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Q9BWD1 - THIC_HUMAN

UniProt

Q9BWD1 - THIC_HUMAN

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Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene

ACAT2

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

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:94. ACAT2.

Subcellular locationi

Cytoplasm

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleolus Source: HPA
  4. nucleoplasm Source: HPA
  5. 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

BgeeiQ9BWD1.
CleanExiHS_ACAT2.
GenevestigatoriQ9BWD1.

Organism-specific databases

HPAiCAB021106.
HPA025736.
HPA025765.
HPA025811.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106557. 24 interactions.
STRINGi9606.ENSP00000356015.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortaliQ9BWD1.
SMRiQ9BWD1. Positions 4-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BWD1.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOVERGENiHBG003112.
InParanoidiQ9BWD1.
KOiK00626.
OMAiDPATMGM.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BWD1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE 
        60         70         80         90        100
DVSEVIFGHV LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC 
       110        120        130        140        150
LAVQSIGIGD SSIVVAGGME NMSKAPHLAY LRTGVKIGEM PLTDSILCDG 
       160        170        180        190        200
LTDAFHNCHM GITAENVAKK WQVSREDQDK VAVLSQNRTE NAQKAGHFDK 
       210        220        230        240        250
EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT DGTGTVTPAN 
       260        270        280        290        300
ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA 
       310        320        330        340        350
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA 
       360        370        380        390 
LGHPLGASGC RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE
Length:397
Mass (Da):41,351
Last modified:September 13, 2004 - v2
Checksum:iE3A8DAFB6F341B18
GO
Isoform 2 (identifier: Q9BWD1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MNAGSDPVVIVSAARTIIG → MGSHPVLRIWGNRRATAASLGRSGGRLSSPRLLRVVAPTLTFAQTSRC

Note: No experimental confirmation available.

Show »
Length:426
Mass (Da):44,643
Checksum:i5C4390424BB96169
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691K → T in AAB30856. (PubMed:7911016)Curated
Sequence conflicti262 – 2621V → A in AAB30856. (PubMed:7911016)Curated
Sequence conflicti375 – 3751R → G in AAM00223. 1 PublicationCurated

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919MNAGS…RTIIG → MGSHPVLRIWGNRRATAASL GRSGGRLSSPRLLRVVAPTL TFAQTSRC in isoform 2. 1 PublicationVSP_056217Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AK294273 mRNA. Translation: BAH11719.1.
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. [Q9BWD1-1]
PIRiJC2378.
RefSeqiNP_005882.2. NM_005891.2. [Q9BWD1-1]
XP_005267037.1. XM_005266980.2. [Q9BWD1-2]
UniGeneiHs.571037.

Genome annotation databases

EnsembliENST00000367048; ENSP00000356015; ENSG00000120437. [Q9BWD1-1]
GeneIDi39.
KEGGihsa:39.
UCSCiuc010kjy.3. human. [Q9BWD1-1]

Polymorphism databases

DMDMi52000838.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AK294273 mRNA. Translation: BAH11719.1.
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. [Q9BWD1-1]
PIRiJC2378.
RefSeqiNP_005882.2. NM_005891.2. [Q9BWD1-1]
XP_005267037.1. XM_005266980.2. [Q9BWD1-2]
UniGeneiHs.571037.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortaliQ9BWD1.
SMRiQ9BWD1. Positions 4-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106557. 24 interactions.
STRINGi9606.ENSP00000356015.

Chemistry

BindingDBiQ9BWD1.

PTM databases

PhosphoSiteiQ9BWD1.

Polymorphism databases

DMDMi52000838.

2D gel databases

OGPiQ9BWD1.
REPRODUCTION-2DPAGEIPI00291419.

Proteomic databases

MaxQBiQ9BWD1.
PaxDbiQ9BWD1.
PeptideAtlasiQ9BWD1.
PRIDEiQ9BWD1.

Protocols and materials databases

DNASUi39.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367048; ENSP00000356015; ENSG00000120437. [Q9BWD1-1]
GeneIDi39.
KEGGihsa:39.
UCSCiuc010kjy.3. human. [Q9BWD1-1]

Organism-specific databases

CTDi39.
GeneCardsiGC06P160182.
HGNCiHGNC:94. ACAT2.
HPAiCAB021106.
HPA025736.
HPA025765.
HPA025811.
MIMi100678. gene+phenotype.
neXtProtiNX_Q9BWD1.
PharmGKBiPA19.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOVERGENiHBG003112.
InParanoidiQ9BWD1.
KOiK00626.
OMAiDPATMGM.
OrthoDBiEOG7JQBNG.
PhylomeDBiQ9BWD1.
TreeFamiTF300650.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000120437-MONOMER.

Miscellaneous databases

ChiTaRSiACAT2. human.
EvolutionaryTraceiQ9BWD1.
GeneWikiiACAT2.
GenomeRNAii39.
NextBioi153.
PROiQ9BWD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWD1.
CleanExiHS_ACAT2.
GenevestigatoriQ9BWD1.

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]
ProtoNetiSearch...

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] (ISOFORM 1), 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] (ISOFORM 1).
    Tissue: Kidney.
  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] (ISOFORM 2).
    Tissue: Amygdala.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1), VARIANT ARG-211.
    Tissue: Lung.
  7. 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.
  8. "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].
  9. "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].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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).
+Additional computationally mapped references.

Entry informationi

Entry nameiTHIC_HUMAN
AccessioniPrimary (citable) accession number: Q9BWD1
Secondary accession number(s): B7Z233
, E1P5B1, Q16146, Q5TCL7, Q8TDM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: February 4, 2015
This is version 129 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

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.