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Q8WU03 (GLYL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine N-acyltransferase-like protein 2

EC=2.3.1.13
Alternative name(s):
Acyl-CoA:glycine N-acyltransferase-like protein 2
Gene names
Name:GLYATL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Conjugates numerous substrates, such as arachidonoyl-CoA and saturated medium and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. Shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor. Does not exhibit any activity toward C22:6-CoA and chenodeoxycholoyl-CoA, nor toward serine or alanine. Ref.5

Catalytic activity

Acyl-CoA + glycine = CoA + N-acylglycine.

Subcellular location

Endoplasmic reticulum Ref.5.

Tissue specificity

Expressed at highest levels in salivary gland and trachea. Also detected in thyroid gland, spinal cord, prostate, lung and fetal brain. Ref.5

Post-translational modification

Acetylation at Lys-19 drastically decreases the production of N-oleoyl and N-arachidonoyl glycines. Ref.6

Sequence similarities

Belongs to the glycine N-acyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=4.4 µM for oleoyl-CoA Ref.5

Vmax=933 nmol/min/mg enzyme with oleoyl-CoA as substrate

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglycine N-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Glycine N-acyltransferase-like protein 2
PRO_0000281875

Amino acid modifications

Modified residue191N6-acetyllysine Ref.6

Natural variations

Natural variant821P → S. Ref.4
Corresponds to variant rs17856514 [ dbSNP | Ensembl ].
VAR_031296
Natural variant1601E → K. Ref.1
Corresponds to variant rs11229651 [ dbSNP | Ensembl ].
VAR_031297
Natural variant1681L → I. Ref.4
Corresponds to variant rs17851433 [ dbSNP | Ensembl ].
VAR_031298

Experimental info

Sequence conflict2191Q → R in AAO73139. Ref.1
Sequence conflict2931Y → C in AAO73139. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8WU03 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: A1F5C3EC989D90D1

FASTA29434,277
        10         20         30         40         50         60 
MLVLHNSQKL QILYKSLEKS IPESIKVYGA IFNIKDKNPF NMEVLVDAWP DYQIVITRPQ 

        70         80         90        100        110        120 
KQEMKDDQDH YTNTYHIFTK APDKLEEVLS YSNVISWEQT LQIQGCQEGL DEAIRKVATS 

       130        140        150        160        170        180 
KSVQVDYMKT ILFIPELPKK HKTSSNDKME LFEVDDDNKE GNFSNMFLDA SHAGLVNEHW 

       190        200        210        220        230        240 
AFGKNERSLK YIERCLQDFL GFGVLGPEGQ LVSWIVMEQS CELRMGYTVP KYRHQGNMLQ 

       250        260        270        280        290 
IGYHLEKYLS QKEIPFYFHV ADNNEKSLQA LNNLGFKICP CGWHQWKCTP KKYC 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a novel BXMAS2-10 gene from IgM cross-linking induced human B cell."
Nakayama Y., Weissman S.M., Bothwell A.L.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-160.
[2]"Designation of enzyme activity of glycine-N-acyltransferase family genes and depression of glycine-N-acyltransferase in human hepatocellular carcinoma."
Matsuo M., Terai K., Kameda N., Matsumoto A., Kurokawa Y., Funase Y., Nishikawa K., Sugaya N., Hiruta N., Kishimoto T.
Biochem. Biophys. Res. Commun. 420:901-906(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANTS SER-82 AND ILE-168.
Tissue: Bone marrow.
[5]"Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a transferase that produces N-acyl glycines in humans."
Waluk D.P., Schultz N., Hunt M.C.
FASEB J. 24:2795-2803(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Reversible lysine acetylation regulates activity of human glycine N-acyltransferase-like 2 (hGLYATL2): implications for production of glycine-conjugated signaling molecules."
Waluk D.P., Sucharski F., Sipos L., Silberring J., Hunt M.C.
J. Biol. Chem. 287:16158-16167(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF426250 mRNA. Translation: AAO73139.1.
AB207211 mRNA. Translation: BAF63415.1.
CH471076 Genomic DNA. Translation: EAW73826.1.
BC016789 mRNA. Translation: AAH16789.1.
BC021682 mRNA. Translation: AAH21682.1.
RefSeqNP_659453.3. NM_145016.3.
UniGeneHs.254271.

3D structure databases

ProteinModelPortalQ8WU03.
SMRQ8WU03. Positions 199-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000287275.

Chemistry

DrugBankDB00145. Glycine.

PTM databases

PhosphoSiteQ8WU03.

Polymorphism databases

DMDM74730653.

Proteomic databases

PaxDbQ8WU03.
PRIDEQ8WU03.

Protocols and materials databases

DNASU219970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287275; ENSP00000287275; ENSG00000156689.
ENST00000532258; ENSP00000434277; ENSG00000156689.
GeneID219970.
KEGGhsa:219970.
UCSCuc001nnd.4. human.

Organism-specific databases

CTD219970.
GeneCardsGC11M058601.
HGNCHGNC:24178. GLYATL2.
HPAHPA060292.
MIM614762. gene.
neXtProtNX_Q8WU03.
PharmGKBPA142671728.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG121427.
HOGENOMHOG000263599.
HOVERGENHBG107953.
InParanoidQ8WU03.
OMAWIVMEQS.
OrthoDBEOG7MKW6X.
PhylomeDBQ8WU03.
TreeFamTF353258.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ8WU03.
BgeeQ8WU03.
CleanExHS_GLYATL2.
GenevestigatorQ8WU03.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR010313. Glycine_N-acyltransferase.
IPR013652. Glycine_N-acyltransferase_C.
IPR015938. Glycine_N-acyltransferase_N.
[Graphical view]
PANTHERPTHR15298. PTHR15298. 1 hit.
PfamPF08444. Gly_acyl_tr_C. 1 hit.
PF06021. Gly_acyl_tr_N. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi219970.
NextBio90902.
PROQ8WU03.
SOURCESearch...

Entry information

Entry nameGLYL2_HUMAN
AccessionPrimary (citable) accession number: Q8WU03
Secondary accession number(s): A5LGC7, Q86WC3, Q96AT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM