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Reviewed, UniProtKB/Swiss-Prot Q5M9N4 (PIGH_MOUSE)

Last modified November 3, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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 By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the PIGH family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidylinositol N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
PRO_0000281862

Amino acid modifications

Modified residue61Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5M9N4-1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: C4C202F84A741A99

FASTA18821,078
        10         20         30         40         50         60 
MEDEKSFSDI CGGRLALRCR YYSPYCREFG LSSARLSLCS LTAVTCAVWL AAYGLFTLCE 

        70         80         90        100        110        120 
NSMVLSATIF ITILGLLGYL HFVKIDQETL LIIDSLGIQM TSSYASGKES TTFIEMDKVK 

       130        140        150        160        170        180 
DIIINEAIYM QKVIYYLCIL LKEPGKPHEI SRVVPVFQSA KPRLDCLIEV YRSCQEVLAH 


QKATATSL

« Hide

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References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: DBA/2.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.

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Cross-references

Sequence databases

AK167892 mRNA. Translation: BAE39904.1.
BC086806 mRNA. Translation: AAH86806.1.
IPIIPI00470085.
RefSeqNP_084264.1.
UniGeneMm.268317

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5M9N4.

PTM databases

PhosphoSiteQ5M9N4.

Proteomic databases

PRIDEQ5M9N4.

Genome annotation databases

EnsemblENSMUST00000072154; ENSMUSP00000072018; ENSMUSG00000021120; Mus musculus. [Genome view]
GeneID110417.
KEGGmmu:110417.
UCSCuc007nzs.1. mouse.

Organism-specific databases

CTD110417.
MGIMGI:99463. Pigh.

Phylogenomic databases

HOVERGENQ5M9N4.
OMAIINEAIY.

Enzyme and pathway databases

BRENDA2.4.1.198. 244.

Gene expression databases

ArrayExpressQ5M9N4.
BgeeQ5M9N4.
GenevestigatorQ5M9N4.

Family and domain databases

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

Other Resources

NextBio363963.
SOURCESearch...

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Entry information

Entry namePIGH_MOUSE
AccessionPrimary (citable) accession number: Q5M9N4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 1, 2005
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents