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Protein

UDP-N-acetylhexosamine pyrophosphorylase

Gene

Uap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP 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).By similarity

Catalytic activityi

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

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. UDP-N-acetylhexosamine pyrophosphorylase (Uap1)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221UTPBy similarity
Binding sitei196 – 1961UTPBy similarity
Binding sitei222 – 2221UTP; via amide nitrogenBy similarity
Binding sitei223 – 2231SubstrateBy similarity
Binding sitei253 – 2531UTPBy similarity
Binding sitei377 – 3771UTPBy similarity
Binding sitei407 – 4071SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00113; UER00533.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylhexosamine pyrophosphorylase
Including the following 2 domains:
UDP-N-acetylgalactosamine pyrophosphorylase (EC:2.7.7.83)
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Gene namesi
Name:Uap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1334459. Uap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522UDP-N-acetylhexosamine pyrophosphorylasePRO_0000185768Add
BLAST

Proteomic databases

EPDiQ91YN5.
MaxQBiQ91YN5.
PaxDbiQ91YN5.
PRIDEiQ91YN5.

PTM databases

iPTMnetiQ91YN5.

Expressioni

Gene expression databases

BgeeiQ91YN5.
CleanExiMM_UAP1.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027981.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Turni12 – 143Combined sources
Helixi16 – 194Combined sources
Helixi22 – 243Combined sources
Helixi27 – 3812Combined sources
Helixi44 – 5613Combined sources
Turni57 – 615Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 703Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 793Combined sources
Turni80 – 823Combined sources
Helixi86 – 9914Combined sources
Beta strandi103 – 1086Combined sources
Turni114 – 1174Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 1243Combined sources
Helixi135 – 15420Combined sources
Beta strandi162 – 1665Combined sources
Turni168 – 1703Combined sources
Helixi171 – 18010Combined sources
Helixi182 – 1854Combined sources
Helixi188 – 1903Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi218 – 2203Combined sources
Helixi225 – 2328Combined sources
Helixi235 – 2428Combined sources
Beta strandi246 – 2516Combined sources
Helixi262 – 2709Combined sources
Beta strandi274 – 2818Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi298 – 3025Combined sources
Turni304 – 3063Combined sources
Helixi309 – 3135Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi325 – 33410Combined sources
Helixi335 – 3439Combined sources
Helixi345 – 3484Combined sources
Beta strandi352 – 3565Combined sources
Beta strandi375 – 3795Combined sources
Helixi382 – 3887Combined sources
Beta strandi390 – 3978Combined sources
Helixi399 – 4024Combined sources
Helixi418 – 43518Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi481 – 4833Combined sources
Turni485 – 4873Combined sources
Beta strandi489 – 4913Combined sources
Helixi495 – 4984Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi505 – 5106Combined sources
Beta strandi513 – 5164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VM8X-ray2.50A/B1-522[»]
ProteinModelPortaliQ91YN5.
SMRiQ91YN5. Positions 2-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91YN5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1114UTP bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 1114Substrate bindingBy similarity
Motifi303 – 3042Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the UDPGP type 1 family.Curated

Phylogenomic databases

eggNOGiKOG2388. Eukaryota.
COG4284. LUCA.
HOGENOMiHOG000186273.
HOVERGENiHBG018024.
InParanoidiQ91YN5.
KOiK00972.
OrthoDBiEOG7PGDQZ.
PhylomeDBiQ91YN5.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR002618. UDPGP_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 2 hits.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform AGX2 (identifier: Q91YN5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNVNDLKQRL SQAGQEHLLQ FWNELSEAQQ VELYMELQAM NFEELNSFFR
60 70 80 90 100
KAIGEFDRSS HQEKVDARME PVPRQVLGSA TRDQEQLQAW ESEGLSQISQ
110 120 130 140 150
NKVAVLLLAG GQGTRLGVSY PKGMYDVGLP SHKTLFQIQA ERILKLQQLA
160 170 180 190 200
EKHHGNKCTI PWYIMTSGRT MESTKEFFTK HKFFGLKKEN VVFFQQGMLP
210 220 230 240 250
AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME QRGICSIHVY
260 270 280 290 300
CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ
310 320 330 340 350
VVEYSEISLA TAQRRSSDGR LLFNAGNIAN HFFTVPFLKD VVNVYEPQLQ
360 370 380 390 400
HHVAQKKIPY VDSQGYFIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE
410 420 430 440 450
DEFSPLKNAD SQNGKDNPTT ARHALMSLHH CWVLNAGGHF IDENGSRLPA
460 470 480 490 500
IPRSATNGKS EAITADVNHN LKDANDVPIQ CEISPLISYA GEGLEGYVAD
510 520
KEFHAPLIID ENGVHELVKN GI
Length:522
Mass (Da):58,609
Last modified:December 1, 2001 - v1
Checksum:i121B4ACCCDDD43B5
GO
Isoform AGX1 (identifier: Q91YN5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-470: Missing.

Show »
Length:505
Mass (Da):56,898
Checksum:i47E48D1243198FCB
GO
Isoform 3 (identifier: Q91YN5-3) [UniParc]FASTAAdd to basket

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

Show »
Length:521
Mass (Da):58,522
Checksum:iBA4CC34659D777D9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti366 – 3661Y → H in strain: C57BL/6J. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 47017Missing in isoform AGX1. 1 PublicationVSP_014525Add
BLAST
Alternative sequencei454 – 4541Missing in isoform 3. 2 PublicationsVSP_014524

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15467.1. [Q91YN5-3]
RefSeqiNP_001291974.1. NM_001305045.1.
NP_001291975.1. NM_001305046.1.
NP_598567.2. NM_133806.5.
XP_006496671.2. XM_006496608.2.
XP_006496673.1. XM_006496610.2.
UniGeneiMm.27969.

Genome annotation databases

GeneIDi107652.
KEGGimmu:107652.
UCSCiuc007dlw.2. mouse. [Q91YN5-3]
uc007dly.2. mouse. [Q91YN5-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15467.1. [Q91YN5-3]
RefSeqiNP_001291974.1. NM_001305045.1.
NP_001291975.1. NM_001305046.1.
NP_598567.2. NM_133806.5.
XP_006496671.2. XM_006496608.2.
XP_006496673.1. XM_006496610.2.
UniGeneiMm.27969.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VM8X-ray2.50A/B1-522[»]
ProteinModelPortaliQ91YN5.
SMRiQ91YN5. Positions 2-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027981.

PTM databases

iPTMnetiQ91YN5.

Proteomic databases

EPDiQ91YN5.
MaxQBiQ91YN5.
PaxDbiQ91YN5.
PRIDEiQ91YN5.

Protocols and materials databases

DNASUi107652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi107652.
KEGGimmu:107652.
UCSCiuc007dlw.2. mouse. [Q91YN5-3]
uc007dly.2. mouse. [Q91YN5-2]

Organism-specific databases

CTDi6675.
MGIiMGI:1334459. Uap1.

Phylogenomic databases

eggNOGiKOG2388. Eukaryota.
COG4284. LUCA.
HOGENOMiHOG000186273.
HOVERGENiHBG018024.
InParanoidiQ91YN5.
KOiK00972.
OrthoDBiEOG7PGDQZ.
PhylomeDBiQ91YN5.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00533.

Miscellaneous databases

EvolutionaryTraceiQ91YN5.
NextBioi359192.
PROiQ91YN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YN5.
CleanExiMM_UAP1.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR002618. UDPGP_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 2 hits.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS AGX2 AND 3).
    Strain: FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "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).

Entry informationi

Entry nameiUAP1_MOUSE
AccessioniPrimary (citable) accession number: Q91YN5
Secondary accession number(s): Q8BG76, Q8BXD6, Q8VD59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.