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Protein

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

Gene

OXCT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Pathway: succinyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetyl-CoA from succinyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial (OXCT2), Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (OXCT1), Succinyl-CoA:3-ketoacid-coenzyme A transferase, Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT1), Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT)
This subpathway is part of the pathway succinyl-CoA degradation, which is itself part of Ketone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetyl-CoA from succinyl-CoA, the pathway succinyl-CoA degradation and in Ketone metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.3.5. 2681.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18606. OXCT2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • motile cilium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38360.

Chemistry

DrugBankiDB00139. Succinic acid.

Polymorphism and mutation databases

BioMutaiOXCT2.
DMDMi48428678.

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei415 – 4151N6-succinyllysineBy similarity
Modified residuei418 – 4181N6-succinyllysineBy similarity
Modified residuei452 – 4521N6-succinyllysineBy similarity

Proteomic databases

MaxQBiQ9BYC2.
PaxDbiQ9BYC2.
PRIDEiQ9BYC2.

PTM databases

PhosphoSiteiQ9BYC2.

Expressioni

Tissue specificityi

Testis specific.1 Publication

Gene expression databases

BgeeiQ9BYC2.
CleanExiHS_OXCT2.
GenevisibleiQ9BYC2. HS.

Organism-specific databases

HPAiHPA053950.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi122037. 3 interactions.
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.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221244.
HOVERGENiHBG002310.
InParanoidiQ9BYC2.
KOiK01027.
OMAiDITQGAR.
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

        10         20         30         40         50
MAALRLLASV LGRGVPAGGS GLALSQGCAR CFATSPRLRA KFYADPVEMV
60 70 80 90 100
KDISDGATVM IGGFGLCGIP ENLIAALLRT RVKDLQVVSS NVGVEDFGLG
110 120 130 140 150
LLLAARQVRR IVCSYVGENT LCESQYLAGE LELELTPQGT LAERIRAGGA
160 170 180 190 200
GVPAFYTPTG YGTLVQEGGA PIRYTPDGHL ALMSQPREVR EFNGDHFLLE
210 220 230 240 250
RAIRADFALV KGWKADRAGN VVFRRSARNF NVPMCKAADV TAVEVEEIVE
260 270 280 290 300
VGAFPPEDIH VPNIYVDRVI KGQKYEKRIE RLTILKEEDG DAGKEEDART
310 320 330 340 350
RIIRRAALEF EDGMYANLGI GIPLLASNFI SPSMTVHLHS ENGILGLGPF
360 370 380 390 400
PTEDEVDADL INAGKQTVTV LPGGCFFASD DSFAMIRGGH IQLTMLGAMQ
410 420 430 440 450
VSKYGDLANW MIPGKKVKGM GGAMDLVSSQ KTRVVVTMQH CTKDNTPKIM
460 470 480 490 500
EKCTMPLTGK RCVDRIITEK AVFDVHRKKE LTLRELWEGL TVDDIKKSTG
510
CAFAVSPNLR PMQQVAP
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi122037. 3 interactions.
STRINGi9606.ENSP00000361914.

Chemistry

DrugBankiDB00139. Succinic acid.

PTM databases

PhosphoSiteiQ9BYC2.

Polymorphism and mutation databases

BioMutaiOXCT2.
DMDMi48428678.

Proteomic databases

MaxQBiQ9BYC2.
PaxDbiQ9BYC2.
PRIDEiQ9BYC2.

Protocols and materials databases

DNASUi64064.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi64064.
GeneCardsiGC01M040235.
H-InvDBHIX0199835.
HGNCiHGNC:18606. OXCT2.
HPAiHPA053950.
MIMi610289. gene.
neXtProtiNX_Q9BYC2.
PharmGKBiPA38360.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1788.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221244.
HOVERGENiHBG002310.
InParanoidiQ9BYC2.
KOiK01027.
OMAiDITQGAR.
OrthoDBiEOG7XH6PR.
PhylomeDBiQ9BYC2.
TreeFamiTF313991.

Enzyme and pathway databases

UniPathwayiUPA00929; UER00894.
BRENDAi2.8.3.5. 2681.

Miscellaneous databases

GenomeRNAii64064.
NextBioi65830.
PROiQ9BYC2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYC2.
CleanExiHS_OXCT2.
GenevisibleiQ9BYC2. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.