Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BYC2

- SCOT2_HUMAN

UniProt

Q9BYC2 - SCOT2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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
Complete GO annotation...

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

MaxQBiQ9BYC2.
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. 2 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.
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

        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:
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. 2 interactions.
STRINGi 9606.ENSP00000361914.

Chemistry

DrugBanki DB00139. Succinic acid.

PTM databases

PhosphoSitei Q9BYC2.

Polymorphism databases

DMDMi 48428678.

Proteomic databases

MaxQBi Q9BYC2.
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.
GeneTreei ENSGT00390000009130.
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

« 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: October 29, 2014
This is version 113 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