SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q16851

- UGPA_HUMAN

UniProt

Q16851 - UGPA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

UTP--glucose-1-phosphate uridylyltransferase

Gene
UGP2, UGP1
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 1271Magnesium By similarity
Metal bindingi253 – 2531Magnesium By similarity
Active sitei396 – 3961 By similarity

GO - Molecular functioni

  1. glucose binding Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  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. small molecule metabolic process Source: Reactome
  7. UDP-glucose metabolic process Source: ProtInc
  8. UDP-glucuronate biosynthetic process Source: Reactome
  9. 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.
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: Chromosome 2

Organism-specific databases

HGNCiHGNC:12527. UGP2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA37172.

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 residuei438 – 4381N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16851.
PaxDbiQ16851.
PRIDEiQ16851.

2D gel databases

REPRODUCTION-2DPAGEIPI00395676.
UCD-2DPAGEQ16851.

PTM databases

PhosphoSiteiQ16851.

Expressioni

Gene expression databases

ArrayExpressiQ16851.
BgeeiQ16851.
CleanExiHS_UGP2.
GenevestigatoriQ16851.

Organism-specific databases

HPAiHPA034696.

Interactioni

Subunit structurei

Homooctamer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629932EBI-743729,EBI-401755

Protein-protein interaction databases

BioGridi113207. 38 interactions.
IntActiQ16851. 6 interactions.
MINTiMINT-1468909.
STRINGi9606.ENSP00000338703.

Structurei

3D structure databases

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

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.

Phylogenomic databases

eggNOGiCOG4284.
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. Align

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

MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH    50
TKKDLDGFRK LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN 100
ISSVLNKLVV VKLNGGLGTS MGCKGPKSLI GVRNENTFLD LTVQQIEHLN 150
KTYNTDVPLV LMNSFNTDED TKKILQKYNH CRVKIYTFNQ SRYPRINKES 200
LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI GEGKEYIFVS 250
NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG 300
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM 350
EIIVNAKTLD GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD 400
LLLVMSNLYS LNAGSLTMSE KREFPTVPLV KLGSSFTKVQ DYLRRFESIP 450
DMLELDHLTV SGDVTFGKNV SLKGTVIIIA NHGDRIDIPP GAVLENKIVS 500
GNLRILDH 508
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.

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

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. VSP_012834Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251R → L1 Publication
Sequence conflicti44 – 441S → T1 Publication
Sequence conflicti48 – 481F → Y1 Publication
Sequence conflicti62 – 621F → Y1 Publication
Sequence conflicti152 – 1521T → S1 Publication
Sequence conflicti202 – 2021L → R1 Publication
Sequence conflicti202 – 2021L → R in AAB05640. 1 Publication
Sequence conflicti210 – 2101Y → S1 Publication
Sequence conflicti214 – 2141N → S1 Publication
Sequence conflicti240 – 2412IG → LE1 Publication
Sequence conflicti356 – 3561A → P1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi59803098.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U27460 mRNA. Translation: AAB05640.1 .
BC000173 mRNA. Translation: AAH00173.2 .
BC002954 mRNA. Translation: AAH02954.1 .
BC047004 mRNA. Translation: AAH47004.1 .
CCDSi CCDS1875.1. [Q16851-1 ]
CCDS42690.1. [Q16851-2 ]
PIRi S35692.
RefSeqi NP_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 ]
UniGenei Hs.516217.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3R2W X-ray 3.60 A/B/C/D 1-508 [» ]
3R3I X-ray 3.57 A/B/C/D 1-508 [» ]
ProteinModelPortali Q16851.
SMRi Q16851. Positions 22-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113207. 38 interactions.
IntActi Q16851. 6 interactions.
MINTi MINT-1468909.
STRINGi 9606.ENSP00000338703.

PTM databases

PhosphoSitei Q16851.

Polymorphism databases

DMDMi 59803098.

2D gel databases

REPRODUCTION-2DPAGE IPI00395676.
UCD-2DPAGE Q16851.

Proteomic databases

MaxQBi Q16851.
PaxDbi Q16851.
PRIDEi Q16851.

Protocols and materials databases

DNASUi 7360.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337130 ; ENSP00000338703 ; ENSG00000169764 . [Q16851-1 ]
ENST00000394417 ; ENSP00000377939 ; ENSG00000169764 . [Q16851-2 ]
ENST00000467648 ; ENSP00000420793 ; ENSG00000169764 . [Q16851-2 ]
GeneIDi 7360.
KEGGi hsa:7360.
UCSCi uc002scl.3. human. [Q16851-1 ]

Organism-specific databases

CTDi 7360.
GeneCardsi GC02P064068.
HGNCi HGNC:12527. UGP2.
HPAi HPA034696.
MIMi 191750. gene.
191760. gene.
neXtProti NX_Q16851.
PharmGKBi PA37172.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4284.
HOGENOMi HOG000113618.
HOVERGENi HBG055396.
InParanoidi Q16851.
KOi K00963.
OrthoDBi EOG7ZPNK4.
PhylomeDBi Q16851.
TreeFami TF300567.

Enzyme and pathway databases

BioCyci MetaCyc:HS10006-MONOMER.
Reactomei REACT_169208. Glycogen synthesis.
REACT_6737. Formation of the active cofactor, UDP-glucuronate.
SABIO-RK Q16851.

Miscellaneous databases

ChiTaRSi UGP2. human.
GenomeRNAii 7360.
NextBioi 28818.
PROi Q16851.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16851.
Bgeei Q16851.
CleanExi HS_UGP2.
Genevestigatori Q16851.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR029044. Nucleotide-diphossugar_trans.
IPR016267. UDPGP_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view ]
PANTHERi PTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
Pfami PF01704. UDPGP. 1 hit.
[Graphical view ]
PIRSFi PIRSF000806. UDPGP. 1 hit.
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. 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.

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: September 3, 2014
This is version 127 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 (1 Publication) probably does not exist and corresponds to UGP2.

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