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P55809

- SCOT1_HUMAN

UniProt

P55809 - SCOT1_HUMAN

Protein

Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial

Gene

OXCT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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.

    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 sitei344 – 34415-glutamyl coenzyme A thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-oxoacid CoA-transferase activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. adipose tissue development Source: Ensembl
    2. brain development Source: Ensembl
    3. cellular ketone body metabolic process Source: UniProtKB
    4. cellular lipid metabolic process Source: Reactome
    5. cellular response to acid chemical Source: Ensembl
    6. cellular response to glucose stimulus Source: Ensembl
    7. heart development Source: Ensembl
    8. ketone body catabolic process Source: Reactome
    9. ketone catabolic process Source: Ensembl
    10. positive regulation of insulin secretion Source: Ensembl
    11. response to activity Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to ethanol Source: Ensembl
    14. response to hormone Source: Ensembl
    15. response to nutrient Source: Ensembl
    16. response to starvation Source: Ensembl
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01447-MONOMER.
    ReactomeiREACT_59. Utilization of Ketone Bodies.
    UniPathwayiUPA00929; UER00894.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (EC:2.8.3.5)
    Alternative name(s):
    3-oxoacid CoA-transferase 1
    Somatic-type succinyl-CoA:3-oxoacid CoA-transferase
    Short name:
    SCOT-s
    Gene namesi
    Name:OXCT1
    Synonyms:OXCT, SCOT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8527. OXCT1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Succinyl-CoA-3-ketoacid-CoA transferase deficiency (SCOTD) [MIM:245050]: A disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331V → E in SCOTD. 1 Publication
    VAR_000696
    Natural varianti215 – 2151A → V in SCOTD; partial loss of activity. 1 Publication
    Corresponds to variant rs201752548 [ dbSNP | Ensembl ].
    VAR_065564
    Natural varianti219 – 2191G → E in SCOTD. 1 Publication
    VAR_010337
    Natural varianti221 – 2211V → M in SCOTD. 1 Publication
    VAR_010338
    Natural varianti226 – 2261S → N in SCOTD; loss of activity. 1 Publication
    VAR_065565
    Natural varianti324 – 3241G → E in SCOTD. 1 Publication
    VAR_010339
    Natural varianti327 – 3271L → P in SCOTD; partial loss of activity. 1 Publication
    VAR_065566
    Natural varianti404 – 4041V → F in SCOTD; loss of activity. 1 Publication
    VAR_065567
    Natural varianti405 – 4051S → P in SCOTD; loss of activity. 1 Publication
    VAR_065568
    Natural varianti456 – 4561C → F in SCOTD. 1 Publication
    VAR_000697
    Natural varianti468 – 4681R → C in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees. 1 Publication
    VAR_065569

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi245050. phenotype.
    Orphaneti832. Succinyl-CoA:3-ketoacid CoA transferase deficiency.
    PharmGKBiPA32855.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939Mitochondrion1 PublicationAdd
    BLAST
    Chaini40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrialPRO_0000002413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei170 – 1701Phosphoserine1 Publication
    Modified residuei185 – 1851N6-succinyllysineBy similarity
    Modified residuei418 – 4181N6-succinyllysineBy similarity
    Modified residuei421 – 4211N6-succinyllysineBy similarity
    Modified residuei455 – 4551N6-succinyllysineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP55809.
    PaxDbiP55809.
    PeptideAtlasiP55809.
    PRIDEiP55809.

    2D gel databases

    UCD-2DPAGEP55809.

    PTM databases

    PhosphoSiteiP55809.

    Expressioni

    Tissue specificityi

    Abundant in heart, followed in order by kidney, brain, and muscle, whereas in liver it is undetectable; also detectable in leukocytes and fibroblasts.

    Gene expression databases

    ArrayExpressiP55809.
    BgeeiP55809.
    CleanExiHS_OXCT1.
    GenevestigatoriP55809.

    Organism-specific databases

    HPAiHPA012047.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi111059. 44 interactions.
    IntActiP55809. 3 interactions.
    STRINGi9606.ENSP00000196371.

    Structurei

    Secondary structure

    1
    520
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 444
    Helixi46 – 505
    Beta strandi58 – 614
    Helixi71 – 8010
    Beta strandi84 – 885
    Helixi100 – 1045
    Beta strandi108 – 1147
    Helixi120 – 1278
    Beta strandi130 – 1356
    Helixi138 – 15013
    Beta strandi154 – 1585
    Turni159 – 1624
    Helixi164 – 1674
    Beta strandi171 – 1744
    Beta strandi178 – 1836
    Beta strandi189 – 1924
    Beta strandi195 – 2017
    Beta strandi205 – 2117
    Beta strandi213 – 2164
    Helixi225 – 2273
    Helixi231 – 2344
    Beta strandi237 – 24913
    Helixi256 – 2583
    Helixi263 – 2653
    Beta strandi268 – 2714
    Helixi300 – 30910
    Helixi310 – 3123
    Beta strandi318 – 3214
    Helixi325 – 3295
    Helixi330 – 3323
    Beta strandi340 – 3434
    Turni344 – 3463
    Beta strandi347 – 3504
    Helixi356 – 3583
    Beta strandi368 – 3703
    Beta strandi373 – 3797
    Helixi382 – 3909
    Beta strandi395 – 3995
    Beta strandi402 – 4054
    Beta strandi413 – 4153
    Turni416 – 4183
    Helixi426 – 4294
    Beta strandi435 – 4406
    Helixi446 – 4483
    Beta strandi450 – 4556
    Beta strandi461 – 4644
    Beta strandi468 – 4703
    Beta strandi472 – 4798
    Turni480 – 4823
    Beta strandi483 – 4897
    Helixi495 – 4995
    Beta strandi502 – 5043
    Beta strandi507 – 5148

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DLXX-ray2.20A/B/C/D40-520[»]
    ProteinModelPortaliP55809.
    SMRiP55809. Positions 40-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55809.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1788.
    HOGENOMiHOG000221244.
    HOVERGENiHBG002310.
    InParanoidiP55809.
    KOiK01027.
    OMAiNAGKEPI.
    OrthoDBiEOG7XH6PR.
    PhylomeDBiP55809.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55809-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALKLLSSG LRLCASARGS GATWYKGCVC SFSTSAHRHT KFYTDPVEAV    50
    KDIPDGATVL VGGFGLCGIP ENLIDALLKT GVKGLTAVSN NAGVDNFGLG 100
    LLLRSKQIKR MVSSYVGENA EFERQYLSGE LEVELTPQGT LAERIRAGGA 150
    GVPAFYTPTG YGTLVQEGGS PIKYNKDGSV AIASKPREVR EFNGQHFILE 200
    EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAET TVVEVEEIVD 250
    IGAFAPEDIH IPQIYVHRLI KGEKYEKRIE RLSIRKEGDG EAKSAKPGDD 300
    VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNITVH LQSENGVLGL 350
    GPYPRQHEAD ADLINAGKET VTILPGASFF SSDESFAMIR GGHVDLTMLG 400
    AMQVSKYGDL ANWMIPGKMV KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH 450
    KIMEKCTLPL TGKQCVNRII TEKAVFDVDK KKGLTLIELW EGLTVDDVQK 500
    STGCDFAVSP KLMPMQQIAN 520
    Length:520
    Mass (Da):56,158
    Last modified:November 1, 1997 - v1
    Checksum:i54DA790FB8EDA546
    GO
    Isoform 2 (identifier: P55809-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-397: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:123
    Mass (Da):13,358
    Checksum:i5B36DC7CF0E0B843
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951D → G in BAG35249. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581T → M.2 Publications
    Corresponds to variant rs75134564 [ dbSNP | Ensembl ].
    VAR_000695
    Natural varianti133 – 1331V → E in SCOTD. 1 Publication
    VAR_000696
    Natural varianti215 – 2151A → V in SCOTD; partial loss of activity. 1 Publication
    Corresponds to variant rs201752548 [ dbSNP | Ensembl ].
    VAR_065564
    Natural varianti219 – 2191G → E in SCOTD. 1 Publication
    VAR_010337
    Natural varianti221 – 2211V → M in SCOTD. 1 Publication
    VAR_010338
    Natural varianti226 – 2261S → N in SCOTD; loss of activity. 1 Publication
    VAR_065565
    Natural varianti324 – 3241G → E in SCOTD. 1 Publication
    VAR_010339
    Natural varianti327 – 3271L → P in SCOTD; partial loss of activity. 1 Publication
    VAR_065566
    Natural varianti404 – 4041V → F in SCOTD; loss of activity. 1 Publication
    VAR_065567
    Natural varianti405 – 4051S → P in SCOTD; loss of activity. 1 Publication
    VAR_065568
    Natural varianti456 – 4561C → F in SCOTD. 1 Publication
    VAR_000697
    Natural varianti468 – 4681R → C in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees. 1 Publication
    VAR_065569

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 397397Missing in isoform 2. 1 PublicationVSP_056310Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62961 mRNA. Translation: AAB07366.1.
    AB029576 Genomic DNA. Translation: BAB13733.1.
    AK298352 mRNA. Translation: BAH12764.1.
    AK312327 mRNA. Translation: BAG35249.1.
    AK315902 mRNA. Translation: BAH14273.1.
    AC008817 Genomic DNA. No translation available.
    AC034222 Genomic DNA. No translation available.
    AC114946 Genomic DNA. No translation available.
    BC009001 mRNA. Translation: AAH09001.1.
    CCDSiCCDS3937.1.
    RefSeqiNP_000427.1. NM_000436.3.
    UniGeneiHs.278277.

    Genome annotation databases

    EnsembliENST00000196371; ENSP00000196371; ENSG00000083720.
    ENST00000510634; ENSP00000423144; ENSG00000083720.
    GeneIDi5019.
    KEGGihsa:5019.
    UCSCiuc003jmn.3. human.

