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Q91YN5 (UAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylhexosamine pyrophosphorylase

Including the following 2 domains:

  1. UDP-N-acetylgalactosamine pyrophosphorylase
    EC=2.7.7.-
  2. UDP-N-acetylglucosamine pyrophosphorylase
    EC=2.7.7.23
Gene names
Name:Uap1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P By similarity.

Catalytic activity

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.

Subunit structure

Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform AGX2 is a monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the UDPGP type 1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionUDP-N-acetylglucosamine diphosphorylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform AGX2 (identifier: Q91YN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform AGX1 (identifier: Q91YN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     454-470: Missing.
Isoform 3 (identifier: Q91YN5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522UDP-N-acetylhexosamine pyrophosphorylase
PRO_0000185768

Regions

Motif108 – 1114Substrate binding By similarity
Motif303 – 3042Substrate binding By similarity

Sites

Binding site2231Substrate By similarity
Binding site4071Substrate By similarity

Amino acid modifications

Modified residue1801N6-acetyllysine By similarity

Natural variations

Alternative sequence454 – 47017Missing in isoform AGX1.
VSP_014525
Alternative sequence4541Missing in isoform 3.
VSP_014524
Natural variant3661Y → H in strain: C57BL/6J. Ref.1

Secondary structure

1 .................................................................................................... 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform AGX2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 121B4ACCCDDD43B5

FASTA52258,609
        10         20         30         40         50         60 
MNVNDLKQRL SQAGQEHLLQ FWNELSEAQQ VELYMELQAM NFEELNSFFR KAIGEFDRSS 

        70         80         90        100        110        120 
HQEKVDARME PVPRQVLGSA TRDQEQLQAW ESEGLSQISQ NKVAVLLLAG GQGTRLGVSY 

       130        140        150        160        170        180 
PKGMYDVGLP SHKTLFQIQA ERILKLQQLA EKHHGNKCTI PWYIMTSGRT MESTKEFFTK 

       190        200        210        220        230        240 
HKFFGLKKEN VVFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME 

       250        260        270        280        290        300 
QRGICSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 

       310        320        330        340        350        360 
VVEYSEISLA TAQRRSSDGR LLFNAGNIAN HFFTVPFLKD VVNVYEPQLQ HHVAQKKIPY 

       370        380        390        400        410        420 
VDSQGYFIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT 

       430        440        450        460        470        480 
ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS EAITADVNHN LKDANDVPIQ 

       490        500        510        520 
CEISPLISYA GEGLEGYVAD KEFHAPLIID ENGVHELVKN GI

« Hide

Isoform AGX1 [UniParc].

Checksum: 47E48D1243198FCB
Show »

FASTA50556,898
Isoform 3 [UniParc].

Checksum: BA4CC34659D777D9
Show »

FASTA52158,522

References

« Hide 'large scale' 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] (ISOFORMS AGX1 AND 3), VARIANT HIS-366.
Strain: C57BL/6J.
Tissue: Cerebellum, Embryo and Head.
[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] (ISOFORMS AGX2 AND 3).
Strain: FVB/N.
Tissue: Mammary tumor and Salivary gland.
[3]"Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (AGX2) from Mus musculus."
Joint center for structural genomics (JCSG)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK047566 mRNA. Translation: BAC33089.1.
AK049519 mRNA. Translation: BAC33791.1.
AK081690 mRNA. Translation: BAC38294.1.
BC016406 mRNA. Translation: AAH16406.1.
BC017547 mRNA. Translation: AAH17547.1.
IPIIPI00387370.
IPI00608037.
IPI00750471.
RefSeqNP_598567.2. NM_133806.4.
UniGeneMm.27969.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VM8X-ray2.50A/B1-522[»]
ProteinModelPortalQ91YN5.
SMRQ91YN5. Positions 2-517.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ91YN5.

Proteomic databases

PRIDEQ91YN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027981; ENSMUSP00000027981; ENSMUSG00000026670.
ENSMUST00000111350; ENSMUSP00000106982; ENSMUSG00000026670.
GeneID107652.
KEGGmmu:107652.
UCSCuc007dlw.1. mouse.
uc007dly.1. mouse.

Organism-specific databases

CTD6675.
MGIMGI:1334459. Uap1.

Phylogenomic databases

GeneTreeENSGT00390000010072.
HOGENOMHBG527090.
HOVERGENHBG018024.
InParanoidQ91YN5.
OrthoDBEOG4PG60V.
PhylomeDBQ91YN5.

Gene expression databases

ArrayExpressQ91YN5.
BgeeQ91YN5.
CleanExMM_UAP1.
GenevestigatorQ91YN5.
GermOnlineENSMUSG00000026670. Mus musculus.

Family and domain databases

InterProIPR002618. UDPGP_trans.
[Graphical view]
KOK00972.
PANTHERPTHR11952. UDPGP_trans. 1 hit.
PfamPF01704. UDPGP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameUAP1_MOUSE
AccessionPrimary (citable) accession number: Q91YN5
Secondary accession number(s): Q8BG76, Q8BXD6, Q8VD59
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents