Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q9BWD1

- THIC_HUMAN

UniProt

Q9BWD1 - THIC_HUMAN

Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene

ACAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (13 Sep 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BWD1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    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]

    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

    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
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiJC2378.
    RefSeqiNP_005882.2. NM_005891.2.
    XP_005267037.1. XM_005266980.2.
    UniGeneiHs.571037.

    Genome annotation databases

    EnsembliENST00000367048; ENSP00000356015; ENSG00000120437.
    ENST00000541436; ENSP00000437850; ENSG00000120437.
    GeneIDi39.
    KEGGihsa:39.
    UCSCiuc010kjy.3. human.

    Polymorphism databases

    DMDMi52000838.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5268.1.
    PIRi JC2378.
    RefSeqi NP_005882.2. NM_005891.2.
    XP_005267037.1. XM_005266980.2.
    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 .
    ENST00000541436 ; ENSP00000437850 ; 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

    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).

    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: October 1, 2014
    This is version 125 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