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Protein

Protein SCO1 homolog, mitochondrial

Gene

SCO1

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

Functioni

Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi169 – 1691Copper
Metal bindingi173 – 1731Copper
Metal bindingi260 – 2601Copper

GO - Molecular functioni

  1. copper ion binding Source: InterPro

GO - Biological processi

  1. cellular copper ion homeostasis Source: InterPro
  2. copper ion transport Source: InterPro
  3. generation of precursor metabolites and energy Source: ProtInc
  4. respiratory chain complex IV assembly Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.
REACT_268444. Orphan transporters.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SCO1 homolog, mitochondrial
Gene namesi
Name:SCO1
Synonyms:SCOD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10603. SCO1.

Subcellular locationi

  1. Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: InterPro
  2. mitochondrion Source: ProtInc
  3. myofibril Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Mitochondrial complex IV deficiency (MT-C4D)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome.

See also OMIM:220110
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741P → L in MT-C4D. 2 Publications
VAR_012109

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi220110. phenotype.
Orphaneti1561. Fatal infantile cytochrome C oxidase deficiency.
PharmGKBiPA35012.

Polymorphism and mutation databases

BioMutaiSCO1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 301Protein SCO1 homolog, mitochondrialPRO_0000031921
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiO75880.
PaxDbiO75880.
PRIDEiO75880.

PTM databases

PhosphoSiteiO75880.

Expressioni

Tissue specificityi

Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain.1 Publication

Gene expression databases

BgeeiO75880.
CleanExiHS_SCO1.
ExpressionAtlasiO75880. baseline and differential.
GenevestigatoriO75880.

Organism-specific databases

HPAiHPA021565.
HPA021579.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi112245. 1 interaction.
DIPiDIP-46086N.
IntActiO75880. 1 interaction.
STRINGi9606.ENSP00000255390.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi141 – 1444Combined sources
Beta strandi149 – 1513Combined sources
Helixi152 – 1554Combined sources
Beta strandi159 – 1657Combined sources
Helixi172 – 18918Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi196 – 2038Combined sources
Turni205 – 2073Combined sources
Helixi210 – 2189Combined sources
Beta strandi225 – 2284Combined sources
Helixi231 – 2399Combined sources
Turni240 – 2423Combined sources
Beta strandi245 – 2506Combined sources
Helixi252 – 2543Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi263 – 2675Combined sources
Helixi269 – 2713Combined sources
Beta strandi273 – 2786Combined sources
Helixi283 – 29412Combined sources
Helixi295 – 2973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WP0X-ray2.80A/B/C138-301[»]
2GGTX-ray2.40A/B135-298[»]
2GQKNMR-A132-301[»]
2GQLNMR-A132-301[»]
2GQMNMR-A132-301[»]
2GT5NMR-A132-301[»]
2GT6NMR-A132-301[»]
2GVPNMR-A132-301[»]
2HRFNMR-A132-301[»]
2HRNNMR-A132-301[»]
ProteinModelPortaliO75880.
SMRiO75880. Positions 135-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75880.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 13114Important for dimerizationAdd
BLAST

Sequence similaritiesi

Belongs to the SCO1/2 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1999.
GeneTreeiENSGT00390000004323.
HOGENOMiHOG000258140.
HOVERGENiHBG000428.
InParanoidiO75880.
KOiK07152.
OMAiKERQRHI.
OrthoDBiEOG7W41C7.
PhylomeDBiO75880.
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.

Sequencei

Sequence statusi: Complete.

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

O75880-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMLVLVPGR VMRPLGGQLW RFLPRGLEFW GPAEGTARVL LRQFCARQAE
60 70 80 90 100
AWRASGRPGY CLGTRPLSTA RPPPPWSQKG PGDSTRPSKP GPVSWKSLAI
110 120 130 140 150
TFAIGGALLA GMKHVKKEKA EKLEKERQRH IGKPLLGGPF SLTTHTGERK
160 170 180 190 200
TDKDYLGQWL LIYFGFTHCP DVCPEELEKM IQVVDEIDSI TTLPDLTPLF
210 220 230 240 250
ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA YRVYYSPGPK
260 270 280 290 300
DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI ATHMRPYRKK

S
Length:301
Mass (Da):33,814
Last modified:November 1, 1998 - v1
Checksum:iC4A0F35A1741894F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581P → S.
Corresponds to variant rs1802083 [ dbSNP | Ensembl ].
VAR_014537
Natural varianti174 – 1741P → L in MT-C4D. 2 Publications
VAR_012109

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026852 mRNA. Translation: AAD08641.1.
AF295386
, AF295381, AF295382, AF295383, AF295384, AF295385 Genomic DNA. Translation: AAG23836.1.
AF183424 mRNA. Translation: AAG09693.1.
AK315595 mRNA. Translation: BAG37967.1.
CH471108 Genomic DNA. Translation: EAW89997.1.
BC015504 mRNA. Translation: AAH15504.1.
AF131816 mRNA. Translation: AAD20051.1.
CCDSiCCDS11158.1.
RefSeqiNP_004580.1. NM_004589.3.
XP_005256808.1. XM_005256751.2.
UniGeneiHs.14511.

Genome annotation databases

EnsembliENST00000255390; ENSP00000255390; ENSG00000133028.
GeneIDi6341.
KEGGihsa:6341.
UCSCiuc002gmr.4. human.

Polymorphism and mutation databases

BioMutaiSCO1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026852 mRNA. Translation: AAD08641.1.
AF295386
, AF295381, AF295382, AF295383, AF295384, AF295385 Genomic DNA. Translation: AAG23836.1.
AF183424 mRNA. Translation: AAG09693.1.
AK315595 mRNA. Translation: BAG37967.1.
CH471108 Genomic DNA. Translation: EAW89997.1.
BC015504 mRNA. Translation: AAH15504.1.
AF131816 mRNA. Translation: AAD20051.1.
CCDSiCCDS11158.1.
RefSeqiNP_004580.1. NM_004589.3.
XP_005256808.1. XM_005256751.2.
UniGeneiHs.14511.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WP0X-ray2.80A/B/C138-301[»]
2GGTX-ray2.40A/B135-298[»]
2GQKNMR-A132-301[»]
2GQLNMR-A132-301[»]
2GQMNMR-A132-301[»]
2GT5NMR-A132-301[»]
2GT6NMR-A132-301[»]
2GVPNMR-A132-301[»]
2HRFNMR-A132-301[»]
2HRNNMR-A132-301[»]
ProteinModelPortaliO75880.
SMRiO75880. Positions 135-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112245. 1 interaction.
DIPiDIP-46086N.
IntActiO75880. 1 interaction.
STRINGi9606.ENSP00000255390.

PTM databases

PhosphoSiteiO75880.

Polymorphism and mutation databases

BioMutaiSCO1.

Proteomic databases

MaxQBiO75880.
PaxDbiO75880.
PRIDEiO75880.

Protocols and materials databases

DNASUi6341.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255390; ENSP00000255390; ENSG00000133028.
GeneIDi6341.
KEGGihsa:6341.
UCSCiuc002gmr.4. human.

Organism-specific databases

CTDi6341.
GeneCardsiGC17M010583.
HGNCiHGNC:10603. SCO1.
HPAiHPA021565.
HPA021579.
MIMi220110. phenotype.
603644. gene.
neXtProtiNX_O75880.
Orphaneti1561. Fatal infantile cytochrome C oxidase deficiency.
PharmGKBiPA35012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1999.
GeneTreeiENSGT00390000004323.
HOGENOMiHOG000258140.
HOVERGENiHBG000428.
InParanoidiO75880.
KOiK07152.
OMAiKERQRHI.
OrthoDBiEOG7W41C7.
PhylomeDBiO75880.
TreeFamiTF313752.

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.
REACT_268444. Orphan transporters.

Miscellaneous databases

ChiTaRSiSCO1. human.
EvolutionaryTraceiO75880.
GeneWikiiSCO1.
GenomeRNAii6341.
NextBioi24624.
PROiO75880.
SOURCEiSearch...

Gene expression databases

BgeeiO75880.
CleanExiHS_SCO1.
ExpressionAtlasiO75880. baseline and differential.
GenevestigatoriO75880.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain."
    Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R., Zeviani M.
    Genomics 54:494-504(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency."
    Horvath R., Lochmuller H., Stucka R., Yao J., Shoubridge E.A., Kim S.-H., Gerbitz K.-D., Jaksch M.
    Biochem. Biophys. Res. Commun. 276:530-533(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A novel gene expressed in human adrenal gland."
    Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adrenal gland.
  4. "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.
    , 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: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Uterus.
  7. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-301.
    Tissue: Brain.
  8. "The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis."
    Leary S.C., Cobine P.A., Kaufman B.A., Guercin G.H., Mattman A., Palaty J., Lockitch G., Winge D.R., Rustin P., Horvath R., Shoubridge E.A.
    Cell Metab. 5:9-20(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT MT-C4D LEU-174.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase 'assembly' protein."
    Williams J.C., Sue C., Banting G.S., Yang H., Glerum D.M., Hendrickson W.A., Schon E.A.
    J. Biol. Chem. 280:15202-15211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 138-301, FUNCTION.
  11. Cited for: STRUCTURE BY NMR OF 132-301 IN COMPLEX WITH METAL IONS, FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  12. Cited for: REVIEW ON MT-C4D.
  13. "Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy."
    Valnot I., Osmond S., Gigarel N., Mehaye B., Amiel J., Cormier-Daire V., Munnich A., Bonnefont J.-P., Rustin P., Rotig A.
    Am. J. Hum. Genet. 67:1104-1109(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MT-C4D LEU-174.

Entry informationi

Entry nameiSCO1_HUMAN
AccessioniPrimary (citable) accession number: O75880
Secondary accession number(s): B2RDM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 29, 2015
This is version 140 of the entry and version 1 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 17
    Human chromosome 17: 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

External Data

Dasty 3

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 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.