Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi133Copper1 Publication1
Metal bindingi137Copper1 Publication1
Metal bindingi224Copper1 Publication1

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

BioCyciZFISH:ENSG00000130489-MONOMER.
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)5 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_070054133C → Y in CEMCOX1. 1 PublicationCorresponds to variant rs28937868dbSNPEnsembl.1
Natural variantiVAR_008874140E → K in CEMCOX1 and MYP6. 5 PublicationsCorresponds to variant rs74315511dbSNPEnsembl.1
Natural variantiVAR_013238171R → W in CEMCOX1; renders the protein unstable. 2 PublicationsCorresponds to variant rs28937598dbSNPEnsembl.1
Natural variantiVAR_076281193G → S in CEMCOX1 and LS. 2 PublicationsCorresponds to variant rs759452074dbSNPEnsembl.1
Natural variantiVAR_008875225S → F in CEMCOX1. 1 PublicationCorresponds to variant rs80358232dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_074010112R → W in MYP6; unknown pathological significance. 1 PublicationCorresponds to variant rs370130010dbSNPEnsembl.1
Natural variantiVAR_070053114R → H in MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%. 2 PublicationsCorresponds to variant rs145100473dbSNPEnsembl.1
Natural variantiVAR_074011120R → W in MYP6; unknown pathological significance. 1 PublicationCorresponds to variant rs375954523dbSNPEnsembl.1
Natural variantiVAR_008874140E → K in CEMCOX1 and MYP6. 5 PublicationsCorresponds to variant rs74315511dbSNPEnsembl.1
Natural variantiVAR_051912259A → V in MYP6. 1 PublicationCorresponds to variant rs8139305dbSNPEnsembl.1
Leigh syndrome (LS)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionAn early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.
See also OMIM:256000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076281193G → S in CEMCOX1 and LS. 2 PublicationsCorresponds to variant rs759452074dbSNPEnsembl.1
Natural variantiVAR_076282258M → T in LS. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Leigh syndrome

Organism-specific databases

DisGeNETi9997.
MalaCardsiSCO2.
MIMi256000. phenotype.
604377. phenotype.
608908. phenotype.
OpenTargetsiENSG00000130489.
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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 41MitochondrionSequence analysisAdd BLAST41
ChainiPRO_000003192242 – 266Protein SCO2 homolog, mitochondrialAdd BLAST225

Proteomic databases

EPDiO43819.
MaxQBiO43819.
PaxDbiO43819.
PeptideAtlasiO43819.
PRIDEiO43819.

PTM databases

iPTMnetiO43819.
PhosphoSitePlusiO43819.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000130489.
CleanExiHS_SCO2.
GenevisibleiO43819. HS.

Organism-specific databases

HPAiHPA056254.

Interactioni

Subunit structurei

Interacts with COA6.1 Publication

Protein-protein interaction databases

BioGridi115317. 43 interactors.
DIPiDIP-46088N.
IntActiO43819. 12 interactors.
MINTiMINT-1161273.
STRINGi9606.ENSP00000252785.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi105 – 108Combined sources4
Beta strandi113 – 115Combined sources3
Turni116 – 121Combined sources6
Beta strandi122 – 129Combined sources8
Beta strandi134 – 136Combined sources3
Helixi137 – 153Combined sources17
Beta strandi160 – 167Combined sources8
Helixi174 – 182Combined sources9
Beta strandi190 – 192Combined sources3
Helixi195 – 204Combined sources10
Beta strandi227 – 231Combined sources5
Beta strandi237 – 244Combined sources8
Helixi247 – 261Combined sources15

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO43819.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 259ThioredoxinPROSITE-ProRule annotationAdd BLAST175

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.
OMAiFTDYYGR.
OrthoDBiEOG091G0DJ5.
PhylomeDBiO43819.
TreeFamiTF313752.

Family and domain databases

CDDicd02968. SCO. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR003782. SCO1/SenC.
IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01173820R → P.2 PublicationsCorresponds to variant rs140523dbSNPEnsembl.1
Natural variantiVAR_074010112R → W in MYP6; unknown pathological significance. 1 PublicationCorresponds to variant rs370130010dbSNPEnsembl.1
Natural variantiVAR_070053114R → H in MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%. 2 PublicationsCorresponds to variant rs145100473dbSNPEnsembl.1
Natural variantiVAR_074011120R → W in MYP6; unknown pathological significance. 1 PublicationCorresponds to variant rs375954523dbSNPEnsembl.1
Natural variantiVAR_070054133C → Y in CEMCOX1. 1 PublicationCorresponds to variant rs28937868dbSNPEnsembl.1
Natural variantiVAR_008874140E → K in CEMCOX1 and MYP6. 5 PublicationsCorresponds to variant rs74315511dbSNPEnsembl.1
Natural variantiVAR_013238171R → W in CEMCOX1; renders the protein unstable. 2 PublicationsCorresponds to variant rs28937598dbSNPEnsembl.1
Natural variantiVAR_076281193G → S in CEMCOX1 and LS. 2 PublicationsCorresponds to variant rs759452074dbSNPEnsembl.1
Natural variantiVAR_008875225S → F in CEMCOX1. 1 PublicationCorresponds to variant rs80358232dbSNPEnsembl.1
Natural variantiVAR_076282258M → T in LS. 1 Publication1
Natural variantiVAR_051912259A → V in MYP6. 1 PublicationCorresponds to variant rs8139305dbSNPEnsembl.1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RLINMR-A100-266[»]
ProteinModelPortaliO43819.
SMRiO43819.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115317. 43 interactors.
DIPiDIP-46088N.
IntActiO43819. 12 interactors.
MINTiMINT-1161273.
STRINGi9606.ENSP00000252785.

PTM databases

iPTMnetiO43819.
PhosphoSitePlusiO43819.

Polymorphism and mutation databases

BioMutaiSCO2.

Proteomic databases

EPDiO43819.
MaxQBiO43819.
PaxDbiO43819.
PeptideAtlasiO43819.
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.
DisGeNETi9997.
GeneCardsiSCO2.
HGNCiHGNC:10604. SCO2.
HPAiHPA056254.
MalaCardsiSCO2.
MIMi256000. phenotype.
604272. gene.
604377. phenotype.
608908. phenotype.
neXtProtiNX_O43819.
OpenTargetsiENSG00000130489.
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.
OMAiFTDYYGR.
OrthoDBiEOG091G0DJ5.
PhylomeDBiO43819.
TreeFamiTF313752.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000130489-MONOMER.
ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-611105. Respiratory electron transport.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000130489.
CleanExiHS_SCO2.
GenevisibleiO43819. HS.

Family and domain databases

CDDicd02968. SCO. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR003782. SCO1/SenC.
IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[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...

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: November 30, 2016
This is version 160 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.