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Protein

Dihydroxyacetone phosphate acyltransferase

Gene

GNPAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. glycerone-phosphate O-acyltransferase activity Source: UniProtKB
  2. palmitoyl-CoA hydrolase activity Source: UniProtKB
  3. receptor binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. cerebellum morphogenesis Source: Ensembl
  3. ether lipid biosynthetic process Source: UniProtKB
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. membrane organization Source: Ensembl
  6. paranodal junction assembly Source: Ensembl
  7. phosphatidic acid biosynthetic process Source: Reactome
  8. phospholipid metabolic process Source: Reactome
  9. response to drug Source: Ensembl
  10. response to fatty acid Source: Ensembl
  11. response to nutrient Source: Ensembl
  12. response to starvation Source: Ensembl
  13. small molecule metabolic process Source: Reactome
  14. synapse assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.42. 2681.
ReactomeiREACT_120906. Synthesis of PA.
REACT_1407. Plasmalogen biosynthesis.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxyacetone phosphate acyltransferase (EC:2.3.1.42)
Short name:
DAP-AT
Short name:
DHAP-AT
Alternative name(s):
Acyl-CoA:dihydroxyacetonephosphateacyltransferase
Glycerone-phosphate O-acyltransferase
Gene namesi
Name:GNPAT
Synonyms:DAPAT, DHAPAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4416. GNPAT.

Subcellular locationi

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

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. mitochondrion Source: Ensembl
  3. peroxisomal matrix Source: Reactome
  4. peroxisomal membrane Source: UniProtKB
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Rhizomelic chondrodysplasia punctata 23 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation.

See also OMIM:222765
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111R → C in RCDP2. 1 Publication
Corresponds to variant rs28939697 [ dbSNP | Ensembl ].
VAR_006357
Natural varianti211 – 2111R → H in RCDP2; complete loss of activity. 2 Publications
Corresponds to variant rs28939696 [ dbSNP | Ensembl ].
VAR_006358
Natural varianti519 – 5191D → G in RCDP2; 70% reduction in activity. 1 Publication
Corresponds to variant rs11558492 [ dbSNP | Ensembl ].
VAR_025897

Keywords - Diseasei

Cataract, Disease mutation, Dwarfism, Rhizomelic chondrodysplasia punctata

Organism-specific databases

MIMi222765. phenotype.
Orphaneti309796. Rhizomelic chondrodysplasia punctata type 2.
PharmGKBiPA28795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 680680Dihydroxyacetone phosphate acyltransferasePRO_0000195246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei643 – 6431N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO15228.
PaxDbiO15228.
PRIDEiO15228.

PTM databases

PhosphoSiteiO15228.

Expressioni

Gene expression databases

BgeeiO15228.
CleanExiHS_GNPAT.
ExpressionAtlasiO15228. baseline and differential.
GenevestigatoriO15228.

Organism-specific databases

HPAiHPA060059.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi114021. 14 interactions.
IntActiO15228. 7 interactions.
STRINGi9606.ENSP00000355607.

Structurei

3D structure databases

ProteinModelPortaliO15228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi162 – 1676HXXXXD motif
Motifi678 – 6803Microbody targeting signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 97Poly-Ser

Domaini

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

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.Curated

Phylogenomic databases

eggNOGiCOG2937.
GeneTreeiENSGT00520000055570.
HOVERGENiHBG051749.
InParanoidiO15228.
KOiK00649.
OMAiPRYIPQK.
OrthoDBiEOG7CCBQT.
PhylomeDBiO15228.
TreeFamiTF313360.

Family and domain databases

InterProiIPR028353. DHAPAT.
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500063. DHAPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15228-1) [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
MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF
60 70 80 90 100
AMKCYTPLVY KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR
110 120 130 140 150
EEVSEILDEM SHKLRLGAIR FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA
160 170 180 190 200
IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL PVPVIAAGMD FLGMKMVGEL
210 220 230 240 250
LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF FLEGTRSRSA
260 270 280 290 300
KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV
310 320 330 340 350
PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV
360 370 380 390 400
PRYIPQKQSE DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM
410 420 430 440 450
DFDALVEKTL WLKGLTQAFG GFLIWPDNKP AEEVVPASIL LHSNIASLVK
460 470 480 490 500
DQVILKVDSG DSEVVDGLML QHITLLMCSA YRNQLLNIFV RPSLVAVALQ
510 520 530 540 550
MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC YLLCKSEAIQ
560 570 580 590 600
VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY
610 620 630 640 650
LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC
660 670 680
IFNVNEPATT KLEEMLGCKT PIGKPATAKL
Length:680
Mass (Da):77,188
Last modified:January 1, 1998 - v1
Checksum:iBDF624CCD4D92477
GO
Isoform 2 (identifier: O15228-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-87: Missing.

Note: No experimental confirmation available.

