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Q9BRB3 (PIGQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 111. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q

EC=2.4.1.198
Alternative name(s):
N-acetylglucosamyl transferase component GPI1
Phosphatidylinositol-glycan biosynthesis class Q protein
Short name=PIG-Q
Gene names
Name:PIGQ
Synonyms:GPI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI 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 PIGA, PIGC, PIGH, PIGP and DPM2. The latter is not essential for activity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the PIGQ family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BRB3-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q9BRB3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     511-581: DKPTALQPRG...HGHSQPSALP → AGVKFRVLRH...PWRQRGDKQD
     582-760: Missing.
Isoform 3 (identifier: Q9BRB3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     275-299: KANTVASVLLDVALGLMLLSWLHGR → CGPALVSAGLGACPLAPSPSPSAPR
     300-760: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 760759Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
PRO_0000215664

Regions

Transmembrane278 – 29821Helical; Potential
Transmembrane349 – 37123Helical; Potential
Transmembrane378 – 40023Helical; Potential
Transmembrane446 – 46823Helical; Potential
Transmembrane475 – 49723Helical; Potential
Compositional bias214 – 536323Leu-rich

Natural variations

Alternative sequence275 – 29925KANTV…WLHGR → CGPALVSAGLGACPLAPSPS PSAPR in isoform 3.
VSP_007279
Alternative sequence300 – 760461Missing in isoform 3.
VSP_007280
Alternative sequence511 – 58171DKPTA…PSALP → AGVKFRVLRHEAGRPLRLLM QINPLPYSRVVHTYRLPSCG CHPKHSWGALCRKLFLGELI YPWRQRGDKQD in isoform 2.
VSP_007281
Alternative sequence582 – 760179Missing in isoform 2.
VSP_007282
Natural variant141T → A. Ref.3 Ref.6
Corresponds to variant rs2071979 [ dbSNP | Ensembl ].
VAR_015596
Natural variant5921C → R.
Corresponds to variant rs1045277 [ dbSNP | Ensembl ].
VAR_053579
Natural variant6681C → R.
Corresponds to variant rs710924 [ dbSNP | Ensembl ].
VAR_053580
Natural variant6681C → Y.
Corresponds to variant rs710925 [ dbSNP | Ensembl ].
VAR_053581

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: DBF900ADCE08DA98

FASTA76084,082
        10         20         30         40         50         60 
MVLKAFFPTC CVSTDSGLLV GRWVPEQSSA VVLAVLHFPF IPIQVKQLLA QVRQASQVGV 

        70         80         90        100        110        120 
AVLGTWCHCR QEPEESLGRF LESLGAVFPH EPWLRLCRER GGTFWSCEAT HRQAPTAPGA 

       130        140        150        160        170        180 
PGEDQVMLIF YDQRQVLLSQ LHLPTVLPDR QAGATTASTG GLAAVFDTVA RSEVLFRSDR 

       190        200        210        220        230        240 
FDEGPVRLSH WQSEGVEASI LAELARRASG PICLLLASLL SLVSAVSACR VFKLWPLSFL 

       250        260        270        280        290        300 
GSKLSTCEQL RHRLEHLTLI FSTRKAENPA QLMRKANTVA SVLLDVALGL MLLSWLHGRS 

       310        320        330        340        350        360 
RIGHLADALV PVADHVAEEL QHLLQWLMGA PAGLKMNRAL DQVLGRFFLY HIHLWISYIH 

       370        380        390        400        410        420 
LMSPFVEHIL WHVGLSACLG LTVALSLLSD IIALLTFHIY CFYVYGARLY CLKIHGLSSL 

       430        440        450        460        470        480 
WRLFRGKKWN VLRQRVDSCS YDLDQLFIGT LLFTILLFLL PTTALYYLVF TLLRLLVVAV 

       490        500        510        520        530        540 
QGLIHLLVDL INSLPLYSLG LRLCRPYRLA DKPTALQPRG AHLPPPQLWL PPQALLGRPV 

       550        560        570        580        590        600 
PQAVPWGAHL PLEAERGQAG LRELLARLAP PHGHSQPSAL PGWHQLSWRM SCALWTLLCA 

       610        620        630        640        650        660 
PEHGRPCYHT LGLEVIGSEQ MWGWPARLAA LHHWHCLPWD PLPTCCGHHG GEHSNPRCPE 

       670        680        690        700        710        720 
HCPMPTLCTQ VQRVRPPQQP QVEGWSPWGL PSGSALAVGV EGPCQDEPPS PRHPLAPSAE 

       730        740        750        760 
QHPASGGLKQ SLTPVPSGPG PSLPEPHGVY LRMFPGEVAL 

« Hide

Isoform 2 [UniParc].

Checksum: A5C055C7C144661D
Show »

FASTA58165,344
Isoform 3 [UniParc].

Checksum: 260AA154769F6F41
Show »

FASTA29932,471

References

« Hide 'large scale' references
[1]"Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants."
Tiede A., Schubert J., Nischan C., Jensen I., Westfall B., Taron C.H., Orlean P., Schmidt R.E.
Biochem. J. 334:609-616(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1."
Watanabe R., Inoue N., Westfall B., Taron C.H., Orlean P., Takeda J., Kinoshita T.
EMBO J. 17:877-885(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-14.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 3), VARIANT ALA-14.
Tissue: Melanoma and Retinoblastoma.
[7]"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2."
Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J., Kangawa K., Julius M., Kinoshita T.
EMBO J. 19:4402-4411(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030177 mRNA. Translation: AAC32661.1.
AB003723 mRNA. Translation: BAA24948.1.
AE006464 Genomic DNA. Translation: AAK61235.1.
Z98883 Genomic DNA. Translation: CAB56148.2.
Z98883 Genomic DNA. Translation: CAM26442.1.
CH471112 Genomic DNA. Translation: EAW85796.1.
CH471112 Genomic DNA. Translation: EAW85797.1.
CH471112 Genomic DNA. Translation: EAW85799.1.
BC006377 mRNA. Translation: AAH06377.1.
BC010094 mRNA. No translation available.
RefSeqNP_004195.2. NM_004204.3.
NP_683721.1. NM_148920.2.
UniGeneHs.741878.
Hs.744949.

3D structure databases

ProteinModelPortalQ9BRB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114545. 6 interactions.
IntActQ9BRB3. 3 interactions.
MINTMINT-1182611.
STRING9606.ENSP00000026218.

PTM databases

PhosphoSiteQ9BRB3.

Polymorphism databases

DMDM30173119.

Proteomic databases

PaxDbQ9BRB3.
PRIDEQ9BRB3.

Protocols and materials databases

DNASU9091.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000026218; ENSP00000026218; ENSG00000007541. [Q9BRB3-1]
ENST00000321878; ENSP00000326674; ENSG00000007541. [Q9BRB3-2]
ENST00000409527; ENSP00000386760; ENSG00000007541. [Q9BRB3-2]
ENST00000470411; ENSP00000439650; ENSG00000007541. [Q9BRB3-3]
GeneID9091.
KEGGhsa:9091.
UCSCuc002chm.3. human. [Q9BRB3-3]
uc002chn.3. human. [Q9BRB3-2]
uc002cho.3. human. [Q9BRB3-1]

Organism-specific databases

CTD9091.
GeneCardsGC16P000616.
HGNCHGNC:14135. PIGQ.
HPAHPA039105.
HPA039828.
MIM605754. gene.
neXtProtNX_Q9BRB3.
PharmGKBPA33299.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242183.
HOVERGENHBG036559.
InParanoidQ9BRB3.
KOK03860.
OrthoDBEOG7K6PTR.
PhylomeDBQ9BRB3.
TreeFamTF321258.

Enzyme and pathway databases

BRENDA2.4.1.198. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ9BRB3.
BgeeQ9BRB3.
CleanExHS_PIGQ.
GenevestigatorQ9BRB3.

Family and domain databases

InterProIPR007720. GlcNAc_Gpi1.
[Graphical view]
PfamPF05024. Gpi1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIGQ. human.
GeneWikiPIGQ.
GenomeRNAi9091.
NextBio34061.
PROQ9BRB3.
SOURCESearch...

Entry information

Entry namePIGQ_HUMAN
AccessionPrimary (citable) accession number: Q9BRB3
Secondary accession number(s): A2IDE1 expand/collapse secondary AC list , D3DU52, O14927, Q96G00, Q96S22, Q9UJH4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 111 of the entry and version 3 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 16

Human chromosome 16: entries, gene names and cross-references to MIM