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Q9BYC2

- SCOT2_HUMAN

UniProt

Q9BYC2 - SCOT2_HUMAN

Protein

Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial

Gene

OXCT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate By similarity.By similarity

    Catalytic activityi

    Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei341 – 34115-glutamyl coenzyme A thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-oxoacid CoA-transferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. ketone body catabolic process Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00929; UER00894.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial (EC:2.8.3.5)
    Alternative name(s):
    3-oxoacid CoA-transferase 2A
    Testis-specific succinyl-CoA:3-oxoacid CoA-transferase
    Short name:
    SCOT-t
    Gene namesi
    Name:OXCT2
    ORF Names:FKSG25
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18606. OXCT2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. motile cilium Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38360.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionBy similarityAdd
    BLAST
    Chaini40 – 517478Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrialPRO_0000002416Add
    BLAST

    Proteomic databases

    PaxDbiQ9BYC2.
    PRIDEiQ9BYC2.

    PTM databases

    PhosphoSiteiQ9BYC2.

    Expressioni

    Tissue specificityi

    Testis specific.1 Publication

    Gene expression databases

    BgeeiQ9BYC2.
    CleanExiHS_OXCT2.
    GenevestigatoriQ9BYC2.

    Organism-specific databases

    HPAiHPA053950.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi122037. 1 interaction.
    STRINGi9606.ENSP00000361914.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BYC2.
    SMRiQ9BYC2. Positions 41-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-oxoacid CoA-transferase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1788.
    HOGENOMiHOG000221244.
    HOVERGENiHBG002310.
    InParanoidiQ9BYC2.
    KOiK01027.
    OMAiNISFEHE.
    OrthoDBiEOG7XH6PR.
    PhylomeDBiQ9BYC2.
    TreeFamiTF313991.

    Family and domain databases

    InterProiIPR012792. 3-oxoacid_CoA-transf_A.
    IPR012791. 3-oxoacid_CoA-transf_B.
    IPR014388. 3-oxoacid_CoA-transferase.
    IPR004165. CoA_trans_fam_I.
    IPR004164. CoA_transf_AS.
    IPR004163. CoA_transf_BS.
    [Graphical view]
    PANTHERiPTHR13707. PTHR13707. 1 hit.
    PfamiPF01144. CoA_trans. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000858. SCOT-t. 1 hit.
    SMARTiSM00882. CoA_trans. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
    TIGR02428. pcaJ_scoB_fam. 1 hit.
    PROSITEiPS01273. COA_TRANSF_1. 1 hit.
    PS01274. COA_TRANSF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BYC2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALRLLASV LGRGVPAGGS GLALSQGCAR CFATSPRLRA KFYADPVEMV    50
    KDISDGATVM IGGFGLCGIP ENLIAALLRT RVKDLQVVSS NVGVEDFGLG 100
    LLLAARQVRR IVCSYVGENT LCESQYLAGE LELELTPQGT LAERIRAGGA 150
    GVPAFYTPTG YGTLVQEGGA PIRYTPDGHL ALMSQPREVR EFNGDHFLLE 200
    RAIRADFALV KGWKADRAGN VVFRRSARNF NVPMCKAADV TAVEVEEIVE 250
    VGAFPPEDIH VPNIYVDRVI KGQKYEKRIE RLTILKEEDG DAGKEEDART 300
    RIIRRAALEF EDGMYANLGI GIPLLASNFI SPSMTVHLHS ENGILGLGPF 350
    PTEDEVDADL INAGKQTVTV LPGGCFFASD DSFAMIRGGH IQLTMLGAMQ 400
    VSKYGDLANW MIPGKKVKGM GGAMDLVSSQ KTRVVVTMQH CTKDNTPKIM 450
    EKCTMPLTGK RCVDRIITEK AVFDVHRKKE LTLRELWEGL TVDDIKKSTG 500
    CAFAVSPNLR PMQQVAP 517
    Length:517
    Mass (Da):56,140
    Last modified:June 7, 2004 - v2
    Checksum:i50EB94A755839B91
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381L → P in BAG37161. (PubMed:14702039)Curated
    Sequence conflicti355 – 3551E → G in BAG37161. (PubMed:14702039)Curated
    Sequence conflicti480 – 4801E → G in BAG37161. (PubMed:14702039)Curated
    Sequence conflicti488 – 4881E → G in BAG37161. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti250 – 2501E → D.
    Corresponds to variant rs7542609 [ dbSNP | Ensembl ].
    VAR_059134
    Natural varianti285 – 2851L → R.
    Corresponds to variant rs230321 [ dbSNP | Ensembl ].
    VAR_059135

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050193 mRNA. Translation: BAB40810.2.
    AY013700 mRNA. Translation: AAG33922.1.
    AK314586 mRNA. Translation: BAG37161.1.
    AL033527 Genomic DNA. Translation: CAI19402.1.
    CCDSiCCDS445.1.
    RefSeqiNP_071403.1. NM_022120.1.
    UniGeneiHs.472491.

