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Q8BWT1

- THIM_MOUSE

UniProt

Q8BWT1 - THIM_MOUSE

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Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

Acaa2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Abolishes BNIP3-mediated apoptosis and mitochondrial damage.By similarity

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC
  2. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. cellular response to hypoxia Source: Ensembl
  2. fatty acid metabolic process Source: UniProtKB-UniPathway
  3. negative regulation of mitochondrial membrane permeability involved in apoptotic process Source: Ensembl
  4. negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase, mitochondrial (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Mitochondrial 3-oxoacyl-CoA thiolase
Gene namesi
Name:Acaa2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1098623. Acaa2.

Subcellular locationi

Mitochondrion By similarity
Note: Colocalizes with BNIP3 in the mitochondria.By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000223300Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleavedBy similarityAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251N6-acetyllysine; alternate1 Publication
Modified residuei25 – 251N6-succinyllysine; alternate1 Publication
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei45 – 451N6-succinyllysine1 Publication
Modified residuei119 – 1191PhosphothreonineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei127 – 1271PhosphotyrosineBy similarity
Modified residuei137 – 1371N6-acetyllysine; alternate1 Publication
Modified residuei137 – 1371N6-succinyllysine; alternate1 Publication
Modified residuei143 – 1431N6-acetyllysine; alternate1 Publication
Modified residuei143 – 1431N6-succinyllysine; alternate1 Publication
Modified residuei158 – 1581N6-acetyllysine; alternate1 Publication
Modified residuei158 – 1581N6-succinyllysine; alternate1 Publication
Modified residuei171 – 1711N6-acetyllysine; alternate1 Publication
Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
Modified residuei191 – 1911N6-acetyllysine; alternate2 Publications
Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
Modified residuei209 – 2091N6-acetyllysine; alternate1 Publication
Modified residuei209 – 2091N6-succinyllysine; alternate1 Publication
Modified residuei211 – 2111N6-succinyllysine1 Publication
Modified residuei212 – 2121N6-succinyllysine1 Publication
Modified residuei214 – 2141N6-succinyllysine1 Publication
Modified residuei234 – 2341N6-acetyllysine; alternate1 Publication
Modified residuei234 – 2341N6-succinyllysine; alternate1 Publication
Modified residuei240 – 2401N6-succinyllysine1 Publication
Modified residuei241 – 2411N6-acetyllysine1 Publication
Modified residuei269 – 2691N6-acetyllysine1 Publication
Modified residuei270 – 2701N6-acetyllysine1 Publication
Modified residuei305 – 3051N6-acetyllysine; alternate1 Publication
Modified residuei305 – 3051N6-succinyllysine; alternate1 Publication
Modified residuei312 – 3121N6-acetyllysine; alternate1 Publication
Modified residuei312 – 3121N6-succinyllysine; alternate1 Publication
Modified residuei340 – 3401N6-acetyllysine1 Publication
Modified residuei375 – 3751N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BWT1.
PaxDbiQ8BWT1.
PRIDEiQ8BWT1.

2D gel databases

REPRODUCTION-2DPAGEQ8BWT1.

PTM databases

PhosphoSiteiQ8BWT1.

Expressioni

Gene expression databases

BgeeiQ8BWT1.
GenevestigatoriQ8BWT1.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi206649. 3 interactions.
IntActiQ8BWT1. 9 interactions.
MINTiMINT-1839761.

Structurei

3D structure databases

ProteinModelPortaliQ8BWT1.
SMRiQ8BWT1. Positions 1-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ8BWT1.
KOiK07508.
OMAiQTLACAD.
OrthoDBiEOG7JQBNG.
TreeFamiTF105696.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
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.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BWT1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALLRGVFIV AAKRTPFGAY GGLLKDFSAT DLTEFAARAA LSAGKVPPET
60 70 80 90 100
IDSVIVGNVM QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV
110 120 130 140 150
SGCQEICSKD AEVVLCGGTE SMSQSPYCVR NVRFGTKFGL DLKLEDTLWA
160 170 180 190 200
GLTDQHVKLP MGMTAENLAA KYNISREDCD RYALQSQQRW KAANEAGYFN
210 220 230 240 250
EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPSVFK KDGTVTAGNA
260 270 280 290 300
SGVSDGAGAV IIASEDAVKK HNFTPLARVV GYFVSGCDPT IMGIGPVPAI
310 320 330 340 350
NGALKKAGLS LKDMDLIDVN EAFAPQFLSV QKALDLDPSK TNVSGGAIAL
360 370 380 390
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA LIIQNTA
Length:397
Mass (Da):41,830
Last modified:July 27, 2011 - v3
Checksum:i856840546F5CB8DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971A → V in AAH28901. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050101 mRNA. Translation: BAC34067.1.
AK167567 mRNA. Translation: BAE39630.1.
AK167715 mRNA. Translation: BAE39757.1.
AK169359 mRNA. Translation: BAE41108.1.
CH466528 Genomic DNA. Translation: EDL09521.1.
BC028901 mRNA. Translation: AAH28901.1.
CCDSiCCDS29342.1.
RefSeqiNP_803421.1. NM_177470.3.
UniGeneiMm.245724.

Genome annotation databases

EnsembliENSMUST00000041053; ENSMUSP00000037348; ENSMUSG00000036880.
GeneIDi52538.
KEGGimmu:52538.
UCSCiuc008fpt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050101 mRNA. Translation: BAC34067.1 .
AK167567 mRNA. Translation: BAE39630.1 .
AK167715 mRNA. Translation: BAE39757.1 .
AK169359 mRNA. Translation: BAE41108.1 .
CH466528 Genomic DNA. Translation: EDL09521.1 .
BC028901 mRNA. Translation: AAH28901.1 .
CCDSi CCDS29342.1.
RefSeqi NP_803421.1. NM_177470.3.
UniGenei Mm.245724.

3D structure databases

ProteinModelPortali Q8BWT1.
SMRi Q8BWT1. Positions 1-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206649. 3 interactions.
IntActi Q8BWT1. 9 interactions.
MINTi MINT-1839761.

PTM databases

PhosphoSitei Q8BWT1.

2D gel databases

REPRODUCTION-2DPAGE Q8BWT1.

Proteomic databases

MaxQBi Q8BWT1.
PaxDbi Q8BWT1.
PRIDEi Q8BWT1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041053 ; ENSMUSP00000037348 ; ENSMUSG00000036880 .
GeneIDi 52538.
KEGGi mmu:52538.
UCSCi uc008fpt.1. mouse.

Organism-specific databases

CTDi 10449.
MGIi MGI:1098623. Acaa2.

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00390000009412.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
InParanoidi Q8BWT1.
KOi K07508.
OMAi QTLACAD.
OrthoDBi EOG7JQBNG.
TreeFami TF105696.

Enzyme and pathway databases

UniPathwayi UPA00199 .

Miscellaneous databases

NextBioi 309107.
PROi Q8BWT1.
SOURCEi Search...

Gene expression databases

Bgeei Q8BWT1.
Genevestigatori Q8BWT1.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
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 PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Heart and Liver.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Strain: FVB/N.
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-45; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-211; LYS-212; LYS-214; LYS-234; LYS-240; LYS-305 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-137; LYS-143; LYS-158; LYS-171; LYS-191; LYS-209; LYS-234; LYS-241; LYS-269; LYS-270; LYS-305; LYS-312; LYS-340 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHIM_MOUSE
AccessioniPrimary (citable) accession number: Q8BWT1
Secondary accession number(s): Q3TIT9, Q8JZR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3