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Protein

Phosphatidylinositol N-acetylglucosaminyltransferase subunit H

Gene

PIGH

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

Functioni

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI 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. catalytic activity Source: ProtInc
  2. phosphatidylinositol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular protein modification process Source: ProtInc
  3. C-terminal protein lipidation Source: Reactome
  4. GPI anchor biosynthetic process Source: ProtInc
  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

Enzyme and pathway databases

ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PIGH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:8964. PIGH.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. endoplasmic reticulum membrane Source: Reactome
  3. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33295.

Polymorphism and mutation databases

BioMutaiPIGH.
DMDMi27151659.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Phosphatidylinositol N-acetylglucosaminyltransferase subunit HPRO_0000058435Add
BLAST

Proteomic databases

MaxQBiQ14442.
PaxDbiQ14442.
PRIDEiQ14442.

PTM databases

PhosphoSiteiQ14442.

Expressioni

Gene expression databases

BgeeiQ14442.
CleanExiHS_PIGH.
ExpressionAtlasiQ14442. baseline and differential.
GenevestigatoriQ14442.

Organism-specific databases

HPAiHPA031624.

Interactioni

Subunit structurei

Associates with PIGA, PIGC, PIGP, PIGQ and DPM2. The latter is not essential for activity.

Protein-protein interaction databases

BioGridi111301. 6 interactions.
IntActiQ14442. 1 interaction.
STRINGi9606.ENSP00000216452.

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGH family.Curated

Phylogenomic databases

eggNOGiNOG266799.
GeneTreeiENSGT00390000011890.
HOGENOMiHOG000059602.
HOVERGENiHBG025632.
InParanoidiQ14442.
KOiK03858.
OMAiLHIHFVK.
PhylomeDBiQ14442.
TreeFamiTF324479.

Family and domain databases

InterProiIPR019328. GPI-GlcNAc_Trfase_PIG-H_dom.
[Graphical view]
PfamiPF10181. PIG-H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDERSFSDI CGGRLALQRR YYSPSCREFC LSCPRLSLRS LTAVTCTVWL
60 70 80 90 100
AAYGLFTLCE NSMILSAAIF ITLLGLLGYL HFVKIDQETL LIIDSLGIQM
110 120 130 140 150
TSSYASGKES TTFIEMGKVK DIVINEAIYM QKVIYYLCIL LKDPVEPHGI
160 170 180
SQVVPVFQSA KPRLDCLIEV YRSCQEILAH QKATSTSP
Length:188
Mass (Da):21,081
Last modified:November 1, 1996 - v1
Checksum:iEE70E4156272AC8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9784.1.
PIRiA48024.
RefSeqiNP_004560.1. NM_004569.3.
UniGeneiHs.553497.

Genome annotation databases

EnsembliENST00000216452; ENSP00000216452; ENSG00000100564.
GeneIDi5283.
KEGGihsa:5283.
UCSCiuc001xjr.1. human.

Polymorphism and mutation databases

BioMutaiPIGH.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Phosphatidylinositol N-acetylglucosaminyltransferase subunit H

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9784.1.
PIRiA48024.
RefSeqiNP_004560.1. NM_004569.3.
UniGeneiHs.553497.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111301. 6 interactions.
IntActiQ14442. 1 interaction.
STRINGi9606.ENSP00000216452.

PTM databases

PhosphoSiteiQ14442.

Polymorphism and mutation databases

BioMutaiPIGH.
DMDMi27151659.

Proteomic databases

MaxQBiQ14442.
PaxDbiQ14442.
PRIDEiQ14442.

Protocols and materials databases

DNASUi5283.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216452; ENSP00000216452; ENSG00000100564.
GeneIDi5283.
KEGGihsa:5283.
UCSCiuc001xjr.1. human.

Organism-specific databases

CTDi5283.
GeneCardsiGC14M068056.
HGNCiHGNC:8964. PIGH.
HPAiHPA031624.
MIMi600154. gene.
neXtProtiNX_Q14442.
PharmGKBiPA33295.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266799.
GeneTreeiENSGT00390000011890.
HOGENOMiHOG000059602.
HOVERGENiHBG025632.
InParanoidiQ14442.
KOiK03858.
OMAiLHIHFVK.
PhylomeDBiQ14442.
TreeFamiTF324479.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiREACT_952. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

GeneWikiiPIGH.
GenomeRNAii5283.
NextBioi20416.
PROiQ14442.
SOURCEiSearch...

Gene expression databases

BgeeiQ14442.
CleanExiHS_PIGH.
ExpressionAtlasiQ14442. baseline and differential.
GenevestigatoriQ14442.

Family and domain databases

InterProiIPR019328. GPI-GlcNAc_Trfase_PIG-H_dom.
[Graphical view]
PfamiPF10181. PIG-H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPIGH_HUMAN
AccessioniPrimary (citable) accession number: Q14442
Secondary accession number(s): B2RAA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 114 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.