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P37287 (PIGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PIGA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Associates with PIGC, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity. Interacts directly with PIGY. Ref.9

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein.

Involvement in disease

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8 Ref.12 Ref.13 Ref.14 Ref.15

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

GPI anchor biosynthetic process

Traceable author statement Ref.9. Source: HGNC

cellular protein metabolic process

Traceable author statement. Source: Reactome

positive regulation of metabolic process

Traceable author statement Ref.9. Source: HGNC

post-translational protein modification

Traceable author statement. Source: Reactome

preassembly of GPI anchor in ER membrane

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Inferred from direct assay Ref.9. Source: HGNC

glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex

Inferred from direct assay Ref.9. Source: HGNC

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionUDP-glycosyltransferase activity

Traceable author statement. Source: Reactome

phosphatidylinositol N-acetylglucosaminyltransferase activity

Traceable author statement Ref.9. Source: HGNC

protein binding

Inferred from physical interaction Ref.9. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P37287-1)

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.
Isoform 2 (identifier: P37287-2)

The sequence of this isoform differs from the canonical sequence as follows:
     115-283: Missing.
Isoform 3 (identifier: P37287-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MACR → MELT
     5-238: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
PRO_0000080326

Regions

Topological domain1 – 421421Cytoplasmic Potential
Transmembrane422 – 44221Helical; Potential
Topological domain443 – 48442Lumenal Potential

Amino acid modifications

Modified residue211Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 44MACR → MELT in isoform 3.
VSP_043366
Alternative sequence5 – 238234Missing in isoform 3.
VSP_043367
Alternative sequence115 – 283169Missing in isoform 2.
VSP_001802
Natural variant191R → W in PNH1. Ref.14
Corresponds to variant rs34422225 [ dbSNP | Ensembl ].
VAR_015442
Natural variant401D → H in PNH1. Ref.14
VAR_015436
Natural variant481G → A in PNH1. Ref.14
VAR_015437
Natural variant481G → D in PNH1. Ref.14
VAR_015438
Natural variant481G → V in PNH1. Ref.15
VAR_015439
Natural variant1281H → R in PNH1. Ref.14
VAR_015440
Natural variant1551S → F in PNH1. Ref.12
VAR_005531
Natural variant2391G → R in PNH1. Ref.14
VAR_015441
Natural variant2971N → D in PNH1. Ref.13
VAR_005532

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 34DCD074A3920852

FASTA48454,127
        10         20         30         40         50         60 
MACRGGAGNG HRASATLSRV SPGSLYTCRT RTHNICMVSD FFYPNMGGVE SHIYQLSQCL 

        70         80         90        100        110        120 
IERGHKVIIV THAYGNRKGI RYLTSGLKVY YLPLKVMYNQ STATTLFHSL PLLRYIFVRE 

       130        140        150        160        170        180 
RVTIIHSHSS FSAMAHDALF HAKTMGLQTV FTDHSLFGFA DVSSVLTNKL LTVSLCDTNH 

       190        200        210        220        230        240 
IICVSYTSKE NTVLRAALNP EIVSVIPNAV DPTDFTPDPF RRHDSITIVV VSRLVYRKGI 

       250        260        270        280        290        300 
DLLSGIIPEL CQKYPDLNFI IGGEGPKRII LEEVRERYQL HDRVRLLGAL EHKDVRNVLV 

       310        320        330        340        350        360 
QGHIFLNTSL TEAFCMAIVE AASCGLQVVS TRVGGIPEVL PENLIILCEP SVKSLCEGLE 

       370        380        390        400        410        420 
KAIFQLKSGT LPAPENIHNI VKTFYTWRNV AERTEKVYDR VSVEAVLPMD KRLDRLISHC 

       430        440        450        460        470        480 
GPVTGYIFAL LAVFNFLFLI FLRWMTPDSI IDVAIDATGP RGAWTNNYSH SKRGGENNEI 


SETR 

« Hide

Isoform 2 [UniParc].

Checksum: 3F443EA94F271865
Show »

FASTA31535,078
Isoform 3 [UniParc].

Checksum: 78823EE49BCD9AF6
Show »

FASTA25028,034

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Phosphatidylinositol N-acetylglucosaminyltransferase subunit A

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11466 mRNA. Translation: BAA02019.1.
X77725 expand/collapse EMBL AC list , 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.
CCDSCCDS14165.1. [P37287-1]
CCDS48086.2. [P37287-3]
PIRA46217.
RefSeqNP_002632.1. NM_002641.3. [P37287-1]
NP_065206.3. NM_020473.3. [P37287-3]
UniGeneHs.137154.

3D structure databases

ProteinModelPortalP37287.
SMRP37287. Positions 43-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111295. 6 interactions.
STRING9606.ENSP00000369820.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSiteP37287.

Polymorphism databases

DMDM585696.

Proteomic databases

MaxQBP37287.
PaxDbP37287.
PRIDEP37287.

Protocols and materials databases

DNASU5277.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333590; ENSP00000369820; ENSG00000165195. [P37287-1]
ENST00000542278; ENSP00000442653; ENSG00000165195. [P37287-3]
GeneID5277.
KEGGhsa:5277.
UCSCuc004cwr.3. human. [P37287-1]
uc010nev.3. human. [P37287-2]
uc011miq.2. human. [P37287-3]

Organism-specific databases

CTD5277.
GeneCardsGC0XM015337.
HGNCHGNC:8957. PIGA.
HPAHPA001174.
MIM300818. phenotype.
300868. phenotype.
311770. gene.
neXtProtNX_P37287.
Orphanet300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2.
447. Paroxysmal nocturnal hemoglobinuria.
3451. West syndrome.
PharmGKBPA33288.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000203293.
HOVERGENHBG008198.
InParanoidP37287.
KOK03857.
OMAHTGRENT.
OrthoDBEOG7DC24J.
PhylomeDBP37287.
TreeFamTF105675.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressP37287.
BgeeP37287.
CleanExHS_PIGA.
GenevestigatorP37287.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view]
PfamPF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPIGA.
GenomeRNAi5277.
NextBio20392.
PROP37287.
SOURCESearch...

Entry information

Entry namePIGA_HUMAN
AccessionPrimary (citable) accession number: P37287
Secondary accession number(s): B4E0V2, Q16025, Q16250
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM