ACOT13

Estruturas disponíveis

PDB

Pesquisa Human UniProt: PDBe RCSB

Lista de códigos id do PDB
2F0X, 2H4U, 3F5O

Identificadores

Nomes alternativos

ACOT13

IDs externos

OMIM: 615652 HomoloGene: 41273 GeneCards: ACOT13

Ontologia genética
Função molecular	• hydrolase activity • acyl-CoA hydrolase activity
Componente celular	• citosol • fuso mitótico • Exossoma • citoesqueleto • mitocôndria • núcleo celular • citoplasma
Processo biológico	• protein homotetramerization • acyl-CoA metabolic process • negative regulation of cold-induced thermogenesis
Sources:Amigo / QuickGO

Ortólogos

Espécie

Humano

Rato

Entrez


55856


n/a

Ensembl


ENSG00000112304


n/a

UniProt


Q9NPJ3


n/a

RefSeq (mRNA)


NM_018473 NM_001160094


n/a

RefSeq (proteína)


NP_001153566 NP_060943


n/a

Localização (UCSC)

n/a

Pesquisa PubMed

^[1]

n/a

Wikidata

Ver/Editar Humano

A acil-CoA tioesterase 13 é uma proteína que em humanos é codificada pelo gene ACOT13.^[2] Este gene codifica um membro da superfamília da tioesterase. Em humanos, a proteína co-localiza-se com microtúbulos e é essencial para a proliferação celular^[3] sustentada.^[2]

Referências

↑ «Human PubMed Reference:»
↑ ^a ^b «Entrez Gene: Acyl-CoA thioesterase 13»
↑ «Cell growth». Biology Online Dictionary. Consultado em 15 de maio de 2011

Leitura adicional

Pinel P, Fauchereau F, Moreno A, Barbot A, Lathrop M, Zelenika D, Le Bihan D, Poline JB, Bourgeron T, Dehaene S (janeiro de 2012). «Genetic variants of FOXP2 and KIAA0319/TTRAP/THEM2 locus are associated with altered brain activation in distinct language-related regions». The Journal of Neuroscience. 32 (3): 817–25. PMID 22262880. doi:10.1523/JNEUROSCI.5996-10.2012
Venkatesh SK, Siddaiah A, Padakannaya P, Ramachandra NB (outubro de 2013). «Lack of association between genetic polymorphisms in ROBO1, MRPL19/C2ORF3 and THEM2 with developmental dyslexia». Gene. 529 (2): 215–9. PMID 23954868. doi:10.1016/j.gene.2013.08.017
Cheng Z, Bao S, Shan X, Xu H, Gong W (dezembro de 2006). «Human thioesterase superfamily member 2 (hTHEM2) is co-localized with beta-tubulin onto the microtubule». Biochemical and Biophysical Research Communications. 350 (4): 850–3. PMID 17045243. doi:10.1016/j.bbrc.2006.09.105
Kanno K, Wu MK, Agate DS, Fanelli BJ, Wagle N, Scapa EF, Ukomadu C, Cohen DE (outubro de 2007). «Interacting proteins dictate function of the minimal START domain phosphatidylcholine transfer protein/StarD2». The Journal of Biological Chemistry. 282 (42): 30728–36. PMID 17704541. doi:10.1074/jbc.M703745200
Walker LC, Waddell N, Ten Haaf A, Grimmond S, Spurdle AB (novembro de 2008). «Use of expression data and the CGEMS genome-wide breast cancer association study to identify genes that may modify risk in BRCA1/2 mutation carriers». Breast Cancer Research and Treatment. 112 (2): 229–36. PMID 18095154. doi:10.1007/s10549-007-9848-5
Cao J, Xu H, Zhao H, Gong W, Dunaway-Mariano D (fevereiro de 2009). «The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis». Biochemistry. 48 (6): 1293–304. PMC 2929599. PMID 19170545. doi:10.1021/bi801879z
Wei J, Kang HW, Cohen DE (julho de 2009). «Thioesterase superfamily member 2 (Them2)/acyl-CoA thioesterase 13 (Acot13): a homotetrameric hotdog fold thioesterase with selectivity for long-chain fatty acyl-CoAs». The Biochemical Journal. 421 (2): 311–22. PMC 3086008. PMID 19405909. doi:10.1042/BJ20090039
Cheng Z, Song F, Shan X, Wei Z, Wang Y, Dunaway-Mariano D, Gong W (outubro de 2006). «Crystal structure of human thioesterase superfamily member 2». Biochemical and Biophysical Research Communications. 349 (1): 172–7. PMID 16934754. doi:10.1016/j.bbrc.2006.08.025