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Q9BWD1

- THIC_HUMAN

UniProt

Q9BWD1 - THIC_HUMAN

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Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene
ACAT2, ACTL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediate
Active sitei353 – 3531Proton acceptor
Active sitei383 – 3831Proton acceptor

GO - Molecular functioni

  1. acetyl-CoA C-acetyltransferase activity Source: BHF-UCL

GO - Biological processi

  1. lipid metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000120437-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, cytosolic (EC:2.3.1.9)
Alternative name(s):
Acetyl-CoA transferase-like protein
Cytosolic acetoacetyl-CoA thiolase
Gene namesi
Name:ACAT2
Synonyms:ACTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:94. ACAT2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MIMi100678. gene+phenotype.
PharmGKBiPA19.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Acetyl-CoA acetyltransferase, cytosolicPRO_0000206409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei200 – 2001N6-acetyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9BWD1.
PaxDbiQ9BWD1.
PeptideAtlasiQ9BWD1.
PRIDEiQ9BWD1.

2D gel databases

OGPiQ9BWD1.
REPRODUCTION-2DPAGEIPI00291419.

PTM databases

PhosphoSiteiQ9BWD1.

Expressioni

Gene expression databases

ArrayExpressiQ9BWD1.
BgeeiQ9BWD1.
CleanExiHS_ACAT2.
GenevestigatoriQ9BWD1.

Organism-specific databases

HPAiCAB021106.
HPA025736.
HPA025765.
HPA025811.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106557. 20 interactions.
STRINGi9606.ENSP00000356015.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158
Turni24 – 274
Helixi30 – 4516
Helixi49 – 513
Beta strandi54 – 585
Helixi69 – 768
Beta strandi85 – 884
Helixi91 – 933
Helixi94 – 10714
Beta strandi112 – 12211
Beta strandi136 – 1383
Helixi145 – 1495
Turni154 – 1563
Helixi160 – 17112
Helixi175 – 19420
Turni195 – 2017
Beta strandi205 – 2095
Beta strandi212 – 2165
Helixi228 – 2325
Turni240 – 2434
Helixi248 – 2503
Beta strandi255 – 26511
Helixi266 – 2716
Beta strandi277 – 28711
Helixi290 – 2956
Helixi297 – 30812
Helixi312 – 3143
Beta strandi317 – 3204
Helixi325 – 33511
Helixi339 – 3413
Helixi348 – 3514
Turni355 – 3573
Helixi358 – 37316
Beta strandi377 – 3848
Turni385 – 3873
Beta strandi388 – 3969

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortaliQ9BWD1.
SMRiQ9BWD1. Positions 4-397.

Miscellaneous databases

EvolutionaryTraceiQ9BWD1.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Phylogenomic databases

eggNOGiCOG0183.
HOVERGENiHBG003112.
InParanoidiQ9BWD1.
KOiK00626.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ9BWD1.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BWD1-1 [UniParc]FASTAAdd to Basket

« Hide

MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE    50
DVSEVIFGHV LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC 100
LAVQSIGIGD SSIVVAGGME NMSKAPHLAY LRTGVKIGEM PLTDSILCDG 150
LTDAFHNCHM GITAENVAKK WQVSREDQDK VAVLSQNRTE NAQKAGHFDK 200
EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT DGTGTVTPAN 250
ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA 300
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA 350
LGHPLGASGC RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE 397
Length:397
Mass (Da):41,351
Last modified:September 13, 2004 - v2
Checksum:iE3A8DAFB6F341B18
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111K → R.1 Publication
Corresponds to variant rs25683 [ dbSNP | Ensembl ].
VAR_019686

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691K → T in AAB30856. 1 Publication
Sequence conflicti262 – 2621V → A in AAB30856. 1 Publication
Sequence conflicti375 – 3751R → G in AAM00223. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AL135914 Genomic DNA. Translation: CAI21850.1.
CH471051 Genomic DNA. Translation: EAW47619.1.
CH471051 Genomic DNA. Translation: EAW47620.1.
BC000408 mRNA. Translation: AAH00408.1.
CCDSiCCDS5268.1.
PIRiJC2378.
RefSeqiNP_005882.2. NM_005891.2.
UniGeneiHs.571037.

Genome annotation databases

EnsembliENST00000367048; ENSP00000356015; ENSG00000120437.
GeneIDi39.
KEGGihsa:39.
UCSCiuc010kjy.3. human.

Polymorphism databases

DMDMi52000838.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S70154 mRNA. Translation: AAB30856.1 .
AF356877 mRNA. Translation: AAM00223.1 .
AL135914 Genomic DNA. Translation: CAI21850.1 .
CH471051 Genomic DNA. Translation: EAW47619.1 .
CH471051 Genomic DNA. Translation: EAW47620.1 .
BC000408 mRNA. Translation: AAH00408.1 .
CCDSi CCDS5268.1.
PIRi JC2378.
RefSeqi NP_005882.2. NM_005891.2.
UniGenei Hs.571037.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WL4 X-ray 1.55 A 1-397 [» ]
1WL5 X-ray 2.26 A 1-397 [» ]
ProteinModelPortali Q9BWD1.
SMRi Q9BWD1. Positions 4-397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106557. 20 interactions.
STRINGi 9606.ENSP00000356015.

PTM databases

PhosphoSitei Q9BWD1.

Polymorphism databases

DMDMi 52000838.

2D gel databases

OGPi Q9BWD1.
REPRODUCTION-2DPAGE IPI00291419.

Proteomic databases

MaxQBi Q9BWD1.
PaxDbi Q9BWD1.
PeptideAtlasi Q9BWD1.
PRIDEi Q9BWD1.

Protocols and materials databases

DNASUi 39.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367048 ; ENSP00000356015 ; ENSG00000120437 .
GeneIDi 39.
KEGGi hsa:39.
UCSCi uc010kjy.3. human.

Organism-specific databases

CTDi 39.
GeneCardsi GC06P160153.
HGNCi HGNC:94. ACAT2.
HPAi CAB021106.
HPA025736.
HPA025765.
HPA025811.
MIMi 100678. gene+phenotype.
neXtProti NX_Q9BWD1.
PharmGKBi PA19.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0183.
HOVERGENi HBG003112.
InParanoidi Q9BWD1.
KOi K00626.
OrthoDBi EOG7JQBNG.
PhylomeDBi Q9BWD1.
TreeFami TF300650.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000120437-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9BWD1.
GeneWikii ACAT2.
GenomeRNAii 39.
NextBioi 153.
PROi Q9BWD1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BWD1.
Bgeei Q9BWD1.
CleanExi HS_ACAT2.
Genevestigatori Q9BWD1.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase."
    Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T., Orii T.
    Biochem. Biophys. Res. Commun. 201:478-485(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Identification of the human acetyl CoA transferase like (ACTL) protein by yeast two-hybrid screen."
    Chen H., Peng J., Huang C.-H.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANT ARG-211.
    Tissue: Lung.
  6. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 16-39; 195-210; 280-302 AND 342-361, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-233 AND LYS-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I."
    Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K.
    J. Mol. Biol. 347:189-201(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).

Entry informationi

Entry nameiTHIC_HUMAN
AccessioniPrimary (citable) accession number: Q9BWD1
Secondary accession number(s): E1P5B1
, Q16146, Q5TCL7, Q8TDM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 124 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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