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P37287

- PIGA_HUMAN

UniProt

P37287 - PIGA_HUMAN

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Protein

Phosphatidylinositol N-acetylglucosaminyltransferase subunit A

Gene

PIGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor 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. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: HGNC
  2. UDP-glycosyltransferase activity Source: Reactome

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. C-terminal protein lipidation Source: Reactome
  3. GPI anchor biosynthetic process Source: HGNC
  4. positive regulation of metabolic process Source: HGNC
  5. post-translational protein modification Source: Reactome
  6. preassembly of GPI anchor in ER membrane Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PIGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8957. PIGA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 421421CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei422 – 44221HelicalSequence AnalysisAdd
BLAST
Topological domaini443 – 48442LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: HGNC
  2. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: HGNC
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191R → W in PNH1. 1 Publication
Corresponds to variant rs34422225 [ dbSNP | Ensembl ].
VAR_015442
Natural varianti40 – 401D → H in PNH1. 1 Publication
VAR_015436
Natural varianti48 – 481G → A in PNH1. 1 Publication
VAR_015437
Natural varianti48 – 481G → D in PNH1. 1 Publication
VAR_015438
Natural varianti48 – 481G → V in PNH1. 1 Publication
VAR_015439
Natural varianti128 – 1281H → R in PNH1. 1 Publication
VAR_015440
Natural varianti155 – 1551S → F in PNH1. 1 Publication
VAR_005531
Natural varianti239 – 2391G → R in PNH1. 1 Publication
VAR_015441
Natural varianti297 – 2971N → D in PNH1. 1 Publication
VAR_005532
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771R → L in MCAHS2. 1 Publication
VAR_071069
Natural varianti93 – 931P → L in MCAHS2. 1 Publication
VAR_071070
Natural varianti119 – 1191R → W in MCAHS2. 1 Publication
VAR_071071
Natural varianti206 – 2061I → F in MCAHS2. 1 Publication
VAR_071072
Natural varianti344 – 3441Missing in MCAHS2. 1 Publication
VAR_071073

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi300818. phenotype.
300868. phenotype.
Orphaneti397922. Ferro-cerebro-cutaneous syndrome.
300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2.
447. Paroxysmal nocturnal hemoglobinuria.
3451. West syndrome.
PharmGKBiPA33288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Phosphatidylinositol N-acetylglucosaminyltransferase subunit APRO_0000080326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP37287.
PaxDbiP37287.
PRIDEiP37287.

PTM databases

PhosphoSiteiP37287.

Expressioni

Gene expression databases

BgeeiP37287.
CleanExiHS_PIGA.
ExpressionAtlasiP37287. baseline and differential.
GenevestigatoriP37287.

Organism-specific databases

HPAiHPA001174.

Interactioni

Subunit structurei

Associates with PIGC, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity. Interacts directly with PIGY.1 Publication

Protein-protein interaction databases

BioGridi111295. 9 interactions.
STRINGi9606.ENSP00000369820.

Structurei

3D structure databases

ProteinModelPortaliP37287.
SMRiP37287. Positions 43-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000014405.
HOGENOMiHOG000203293.
HOVERGENiHBG008198.
InParanoidiP37287.
KOiK03857.
OMAiHTGRENT.
OrthoDBiEOG7DC24J.
PhylomeDBiP37287.
TreeFamiTF105675.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P37287-1) [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

        10         20         30         40         50
MACRGGAGNG HRASATLSRV SPGSLYTCRT RTHNICMVSD FFYPNMGGVE
60 70 80 90 100
SHIYQLSQCL IERGHKVIIV THAYGNRKGI RYLTSGLKVY YLPLKVMYNQ
110 120 130 140 150
STATTLFHSL PLLRYIFVRE RVTIIHSHSS FSAMAHDALF HAKTMGLQTV
160 170 180 190 200
FTDHSLFGFA DVSSVLTNKL LTVSLCDTNH IICVSYTSKE NTVLRAALNP
210 220 230 240 250
EIVSVIPNAV DPTDFTPDPF RRHDSITIVV VSRLVYRKGI DLLSGIIPEL
260 270 280 290 300
CQKYPDLNFI IGGEGPKRII LEEVRERYQL HDRVRLLGAL EHKDVRNVLV
310 320 330 340 350
QGHIFLNTSL TEAFCMAIVE AASCGLQVVS TRVGGIPEVL PENLIILCEP
360 370 380 390 400
SVKSLCEGLE KAIFQLKSGT LPAPENIHNI VKTFYTWRNV AERTEKVYDR
410 420 430 440 450
VSVEAVLPMD KRLDRLISHC GPVTGYIFAL LAVFNFLFLI FLRWMTPDSI
460 470 480
IDVAIDATGP RGAWTNNYSH SKRGGENNEI SETR
Length:484
Mass (Da):54,127
Last modified:October 1, 1994 - v1
Checksum:i34DCD074A3920852
GO
Isoform 2 (identifier: P37287-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-283: Missing.

Show »
Length:315
Mass (Da):35,078
Checksum:i3F443EA94F271865
GO
Isoform 3 (identifier: P37287-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MACR → MELT
     5-238: Missing.

Note: No experimental confirmation available.

Show »
Length:250
Mass (Da):28,034
Checksum:i78823EE49BCD9AF6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191R → W in PNH1. 1 Publication
Corresponds to variant rs34422225 [ dbSNP | Ensembl ].
VAR_015442
Natural varianti40 – 401D → H in PNH1. 1 Publication
VAR_015436
Natural varianti48 – 481G → A in PNH1. 1 Publication
VAR_015437
Natural varianti48 – 481G → D in PNH1. 1 Publication
VAR_015438
Natural varianti48 – 481G → V in PNH1. 1 Publication
VAR_015439
Natural varianti77 – 771R → L in MCAHS2. 1 Publication
VAR_071069
Natural varianti93 – 931P → L in MCAHS2. 1 Publication
VAR_071070
Natural varianti119 – 1191R → W in MCAHS2. 1 Publication
VAR_071071
Natural varianti128 – 1281H → R in PNH1. 1 Publication
VAR_015440
Natural varianti155 – 1551S → F in PNH1. 1 Publication
VAR_005531
Natural varianti206 – 2061I → F in MCAHS2. 1 Publication
VAR_071072
Natural varianti239 – 2391G → R in PNH1. 1 Publication
VAR_015441
Natural varianti297 – 2971N → D in PNH1. 1 Publication
VAR_005532
Natural varianti344 – 3441Missing in MCAHS2. 1 Publication
VAR_071073

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MACR → MELT in isoform 3. 1 PublicationVSP_043366
Alternative sequencei5 – 238234Missing in isoform 3. 1 PublicationVSP_043367Add
BLAST
Alternative sequencei115 – 283169Missing in isoform 2. 1 PublicationVSP_001802Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14165.1. [P37287-1]
CCDS48086.2. [P37287-3]
PIRiA46217.
RefSeqiNP_002632.1. NM_002641.3. [P37287-1]
NP_065206.3. NM_020473.3. [P37287-3]
UniGeneiHs.137154.

Genome annotation databases

EnsembliENST00000333590; ENSP00000369820; ENSG00000165195. [P37287-1]
ENST00000542278; ENSP00000442653; ENSG00000165195. [P37287-3]
GeneIDi5277.
KEGGihsa:5277.
UCSCiuc004cwr.3. human. [P37287-1]
uc010nev.3. human. [P37287-2]
uc011miq.2. human. [P37287-3]

Polymorphism databases

DMDMi585696.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Phosphatidylinositol N-acetylglucosaminyltransferase subunit A

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS14165.1. [P37287-1 ]
CCDS48086.2. [P37287-3 ]
PIRi A46217.
RefSeqi NP_002632.1. NM_002641.3. [P37287-1 ]
NP_065206.3. NM_020473.3. [P37287-3 ]
UniGenei Hs.137154.

3D structure databases

ProteinModelPortali P37287.
SMRi P37287. Positions 43-407.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111295. 9 interactions.
STRINGi 9606.ENSP00000369820.

Protein family/group databases

CAZyi GT4. Glycosyltransferase Family 4.

PTM databases

PhosphoSitei P37287.

Polymorphism databases

DMDMi 585696.

Proteomic databases

MaxQBi P37287.
PaxDbi P37287.
PRIDEi P37287.

Protocols and materials databases

DNASUi 5277.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333590 ; ENSP00000369820 ; ENSG00000165195 . [P37287-1 ]
ENST00000542278 ; ENSP00000442653 ; ENSG00000165195 . [P37287-3 ]
GeneIDi 5277.
KEGGi hsa:5277.
UCSCi uc004cwr.3. human. [P37287-1 ]
uc010nev.3. human. [P37287-2 ]
uc011miq.2. human. [P37287-3 ]

Organism-specific databases

CTDi 5277.
GeneCardsi GC0XM015337.
HGNCi HGNC:8957. PIGA.
HPAi HPA001174.
MIMi 300818. phenotype.
300868. phenotype.
311770. gene.
neXtProti NX_P37287.
Orphaneti 397922. Ferro-cerebro-cutaneous syndrome.
300496. Multiple congenital anomalies-hypotonia-seizures syndrome type 2.
447. Paroxysmal nocturnal hemoglobinuria.
3451. West syndrome.
PharmGKBi PA33288.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0438.
GeneTreei ENSGT00390000014405.
HOGENOMi HOG000203293.
HOVERGENi HBG008198.
InParanoidi P37287.
KOi K03857.
OMAi HTGRENT.
OrthoDBi EOG7DC24J.
PhylomeDBi P37287.
TreeFami TF105675.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii PIGA.
GenomeRNAii 5277.
NextBioi 20392.
PROi P37287.
SOURCEi Search...

Gene expression databases

Bgeei P37287.
CleanExi HS_PIGA.
ExpressionAtlasi P37287. baseline and differential.
Genevestigatori P37287.

Family and domain databases

InterProi IPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view ]
Pfami PF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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.
  16. "A novel germline PIGA mutation in Ferro-Cerebro-Cutaneous syndrome: a neurodegenerative X-linked epileptic encephalopathy with systemic iron-overload."
    Swoboda K.J., Margraf R.L., Carey J.C., Zhou H., Newcomb T.M., Coonrod E., Durtschi J., Mallempati K., Kumanovics A., Katz B.E., Voelkerding K.V., Opitz J.M.
    Am. J. Med. Genet. A 164A:17-28(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MCAHS2 LEU-344 DEL.
  17. "Expanding the spectrum of phenotypes associated with germline PIGA mutations: a child with developmental delay, accelerated linear growth, facial dysmorphisms, elevated alkaline phosphatase, and progressive CNS abnormalities."
    van der Crabben S.N., Harakalova M., Brilstra E.H., van Berkestijn F.M., Hofstede F.C., van Vught A.J., Cuppen E., Kloosterman W., Ploos van Amstel H.K., van Haaften G., van Haelst M.M.
    Am. J. Med. Genet. A 164A:29-35(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MCAHS2 LEU-93.
  18. Cited for: VARIANTS MCAHS2 LEU-77; TRP-119 AND PHE-206.

Entry informationi

Entry nameiPIGA_HUMAN
AccessioniPrimary (citable) accession number: P37287
Secondary accession number(s): B4E0V2, Q16025, Q16250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 139 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 X
    Human chromosome X: 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

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