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Q92643

- GPI8_HUMAN

UniProt

Q92643 - GPI8_HUMAN

Protein

GPI-anchor transamidase

Gene

PIGK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (11 Jul 2002)
      Previous versions | rss
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    Functioni

    Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei164 – 16411 Publication
    Active sitei206 – 20611 Publication

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. GPI-anchor transamidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein disulfide isomerase activity Source: UniProtKB

    GO - Biological processi

    1. attachment of GPI anchor to protein Source: UniProtKB
    2. cellular protein metabolic process Source: Reactome
    3. C-terminal protein lipidation Source: Reactome
    4. post-translational protein modification Source: Reactome
    5. protein folding Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    GPI-anchor biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1830. Attachment of GPI anchor to uPAR.
    UniPathwayiUPA00196.

    Protein family/group databases

    MEROPSiC13.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GPI-anchor transamidase (EC:3.-.-.-)
    Short name:
    GPI transamidase
    Alternative name(s):
    GPI8 homolog
    Short name:
    hGPI8
    Phosphatidylinositol-glycan biosynthesis class K protein
    Short name:
    PIG-K
    Gene namesi
    Name:PIGK
    Synonyms:GPI8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8965. PIGK.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. GPI-anchor transamidase complex Source: UniProtKB
    3. integral component of endoplasmic reticulum membrane Source: UniProtKB
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921C → A: Partial loss of activity. 2 Publications
    Mutagenesisi92 – 921C → S: Decrease in activity. 2 Publications
    Mutagenesisi164 – 1641H → A: Loss of activity. 1 Publication
    Mutagenesisi206 – 2061C → A: Loss of activity. 1 Publication
    Mutagenesisi311 – 39585Missing: Loss of activity. Add
    BLAST

    Organism-specific databases

    PharmGKBiPA33296.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 395368GPI-anchor transamidasePRO_0000026529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi92 – 92Interchain (with C-182 in PIGT)1 Publication

    Post-translational modificationi

    The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ92643.
    PaxDbiQ92643.
    PRIDEiQ92643.

    PTM databases

    PhosphoSiteiQ92643.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92643.
    BgeeiQ92643.
    CleanExiHS_PIGK.
    GenevestigatoriQ92643.

    Organism-specific databases

    HPAiHPA056383.
    HPA057040.

    Interactioni

    Subunit structurei

    Forms a complex with PIGT, PIGS, PIGU and GAA1.2 Publications

    Protein-protein interaction databases

    BioGridi115343. 9 interactions.
    IntActiQ92643. 1 interaction.
    MINTiMINT-2813159.
    STRINGi9606.ENSP00000359848.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92643.
    SMRiQ92643. Positions 43-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 367340LumenalSequence AnalysisAdd
    BLAST
    Topological domaini389 – 3957CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei368 – 38821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni311 – 32111Essential for GPI attachmentAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C13 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5206.
    HOGENOMiHOG000204398.
    HOVERGENiHBG027488.
    InParanoidiQ92643.
    KOiK05290.
    OMAiNVLSMYR.
    OrthoDBiEOG70W3DZ.
    PhylomeDBiQ92643.
    TreeFamiTF300848.

    Family and domain databases

    InterProiIPR028361. GPI_transamidase.
    IPR001096. Peptidase_C13.
    [Graphical view]
    PANTHERiPTHR12000. PTHR12000. 1 hit.
    PfamiPF01650. Peptidase_C13. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500138. GPI8. 1 hit.
    PIRSF019663. Legumain. 1 hit.
    PRINTSiPR00776. HEMOGLOBNASE.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92643-1) [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

    MAVTDSLSRA ATVLATVLLL SFGSVAASHI EDQAEQFFRS GHTNNWAVLV    50
    CTSRFWFNYR HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNPRNPKPA 100
    TVFSHKNMEL NVYGDDVEVD YRSYEVTVEN FLRVLTGRIP PSTPRSKRLL 150
    SDDRSNILIY MTGHGGNGFL KFQDSEEITN IELADAFEQM WQKRRYNELL 200
    FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA IGVHLMDRYT 250
    FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI 300
    TDFFGSVRKV EITTETIKLQ QDSEIMESSY KEDQMDEKLM EPLKYAEQLP 350
    VAQIIHQKPK LKDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF 395
    Length:395
    Mass (Da):45,252
    Last modified:July 11, 2002 - v2
    Checksum:iAF706DDDAD13EFB2
    GO
    Isoform 2 (identifier: Q92643-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-125: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:319
    Mass (Da):36,416
    Checksum:i994A9F50C02CAEB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 44MAVT → SLHEA(PubMed:8978684)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161T → A.
    Corresponds to variant rs12723684 [ dbSNP | Ensembl ].
    VAR_051518

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 12576Missing in isoform 2. 1 PublicationVSP_056457Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07596 mRNA. Translation: CAA68871.1.
    AF022913 mRNA. Translation: AAB81597.1.
    AK304340 mRNA. Translation: BAG65185.1.
    AK313015 mRNA. Translation: BAG35850.1.
    AL035409, AC093433, AC113935 Genomic DNA. Translation: CAI21819.1.
    CH471059 Genomic DNA. Translation: EAX06380.1.
    BC020737 mRNA. Translation: AAH20737.1.
    CCDSiCCDS674.1.
    RefSeqiNP_005473.1. NM_005482.2.
    UniGeneiHs.178305.

    Genome annotation databases

    EnsembliENST00000370812; ENSP00000359848; ENSG00000142892.
    ENST00000370813; ENSP00000359849; ENSG00000142892.
    GeneIDi10026.
    KEGGihsa:10026.
    UCSCiuc001dhk.3. human.

    Polymorphism databases

    DMDMi22001630.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07596 mRNA. Translation: CAA68871.1 .
    AF022913 mRNA. Translation: AAB81597.1 .
    AK304340 mRNA. Translation: BAG65185.1 .
    AK313015 mRNA. Translation: BAG35850.1 .
    AL035409 , AC093433 , AC113935 Genomic DNA. Translation: CAI21819.1 .
    CH471059 Genomic DNA. Translation: EAX06380.1 .
    BC020737 mRNA. Translation: AAH20737.1 .
    CCDSi CCDS674.1.
    RefSeqi NP_005473.1. NM_005482.2.
    UniGenei Hs.178305.

    3D structure databases

    ProteinModelPortali Q92643.
    SMRi Q92643. Positions 43-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115343. 9 interactions.
    IntActi Q92643. 1 interaction.
    MINTi MINT-2813159.
    STRINGi 9606.ENSP00000359848.

    Protein family/group databases

    MEROPSi C13.005.

    PTM databases

    PhosphoSitei Q92643.

    Polymorphism databases

    DMDMi 22001630.

    Proteomic databases

    MaxQBi Q92643.
    PaxDbi Q92643.
    PRIDEi Q92643.

    Protocols and materials databases

    DNASUi 10026.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370812 ; ENSP00000359848 ; ENSG00000142892 .
    ENST00000370813 ; ENSP00000359849 ; ENSG00000142892 .
    GeneIDi 10026.
    KEGGi hsa:10026.
    UCSCi uc001dhk.3. human.

    Organism-specific databases

    CTDi 10026.
    GeneCardsi GC01M077554.
    HGNCi HGNC:8965. PIGK.
    HPAi HPA056383.
    HPA057040.
    MIMi 605087. gene.
    neXtProti NX_Q92643.
    PharmGKBi PA33296.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5206.
    HOGENOMi HOG000204398.
    HOVERGENi HBG027488.
    InParanoidi Q92643.
    KOi K05290.
    OMAi NVLSMYR.
    OrthoDBi EOG70W3DZ.
    PhylomeDBi Q92643.
    TreeFami TF300848.

    Enzyme and pathway databases

    UniPathwayi UPA00196 .
    Reactomei REACT_1830. Attachment of GPI anchor to uPAR.

    Miscellaneous databases

    ChiTaRSi PIGK. human.
    GeneWikii PIGK.
    GenomeRNAii 10026.
    NextBioi 37889.
    PROi Q92643.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92643.
    Bgeei Q92643.
    CleanExi HS_PIGK.
    Genevestigatori Q92643.

    Family and domain databases

    InterProi IPR028361. GPI_transamidase.
    IPR001096. Peptidase_C13.
    [Graphical view ]
    PANTHERi PTHR12000. PTHR12000. 1 hit.
    Pfami PF01650. Peptidase_C13. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500138. GPI8. 1 hit.
    PIRSF019663. Legumain. 1 hit.
    PRINTSi PR00776. HEMOGLOBNASE.
    ProtoNeti Search...

    Publicationsi

    1. "Yeast Gpi8p is essential for GPI anchor attachment onto proteins."
      Benghezal M., Benachour A., Rusconi S., Aebi M., Conzelmann A.
      EMBO J. 15:6575-6583(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase."
      Yu J., Nagarajan S., Knez J.J., Udenfriend S., Chen R., Medof M.E.
      Proc. Natl. Acad. Sci. U.S.A. 94:12580-12585(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum and Trachea.
    4. "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].
    5. 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).
      Tissue: Liver.
    7. "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins."
      Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., Kinoshita T.
      Mol. Biol. Cell 11:1523-1533(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, ACTIVE SITE, MUTAGENESIS OF CYS-92; HIS-164; CYS-206 AND 311-GLU--PHE-395.
    8. "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8."
      Ohishi K., Inoue N., Kinoshita T.
      EMBO J. 20:4088-4098(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-47, SUBUNIT, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
    9. "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge."
      Ohishi K., Nagamune K., Maeda Y., Kinoshita T.
      J. Biol. Chem. 278:13959-13967(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND FORMATION WITH PIGT, MUTAGENESIS OF CYS-92.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGPI8_HUMAN
    AccessioniPrimary (citable) accession number: Q92643
    Secondary accession number(s): B2R7K3
    , B4E2M3, O14822, Q5TG77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: July 11, 2002
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3