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Protein

UTP--glucose-1-phosphate uridylyltransferase

Gene

UGP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271MagnesiumBy similarity
Metal bindingi253 – 2531MagnesiumBy similarity
Active sitei396 – 3961By similarity

GO - Molecular functioni

  1. glucose binding Source: Ensembl
  2. identical protein binding Source: IntAct
  3. metal ion binding Source: UniProtKB-KW
  4. pyrimidine ribonucleotide binding Source: Ensembl
  5. UTP:glucose-1-phosphate uridylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular glucuronidation Source: Reactome
  3. glucose 1-phosphate metabolic process Source: Ensembl
  4. glucose metabolic process Source: Reactome
  5. glycogen biosynthetic process Source: Reactome
  6. pathogenesis Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. UDP-glucose metabolic process Source: ProtInc
  9. UDP-glucuronate biosynthetic process Source: Reactome
  10. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10006-MONOMER.
BRENDAi2.7.7.9. 2681.
ReactomeiREACT_169208. Glycogen synthesis.
REACT_6737. Formation of the active cofactor, UDP-glucuronate.
SABIO-RKQ16851.

Names & Taxonomyi

Protein namesi
Recommended name:
UTP--glucose-1-phosphate uridylyltransferase (EC:2.7.7.9)
Alternative name(s):
UDP-glucose pyrophosphorylase
Short name:
UDPGP
Short name:
UGPase
Gene namesi
Name:UGP2
Synonyms:UGP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12527. UGP2.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi123 – 1231C → S: No significant loss of activity. 1 Publication
Mutagenesisi218 – 2181W → S: No significant loss of activity. 1 Publication
Mutagenesisi266 – 2661H → R: No significant loss of activity. 1 Publication
Mutagenesisi333 – 3331W → S: Loss of activity; possibly due to folding defect. 1 Publication
Mutagenesisi389 – 3891R → H: No significant loss of activity. 1 Publication
Mutagenesisi391 – 3911R → H: Loss of activity; possibly due to folding defect. 1 Publication
Mutagenesisi422 – 4221R → H: No significant loss of activity. 1 Publication
Mutagenesisi445 – 4451R → H: No significant loss of activity. 1 Publication
Mutagenesisi502 – 5032NL → PE: Abolishes oligomerization and significantly increases enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA37172.

Polymorphism and mutation databases

BioMutaiUGP2.
DMDMi59803098.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508UTP--glucose-1-phosphate uridylyltransferasePRO_0000185752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine2 Publications
Modified residuei426 – 4261Phosphothreonine1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei438 – 4381N6-acetyllysine1 Publication
Modified residuei448 – 4481Phosphoserine1 Publication
Modified residuei461 – 4611Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16851.
PaxDbiQ16851.
PRIDEiQ16851.

2D gel databases

REPRODUCTION-2DPAGEIPI00395676.
UCD-2DPAGEQ16851.

PTM databases

PhosphoSiteiQ16851.

Expressioni

Gene expression databases

BgeeiQ16851.
CleanExiHS_UGP2.
ExpressionAtlasiQ16851. baseline and differential.
GenevestigatoriQ16851.

Organism-specific databases

HPAiHPA034696.

Interactioni

Subunit structurei

Homooctamer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-743729,EBI-743729
ARIH2O953764EBI-743729,EBI-711158
GLRX3O760033EBI-743729,EBI-374781
GRB2P629932EBI-743729,EBI-401755

Protein-protein interaction databases

BioGridi113207. 44 interactions.
IntActiQ16851. 7 interactions.
MINTiMINT-1468909.
STRINGi9606.ENSP00000338703.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R2WX-ray3.60A/B/C/D1-508[»]
3R3IX-ray3.57A/B/C/D1-508[»]
ProteinModelPortaliQ16851.
SMRiQ16851. Positions 22-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni457 – 50852OligomerizationAdd
BLAST
Regioni502 – 5032Critical for end-to-end subunit interaction

Sequence similaritiesi

Belongs to the UDPGP type 1 family.Curated

Phylogenomic databases

eggNOGiCOG4284.
GeneTreeiENSGT00390000003174.
HOGENOMiHOG000113618.
HOVERGENiHBG055396.
InParanoidiQ16851.
KOiK00963.
OrthoDBiEOG7ZPNK4.
PhylomeDBiQ16851.
TreeFamiTF300567.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR016267. UDPGP_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFiPIRSF000806. UDPGP. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16851-1) [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
MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH
60 70 80 90 100
TKKDLDGFRK LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN
110 120 130 140 150
ISSVLNKLVV VKLNGGLGTS MGCKGPKSLI GVRNENTFLD LTVQQIEHLN
160 170 180 190 200
KTYNTDVPLV LMNSFNTDED TKKILQKYNH CRVKIYTFNQ SRYPRINKES
210 220 230 240 250
LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI GEGKEYIFVS
260 270 280 290 300
NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
310 320 330 340 350
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM
360 370 380 390 400
EIIVNAKTLD GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD
410 420 430 440 450
LLLVMSNLYS LNAGSLTMSE KREFPTVPLV KLGSSFTKVQ DYLRRFESIP
460 470 480 490 500
DMLELDHLTV SGDVTFGKNV SLKGTVIIIA NHGDRIDIPP GAVLENKIVS

GNLRILDH
Length:508
Mass (Da):56,940
Last modified:January 23, 2007 - v5
Checksum:i60E54806807AB470
GO
Isoform 2 (identifier: Q16851-2) [UniParc]FASTAAdd to basket

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

Note: Initiator Met-1 is removed. Contains a N-acetylserine at position 2. Contains a phosphoserine at position 2.3 Publications

Show »
Length:497
Mass (Da):55,677
Checksum:i2B3FD9731E371E47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251R → L (PubMed:8354390).Curated
Sequence conflicti44 – 441S → T (PubMed:8354390).Curated
Sequence conflicti48 – 481F → Y (PubMed:8354390).Curated
Sequence conflicti62 – 621F → Y (PubMed:8354390).Curated
Sequence conflicti152 – 1521T → S (PubMed:8354390).Curated
Sequence conflicti202 – 2021L → R (PubMed:8354390).Curated
Sequence conflicti202 – 2021L → R in AAB05640 (PubMed:8631325).Curated
Sequence conflicti210 – 2101Y → S (PubMed:8354390).Curated
Sequence conflicti214 – 2141N → S (PubMed:8354390).Curated
Sequence conflicti240 – 2412IG → LE (PubMed:8354390).Curated
Sequence conflicti356 – 3561A → P (PubMed:8354390).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681M → I.2 Publications
Corresponds to variant rs1130982 [ dbSNP | Ensembl ].
VAR_033042

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111Missing in isoform 2. 2 PublicationsVSP_012834Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27460 mRNA. Translation: AAB05640.1.
BC000173 mRNA. Translation: AAH00173.2.
BC002954 mRNA. Translation: AAH02954.1.
BC047004 mRNA. Translation: AAH47004.1.
CCDSiCCDS1875.1. [Q16851-1]
CCDS42690.1. [Q16851-2]
PIRiS35692.
RefSeqiNP_001001521.1. NM_001001521.1. [Q16851-2]
NP_006750.3. NM_006759.3. [Q16851-1]
XP_005264594.1. XM_005264537.2. [Q16851-2]
XP_005264595.1. XM_005264538.1. [Q16851-2]
UniGeneiHs.516217.

Genome annotation databases

EnsembliENST00000337130; ENSP00000338703; ENSG00000169764. [Q16851-1]
ENST00000394417; ENSP00000377939; ENSG00000169764. [Q16851-2]
ENST00000467648; ENSP00000420793; ENSG00000169764. [Q16851-2]
GeneIDi7360.
KEGGihsa:7360.
UCSCiuc002scl.3. human. [Q16851-1]

Polymorphism and mutation databases

BioMutaiUGP2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27460 mRNA. Translation: AAB05640.1.
BC000173 mRNA. Translation: AAH00173.2.
BC002954 mRNA. Translation: AAH02954.1.
BC047004 mRNA. Translation: AAH47004.1.
CCDSiCCDS1875.1. [Q16851-1]
CCDS42690.1. [Q16851-2]
PIRiS35692.
RefSeqiNP_001001521.1. NM_001001521.1. [Q16851-2]
NP_006750.3. NM_006759.3. [Q16851-1]
XP_005264594.1. XM_005264537.2. [Q16851-2]
XP_005264595.1. XM_005264538.1. [Q16851-2]
UniGeneiHs.516217.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R2WX-ray3.60A/B/C/D1-508[»]
3R3IX-ray3.57A/B/C/D1-508[»]
ProteinModelPortaliQ16851.
SMRiQ16851. Positions 22-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113207. 44 interactions.
IntActiQ16851. 7 interactions.
MINTiMINT-1468909.
STRINGi9606.ENSP00000338703.

PTM databases

PhosphoSiteiQ16851.

Polymorphism and mutation databases

BioMutaiUGP2.
DMDMi59803098.

2D gel databases

REPRODUCTION-2DPAGEIPI00395676.
UCD-2DPAGEQ16851.

Proteomic databases

MaxQBiQ16851.
PaxDbiQ16851.
PRIDEiQ16851.

Protocols and materials databases

DNASUi7360.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337130; ENSP00000338703; ENSG00000169764. [Q16851-1]
ENST00000394417; ENSP00000377939; ENSG00000169764. [Q16851-2]
ENST00000467648; ENSP00000420793; ENSG00000169764. [Q16851-2]
GeneIDi7360.
KEGGihsa:7360.
UCSCiuc002scl.3. human. [Q16851-1]

Organism-specific databases

CTDi7360.
GeneCardsiGC02P064068.
HGNCiHGNC:12527. UGP2.
HPAiHPA034696.
MIMi191750. gene.
191760. gene.
neXtProtiNX_Q16851.
PharmGKBiPA37172.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4284.
GeneTreeiENSGT00390000003174.
HOGENOMiHOG000113618.
HOVERGENiHBG055396.
InParanoidiQ16851.
KOiK00963.
OrthoDBiEOG7ZPNK4.
PhylomeDBiQ16851.
TreeFamiTF300567.

Enzyme and pathway databases

BioCyciMetaCyc:HS10006-MONOMER.
BRENDAi2.7.7.9. 2681.
ReactomeiREACT_169208. Glycogen synthesis.
REACT_6737. Formation of the active cofactor, UDP-glucuronate.
SABIO-RKQ16851.

Miscellaneous databases

ChiTaRSiUGP2. human.
GenomeRNAii7360.
NextBioi28818.
PROiQ16851.
SOURCEiSearch...

Gene expression databases

BgeeiQ16851.
CleanExiHS_UGP2.
ExpressionAtlasiQ16851. baseline and differential.
GenevestigatoriQ16851.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR016267. UDPGP_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFiPIRSF000806. UDPGP. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2).
    Tissue: Cervix carcinoma.
  7. 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2).
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2).
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-426; SER-434; SER-448 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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.

Entry informationi

Entry nameiUGPA_HUMAN
AccessioniPrimary (citable) accession number: Q16851
Secondary accession number(s): Q07131
, Q0P6K2, Q86Y81, Q9BU15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 134 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 (PubMed:8354390) probably does not exist and corresponds to UGP2.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.