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O15228 (GNPAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Dihydroxyacetone phosphate acyltransferase

Short name=DAP-AT
Short name=DHAP-AT
EC=2.3.1.42
Alternative name(s):
Acyl-CoA:dihydroxyacetonephosphateacyltransferase
Glycerone-phosphate O-acyltransferase
Gene names
Name:GNPAT
Synonyms:DAPAT, DHAPAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Subunit structure

May be part of a heterotrimeric complex composed of DAP-AT, ADAP-S and a modified form of DAP-AT.

Subcellular location

Peroxisome membrane; Peripheral membrane protein; Matrix side By similarity. Note: Exclusively localized to the lumenal side of the peroxisomal membrane By similarity.

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.

Involvement in disease

Rhizomelic chondrodysplasia punctata 2 (RCDP2) [MIM:222765]: A disease characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.8 Ref.9

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Cellular componentMembrane
Peroxisome
   DiseaseCataract
Disease mutation
Dwarfism
Rhizomelic chondrodysplasia punctata
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

cerebellum morphogenesis

Inferred from electronic annotation. Source: Ensembl

ether lipid biosynthetic process

Inferred from direct assay PubMed 15687349. Source: UniProtKB

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

paranodal junction assembly

Inferred from electronic annotation. Source: Ensembl

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

response to drug

Inferred from electronic annotation. Source: Ensembl

response to fatty acid

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

synapse assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisomal membrane

Inferred from direct assay PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 15687349. Source: UniProtKB

   Molecular_functionglycerone-phosphate O-acyltransferase activity

Inferred from direct assay PubMed 15687349PubMed 8186247Ref.2. Source: UniProtKB

palmitoyl-CoA hydrolase activity

Inferred from direct assay PubMed 8186247. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 680680Dihydroxyacetone phosphate acyltransferase
PRO_0000195246

Regions

Motif162 – 1676HXXXXD motif
Motif678 – 6803Microbody targeting signal Potential
Compositional bias3 – 97Poly-Ser

Amino acid modifications

Modified residue6431N6-acetyllysine Ref.6

Natural variations

Natural variant2111R → C in RCDP2. Ref.2
Corresponds to variant rs28939697 [ dbSNP | Ensembl ].
VAR_006357
Natural variant2111R → H in RCDP2; complete loss of activity. Ref.2 Ref.9
Corresponds to variant rs28939696 [ dbSNP | Ensembl ].
VAR_006358
Natural variant4951V → I.
Corresponds to variant rs11122266 [ dbSNP | Ensembl ].
VAR_030696
Natural variant5191D → G in RCDP2; 70% reduction in activity. Ref.9
Corresponds to variant rs11558492 [ dbSNP | Ensembl ].
VAR_025897
Natural variant5861Y → H. Ref.5
Corresponds to variant rs17849315 [ dbSNP | Ensembl ].
VAR_030697

Experimental info

Sequence conflict261S → K AA sequence Ref.2
Sequence conflict311K → N AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
O15228 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BDF624CCD4D92477

FASTA68077,188
        10         20         30         40         50         60 
MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF AMKCYTPLVY 

        70         80         90        100        110        120 
KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR EEVSEILDEM SHKLRLGAIR 

       130        140        150        160        170        180 
FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL 

       190        200        210        220        230        240 
PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF 

       250        260        270        280        290        300 
FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV 

       310        320        330        340        350        360 
PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE 

       370        380        390        400        410        420 
DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL WLKGLTQAFG 

       430        440        450        460        470        480 
GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG DSEVVDGLML QHITLLMCSA 

       490        500        510        520        530        540 
YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC 

       550        560        570        580        590        600 
YLLCKSEAIQ VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY 

       610        620        630        640        650        660 
LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC IFNVNEPATT 

       670        680 
KLEEMLGCKT PIGKPATAKL 

« Hide

References

« Hide 'large scale' references
[1]"Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase."
Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K., Just W.W.
FEBS Lett. 420:205-211(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2."
Ofman R., Hettema E.H., Hogenhout E.M., Caruso U., Muijsers A.O., Wanders R.J.A.
Hum. Mol. Genet. 7:847-853(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-33, VARIANTS RCDP2 CYS-211 AND HIS-211.
[3]"Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human GNPAT gene and its use in the identification of novel mutations."
Ofman R., Lajmir S., Wanders R.J.A.
Biochem. Biophys. Res. Commun. 281:754-760(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT HIS-586.
Tissue: Lung.
[6]"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-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Functional characterization of novel mutations in GNPAT and AGPS, causing rhizomelic chondrodysplasia punctata (RCDP) types 2 and 3."
Itzkovitz B., Jiralerspong S., Nimmo G., Loscalzo M., Horovitz D.D., Snowden A., Moser A., Steinberg S., Braverman N.
Hum. Mutat. 33:189-197(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RCDP2.
[9]"Impaired membrane traffic in defective ether lipid biosynthesis."
Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K., Just W.W.
Hum. Mol. Genet. 10:127-136(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RCDP2 HIS-211 AND GLY-519, CHARACTERIZATION OF VARIANTS RCDP2 HIS-211 AND GLY-519.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ002190 mRNA. Translation: CAA05242.1.
AF043937 mRNA. Translation: AAC24505.1.
AF218233 expand/collapse EMBL AC list , AF218223, AF218224, AF218225, AF218226, AF218227, AF218228, AF218229, AF218230, AF218231, AF218232 Genomic DNA. Translation: AAG17547.1.
AL137801, AL117352 Genomic DNA. Translation: CAI21988.1.
AL117352, AL137801 Genomic DNA. Translation: CAI23094.1.
BC000450 mRNA. Translation: AAH00450.1.
CCDSCCDS1592.1.
RefSeqNP_055051.1. NM_014236.3.
UniGeneHs.498028.

3D structure databases

ProteinModelPortalO15228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114021. 8 interactions.
IntActO15228. 6 interactions.
STRING9606.ENSP00000355607.

Chemistry

BindingDBO15228.
ChEMBLCHEMBL4494.

PTM databases

PhosphoSiteO15228.

Proteomic databases

MaxQBO15228.
PaxDbO15228.
PRIDEO15228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366647; ENSP00000355607; ENSG00000116906.
GeneID8443.
KEGGhsa:8443.
UCSCuc001hup.4. human.

Organism-specific databases

CTD8443.
GeneCardsGC01P231376.
HGNCHGNC:4416. GNPAT.
HPAHPA060059.
MIM222765. phenotype.
602744. gene.
neXtProtNX_O15228.
Orphanet309796. Rhizomelic chondrodysplasia punctata type 2.
PharmGKBPA28795.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2937.
HOVERGENHBG051749.
InParanoidO15228.
KOK00649.
OMAPRYIPQK.
OrthoDBEOG7CCBQT.
PhylomeDBO15228.
TreeFamTF313360.

Enzyme and pathway databases

BRENDA2.3.1.42. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00940.

Gene expression databases

ArrayExpressO15228.
BgeeO15228.
CleanExHS_GNPAT.
GenevestigatorO15228.

Family and domain databases

InterProIPR028353. DHAPAT.
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERPTHR12563. PTHR12563. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF500063. DHAPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNPAT. human.
GenomeRNAi8443.
NextBio31586.
PROO15228.
SOURCESearch...

Entry information

Entry nameGNPAT_HUMAN
AccessionPrimary (citable) accession number: O15228
Secondary accession number(s): Q5TBH7, Q9BWC2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 138 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 1

Human chromosome 1: entries, gene names and cross-references to MIM