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Protein

Glycine N-acyltransferase

Gene

Glyat

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

Functioni

Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate a multitude of substrates to form a variety of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid.By similarity

Catalytic activityi

Acyl-CoA + glycine = CoA + N-acylglycine.By similarity
Benzoyl-CoA + glycine = CoA + hippurate.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

ReactomeiR-MMU-177128. Conjugation of salicylate with glycine.
R-MMU-177135. Conjugation of benzoate with glycine.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine N-acyltransferase (EC:2.3.1.13By similarity)
Alternative name(s):
Acyl-CoA:glycine N-acyltransferase
Short name:
AAc
Aralkyl acyl-CoA N-acyltransferase
Aralkyl acyl-CoA:amino acid N-acyltransferase
Benzoyl-coenzyme A:glycine N-acyltransferase
Glycine N-benzoyltransferase (EC:2.3.1.71By similarity)
Gene namesi
Name:Glyat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2147502. Glyat.

Subcellular locationi

  • Mitochondrion By similarity

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Glycine N-acyltransferasePRO_0000281870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161N6-acetyllysine; alternateCombined sources
Modified residuei16 – 161N6-succinyllysine; alternateCombined sources
Modified residuei113 – 1131N6-acetyllysineCombined sources
Modified residuei127 – 1271N6-acetyllysine; alternateCombined sources
Modified residuei127 – 1271N6-succinyllysine; alternateCombined sources
Modified residuei141 – 1411N6-acetyllysine; alternateCombined sources
Modified residuei141 – 1411N6-succinyllysine; alternateCombined sources
Modified residuei142 – 1421N6-acetyllysine; alternateCombined sources
Modified residuei142 – 1421N6-succinyllysine; alternateCombined sources
Modified residuei159 – 1591N6-acetyllysineCombined sources
Modified residuei167 – 1671N6-acetyllysineCombined sources
Modified residuei169 – 1691N6-succinyllysineCombined sources
Modified residuei183 – 1831N6-acetyllysine; alternateCombined sources
Modified residuei183 – 1831N6-succinyllysine; alternateCombined sources
Modified residuei256 – 2561N6-acetyllysine; alternateCombined sources
Modified residuei256 – 2561N6-succinyllysine; alternateCombined sources
Modified residuei267 – 2671N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ91XE0.
MaxQBiQ91XE0.
PaxDbiQ91XE0.
PeptideAtlasiQ91XE0.
PRIDEiQ91XE0.

PTM databases

iPTMnetiQ91XE0.
PhosphoSiteiQ91XE0.

Expressioni

Gene expression databases

BgeeiQ91XE0.
CleanExiMM_GLYAT.
GenevisibleiQ91XE0. MM.

Interactioni

Protein-protein interaction databases

IntActiQ91XE0. 2 interactions.
MINTiMINT-1860765.
STRINGi10090.ENSMUSP00000043308.

Structurei

3D structure databases

ProteinModelPortaliQ91XE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycine N-acyltransferase family.Curated

Phylogenomic databases

eggNOGiENOG410IJUM. Eukaryota.
ENOG4111428. LUCA.
GeneTreeiENSGT00390000004997.
HOGENOMiHOG000263599.
HOVERGENiHBG107953.
InParanoidiQ91XE0.
KOiK00628.
OMAiPKAINED.
OrthoDBiEOG7MKW6X.
PhylomeDBiQ91XE0.
TreeFamiTF353258.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR010313. Glycine_N-acyltransferase.
IPR013652. Glycine_N-acyltransferase_C.
IPR015938. Glycine_N-acyltransferase_N.
[Graphical view]
PANTHERiPTHR15298. PTHR15298. 1 hit.
PfamiPF08444. Gly_acyl_tr_C. 1 hit.
PF06021. Gly_acyl_tr_N. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91XE0-1) [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
MIVPLQGAQM LQMLEKSLRK YLPESLKVYG TVYHMIHGNP FNLKALVDKW
60 70 80 90 100
PDFNTVVVRP QEQEMTDDLD FYINTYQVYS KDPQNCQEFL ESSEVINWKQ
110 120 130 140 150
HLQIQSSQSH LNKTIQNLAS IQSFQIKHSE NILYVSSETI KKLFPSLLDT
160 170 180 190 200
KNLSTGSGKP KAIDQDKFKL SSLDVVHAAL VNKFWLFGGN ERSQRFIERC
210 220 230 240 250
IKNFPSSCVL GPEGTPASWT LMDQTGEMRM GGTMPEYRLQ GLVSFVVHSQ
260 270 280 290
DQIMTKRGYP VYSHTEKSNI AMQKMSYTLQ HLPMPCAWNQ WKCMPM
Length:296
Mass (Da):34,098
Last modified:December 1, 2001 - v1
Checksum:i2825F8C6F7BA2C96
GO
Isoform 2 (identifier: Q91XE0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Note: No experimental confirmation available.
Show »
Length:262
Mass (Da):30,150
Checksum:i6DA04B8D9A92AC01
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 2. 1 PublicationVSP_024075Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039262 mRNA. Translation: BAC30297.1.
AK143901 mRNA. Translation: BAE25590.1.
AK143803 mRNA. Translation: BAE25544.1.
BC010799 mRNA. Translation: AAH10799.1.
BC015294 mRNA. Translation: AAH15294.1.
BC024434 mRNA. Translation: AAH24434.1.
CCDSiCCDS29633.1. [Q91XE0-1]
RefSeqiNP_666047.1. NM_145935.3. [Q91XE0-1]
UniGeneiMm.39974.

Genome annotation databases

EnsembliENSMUST00000044976; ENSMUSP00000043308; ENSMUSG00000063683. [Q91XE0-1]
ENSMUST00000119960; ENSMUSP00000114002; ENSMUSG00000063683. [Q91XE0-2]
GeneIDi107146.
KEGGimmu:107146.
UCSCiuc008guh.1. mouse. [Q91XE0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039262 mRNA. Translation: BAC30297.1.
AK143901 mRNA. Translation: BAE25590.1.
AK143803 mRNA. Translation: BAE25544.1.
BC010799 mRNA. Translation: AAH10799.1.
BC015294 mRNA. Translation: AAH15294.1.
BC024434 mRNA. Translation: AAH24434.1.
CCDSiCCDS29633.1. [Q91XE0-1]
RefSeqiNP_666047.1. NM_145935.3. [Q91XE0-1]
UniGeneiMm.39974.

3D structure databases

ProteinModelPortaliQ91XE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91XE0. 2 interactions.
MINTiMINT-1860765.
STRINGi10090.ENSMUSP00000043308.

PTM databases

iPTMnetiQ91XE0.
PhosphoSiteiQ91XE0.

Proteomic databases

EPDiQ91XE0.
MaxQBiQ91XE0.
PaxDbiQ91XE0.
PeptideAtlasiQ91XE0.
PRIDEiQ91XE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044976; ENSMUSP00000043308; ENSMUSG00000063683. [Q91XE0-1]
ENSMUST00000119960; ENSMUSP00000114002; ENSMUSG00000063683. [Q91XE0-2]
GeneIDi107146.
KEGGimmu:107146.
UCSCiuc008guh.1. mouse. [Q91XE0-1]

Organism-specific databases

CTDi10249.
MGIiMGI:2147502. Glyat.

Phylogenomic databases

eggNOGiENOG410IJUM. Eukaryota.
ENOG4111428. LUCA.
GeneTreeiENSGT00390000004997.
HOGENOMiHOG000263599.
HOVERGENiHBG107953.
InParanoidiQ91XE0.
KOiK00628.
OMAiPKAINED.
OrthoDBiEOG7MKW6X.
PhylomeDBiQ91XE0.
TreeFamiTF353258.

Enzyme and pathway databases

ReactomeiR-MMU-177128. Conjugation of salicylate with glycine.
R-MMU-177135. Conjugation of benzoate with glycine.

Miscellaneous databases

ChiTaRSiGlyat. mouse.
PROiQ91XE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XE0.
CleanExiMM_GLYAT.
GenevisibleiQ91XE0. MM.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR010313. Glycine_N-acyltransferase.
IPR013652. Glycine_N-acyltransferase_C.
IPR015938. Glycine_N-acyltransferase_N.
[Graphical view]
PANTHERiPTHR15298. PTHR15298. 1 hit.
PfamiPF08444. Gly_acyl_tr_C. 1 hit.
PF06021. Gly_acyl_tr_N. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
ProtoNetiSearch...

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: Kidney, Spinal cord and Spleen.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  4. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-127; LYS-141; LYS-142; LYS-169; LYS-183; LYS-256 AND LYS-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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-16; LYS-113; LYS-127; LYS-141; LYS-142; LYS-159; LYS-167; LYS-183 AND LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLYAT_MOUSE
AccessioniPrimary (citable) accession number: Q91XE0
Secondary accession number(s): Q05DG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 112 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.