    Polymorphism databases

    DMDMi2492998.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62961 mRNA. Translation: AAB07366.1 .
    AB029576 Genomic DNA. Translation: BAB13733.1 .
    AK298352 mRNA. Translation: BAH12764.1 .
    AK312327 mRNA. Translation: BAG35249.1 .
    AK315902 mRNA. Translation: BAH14273.1 .
    AC008817 Genomic DNA. No translation available.
    AC034222 Genomic DNA. No translation available.
    AC114946 Genomic DNA. No translation available.
    BC009001 mRNA. Translation: AAH09001.1 .
    CCDSi CCDS3937.1.
    RefSeqi NP_000427.1. NM_000436.3.
    UniGenei Hs.278277.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DLX X-ray 2.20 A/B/C/D 40-520 [» ]
    ProteinModelPortali P55809.
    SMRi P55809. Positions 40-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111059. 44 interactions.
    IntActi P55809. 3 interactions.
    STRINGi 9606.ENSP00000196371.

    Chemistry

    DrugBanki DB00139. Succinic acid.

    PTM databases

    PhosphoSitei P55809.

    Polymorphism databases

    DMDMi 2492998.

    2D gel databases

    UCD-2DPAGE P55809.

    Proteomic databases

    MaxQBi P55809.
    PaxDbi P55809.
    PeptideAtlasi P55809.
    PRIDEi P55809.

    Protocols and materials databases

    DNASUi 5019.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000196371 ; ENSP00000196371 ; ENSG00000083720 .
    ENST00000510634 ; ENSP00000423144 ; ENSG00000083720 .
    GeneIDi 5019.
    KEGGi hsa:5019.
    UCSCi uc003jmn.3. human.

    Organism-specific databases

    CTDi 5019.
    GeneCardsi GC05M041765.
    HGNCi HGNC:8527. OXCT1.
    HPAi HPA012047.
    MIMi 245050. phenotype.
    601424. gene.
    neXtProti NX_P55809.
    Orphaneti 832. Succinyl-CoA:3-ketoacid CoA transferase deficiency.
    PharmGKBi PA32855.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1788.
    HOGENOMi HOG000221244.
    HOVERGENi HBG002310.
    InParanoidi P55809.
    KOi K01027.
    OMAi NAGKEPI.
    OrthoDBi EOG7XH6PR.
    PhylomeDBi P55809.
    TreeFami TF313991.

    Enzyme and pathway databases

    UniPathwayi UPA00929 ; UER00894 .
    BioCyci MetaCyc:HS01447-MONOMER.
    Reactomei REACT_59. Utilization of Ketone Bodies.

    Miscellaneous databases

    EvolutionaryTracei P55809.
    GeneWikii OXCT1.
    GenomeRNAii 5019.
    NextBioi 19324.
    PROi P55809.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55809.
    Bgeei P55809.
    CleanExi HS_OXCT1.
    Genevestigatori P55809.

    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. "Succinyl CoA:3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient."
      Kassovska-Bratinova S., Fukao T., Song X.-Q., Duncan A.M.V., Chen H.S., Robert M.-F., Perez-Cerda C., Ugarte M., Chartrand C., Vobecky S., Kondo N., Mitchell G.A.
      Am. J. Hum. Genet. 59:519-528(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Heart.
    2. "Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations."
      Fukao T., Mitchell G.A., Song X.-Q., Nakamura H., Kassovska-Bratinova S., Orii K.E., Wraith J.E., Besley G., Wanders R.J.A., Niezen-Koning K.E., Berry G.T., Palmieri M., Kondo N.
      Genomics 68:144-151(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCOTD GLU-219; MET-221 AND GLU-324.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum and Kidney.
    5. "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] (ISOFORM 1).
      Tissue: Brain.
    6. Cited for: PROTEIN SEQUENCE OF 40-50.
      Tissue: Colon.
    7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 84-104; 111-124; 147-173; 191-211; 391-418; 422-434 AND 501-511, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of human 3-oxoacid CoA transferase 1."
      Structural genomics consortium (SGC)
      Submitted (AUG-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 40-520.
    12. "Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings."
      Song X.-Q., Fukao T., Watanabe H., Shintaku H., Hirayama K., Kassovska-Bratinova S., Kondo N., Mitchell G.A.
      Hum. Mutat. 12:83-88(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SCOTD GLU-133 AND PHE-456, VARIANT MET-58.
    13. "Clinical and molecular characterization of five patients with succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency."
      Fukao T., Sass J.O., Kursula P., Thimm E., Wendel U., Ficicioglu C., Monastiri K., Guffon N., Baric I., Zabot M.T., Kondo N.
      Biochim. Biophys. Acta 1812:619-624(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468, VARIANT MET-58, CHARACTERIZATION OF VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468.

    Entry informationi

    Entry nameiSCOT1_HUMAN
    AccessioniPrimary (citable) accession number: P55809
    Secondary accession number(s): B2R5V2, B7Z528
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 144 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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