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Q16851 (UGPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UTP--glucose-1-phosphate uridylyltransferase

EC=2.7.7.9
Alternative name(s):
UDP-glucose pyrophosphorylase
Short name=UDPGP
Short name=UGPase
Gene names
Name:UGP2
Synonyms:UGP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a central role as a glucosyl donor in cellular metabolic pathways.

Catalytic activity

UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

Subunit structure

Homooctamer. Ref.10

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the UDPGP type 1 family.

Caution

The human genome was initially thought to contain 2 genes for UTP--glucose-1-phosphate uridylyltransferase: UGP1 and UGP2. However, the sequence defined as UGP1 (Ref.1) probably does not exist and corresponds to UGP2.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB2P629932EBI-743729,EBI-401755

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16851-1)

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 2 (identifier: Q16851-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508UTP--glucose-1-phosphate uridylyltransferase
PRO_0000185752

Regions

Region457 – 50852Oligomerization
Region502 – 5032Critical for end-to-end subunit interaction

Sites

Active site3961 By similarity
Metal binding1271Magnesium By similarity
Metal binding2531Magnesium By similarity

Amino acid modifications

Modified residue131Phosphoserine Ref.6 Ref.8
Modified residue4381N6-acetyllysine Ref.5

Natural variations

Alternative sequence1 – 1111Missing in isoform 2.
VSP_012834
Natural variant2681M → I. Ref.1 Ref.2
Corresponds to variant rs1130982 [ dbSNP | Ensembl ].
VAR_033042

Experimental info

Mutagenesis1231C → S: No significant loss of activity.
Mutagenesis2181W → S: No significant loss of activity.
Mutagenesis2661H → R: No significant loss of activity.
Mutagenesis3331W → S: Loss of activity; possibly due to folding defect.
Mutagenesis3891R → H: No significant loss of activity.
Mutagenesis3911R → H: Loss of activity; possibly due to folding defect.
Mutagenesis4221R → H: No significant loss of activity.
Mutagenesis4451R → H: No significant loss of activity.
Mutagenesis502 – 5032NL → PE: Abolishes oligomerization and significantly increases enzymatic activity. Ref.10
Sequence conflict251R → L Ref.1
Sequence conflict441S → T Ref.1
Sequence conflict481F → Y Ref.1
Sequence conflict621F → Y Ref.1
Sequence conflict1521T → S Ref.1
Sequence conflict2021L → R Ref.1
Sequence conflict2021L → R in AAB05640. Ref.2
Sequence conflict2101Y → S Ref.1
Sequence conflict2141N → S Ref.1
Sequence conflict240 – 2412IG → LE Ref.1
Sequence conflict3561A → P Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 60E54806807AB470

FASTA50856,940
        10         20         30         40         50         60 
MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH TKKDLDGFRK 

        70         80         90        100        110        120 
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS 

       130        140        150        160        170        180 
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH 

       190        200        210        220        230        240 
CRVKIYTFNQ SRYPRINKES LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI 

       250        260        270        280        290        300 
GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG 

       310        320        330        340        350        360 
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNAKTLD 

       370        380        390        400        410        420 
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE 

       430        440        450        460        470        480 
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA 

       490        500 
NHGDRIDIPP GAVLENKIVS GNLRILDH 

« Hide

Isoform 2 [UniParc].

Checksum: 2B3FD9731E371E47
Show »

FASTA49755,677

References

« Hide 'large scale' references
[1]"Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation."
Peng H.-L., Chang H.-Y.
FEBS Lett. 329:153-158(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT ILE-268.
Tissue: Liver.
[2]"Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli."
Duggleby R.G., Chao Y.C., Huang J.G., Peng H.-L., Chang H.-Y.
Eur. J. Biochem. 235:173-179(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ILE-268.
Tissue: Skeletal muscle.
[3]"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 1 AND 2).
Tissue: Cervix, Lymph and Skin.
[4]"The importance of conserved residues in human liver UDPglucose pyrophosphorylase."
Chang H.-Y., Peng H.-L., Chao Y.C., Duggleby R.G.
Eur. J. Biochem. 236:723-728(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity."
Yu Q., Zheng X.
Biochem. J. 442:283-291(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.57 ANGSTROMS), SUBUNIT, MUTAGENESIS OF 502-ASP--LEU-503.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27460 mRNA. Translation: AAB05640.1.
BC000173 mRNA. Translation: AAH00173.2.
BC002954 mRNA. Translation: AAH02954.1.
BC047004 mRNA. Translation: AAH47004.1.
PIRS35692.
RefSeqNP_001001521.1. NM_001001521.1.
NP_006750.3. NM_006759.3.
XP_005264594.1. XM_005264537.1.
XP_005264595.1. XM_005264538.1.
UniGeneHs.516217.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R2WX-ray3.60A/B/C/D1-508[»]
3R3IX-ray3.57A/B/C/D1-508[»]
ProteinModelPortalQ16851.
SMRQ16851. Positions 22-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113207. 38 interactions.
IntActQ16851. 6 interactions.
MINTMINT-1468909.
STRING9606.ENSP00000338703.

PTM databases

PhosphoSiteQ16851.

Polymorphism databases

DMDM59803098.

2D gel databases

REPRODUCTION-2DPAGEIPI00395676.
UCD-2DPAGEQ16851.

Proteomic databases

PaxDbQ16851.
PRIDEQ16851.

Protocols and materials databases

DNASU7360.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337130; ENSP00000338703; ENSG00000169764. [Q16851-1]
ENST00000394417; ENSP00000377939; ENSG00000169764. [Q16851-2]
ENST00000467648; ENSP00000420793; ENSG00000169764. [Q16851-2]
GeneID7360.
KEGGhsa:7360.
UCSCuc002scl.3. human. [Q16851-1]

Organism-specific databases

CTD7360.
GeneCardsGC02P064068.
HGNCHGNC:12527. UGP2.
HPAHPA034696.
MIM191750. gene.
191760. gene.
neXtProtNX_Q16851.
PharmGKBPA37172.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4284.
HOGENOMHOG000113618.
HOVERGENHBG055396.
InParanoidQ16851.
KOK00963.
OrthoDBEOG7ZPNK4.
PhylomeDBQ16851.
TreeFamTF300567.

Enzyme and pathway databases

BioCycMetaCyc:HS10006-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ16851.

Gene expression databases

ArrayExpressQ16851.
BgeeQ16851.
CleanExHS_UGP2.
GenevestigatorQ16851.

Family and domain databases

InterProIPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]
PANTHERPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFPIRSF000806. UDPGP. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUGP2. human.
GenomeRNAi7360.
NextBio28818.
PROQ16851.
SOURCESearch...

Entry information

Entry nameUGPA_HUMAN
AccessionPrimary (citable) accession number: Q16851
Secondary accession number(s): Q07131 expand/collapse secondary AC list , Q0P6K2, Q86Y81, Q9BU15
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 122 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM