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Q92535

- PIGC_HUMAN

UniProt

Q92535 - PIGC_HUMAN

Protein

Phosphatidylinositol N-acetylglucosaminyltransferase subunit C

Gene

PIGC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI 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. catalytic activity Source: ProtInc
    2. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. C-terminal protein lipidation Source: Reactome
    3. GPI anchor biosynthetic process Source: ProtInc
    4. post-translational protein modification Source: Reactome
    5. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase subunit C (EC:2.4.1.198)
    Alternative name(s):
    Phosphatidylinositol-glycan biosynthesis class C protein
    Short name:
    PIG-C
    Gene namesi
    Name:PIGC
    Synonyms:GPI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8960. PIGC.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33291.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Phosphatidylinositol N-acetylglucosaminyltransferase subunit CPRO_0000058431Add
    BLAST

    Proteomic databases

    MaxQBiQ92535.
    PaxDbiQ92535.
    PRIDEiQ92535.

    PTM databases

    PhosphoSiteiQ92535.

    Expressioni

    Gene expression databases

    BgeeiQ92535.
    CleanExiHS_PIGC.
    GenevestigatoriQ92535.

    Organism-specific databases

    HPAiHPA036663.

    Interactioni

    Subunit structurei

    Associates with PIGA, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity.

    Protein-protein interaction databases

    BioGridi111297. 3 interactions.
    IntActiQ92535. 2 interactions.
    MINTiMINT-1424659.
    STRINGi9606.ENSP00000258324.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92535.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei51 – 7121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei80 – 10021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei154 – 17421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei239 – 25921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PIGC family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG275923.
    HOGENOMiHOG000194668.
    HOVERGENiHBG009071.
    InParanoidiQ92535.
    KOiK03859.
    OMAiNIHARKY.
    OrthoDBiEOG7KSX8X.
    PhylomeDBiQ92535.
    TreeFamiTF314325.

    Family and domain databases

    InterProiIPR009450. Plno_GlcNAc_GPI2.
    [Graphical view]
    PANTHERiPTHR12982. PTHR12982. 1 hit.
    PfamiPF06432. GPI2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016104. GPI2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q92535-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYAQPVTNTK EVKWQKVLYE RQPFPDNYVD RRFLEELRKN IHARKYQYWA    50
    VVFESSVVIQ QLCSVCVFVV IWWYMDEGLL APHWLLGTGL ASSLIGYVLF 100
    DLIDGGEGRK KSGQTRWADL KSALVFITFT YGFSPVLKTL TESVSTDTIY 150
    AMSVFMLLGH LIFFDYGANA AIVSSTLSLN MAIFASVCLA SRLPRSLHAF 200
    IMVTFAIQIF ALWPMLQKKL KACTPRSYVG VTLLFAFSAV GGLLSISAVG 250
    AVLFALLLMS ISCLCPFYLI RLQLFKENIH GPWDEAEIKE DLSRFLS 297
    Length:297
    Mass (Da):33,583
    Last modified:February 1, 1997 - v1
    Checksum:iBD9584C5D5203A4B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti266 – 2661P → S.1 Publication
    Corresponds to variant rs1063412 [ dbSNP | Ensembl ].
    VAR_011360

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85418 mRNA. Translation: BAA12812.1.
    AB000360 Genomic DNA. Translation: BAA22866.1.
    BT006734 mRNA. Translation: AAP35380.1.
    CR450292 mRNA. Translation: CAG29288.1.
    Z97195 Genomic DNA. Translation: CAB10071.1.
    BC006539 mRNA. Translation: AAH06539.1.
    CCDSiCCDS1302.1.
    PIRiJC4969.
    RefSeqiNP_002633.1. NM_002642.3.
    NP_714969.1. NM_153747.1.
    XP_006711446.1. XM_006711383.1.
    UniGeneiHs.188456.

    Genome annotation databases

    EnsembliENST00000344529; ENSP00000356701; ENSG00000135845.
    ENST00000367728; ENSP00000356702; ENSG00000135845.
    GeneIDi5279.
    KEGGihsa:5279.
    UCSCiuc001gin.3. human.

    Polymorphism databases

    DMDMi14916629.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Phosphatidylinositol N-acetylglucosaminyltransferase subunit C8

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85418 mRNA. Translation: BAA12812.1 .
    AB000360 Genomic DNA. Translation: BAA22866.1 .
    BT006734 mRNA. Translation: AAP35380.1 .
    CR450292 mRNA. Translation: CAG29288.1 .
    Z97195 Genomic DNA. Translation: CAB10071.1 .
    BC006539 mRNA. Translation: AAH06539.1 .
    CCDSi CCDS1302.1.
    PIRi JC4969.
    RefSeqi NP_002633.1. NM_002642.3.
    NP_714969.1. NM_153747.1.
    XP_006711446.1. XM_006711383.1.
    UniGenei Hs.188456.

    3D structure databases

    ProteinModelPortali Q92535.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111297. 3 interactions.
    IntActi Q92535. 2 interactions.
    MINTi MINT-1424659.
    STRINGi 9606.ENSP00000258324.

    PTM databases

    PhosphoSitei Q92535.

    Polymorphism databases

    DMDMi 14916629.

    Proteomic databases

    MaxQBi Q92535.
    PaxDbi Q92535.
    PRIDEi Q92535.

    Protocols and materials databases

    DNASUi 5279.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344529 ; ENSP00000356701 ; ENSG00000135845 .
    ENST00000367728 ; ENSP00000356702 ; ENSG00000135845 .
    GeneIDi 5279.
    KEGGi hsa:5279.
    UCSCi uc001gin.3. human.

    Organism-specific databases

    CTDi 5279.
    GeneCardsi GC01M172339.
    HGNCi HGNC:8960. PIGC.
    HPAi HPA036663.
    MIMi 601730. gene.
    neXtProti NX_Q92535.
    PharmGKBi PA33291.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275923.
    HOGENOMi HOG000194668.
    HOVERGENi HBG009071.
    InParanoidi Q92535.
    KOi K03859.
    OMAi NIHARKY.
    OrthoDBi EOG7KSX8X.
    PhylomeDBi Q92535.
    TreeFami TF314325.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii PIGC.
    GenomeRNAii 5279.
    NextBioi 20400.
    PROi Q92535.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92535.
    CleanExi HS_PIGC.
    Genevestigatori Q92535.

    Family and domain databases

    InterProi IPR009450. Plno_GlcNAc_GPI2.
    [Graphical view ]
    PANTHERi PTHR12982. PTHR12982. 1 hit.
    Pfami PF06432. GPI2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016104. GPI2. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2."
      Inoue N., Watanabe R., Takeda J., Kinoshita T.
      Biochem. Biophys. Res. Commun. 226:193-199(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1."
      Hong Y., Ohishi K., Inoue N., Endo Y., Fujita T., Takeda J., Kinoshita T.
      Genomics 44:347-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-266.
      Tissue: Fibroblast.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Lung.

    Entry informationi

    Entry nameiPIGC_HUMAN
    AccessioniPrimary (citable) accession number: Q92535
    Secondary accession number(s): O14491
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 122 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 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