PIGH_HUMAN
ID PIGH_HUMAN Reviewed; 188 AA.
AC Q14442; B2RAA4;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit H {ECO:0000305};
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class H protein;
DE Short=PIG-H;
GN Name=PIGH {ECO:0000312|HGNC:HGNC:8964};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8407896; DOI=10.1016/s0021-9258(19)36842-5;
RA Kamitani T., Chang H.M., Rollins C., Waneck G.L., Yeh E.T.;
RT "Correction of the class H defect in glycosylphosphatidylinositol anchor
RT biosynthesis in Ltk- cells by a human cDNA clone.";
RL J. Biol. Chem. 268:20733-20736(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP COMPONENT OF GPI-GNT COMPLEX, INTERACTION WITH PIGQ, AND FUNCTION.
RX PubMed=9463366; DOI=10.1093/emboj/17.4.877;
RA Watanabe R., Inoue N., Westfall B., Taron C.H., Orlean P., Takeda J.,
RA Kinoshita T.;
RT "The first step of glycosylphosphatidylinositol biosynthesis is mediated by
RT a complex of PIG-A, PIG-H, PIG-C and GPI1.";
RL EMBO J. 17:877-885(1998).
RN [7]
RP COMPONENT OF GPI-GNT COMPLEX, AND FUNCTION.
RX PubMed=16162815; DOI=10.1091/mbc.e05-08-0743;
RA Murakami Y., Siripanyaphinyo U., Hong Y., Tashima Y., Maeda Y.,
RA Kinoshita T.;
RT "The initial enzyme for glycosylphosphatidylinositol biosynthesis requires
RT PIG-Y, a seventh component.";
RL Mol. Biol. Cell 16:5236-5246(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP INVOLVEMENT IN GPIBD17.
RX PubMed=29573052; DOI=10.1002/humu.23420;
RA Pagnamenta A.T., Murakami Y., Anzilotti C., Titheradge H., Oates A.J.,
RA Morton J., Kinoshita T., Kini U., Taylor J.C.;
RT "A homozygous variant disrupting the PIGH start-codon is associated with
RT developmental delay, epilepsy, and microcephaly.";
RL Hum. Mutat. 39:822-826(2018).
RN [10]
RP INVOLVEMENT IN GPIBD17, VARIANT GPIBD17 PRO-103, AND CHARACTERIZATION OF
RP VARIANT GPIBD17 PRO-103.
RX PubMed=29603516; DOI=10.1002/humu.23426;
RA Nguyen T.T.M., Mahida S., Smith-Hicks C., Campeau P.M.;
RT "A PIGH mutation leading to GPI deficiency is associated with developmental
RT delay and autism.";
RL Hum. Mutat. 39:827-829(2018).
CC -!- FUNCTION: Part of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the
CC transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to
CC phosphatidylinositol and participates in the first step of GPI
CC biosynthesis. {ECO:0000269|PubMed:16162815,
CC ECO:0000269|PubMed:9463366}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000269|PubMed:16162815,
CC ECO:0000269|PubMed:9463366}.
CC -!- SUBUNIT: Component of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2 (PubMed:16162815,
CC PubMed:9463366). Interacts with PIGQ (PubMed:9463366).
CC {ECO:0000269|PubMed:16162815, ECO:0000269|PubMed:9463366}.
CC -!- INTERACTION:
CC Q14442; P37287: PIGA; NbExp=5; IntAct=EBI-2803676, EBI-26643054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISEASE: Glycosylphosphatidylinositol biosynthesis defect 17 (GPIBD17)
CC [MIM:618010]: An autosomal recessive disorder characterized by variable
CC neurologic deficits that become apparent in infancy or early childhood.
CC Clinical features include learning disabilities, mild-to-moderate
CC developmental delay, seizures of variable severity, aggressive or over-
CC friendly behavior, and autistic features. {ECO:0000269|PubMed:29573052,
CC ECO:0000269|PubMed:29603516}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PIGH family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit H;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_557";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L19783; AAA03545.1; -; mRNA.
DR EMBL; BT006804; AAP35450.1; -; mRNA.
DR EMBL; AK314108; BAG36801.1; -; mRNA.
DR EMBL; CH471061; EAW80942.1; -; Genomic_DNA.
DR EMBL; BC004100; AAH04100.1; -; mRNA.
DR EMBL; BC071849; AAH71849.1; -; mRNA.
DR CCDS; CCDS9784.1; -.
DR PIR; A48024; A48024.
DR RefSeq; NP_004560.1; NM_004569.3.
DR AlphaFoldDB; Q14442; -.
DR BioGRID; 111301; 180.
DR ComplexPortal; CPX-6502; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR CORUM; Q14442; -.
DR IntAct; Q14442; 9.
DR MINT; Q14442; -.
DR STRING; 9606.ENSP00000216452; -.
DR iPTMnet; Q14442; -.
DR PhosphoSitePlus; Q14442; -.
DR BioMuta; PIGH; -.
DR DMDM; 27151659; -.
DR EPD; Q14442; -.
DR jPOST; Q14442; -.
DR MassIVE; Q14442; -.
DR MaxQB; Q14442; -.
DR PaxDb; Q14442; -.
DR PeptideAtlas; Q14442; -.
DR PRIDE; Q14442; -.
DR ProteomicsDB; 59991; -.
DR Antibodypedia; 24854; 153 antibodies from 23 providers.
DR DNASU; 5283; -.
DR Ensembl; ENST00000216452.9; ENSP00000216452.4; ENSG00000100564.9.
DR GeneID; 5283; -.
DR KEGG; hsa:5283; -.
DR MANE-Select; ENST00000216452.9; ENSP00000216452.4; NM_004569.5; NP_004560.1.
DR UCSC; uc001xjr.2; human.
DR CTD; 5283; -.
DR DisGeNET; 5283; -.
DR GeneCards; PIGH; -.
DR HGNC; HGNC:8964; PIGH.
DR HPA; ENSG00000100564; Low tissue specificity.
DR MalaCards; PIGH; -.
DR MIM; 600154; gene.
DR MIM; 618010; phenotype.
DR neXtProt; NX_Q14442; -.
DR OpenTargets; ENSG00000100564; -.
DR PharmGKB; PA33295; -.
DR VEuPathDB; HostDB:ENSG00000100564; -.
DR eggNOG; KOG4551; Eukaryota.
DR GeneTree; ENSGT00390000011890; -.
DR InParanoid; Q14442; -.
DR OMA; FVKIDHE; -.
DR OrthoDB; 1431299at2759; -.
DR PhylomeDB; Q14442; -.
DR TreeFam; TF324479; -.
DR PathwayCommons; Q14442; -.
DR Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR SignaLink; Q14442; -.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 5283; 90 hits in 1072 CRISPR screens.
DR ChiTaRS; PIGH; human.
DR GeneWiki; PIGH; -.
DR GenomeRNAi; 5283; -.
DR Pharos; Q14442; Tbio.
DR PRO; PR:Q14442; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q14442; protein.
DR Bgee; ENSG00000100564; Expressed in body of pancreas and 192 other tissues.
DR ExpressionAtlas; Q14442; baseline and differential.
DR Genevisible; Q14442; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR InterPro; IPR019328; GPI-GlcNAc_Trfase_PIG-H_dom.
DR InterPro; IPR044215; PIG-H.
DR PANTHER; PTHR15231; PTHR15231; 1.
DR Pfam; PF10181; PIG-H; 1.
PE 1: Evidence at protein level;
KW Autism spectrum disorder; Cytoplasm; Disease variant; Epilepsy;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit H"
FT /id="PRO_0000058435"
FT VARIANT 103
FT /note="S -> P (in GPIBD17; decreased expression of GPI-
FT anchored proteins, including FCGR3B/CD16B and CD55, in
FT patient's granulocytes; dbSNP:rs776038451)"
FT /evidence="ECO:0000269|PubMed:29603516"
FT /id="VAR_080993"
SQ SEQUENCE 188 AA; 21081 MW; EE70E4156272AC8B CRC64;
MEDERSFSDI CGGRLALQRR YYSPSCREFC LSCPRLSLRS LTAVTCTVWL AAYGLFTLCE
NSMILSAAIF ITLLGLLGYL HFVKIDQETL LIIDSLGIQM TSSYASGKES TTFIEMGKVK
DIVINEAIYM QKVIYYLCIL LKDPVEPHGI SQVVPVFQSA KPRLDCLIEV YRSCQEILAH
QKATSTSP
