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P37287

- PIGA_HUMAN

UniProt

P37287 - PIGA_HUMAN

Protein

Phosphatidylinositol N-acetylglucosaminyltransferase subunit A

Gene

PIGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

    Pathwayi

    GO - Molecular functioni

    1. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: HGNC
    2. protein binding Source: HGNC
    3. UDP-glycosyltransferase activity Source: Reactome

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. C-terminal protein lipidation Source: Reactome
    3. GPI anchor biosynthetic process Source: HGNC
    4. positive regulation of metabolic process Source: HGNC
    5. post-translational protein modification Source: Reactome
    6. preassembly of GPI anchor in ER membrane Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    GPI-anchor biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
    UniPathwayiUPA00196.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase subunit A (EC:2.4.1.198)
    Alternative name(s):
    GlcNAc-PI synthesis protein
    Phosphatidylinositol-glycan biosynthesis class A protein
    Short name:
    PIG-A
    Gene namesi
    Name:PIGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8957. PIGA.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: HGNC
    2. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: HGNC
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Paroxysmal nocturnal hemoglobinuria 1 (PNH1) [MIM:300818]: A disorder characterized by hemolytic anemia with hemoglobinuria, thromboses in large vessels, and a deficiency in hematopoiesis. Red blood cell breakdown with release of hemoglobin into the urine is manifested most prominently by dark-colored urine in the morning.5 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191R → W in PNH1. 1 Publication
    Corresponds to variant rs34422225 [ dbSNP | Ensembl ].
    VAR_015442
    Natural varianti40 – 401D → H in PNH1. 1 Publication
    VAR_015436
    Natural varianti48 – 481G → A in PNH1. 1 Publication
    VAR_015437
    Natural varianti48 – 481G → D in PNH1. 1 Publication
    VAR_015438
    Natural varianti48 – 481G → V in PNH1. 1 Publication
    VAR_015439
    Natural varianti128 – 1281H → R in PNH1. 1 Publication
    VAR_015440
    Natural varianti155 – 1551S → F in PNH1. 1 Publication
    VAR_005531
    Natural varianti239 – 2391G → R in PNH1. 1 Publication
    VAR_015441
    Natural varianti297 – 2971N → D in PNH1. 1 Publication
    VAR_005532
    Multiple congenital anomalies-hypotonia-seizures syndrome 2 (MCAHS2) [MIM:300868]: An X-linked recessive developmental disorder characterized by dysmorphic features, neonatal hypotonia, myoclonic seizures, and variable congenital anomalies involving the central nervous, cardiac, and urinary systems. Most affected individuals die in infancy.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771R → L in MCAHS2. 1 Publication
    VAR_071069
    Natural varianti93 – 931P → L in MCAHS2. 1 Publication
    VAR_071070
    Natural varianti119 – 1191R → W in MCAHS2. 1 Publication
    VAR_071071
    Natural varianti206 – 2061I → F in MCAHS2. 1 Publication
    VAR_071072
    Natural varianti344 – 3441Missing in MCAHS2. 1 Publication
    VAR_071073

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi300818. phenotype.
    300868. phenotype.
    Orphaneti300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2.
    447. Paroxysmal nocturnal hemoglobinuria.
    3451. West syndrome.
    PharmGKBiPA33288.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Phosphatidylinositol N-acetylglucosaminyltransferase subunit APRO_0000080326Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP37287.
    PaxDbiP37287.
    PRIDEiP37287.

    PTM databases

    PhosphoSiteiP37287.

    Expressioni

    Gene expression databases

    ArrayExpressiP37287.
    BgeeiP37287.
    CleanExiHS_PIGA.
    GenevestigatoriP37287.

    Organism-specific databases

    HPAiHPA001174.

    Interactioni

    Subunit structurei

    Associates with PIGC, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity. Interacts directly with PIGY.1 Publication

    Protein-protein interaction databases

    BioGridi111295. 6 interactions.
    STRINGi9606.ENSP00000369820.

    Structurei

    3D structure databases

    ProteinModelPortaliP37287.
    SMRiP37287. Positions 43-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 421421CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini443 – 48442LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei422 – 44221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0438.
    HOGENOMiHOG000203293.
    HOVERGENiHBG008198.
    InParanoidiP37287.
    KOiK03857.
    OMAiHTGRENT.
    OrthoDBiEOG7DC24J.
    PhylomeDBiP37287.
    TreeFamiTF105675.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    IPR013234. PIGA_GPI_anchor_biosynthesis.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    PF08288. PIGA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P37287-1) [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

    MACRGGAGNG HRASATLSRV SPGSLYTCRT RTHNICMVSD FFYPNMGGVE    50
    SHIYQLSQCL IERGHKVIIV THAYGNRKGI RYLTSGLKVY YLPLKVMYNQ 100
    STATTLFHSL PLLRYIFVRE RVTIIHSHSS FSAMAHDALF HAKTMGLQTV 150
    FTDHSLFGFA DVSSVLTNKL LTVSLCDTNH IICVSYTSKE NTVLRAALNP 200
    EIVSVIPNAV DPTDFTPDPF RRHDSITIVV VSRLVYRKGI DLLSGIIPEL 250
    CQKYPDLNFI IGGEGPKRII LEEVRERYQL HDRVRLLGAL EHKDVRNVLV 300
    QGHIFLNTSL TEAFCMAIVE AASCGLQVVS TRVGGIPEVL PENLIILCEP 350
    SVKSLCEGLE KAIFQLKSGT LPAPENIHNI VKTFYTWRNV AERTEKVYDR 400
    VSVEAVLPMD KRLDRLISHC GPVTGYIFAL LAVFNFLFLI FLRWMTPDSI 450
    IDVAIDATGP RGAWTNNYSH SKRGGENNEI SETR 484
    Length:484
    Mass (Da):54,127
    Last modified:October 1, 1994 - v1
    Checksum:i34DCD074A3920852
    GO
    Isoform 2 (identifier: P37287-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         115-283: Missing.

    Show »
    Length:315
    Mass (Da):35,078
    Checksum:i3F443EA94F271865
    GO
    Isoform 3 (identifier: P37287-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MACR → MELT
         5-238: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:250
    Mass (Da):28,034
    Checksum:i78823EE49BCD9AF6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191R → W in PNH1. 1 Publication
    Corresponds to variant rs34422225 [ dbSNP | Ensembl ].
    VAR_015442
    Natural varianti40 – 401D → H in PNH1. 1 Publication
    VAR_015436
    Natural varianti48 – 481G → A in PNH1. 1 Publication
    VAR_015437
    Natural varianti48 – 481G → D in PNH1. 1 Publication
    VAR_015438
    Natural varianti48 – 481G → V in PNH1. 1 Publication
    VAR_015439
    Natural varianti77 – 771R → L in MCAHS2. 1 Publication
    VAR_071069
    Natural varianti93 – 931P → L in MCAHS2. 1 Publication
    VAR_071070
    Natural varianti119 – 1191R → W in MCAHS2. 1 Publication
    VAR_071071
    Natural varianti128 – 1281H → R in PNH1. 1 Publication
    VAR_015440
    Natural varianti155 – 1551S → F in PNH1. 1 Publication
    VAR_005531
    Natural varianti206 – 2061I → F in MCAHS2. 1 Publication
    VAR_071072
    Natural varianti239 – 2391G → R in PNH1. 1 Publication
    VAR_015441
    Natural varianti297 – 2971N → D in PNH1. 1 Publication
    VAR_005532
    Natural varianti344 – 3441Missing in MCAHS2. 1 Publication
    VAR_071073

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MACR → MELT in isoform 3. 1 PublicationVSP_043366
    Alternative sequencei5 – 238234Missing in isoform 3. 1 PublicationVSP_043367Add
    BLAST
    Alternative sequencei115 – 283169Missing in isoform 2. 1 PublicationVSP_001802Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11466 mRNA. Translation: BAA02019.1.
    X77725
    , X77726, X77727, X77728 Genomic DNA. Translation: CAB57276.1. Sequence problems.
    D28791 Genomic DNA. Translation: BAA05966.1.
    S74936 mRNA. Translation: AAD14160.1.
    AK303538 mRNA. Translation: BAG64564.1.
    AC095351 Genomic DNA. No translation available.
    BC038236 mRNA. Translation: AAH38236.1.
    S61523 mRNA. Translation: AAD13929.1.
    CCDSiCCDS14165.1. [P37287-1]
    CCDS48086.2. [P37287-3]
    PIRiA46217.
    RefSeqiNP_002632.1. NM_002641.3. [P37287-1]
    NP_065206.3. NM_020473.3. [P37287-3]
    UniGeneiHs.137154.

    Genome annotation databases

    EnsembliENST00000333590; ENSP00000369820; ENSG00000165195. [P37287-1]
    ENST00000542278; ENSP00000442653; ENSG00000165195. [P37287-3]
    GeneIDi5277.
    KEGGihsa:5277.
    UCSCiuc004cwr.3. human. [P37287-1]
    uc010nev.3. human. [P37287-2]
    uc011miq.2. human. [P37287-3]

    Polymorphism databases

    DMDMi585696.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Phosphatidylinositol N-acetylglucosaminyltransferase subunit A

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11466 mRNA. Translation: BAA02019.1 .
    X77725
    , X77726 , X77727 , X77728 Genomic DNA. Translation: CAB57276.1 . Sequence problems.
    D28791 Genomic DNA. Translation: BAA05966.1 .
    S74936 mRNA. Translation: AAD14160.1 .
    AK303538 mRNA. Translation: BAG64564.1 .
    AC095351 Genomic DNA. No translation available.
    BC038236 mRNA. Translation: AAH38236.1 .
    S61523 mRNA. Translation: AAD13929.1 .
    CCDSi CCDS14165.1. [P37287-1 ]
    CCDS48086.2. [P37287-3 ]
    PIRi A46217.
    RefSeqi NP_002632.1. NM_002641.3. [P37287-1 ]
    NP_065206.3. NM_020473.3. [P37287-3 ]
    UniGenei Hs.137154.

    3D structure databases

    ProteinModelPortali P37287.
    SMRi P37287. Positions 43-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111295. 6 interactions.
    STRINGi 9606.ENSP00000369820.

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    PTM databases

    PhosphoSitei P37287.

    Polymorphism databases

    DMDMi 585696.

    Proteomic databases

    MaxQBi P37287.
    PaxDbi P37287.
    PRIDEi P37287.

    Protocols and materials databases

    DNASUi 5277.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333590 ; ENSP00000369820 ; ENSG00000165195 . [P37287-1 ]
    ENST00000542278 ; ENSP00000442653 ; ENSG00000165195 . [P37287-3 ]
    GeneIDi 5277.
    KEGGi hsa:5277.
    UCSCi uc004cwr.3. human. [P37287-1 ]
    uc010nev.3. human. [P37287-2 ]
    uc011miq.2. human. [P37287-3 ]

    Organism-specific databases

    CTDi 5277.
    GeneCardsi GC0XM015337.
    HGNCi HGNC:8957. PIGA.
    HPAi HPA001174.
    MIMi 300818. phenotype.
    300868. phenotype.
    311770. gene.
    neXtProti NX_P37287.
    Orphaneti 300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2.
    447. Paroxysmal nocturnal hemoglobinuria.
    3451. West syndrome.
    PharmGKBi PA33288.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0438.
    HOGENOMi HOG000203293.
    HOVERGENi HBG008198.
    InParanoidi P37287.
    KOi K03857.
    OMAi HTGRENT.
    OrthoDBi EOG7DC24J.
    PhylomeDBi P37287.
    TreeFami TF105675.

    Enzyme and pathway databases

    UniPathwayi UPA00196 .
    Reactomei REACT_952. Synthesis of glycosylphosphatidylinositol (GPI).

    Miscellaneous databases

    GeneWikii PIGA.
    GenomeRNAii 5277.
    NextBioi 20392.
    PROi P37287.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37287.
    Bgeei P37287.
    CleanExi HS_PIGA.
    Genevestigatori P37287.

    Family and domain databases

    InterProi IPR001296. Glyco_trans_1.
    IPR013234. PIGA_GPI_anchor_biosynthesis.
    [Graphical view ]
    Pfami PF00534. Glycos_transf_1. 1 hit.
    PF08288. PIGA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis."
      Miyata T., Takeda J., Iida Y., Yamada N., Inoue N., Takahashi M., Maeda K., Kitani T., Kinoshita T.
      Science 259:1318-1320(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21."
      Bessler M., Hillmen P., Longo L., Luzzatto L., Mason P.J.
      Hum. Mol. Genet. 3:751-757(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria."
      Iida Y., Takeda J., Miyata T., Inoue N., Nishimura J., Kitani T., Maeda K., Kinoshita T.
      Blood 83:3126-3131(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells."
      Yu J., Nagarajan S., Ueda E., Knez J.J., Petersen R.B., Medof M.E.
      Braz. J. Med. Biol. Res. 27:195-201(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "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 3).
      Tissue: Thymus.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Brain.
    8. "Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria."
      Takeda J., Miyata T., Kawagoe K., Iida Y., Endo Y., Fujita T., Takahashi M., Kitani T., Kinoshita T.
      Cell 73:703-711(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-420, INVOLVEMENT IN PNH1.
    9. "The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component."
      Murakami Y., Siripanyaphinyo U., Hong Y., Tashima Y., Maeda Y., Kinoshita T.
      Mol. Biol. Cell 16:5236-5246(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIGY.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "The phenotype of a germline mutation in PIGA: the gene somatically mutated in paroxysmal nocturnal hemoglobinuria."
      Johnston J.J., Gropman A.L., Sapp J.C., Teer J.K., Martin J.M., Liu C.F., Yuan X., Ye Z., Cheng L., Brodsky R.A., Biesecker L.G.
      Am. J. Hum. Genet. 90:295-300(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MCAHS2.
    12. "Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene."
      Bessler M., Mason P.J., Hilmen P., Miyata T., Yamada N., Takeda J., Luzzato L., Kinoshita T.
      EMBO J. 13:110-117(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PNH1 PHE-155.
    13. "Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria."
      Ware R.E., Rosse W.F., Howard T.A.
      Blood 83:2418-2422(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PNH1 ASP-297.
    14. "The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications."
      Nafa K., Bessler M., Castro-Malaspina H., Jhanwar S., Luzzatto L.
      Blood Cells Mol. Dis. 24:370-384(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PNH1 TRP-19; HIS-40; ALA-48; ASP-48; ARG-128 AND ARG-239.
    15. "Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria."
      Yoon J.H., Cho H.I., Park S.S., Chang Y.H., Kim B.K.
      J. Clin. Pathol. 55:410-413(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PNH1 VAL-48.
    16. "A novel germline PIGA mutation in Ferro-Cerebro-Cutaneous syndrome: a neurodegenerative X-linked epileptic encephalopathy with systemic iron-overload."
      Swoboda K.J., Margraf R.L., Carey J.C., Zhou H., Newcomb T.M., Coonrod E., Durtschi J., Mallempati K., Kumanovics A., Katz B.E., Voelkerding K.V., Opitz J.M.
      Am. J. Med. Genet. A 164A:17-28(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MCAHS2 LEU-344 DEL.
    17. "Expanding the spectrum of phenotypes associated with germline PIGA mutations: a child with developmental delay, accelerated linear growth, facial dysmorphisms, elevated alkaline phosphatase, and progressive CNS abnormalities."
      van der Crabben S.N., Harakalova M., Brilstra E.H., van Berkestijn F.M., Hofstede F.C., van Vught A.J., Cuppen E., Kloosterman W., Ploos van Amstel H.K., van Haaften G., van Haelst M.M.
      Am. J. Med. Genet. A 164A:29-35(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MCAHS2 LEU-93.
    18. Cited for: VARIANTS MCAHS2 LEU-77; TRP-119 AND PHE-206.

    Entry informationi

    Entry nameiPIGA_HUMAN
    AccessioniPrimary (citable) accession number: P37287
    Secondary accession number(s): B4E0V2, Q16025, Q16250
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 138 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, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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

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