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Q9BYC2 (SCOT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:OXCT2
ORF Names:FKSG25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Pathway

Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

Testis specific. Ref.1

Sequence similarities

Belongs to the 3-oxoacid CoA-transferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processketone body catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from direct assay Ref.1. Source: MGI

motile cilium

Inferred from direct assay Ref.1. Source: MGI

   Molecular_function3-oxoacid CoA-transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion By similarity
Chain40 – 517478Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
PRO_0000002416

Sites

Active site34115-glutamyl coenzyme A thioester intermediate By similarity

Natural variations

Natural variant2501E → D.
Corresponds to variant rs7542609 [ dbSNP | Ensembl ].
VAR_059134
Natural variant2851L → R.
Corresponds to variant rs230321 [ dbSNP | Ensembl ].
VAR_059135

Experimental info

Sequence conflict381L → P in BAG37161. Ref.4
Sequence conflict3551E → G in BAG37161. Ref.4
Sequence conflict4801E → G in BAG37161. Ref.4
Sequence conflict4881E → G in BAG37161. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9BYC2 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 50EB94A755839B91

FASTA51756,140
        10         20         30         40         50         60 
MAALRLLASV LGRGVPAGGS GLALSQGCAR CFATSPRLRA KFYADPVEMV KDISDGATVM 

        70         80         90        100        110        120 
IGGFGLCGIP ENLIAALLRT RVKDLQVVSS NVGVEDFGLG LLLAARQVRR IVCSYVGENT 

       130        140        150        160        170        180 
LCESQYLAGE LELELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGA PIRYTPDGHL 

       190        200        210        220        230        240 
ALMSQPREVR EFNGDHFLLE RAIRADFALV KGWKADRAGN VVFRRSARNF NVPMCKAADV 

       250        260        270        280        290        300 
TAVEVEEIVE VGAFPPEDIH VPNIYVDRVI KGQKYEKRIE RLTILKEEDG DAGKEEDART 

       310        320        330        340        350        360 
RIIRRAALEF EDGMYANLGI GIPLLASNFI SPSMTVHLHS ENGILGLGPF PTEDEVDADL 

       370        380        390        400        410        420 
INAGKQTVTV LPGGCFFASD DSFAMIRGGH IQLTMLGAMQ VSKYGDLANW MIPGKKVKGM 

       430        440        450        460        470        480 
GGAMDLVSSQ KTRVVVTMQH CTKDNTPKIM EKCTMPLTGK RCVDRIITEK AVFDVHRKKE 

       490        500        510 
LTLRELWEGL TVDDIKKSTG CAFAVSPNLR PMQQVAP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB050193 mRNA. Translation: BAB40810.2.
AY013700 mRNA. Translation: AAG33922.1.
AK314586 mRNA. Translation: BAG37161.1.
AL033527 Genomic DNA. Translation: CAI19402.1.
CCDSCCDS445.1.
RefSeqNP_071403.1. NM_022120.1.
UniGeneHs.472491.

3D structure databases

ProteinModelPortalQ9BYC2.
SMRQ9BYC2. Positions 41-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122037. 1 interaction.
STRING9606.ENSP00000361914.

Chemistry

DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteQ9BYC2.

Polymorphism databases

DMDM48428678.

Proteomic databases

PaxDbQ9BYC2.
PRIDEQ9BYC2.

Protocols and materials databases

DNASU64064.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327582; ENSP00000361914; ENSG00000198754.
GeneID64064.
KEGGhsa:64064.
UCSCuc001ceb.1. human.

Organism-specific databases

CTD64064.
GeneCardsGC01M040235.
H-InvDBHIX0199835.
HGNCHGNC:18606. OXCT2.
HPAHPA053950.
MIM610289. gene.
neXtProtNX_Q9BYC2.
PharmGKBPA38360.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1788.
HOGENOMHOG000221244.
HOVERGENHBG002310.
InParanoidQ9BYC2.
KOK01027.
OMANISFEHE.
OrthoDBEOG7XH6PR.
PhylomeDBQ9BYC2.
TreeFamTF313991.

Enzyme and pathway databases

UniPathwayUPA00929; UER00894.

Gene expression databases

BgeeQ9BYC2.
CleanExHS_OXCT2.
GenevestigatorQ9BYC2.

Family and domain databases

InterProIPR012792. 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]
PANTHERPTHR13707. PTHR13707. 1 hit.
PfamPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFPIRSF000858. SCOT-t. 1 hit.
SMARTSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi64064.
NextBio65830.
PROQ9BYC2.
SOURCESearch...

Entry information

Entry nameSCOT2_HUMAN
AccessionPrimary (citable) accession number: Q9BYC2
Secondary accession number(s): B2RBB4 expand/collapse secondary AC list , Q5QPK4, Q8NHR1, Q9H1I4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM