2F40E057329BF3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → P.1 Publication
Corresponds to variant rs140523 [ dbSNP | Ensembl ].
VAR_011738
Natural varianti112 – 1121R → W in MYP6; unknown pathological significance. 1 Publication
VAR_074010
Natural varianti114 – 1141R → H in MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%. 2 Publications
VAR_070053
Natural varianti120 – 1201R → W in MYP6; unknown pathological significance. 1 Publication
VAR_074011
Natural varianti133 – 1331C → Y in CEMCOX1. 1 Publication
VAR_070054
Natural varianti140 – 1401E → K in CEMCOX1 and MYP6. 5 Publications
VAR_008874
Natural varianti171 – 1711R → W in CEMCOX1; renders the protein unstable. 2 Publications
Corresponds to variant rs28937598 [ dbSNP | Ensembl ].
VAR_013238
Natural varianti225 – 2251S → F in CEMCOX1. 1 Publication
VAR_008875
Natural varianti259 – 2591A → V in MYP6. 1 Publication
Corresponds to variant rs8139305 [ dbSNP | Ensembl ].
VAR_051912

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177385 Genomic DNA. Translation: AAF05313.1.
AL021683 mRNA. Translation: CAA16671.1.
CR456569 mRNA. Translation: CAG30455.1.
BC102024 mRNA. Translation: AAI02025.1.
BC102025 mRNA. Translation: AAI02026.1.
CCDSiCCDS14095.1.
RefSeqiNP_001162580.1. NM_001169109.1.
NP_001162581.1. NM_001169110.1.
NP_001162582.1. NM_001169111.1.
NP_005129.2. NM_005138.2.
UniGeneiHs.180903.
Hs.730607.

Genome annotation databases

EnsembliENST00000252785; ENSP00000252785; ENSG00000130489.
ENST00000395693; ENSP00000379046; ENSG00000130489.
ENST00000535425; ENSP00000444242; ENSG00000130489.
ENST00000543927; ENSP00000444433; ENSG00000130489.
GeneIDi9997.
KEGGihsa:9997.
UCSCiuc003blz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177385 Genomic DNA. Translation: AAF05313.1.
AL021683 mRNA. Translation: CAA16671.1.
CR456569 mRNA. Translation: CAG30455.1.
BC102024 mRNA. Translation: AAI02025.1.
BC102025 mRNA. Translation: AAI02026.1.
CCDSiCCDS14095.1.
RefSeqiNP_001162580.1. NM_001169109.1.
NP_001162581.1. NM_001169110.1.
NP_001162582.1. NM_001169111.1.
NP_005129.2. NM_005138.2.
UniGeneiHs.180903.
Hs.730607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RLINMR-A100-266[»]
ProteinModelPortaliO43819.
SMRiO43819. Positions 100-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115317. 38 interactions.
DIPiDIP-46088N.
IntActiO43819. 9 interactions.
MINTiMINT-1161273.
STRINGi9606.ENSP00000252785.

PTM databases

iPTMnetiO43819.
PhosphoSiteiO43819.

Polymorphism and mutation databases

BioMutaiSCO2.

Proteomic databases

EPDiO43819.
MaxQBiO43819.
PaxDbiO43819.
PRIDEiO43819.

Protocols and materials databases

DNASUi9997.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252785; ENSP00000252785; ENSG00000130489.
ENST00000395693; ENSP00000379046; ENSG00000130489.
ENST00000535425; ENSP00000444242; ENSG00000130489.
ENST00000543927; ENSP00000444433; ENSG00000130489.
GeneIDi9997.
KEGGihsa:9997.
UCSCiuc003blz.5. human.

Organism-specific databases

CTDi9997.
GeneCardsiSCO2.
HGNCiHGNC:10604. SCO2.
HPAiHPA056254.
MalaCardsiSCO2.
MIMi604272. gene.
604377. phenotype.
608908. phenotype.
neXtProtiNX_O43819.
Orphaneti1561. Fatal infantile cytochrome C oxidase deficiency.
70474. Leigh syndrome with cardiomyopathy.
98619. Rare isolated myopia.
PharmGKBiPA35013.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2792. Eukaryota.
COG1999. LUCA.
GeneTreeiENSGT00390000004323.
HOGENOMiHOG000258140.
HOVERGENiHBG000428.
InParanoidiO43819.
KOiK07152.
OMAiHSYRVYY.
OrthoDBiEOG7W41C7.
PhylomeDBiO43819.
TreeFamiTF313752.

Enzyme and pathway databases

ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-611105. Respiratory electron transport.

Miscellaneous databases

EvolutionaryTraceiO43819.
GeneWikiiSCO2.
GenomeRNAii9997.
PROiO43819.
SOURCEiSearch...

Gene expression databases

BgeeiO43819.
CleanExiHS_SCO2.
ExpressionAtlasiO43819. baseline and differential.
GenevisibleiO43819. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR003782. SCO1/SenC.
IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR12151. PTHR12151. 1 hit.
PfamiPF02630. SCO1-SenC. 1 hit.
[Graphical view]
PIRSFiPIRSF037736. SCO1. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CEMCOX1 LYS-140 AND PHE-225.
  2. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Monocyte.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-20.
  4. "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].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c oxidase assembly links two mitochondrial cardiomyopathies."
    Pacheu-Grau D., Bareth B., Dudek J., Juris L., Voegtle F.N., Wissel M., Leary S.C., Dennerlein S., Rehling P., Deckers M.
    Cell Metab. 21:823-833(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COA6, CHARACTERIZATION OF VARIANT MYP6 HIS-114, CHARACTERIZATION OF VARIANT CEMCOX1 TRP-171.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: STRUCTURE BY NMR OF 100-266 ALONE AND IN COMPLEX WITH COPPER, COPPER-BINDING SITES.
  9. "Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency."
    Jaksch M., Ogilvie I., Yao J., Kortenhaus G., Bresser H.G., Gerbitz K.D., Shoubridge E.A.
    Hum. Mol. Genet. 9:795-801(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CEMCOX1 LYS-140 AND TRP-171.
  10. Cited for: VARIANT CEMCOX1 LYS-140.
  11. "Novel SCO2 mutation (G1521A) presenting as a spinal muscular atrophy type I phenotype."
    Tarnopolsky M.A., Bourgeois J.M., Fu M.H., Kataeva G., Shah J., Simon D.K., Mahoney D., Johns D., MacKay N., Robinson B.H.
    Am. J. Med. Genet. A 125A:310-314(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CEMCOX1 TYR-133 AND LYS-140.
  12. Cited for: VARIANTS MYP6 HIS-114; LYS-140 AND VAL-259.
  13. "Detection of mutations in LRPAP1, CTSH, LEPREL1, ZNF644, SLC39A5, and SCO2 in 298 families with early-onset high myopia by exome sequencing."
    Jiang D., Li J., Xiao X., Li S., Jia X., Sun W., Guo X., Zhang Q.
    Invest. Ophthalmol. Vis. Sci. 56:339-345(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MYP6 TRP-112 AND TRP-120.

Entry informationi

Entry nameiSCO2_HUMAN
AccessioniPrimary (citable) accession number: O43819
Secondary accession number(s): Q3T1B5, Q9UK87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 8, 2016
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.