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O75880

- SCO1_HUMAN

UniProt

O75880 - SCO1_HUMAN

Protein

Protein SCO1 homolog, mitochondrial

Gene

SCO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Copper, Metal-binding

    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: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:10603. SCO1.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti174 – 1741P → L in MT-C4D. 1 Publication
    VAR_012109

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    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

    ArrayExpressiO75880.
    BgeeiO75880.
    CleanExiHS_SCO1.
    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 – 1444
    Beta strandi149 – 1513
    Helixi152 – 1554
    Beta strandi159 – 1657
    Helixi172 – 18918
    Beta strandi190 – 1934
    Beta strandi196 – 2038
    Turni205 – 2073
    Helixi210 – 2189
    Beta strandi225 – 2284
    Helixi231 – 2399
    Turni240 – 2423
    Beta strandi245 – 2506
    Helixi252 – 2543
    Beta strandi256 – 2605
    Beta strandi263 – 2675
    Helixi269 – 2713
    Beta strandi273 – 2786
    Helixi283 – 29412
    Helixi295 – 2973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000258140.
    HOVERGENiHBG000428.
    InParanoidiO75880.
    KOiK07152.
    OMAiNDFVECI.
    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

    MAMLVLVPGR VMRPLGGQLW RFLPRGLEFW GPAEGTARVL LRQFCARQAE    50
    AWRASGRPGY CLGTRPLSTA RPPPPWSQKG PGDSTRPSKP GPVSWKSLAI 100
    TFAIGGALLA GMKHVKKEKA EKLEKERQRH IGKPLLGGPF SLTTHTGERK 150
    TDKDYLGQWL LIYFGFTHCP DVCPEELEKM IQVVDEIDSI TTLPDLTPLF 200
    ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA YRVYYSPGPK 250
    DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI ATHMRPYRKK 300
    S 301
    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. 1 Publication
    VAR_012109

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11158.1.
    RefSeqi NP_004580.1. NM_004589.3.
    XP_005256808.1. XM_005256751.2.
    UniGenei Hs.14511.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WP0 X-ray 2.80 A/B/C 138-301 [» ]
    2GGT X-ray 2.40 A/B 135-298 [» ]
    2GQK NMR - A 132-301 [» ]
    2GQL NMR - A 132-301 [» ]
    2GQM NMR - A 132-301 [» ]
    2GT5 NMR - A 132-301 [» ]
    2GT6 NMR - A 132-301 [» ]
    2GVP NMR - A 132-301 [» ]
    2HRF NMR - A 132-301 [» ]
    2HRN NMR - A 132-301 [» ]
    ProteinModelPortali O75880.
    SMRi O75880. Positions 135-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112245. 1 interaction.
    DIPi DIP-46086N.
    IntActi O75880. 1 interaction.
    STRINGi 9606.ENSP00000255390.

    PTM databases

    PhosphoSitei O75880.

    Proteomic databases

    MaxQBi O75880.
    PaxDbi O75880.
    PRIDEi O75880.

    Protocols and materials databases

    DNASUi 6341.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255390 ; ENSP00000255390 ; ENSG00000133028 .
    GeneIDi 6341.
    KEGGi hsa:6341.
    UCSCi uc002gmr.4. human.

    Organism-specific databases

    CTDi 6341.
    GeneCardsi GC17M010583.
    HGNCi HGNC:10603. SCO1.
    HPAi HPA021565.
    HPA021579.
    MIMi 220110. phenotype.
    603644. gene.
    neXtProti NX_O75880.
    Orphaneti 1561. Fatal infantile cytochrome C oxidase deficiency.
    PharmGKBi PA35012.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1999.
    HOGENOMi HOG000258140.
    HOVERGENi HBG000428.
    InParanoidi O75880.
    KOi K07152.
    OMAi NDFVECI.
    OrthoDBi EOG7W41C7.
    PhylomeDBi O75880.
    TreeFami TF313752.

    Miscellaneous databases

    EvolutionaryTracei O75880.
    GeneWikii SCO1.
    GenomeRNAii 6341.
    NextBioi 24624.
    PROi O75880.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75880.
    Bgeei O75880.
    CleanExi HS_SCO1.
    Genevestigatori O75880.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR003782. SCO1/SenC.
    IPR017276. Synth_of_cyt-c-oxidase_Sco1/2.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    PANTHERi PTHR12151. PTHR12151. 1 hit.
    Pfami PF02630. SCO1-SenC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037736. SCO1. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 134 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