Show »
Length:619
Mass (Da):69,906
Checksum:i50737E7FF854E8FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261S → K AA sequence (PubMed:9536089)Curated
Sequence conflicti31 – 311K → N AA sequence (PubMed:9536089)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111R → C in RCDP2. 1 Publication
Corresponds to variant rs28939697 [ dbSNP | Ensembl ].
VAR_006357
Natural varianti211 – 2111R → H in RCDP2; complete loss of activity. 2 Publications
Corresponds to variant rs28939696 [ dbSNP | Ensembl ].
VAR_006358
Natural varianti495 – 4951V → I.
Corresponds to variant rs11122266 [ dbSNP | Ensembl ].
VAR_030696
Natural varianti519 – 5191D → G in RCDP2; 70% reduction in activity. 1 Publication
Corresponds to variant rs11558492 [ dbSNP | Ensembl ].
VAR_025897
Natural varianti586 – 5861Y → H.1 Publication
Corresponds to variant rs17849315 [ dbSNP | Ensembl ].
VAR_030697

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 8761Missing in isoform 2. 1 PublicationVSP_056435Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002190 mRNA. Translation: CAA05242.1.
AF043937 mRNA. Translation: AAC24505.1.
AF218233
, AF218223, AF218224, AF218225, AF218226, AF218227, AF218228, AF218229, AF218230, AF218231, AF218232 Genomic DNA. Translation: AAG17547.1.
AK297982 mRNA. Translation: BAG60291.1.
AL137801, AL117352 Genomic DNA. Translation: CAI21988.1.
AL117352, AL137801 Genomic DNA. Translation: CAI23094.1.
BC000450 mRNA. Translation: AAH00450.1.
CCDSiCCDS1592.1. [O15228-1]
RefSeqiNP_055051.1. NM_014236.3. [O15228-1]
XP_005273371.1. XM_005273314.2. [O15228-2]
UniGeneiHs.498028.

Genome annotation databases

EnsembliENST00000366647; ENSP00000355607; ENSG00000116906. [O15228-1]
GeneIDi8443.
KEGGihsa:8443.
UCSCiuc001hup.4. human. [O15228-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002190 mRNA. Translation: CAA05242.1.
AF043937 mRNA. Translation: AAC24505.1.
AF218233
, AF218223, AF218224, AF218225, AF218226, AF218227, AF218228, AF218229, AF218230, AF218231, AF218232 Genomic DNA. Translation: AAG17547.1.
AK297982 mRNA. Translation: BAG60291.1.
AL137801, AL117352 Genomic DNA. Translation: CAI21988.1.
AL117352, AL137801 Genomic DNA. Translation: CAI23094.1.
BC000450 mRNA. Translation: AAH00450.1.
CCDSiCCDS1592.1. [O15228-1]
RefSeqiNP_055051.1. NM_014236.3. [O15228-1]
XP_005273371.1. XM_005273314.2. [O15228-2]
UniGeneiHs.498028.

3D structure databases

ProteinModelPortaliO15228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114021. 14 interactions.
IntActiO15228. 7 interactions.
STRINGi9606.ENSP00000355607.

Chemistry

BindingDBiO15228.
ChEMBLiCHEMBL4494.

PTM databases

PhosphoSiteiO15228.

Proteomic databases

MaxQBiO15228.
PaxDbiO15228.
PRIDEiO15228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366647; ENSP00000355607; ENSG00000116906. [O15228-1]
GeneIDi8443.
KEGGihsa:8443.
UCSCiuc001hup.4. human. [O15228-1]

Organism-specific databases

CTDi8443.
GeneCardsiGC01P231376.
HGNCiHGNC:4416. GNPAT.
HPAiHPA060059.
MIMi222765. phenotype.
602744. gene.
neXtProtiNX_O15228.
Orphaneti309796. Rhizomelic chondrodysplasia punctata type 2.
PharmGKBiPA28795.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2937.
GeneTreeiENSGT00520000055570.
HOVERGENiHBG051749.
InParanoidiO15228.
KOiK00649.
OMAiPRYIPQK.
OrthoDBiEOG7CCBQT.
PhylomeDBiO15228.
TreeFamiTF313360.

Enzyme and pathway databases

UniPathwayiUPA00940.
BRENDAi2.3.1.42. 2681.
ReactomeiREACT_120906. Synthesis of PA.
REACT_1407. Plasmalogen biosynthesis.

Miscellaneous databases

ChiTaRSiGNPAT. human.
GenomeRNAii8443.
NextBioi31586.
PROiO15228.
SOURCEiSearch...

Gene expression databases

BgeeiO15228.
CleanExiHS_GNPAT.
ExpressionAtlasiO15228. baseline and differential.
GenevestigatoriO15228.

Family and domain databases

InterProiIPR028353. DHAPAT.
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500063. DHAPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1), 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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "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.
    , 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].
  6. "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] (ISOFORM 1), VARIANT HIS-586.
    Tissue: Lung.
  7. "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].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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.

Entry informationi

Entry nameiGNPAT_HUMAN
AccessioniPrimary (citable) accession number: O15228
Secondary accession number(s): B4DNM9, Q5TBH7, Q9BWC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.