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Q92643

- GPI8_HUMAN

UniProt

Q92643 - GPI8_HUMAN

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Protein
GPI-anchor transamidase
Gene
PIGK, GPI8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

GO - Biological processi

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

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; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 367340Lumenal Reviewed prediction
Add
BLAST
Transmembranei368 – 38821Helical; Reviewed prediction
Add
BLAST
Topological domaini389 – 3957Cytoplasmic Reviewed prediction

GO - Cellular componenti

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

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. 1 Publication
Add
BLAST

Organism-specific databases

PharmGKBiPA33296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 Publication
Add
BLAST
Chaini28 – 395368GPI-anchor transamidase
PRO_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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase C13 family.

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.

Sequencei

Sequence statusi: Complete.

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

Q92643-1 [UniParc]FASTAAdd to Basket

« 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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MAVT → SLHEA1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07596 mRNA. Translation: CAA68871.1.
AF022913 mRNA. Translation: AAB81597.1.
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.
GeneIDi10026.
KEGGihsa:10026.
UCSCiuc001dhk.3. human.

Polymorphism databases

DMDMi22001630.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07596 mRNA. Translation: CAA68871.1 .
AF022913 mRNA. Translation: AAB81597.1 .
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 .
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

« Hide 'large scale' publications
  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].
  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].
  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].
    Tissue: Cerebellum.
  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].
    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, O14822, Q5TG77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: September 3, 2014
This is version 120 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

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