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P55809

- SCOT1_HUMAN

UniProt

P55809 - SCOT1_HUMAN

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Protein
Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
Gene
OXCT1, OXCT, SCOT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei344 – 34415-glutamyl coenzyme A thioester intermediate By similarity

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 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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 Publication
Add
BLAST
Chaini40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
PRO_0000002413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphoserine1 Publication
Modified residuei185 – 1851N6-succinyllysine By similarity
Modified residuei418 – 4181N6-succinyllysine By similarity
Modified residuei421 – 4211N6-succinyllysine By similarity
Modified residuei455 – 4551N6-succinyllysine By 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. 43 interactions.
IntActiP55809. 3 interactions.
STRINGi9606.ENSP00000196371.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP55809.

Family & Domainsi

Sequence similaritiesi

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]

Sequencei

Sequence statusi: Complete.

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

P55809-1 [UniParc]FASTAAdd to Basket

« 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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951D → G in BAG35249. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U62961 mRNA. Translation: AAB07366.1.
AB029576 Genomic DNA. Translation: BAB13733.1.
AK312327 mRNA. Translation: BAG35249.1.
BC009001 mRNA. Translation: AAH09001.1.
CCDSiCCDS3937.1.
RefSeqiNP_000427.1. NM_000436.3.
UniGeneiHs.278277.

Genome annotation databases

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

Polymorphism databases

DMDMi2492998.

Keywords - Coding sequence diversityi

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 .
AK312327 mRNA. Translation: BAG35249.1 .
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. 43 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 .
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

« Hide 'large scale' publications
  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], 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. "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: Cerebellum.
  4. "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: Brain.
  5. Cited for: PROTEIN SEQUENCE OF 40-50.
    Tissue: Colon.
  6. 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.
  7. "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].
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. "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.
  12. "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
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 143 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

Dasty 3

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