    Genome annotation databases

    EnsembliENST00000327582; ENSP00000361914; ENSG00000198754.
    GeneIDi64064.
    KEGGihsa:64064.
    UCSCiuc001ceb.1. human.

    Polymorphism databases

    DMDMi48428678.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050193 mRNA. Translation: BAB40810.2 .
    AY013700 mRNA. Translation: AAG33922.1 .
    AK314586 mRNA. Translation: BAG37161.1 .
    AL033527 Genomic DNA. Translation: CAI19402.1 .
    CCDSi CCDS445.1.
    RefSeqi NP_071403.1. NM_022120.1.
    UniGenei Hs.472491.

    3D structure databases

    ProteinModelPortali Q9BYC2.
    SMRi Q9BYC2. Positions 41-515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122037. 1 interaction.
    STRINGi 9606.ENSP00000361914.

    Chemistry

    DrugBanki DB00139. Succinic acid.

    PTM databases

    PhosphoSitei Q9BYC2.

    Polymorphism databases

    DMDMi 48428678.

    Proteomic databases

    PaxDbi Q9BYC2.
    PRIDEi Q9BYC2.

    Protocols and materials databases

    DNASUi 64064.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327582 ; ENSP00000361914 ; ENSG00000198754 .
    GeneIDi 64064.
    KEGGi hsa:64064.
    UCSCi uc001ceb.1. human.

    Organism-specific databases

    CTDi 64064.
    GeneCardsi GC01M040235.
    H-InvDB HIX0199835.
    HGNCi HGNC:18606. OXCT2.
    HPAi HPA053950.
    MIMi 610289. gene.
    neXtProti NX_Q9BYC2.
    PharmGKBi PA38360.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1788.
    HOGENOMi HOG000221244.
    HOVERGENi HBG002310.
    InParanoidi Q9BYC2.
    KOi K01027.
    OMAi NISFEHE.
    OrthoDBi EOG7XH6PR.
    PhylomeDBi Q9BYC2.
    TreeFami TF313991.

    Enzyme and pathway databases

    UniPathwayi UPA00929 ; UER00894 .

    Miscellaneous databases

    GenomeRNAii 64064.
    NextBioi 65830.
    PROi Q9BYC2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BYC2.
    CleanExi HS_OXCT2.
    Genevestigatori Q9BYC2.

    Family and domain databases

    InterProi IPR012792. 3-oxoacid_CoA-transf_A.
    IPR012791. 3-oxoacid_CoA-transf_B.
    IPR014388. 3-oxoacid_CoA-transferase.
    IPR004165. CoA_trans_fam_I.
    IPR004164. CoA_transf_AS.
    IPR004163. CoA_transf_BS.
    [Graphical view ]
    PANTHERi PTHR13707. PTHR13707. 1 hit.
    Pfami PF01144. CoA_trans. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000858. SCOT-t. 1 hit.
    SMARTi SM00882. CoA_trans. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR02429. pcaI_scoA_fam. 1 hit.
    TIGR02428. pcaJ_scoB_fam. 1 hit.
    PROSITEi PS01273. COA_TRANSF_1. 1 hit.
    PS01274. COA_TRANSF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a human orthologue of testis-specific succinyl CoA:3-oxo acid CoA transferase (Scot-t) cDNA."
      Tanaka H., Kohroki J., Iguchi N., Onishi M., Nishimune Y.
      Mol. Hum. Reprod. 8:16-23(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. Kohroki J., Tanaka H.
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 352.
    3. "Cloning and characterization of FKSG25, a novel gene located on human chromosome 1p34."
      Wang Y.-G., Gong L.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Testis.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiSCOT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYC2
    Secondary accession number(s): B2RBB4
    , Q5QPK4, Q8NHR1, Q9H1I4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3