Q9BRB3 (PIGQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	760 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	C-terminal protein lipidation Traceable author statement. Source: Reactome carbohydrate metabolic process Traceable author statement Ref.1. Source: ProtInc preassembly of GPI anchor in ER membrane Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	phosphatidylinositol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 760	759	Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q		PRO_0000215664
Regions
	Transmembrane	278 – 298	21	Helical; Potential
	Transmembrane	349 – 371	23	Helical; Potential
	Transmembrane	378 – 400	23	Helical; Potential
	Transmembrane	446 – 468	23	Helical; Potential
	Transmembrane	475 – 497	23	Helical; Potential
	Compositional bias	214 – 536	323	Leu-rich
Natural variations
	Alternative sequence	275 – 299	25	KANTV…WLHGR → CGPALVSAGLGACPLAPSPS PSAPR in isoform 3.		VSP_007279
	Alternative sequence	300 – 760	461	Missing in isoform 3.		VSP_007280
	Alternative sequence	511 – 581	71	DKPTA…PSALP → AGVKFRVLRHEAGRPLRLLM QINPLPYSRVVHTYRLPSCG CHPKHSWGALCRKLFLGELI YPWRQRGDKQD in isoform 2.		VSP_007281
	Alternative sequence	582 – 760	179	Missing in isoform 2.		VSP_007282
	Natural variant	14	1	T → A. Ref.3 Ref.6 Corresponds to variant rs2071979 [ dbSNP | Ensembl ].		VAR_015596
	Natural variant	592	1	C → R. Corresponds to variant rs1045277 [ dbSNP | Ensembl ].		VAR_053579
	Natural variant	668	1	C → R. Corresponds to variant rs710924 [ dbSNP | Ensembl ].		VAR_053580
	Natural variant	668	1	C → Y. Corresponds to variant rs710925 [ dbSNP | Ensembl ].		VAR_053581

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DBF900ADCE08DA98	FASTA	760	84,082
	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
	Isoform 2 [UniParc]. Checksum: A5C055C7C144661D	FASTA	581	65,344
	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 AGVKFRVLRH EAGRPLRLLM QINPLPYSRV 550 560 570 580 VHTYRLPSCG CHPKHSWGAL CRKLFLGELI YPWRQRGDKQ D
	Isoform 3 [UniParc]. Checksum: 260AA154769F6F41	FASTA	299	32,471
	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 GSKLSTCEQL RHRLEHLTLI FSTRKAENPA QLMRCGPALV SAGLGACPLA PSPSPSAPR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00009447. IPI00062113. IPI00163323.
RefSeq	NP_004195.2. NM_004204.3. NP_683721.1. NM_148920.2.
UniGene	Hs.644153. Hs.741878.
3D structure databases
ProteinModelPortal	Q9BRB3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BRB3. 2 interactions.
MINT	MINT-1182611.
STRING	9606.ENSP00000026218.
PTM databases
PhosphoSite	Q9BRB3.
Polymorphism databases
DMDM	30173119.
Proteomic databases
PaxDb	Q9BRB3.
PRIDE	Q9BRB3.
Protocols and materials databases
DNASU	9091.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000026218; ENSP00000026218; ENSG00000007541. ENST00000321878; ENSP00000326674; ENSG00000007541. ENST00000409527; ENSP00000386760; ENSG00000007541. ENST00000470411; ENSP00000439650; ENSG00000007541.
GeneID	9091.
KEGG	hsa:9091.
UCSC	uc002chm.3. human. uc002chn.3. human. uc002cho.3. human.
Organism-specific databases
CTD	9091.
GeneCards	GC16P000616.
HGNC	HGNC:14135. PIGQ.
HPA	HPA039105. HPA039828.
MIM	605754. gene.
neXtProt	NX_Q9BRB3.
PharmGKB	PA33299.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG242183.
HOVERGEN	HBG036559.
InParanoid	Q9BRB3.
KO	K03860.
PhylomeDB	Q9BRB3.
Enzyme and pathway databases
BRENDA	2.4.1.198. 2681.
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00196.
Gene expression databases
ArrayExpress	Q9BRB3.
Bgee	Q9BRB3.
CleanEx	HS_PIGQ.
Genevestigator	Q9BRB3.
GermOnline	ENSG00000007541. Homo sapiens.
Family and domain databases
InterPro	IPR007720. GlcNAc_Gpi1. [Graphical view]
Pfam	PF05024. Gpi1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PIGQ. human.
GenomeRNAi	9091.
NextBio	34061.
SOURCE	Search...

Entry information

Entry name

PIGQ_HUMAN

Accession

Primary (citable) accession number: Q9BRB3
Secondary accession number(s): A2IDE1 , D3DU52, O14927, Q96G00, Q96S22, Q9UJH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 105 of the entry and version 3 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.