P37287 (PIGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PIGA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence 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 (PNH) [MIM:300818]: A disorder characterized by hemolytic anemia with hemoglobinuria, thromboses in large vessels, and a deficiency in hematopoiesis. Clinical manifestation of red blood cell breakdown with release of hemoglobin into the urine is manifested most prominently by dark-colored urine in the morning. Note: The disease is caused by mutations 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.8 Ref.11
Sequence similarities	Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-terminal protein lipidation Traceable author statement. Source: Reactome positive regulation of metabolic process Traceable author statement Ref.9. Source: HGNC preassembly of GPI anchor in ER membrane Traceable author statement. Source: Reactome
Cellular_component	endoplasmic 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	phosphatidylinositol N-acetylglucosaminyltransferase activity Traceable author statement 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 484	484	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A		PRO_0000080326
Regions
	Topological domain	1 – 421	421	Cytoplasmic Potential
	Transmembrane	422 – 442	21	Helical; Potential
	Topological domain	443 – 484	42	Lumenal Potential
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 4	4	MACR → MELT in isoform 3.		VSP_043366
	Alternative sequence	5 – 238	234	Missing in isoform 3.		VSP_043367
	Alternative sequence	115 – 283	169	Missing in isoform 2.		VSP_001802
	Natural variant	19	1	R → W in PNH. Ref.14 Corresponds to variant rs34422225 [ dbSNP | Ensembl ].		VAR_015442
	Natural variant	40	1	D → H in PNH. Ref.14		VAR_015436
	Natural variant	48	1	G → A in PNH. Ref.14		VAR_015437
	Natural variant	48	1	G → D in PNH. Ref.14		VAR_015438
	Natural variant	48	1	G → V in PNH. Ref.15		VAR_015439
	Natural variant	128	1	H → R in PNH. Ref.14		VAR_015440
	Natural variant	155	1	S → F in PNH. Ref.12		VAR_005531
	Natural variant	239	1	G → R in PNH. Ref.14		VAR_015441
	Natural variant	297	1	N → D in PNH. Ref.13		VAR_005532

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 34DCD074A3920852	FASTA	484	54,127
	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
	Isoform 2 [UniParc]. Checksum: 3F443EA94F271865	FASTA	315	35,078
	10 20 30 40 50 60 MACRGGAGNG HRASATLSRV SPGSLYTCRT RTHNICMVSD FFYPNMGGVE SHIYQLSQCL 70 80 90 100 110 120 IERGHKVIIV THAYGNRKGI RYLTSGLKVY YLPLKVMYNQ STATTLFHSL PLLRVRLLGA 130 140 150 160 170 180 LEHKDVRNVL VQGHIFLNTS LTEAFCMAIV EAASCGLQVV STRVGGIPEV LPENLIILCE 190 200 210 220 230 240 PSVKSLCEGL EKAIFQLKSG TLPAPENIHN IVKTFYTWRN VAERTEKVYD RVSVEAVLPM 250 260 270 280 290 300 DKRLDRLISH CGPVTGYIFA LLAVFNFLFL IFLRWMTPDS IIDVAIDATG PRGAWTNNYS 310 HSKRGGENNE ISETR
	Isoform 3 [UniParc]. Checksum: 78823EE49BCD9AF6	FASTA	250	28,034
	10 20 30 40 50 60 MELTGIDLLS GIIPELCQKY PDLNFIIGGE GPKRIILEEV RERYQLHDRV RLLGALEHKD 70 80 90 100 110 120 VRNVLVQGHI FLNTSLTEAF CMAIVEAASC GLQVVSTRVG GIPEVLPENL IILCEPSVKS 130 140 150 160 170 180 LCEGLEKAIF QLKSGTLPAP ENIHNIVKTF YTWRNVAERT EKVYDRVSVE AVLPMDKRLD 190 200 210 220 230 240 RLISHCGPVT GYIFALLAVF NFLFLIFLRW MTPDSIIDVA IDATGPRGAW TNNYSHSKRG 250 GENNEISETR

References

	« Hide 'large scale' referencesShow '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. , 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, DISEASE.
[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, MASS SPECTROMETRY. 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 PNH 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 PNH 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 PNH 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 PNH 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 , 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.
IPI	IPI00020966. IPI00220404. IPI00942148.
PIR	A46217.
RefSeq	NP_002632.1. NM_002641.3. NP_065206.3. NM_020473.3.
UniGene	Hs.137154.
3D structure databases
ProteinModelPortal	P37287.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000369820.
Protein family/group databases
CAZy	GT4. Glycosyltransferase Family 4.
PTM databases
PhosphoSite	P37287.
Polymorphism databases
DMDM	585696.
Proteomic databases
PaxDb	P37287.
PRIDE	P37287.
Protocols and materials databases
DNASU	5277.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000333590; ENSP00000369820; ENSG00000165195. ENST00000542278; ENSP00000442653; ENSG00000165195.
GeneID	5277.
KEGG	hsa:5277.
UCSC	uc004cwr.3. human. uc010nev.3. human.
Organism-specific databases
CTD	5277.
GeneCards	GC0XM015337.
HGNC	HGNC:8957. PIGA.
HPA	HPA001174.
MIM	300818. phenotype. 300868. phenotype. 311770. gene.
neXtProt	NX_P37287.
Orphanet	300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2. 447. Paroxysmal nocturnal hemoglobinuria.
PharmGKB	PA33288.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0438.
HOGENOM	HOG000203293.
HOVERGEN	HBG008198.
InParanoid	P37287.
KO	K03857.
OMA	VHGHSAF.
OrthoDB	EOG4GF3F7.
PhylomeDB	P37287.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00196.
Gene expression databases
ArrayExpress	P37287.
Bgee	P37287.
CleanEx	HS_PIGA.
Genevestigator	P37287.
GermOnline	ENSG00000165195. Homo sapiens.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. IPR013234. PIGA_GPI_anchor_biosynthesis. [Graphical view]
Pfam	PF00534. Glycos_transf_1. 1 hit. PF08288. PIGA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5277.
NextBio	20392.
SOURCE	Search...

Entry information

Entry name

PIGA_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.