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O15228

- GNPAT_HUMAN

UniProt

O15228 - GNPAT_HUMAN

Protein

Dihydroxyacetone phosphate acyltransferase

Gene

GNPAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. paranodal junction assembly Source: Ensembl
    6. phosphatidic acid biosynthetic process Source: Reactome
    7. phospholipid metabolic process Source: Reactome
    8. response to drug Source: Ensembl
    9. response to fatty acid Source: Ensembl
    10. response to nutrient Source: Ensembl
    11. response to starvation Source: Ensembl
    12. small molecule metabolic process Source: Reactome
    13. synapse assembly Source: Ensembl

    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

    Keywords - Cellular componenti

    Membrane, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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

    ArrayExpressiO15228.
    BgeeiO15228.
    CleanExiHS_GNPAT.
    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. 8 interactions.
    IntActiO15228. 6 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.
    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

    MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF    50
    AMKCYTPLVY KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR 100
    EEVSEILDEM SHKLRLGAIR FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA 150
    IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL PVPVIAAGMD FLGMKMVGEL 200
    LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF FLEGTRSRSA 250
    KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV 300
    PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV 350
    PRYIPQKQSE DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM 400
    DFDALVEKTL WLKGLTQAFG GFLIWPDNKP AEEVVPASIL LHSNIASLVK 450
    DQVILKVDSG DSEVVDGLML QHITLLMCSA YRNQLLNIFV RPSLVAVALQ 500
    MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC YLLCKSEAIQ 550
    VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY 600
    LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC 650
    IFNVNEPATT KLEEMLGCKT PIGKPATAKL 680
    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_055051.1. NM_014236.3.
    XP_005273371.1. XM_005273314.2.
    UniGeneiHs.498028.

    Genome annotation databases

    EnsembliENST00000366646; ENSP00000355606; ENSG00000116906.
    ENST00000366647; ENSP00000355607; ENSG00000116906.
    GeneIDi8443.
    KEGGihsa:8443.
    UCSCiuc001hup.4. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1592.1.
    RefSeqi NP_055051.1. NM_014236.3.
    XP_005273371.1. XM_005273314.2.
    UniGenei Hs.498028.

    3D structure databases

    ProteinModelPortali O15228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114021. 8 interactions.
    IntActi O15228. 6 interactions.
    STRINGi 9606.ENSP00000355607.

    Chemistry

    BindingDBi O15228.
    ChEMBLi CHEMBL4494.

    PTM databases

    PhosphoSitei O15228.

    Proteomic databases

    MaxQBi O15228.
    PaxDbi O15228.
    PRIDEi O15228.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366646 ; ENSP00000355606 ; ENSG00000116906 .
    ENST00000366647 ; ENSP00000355607 ; ENSG00000116906 .
    GeneIDi 8443.
    KEGGi hsa:8443.
    UCSCi uc001hup.4. human.

    Organism-specific databases

    CTDi 8443.
    GeneCardsi GC01P231376.
    HGNCi HGNC:4416. GNPAT.
    HPAi HPA060059.
    MIMi 222765. phenotype.
    602744. gene.
    neXtProti NX_O15228.
    Orphaneti 309796. Rhizomelic chondrodysplasia punctata type 2.
    PharmGKBi PA28795.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2937.
    HOVERGENi HBG051749.
    InParanoidi O15228.
    KOi K00649.
    OMAi PRYIPQK.
    OrthoDBi EOG7CCBQT.
    PhylomeDBi O15228.
    TreeFami TF313360.

    Enzyme and pathway databases

    UniPathwayi UPA00940 .
    BRENDAi 2.3.1.42. 2681.
    Reactomei REACT_120906. Synthesis of PA.
    REACT_1407. Plasmalogen biosynthesis.

    Miscellaneous databases

    ChiTaRSi GNPAT. human.
    GenomeRNAii 8443.
    NextBioi 31586.
    PROi O15228.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15228.
    Bgeei O15228.
    CleanExi HS_GNPAT.
    Genevestigatori O15228.

    Family and domain databases

    InterProi IPR028353. DHAPAT.
    IPR022284. GPAT/DHAPAT.
    IPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view ]
    PANTHERi PTHR12563. PTHR12563. 1 hit.
    Pfami PF01553. Acyltransferase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500063. DHAPAT. 1 hit.
    PIRSF000437. GPAT_DHAPAT. 1 hit.
    SMARTi SM00563. PlsC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 140 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