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Q5TBH8

- Q5TBH8_HUMAN

UniProt

Q5TBH8 - Q5TBH8_HUMAN

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Protein
Submitted name:

Dihydroxyacetone phosphate acyltransferase

Gene
GNPAT
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. O-acyltransferase activity Source: InterPro

GO - Biological processi

  1. cellular lipid metabolic process Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Dihydroxyacetone phosphate acyltransferaseImported
Gene namesi
Name:GNPATImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4416. GNPAT.

PTM / Processingi

Proteomic databases

PRIDEiQ5TBH8.

Expressioni

Gene expression databases

ArrayExpressiQ5TBH8.

Interactioni

Protein-protein interaction databases

MINTiMINT-1402298.

Structurei

3D structure databases

ProteinModelPortaliQ5TBH8.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000112751.
HOVERGENiHBG051749.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q5TBH8-1 [UniParc]FASTAAdd to Basket

« Hide

MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF    50
AMKCYTPLVY KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR 100
EEVSEILDEM SHKLRLGAIR FCAFTLSKVF KQIFSKLQRA IQEHPVVLLP 150
SHRSYIDFLM LSFLLYNYDL PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR 200
RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF FLEGTRSRSA KTLTPKFGLL 250
NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV PKPKESTTGL 300
LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE 350
DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL 400
WLKGLTQAFG GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG 450
DSEVVDGLML QHITLLMCSA YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV 500
YSCFRFLRDV FADEFIFLPG NTLKDFEEGC YLLCKSEAIQ VTTKDILVTE 550
KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSE 587
Length:587
Mass (Da):67,046
Last modified:December 21, 2004 - v1
Checksum:i5D0D976411EA9F40
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei587 – 5871Imported

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL117352 Genomic DNA. No translation available.
AL137801 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000416000; ENSP00000411640; ENSG00000116906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL117352 Genomic DNA. No translation available.
AL137801 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortali Q5TBH8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1402298.

Proteomic databases

PRIDEi Q5TBH8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000416000 ; ENSP00000411640 ; ENSG00000116906 .

Organism-specific databases

HGNCi HGNC:4416. GNPAT.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000112751.
HOVERGENi HBG051749.

Miscellaneous databases

ChiTaRSi GNPAT. human.

Gene expression databases

ArrayExpressi Q5TBH8.

Family and domain databases

InterProi IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
PANTHERi PTHR12563. PTHR12563. 1 hit.
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , 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., 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., 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., 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., McLaren S., Milne S., Mistry S., Moore M.J., 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., 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., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiQ5TBH8_HUMAN
AccessioniPrimary (citable) accession number: Q5TBH8
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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