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Q14442 (PIGH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase subunit H

EC=2.4.1.198
Alternative name(s):
Phosphatidylinositol-glycan biosynthesis class H protein
Short name=PIG-H
Gene names
Name:PIGH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
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, PIGP, PIGQ and DPM2. The latter is not essential for activity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the PIGH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
PRO_0000058435

Sequences

Sequence LengthMass (Da)Tools
Q14442 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EE70E4156272AC8B

FASTA18821,081
        10         20         30         40         50         60 
MEDERSFSDI CGGRLALQRR YYSPSCREFC LSCPRLSLRS LTAVTCTVWL AAYGLFTLCE 

        70         80         90        100        110        120 
NSMILSAAIF ITLLGLLGYL HFVKIDQETL LIIDSLGIQM TSSYASGKES TTFIEMGKVK 

       130        140        150        160        170        180 
DIVINEAIYM QKVIYYLCIL LKDPVEPHGI SQVVPVFQSA KPRLDCLIEV YRSCQEILAH 


QKATSTSP 

« Hide

References

« Hide 'large scale' references
[1]"Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone."
Kamitani T., Chang H.M., Rollins C., Waneck G.L., Yeh E.T.
J. Biol. Chem. 268:20733-20736(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
Tissue: Brain cortex.
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Blood and Lung.
[6]"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: INTERACTION WITH PIGA; PIGC AND PIGQ.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Phosphatidylinositol N-acetylglucosaminyltransferase subunit H

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19783 mRNA. Translation: AAA03545.1.
BT006804 mRNA. Translation: AAP35450.1.
AK314108 mRNA. Translation: BAG36801.1.
CH471061 Genomic DNA. Translation: EAW80942.1.
BC004100 mRNA. Translation: AAH04100.1.
BC071849 mRNA. Translation: AAH71849.1.
CCDSCCDS9784.1.
PIRA48024.
RefSeqNP_004560.1. NM_004569.3.
UniGeneHs.553497.

3D structure databases

ProteinModelPortalQ14442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111301. 5 interactions.
IntActQ14442. 1 interaction.
STRING9606.ENSP00000216452.

PTM databases

PhosphoSiteQ14442.

Polymorphism databases

DMDM27151659.

Proteomic databases

MaxQBQ14442.
PaxDbQ14442.
PRIDEQ14442.

Protocols and materials databases

DNASU5283.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216452; ENSP00000216452; ENSG00000100564.
GeneID5283.
KEGGhsa:5283.
UCSCuc001xjr.1. human.

Organism-specific databases

CTD5283.
GeneCardsGC14M068056.
HGNCHGNC:8964. PIGH.
HPAHPA031624.
MIM600154. gene.
neXtProtNX_Q14442.
PharmGKBPA33295.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266799.
HOGENOMHOG000059602.
HOVERGENHBG025632.
InParanoidQ14442.
KOK03858.
OMATKRICRC.
PhylomeDBQ14442.
TreeFamTF324479.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ14442.
BgeeQ14442.
CleanExHS_PIGH.
GenevestigatorQ14442.

Family and domain databases

InterProIPR019328. GPI-GlcNAc_Trfase_PIG-H_dom.
[Graphical view]
PfamPF10181. PIG-H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPIGH.
GenomeRNAi5283.
NextBio20416.
PROQ14442.
SOURCESearch...

Entry information

Entry namePIGH_HUMAN
AccessionPrimary (citable) accession number: Q14442
Secondary accession number(s): B2RAA4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 108 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 chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM