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P42881 (GPT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

EC=2.7.8.15
Alternative name(s):
GlcNAc-1-P transferase
Short name=G1PT
Short name=GPT
N-acetylglucosamine-1-phosphate transferase
Gene names
Name:gpt2
Synonyms:gpt
ORF Names:SPBC15D4.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.

Catalytic activity

UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.

Enzyme regulation

Inhibited by tunicamycin.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
PRO_0000108764

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane25 – 4521Helical; Potential
Transmembrane73 – 9321Helical; Potential
Transmembrane123 – 14321Helical; Potential
Transmembrane155 – 17521Helical; Potential
Transmembrane191 – 21121Helical; Potential
Transmembrane216 – 23621Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane282 – 30221Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane412 – 43221Helical; Potential

Amino acid modifications

Glycosylation3951N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P42881 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 16CAB90E5FBFF15F

FASTA44649,855
        10         20         30         40         50         60 
MIESCFNVGI WATGLALLMN QGQSPLLSNV GLSVLAYKAT AMFIPRVGPS FIKRGFSGKD 

        70         80         90        100        110        120 
MNKVEKYVIP ETMGAVSALV YFMCMIIFIP VLFYKYLVPN HNPNLPSDGS VAEVAKSQFP 

       130        140        150        160        170        180 
HDLLGAYLSA LLSILSVSLL GILDDLFDIR WRHKFFLPAI AAIPLLVVYY VDYGVTYVSV 

       190        200        210        220        230        240 
PSIVRPFLKR SLINLGFLYY FYMAAVAIFC PNSINIIAGV NGVEAGQSLV LALVIACNDL 

       250        260        270        280        290        300 
FYVLSPKNKD ALRAHLLSLY LVLPLIGVTA GLLKYNWWPS RVFVGDTFCY FAGMVMAVVG 

       310        320        330        340        350        360 
ILGHFSKTLM LFFIPQIFNF ALSVPQLFGL VECPRHRLPK LNVKTGLLEN SYTEFSLNEH 

       370        380        390        400        410        420 
PLPKKTLLTI SIFEKLRLIR VEYDPSTGRP LRCTNFTIIN FVLYHLGPMR EDHLTICIMG 

       430        440 
LQLLTGIFGL IIRHFVAPLV YPEDNI 

« Hide

References

« Hide 'large scale' references
[1]"Asparagine-linked glycosylation in Schizosaccharomyces pombe: functional conservation of the first step in oligosaccharide-lipid assembly."
Zou J., Scocca J.R., Krag S.S.
Arch. Biochem. Biophys. 317:487-496(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09454 Genomic DNA. Translation: AAA92799.1.
CU329671 Genomic DNA. Translation: CAA20479.1.
PIRS71622.
RefSeqNP_596244.1. NM_001022163.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4690327.
STRING4896.SPBC15D4.04-1.

Proteomic databases

MaxQBP42881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC15D4.04.1; SPBC15D4.04.1:pep; SPBC15D4.04.
GeneID2539795.
KEGGspo:SPBC15D4.04.

Organism-specific databases

PomBaseSPBC15D4.04.

Phylogenomic databases

eggNOGCOG0472.
HOGENOMHOG000163915.
KOK01001.
OMAIHERNLT.
OrthoDBEOG7380DT.
PhylomeDBP42881.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

InterProIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800944.
PROP42881.

Entry information

Entry nameGPT_SCHPO
AccessionPrimary (citable) accession number: P42881
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways