Q16851 (UGPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UGP2
Synonyms:	UGP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucose metabolic process Traceable author statement Ref.2. Source: ProtInc UDP-glucuronate biosynthetic process Traceable author statement. Source: Reactome glucose metabolic process Traceable author statement. Source: Reactome glycogen biosynthetic process Traceable author statement. Source: Reactome phosphorylation Non-traceable author statement. Source: UniProtKB xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity Traceable author statement Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 508	508	UTP--glucose-1-phosphate uridylyltransferase		PRO_0000185752
Regions
	Region	457 – 508	52	Oligomerization By similarity
Sites
	Active site	396	1	By similarity
	Metal binding	127	1	Magnesium By similarity
	Metal binding	253	1	Magnesium By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.6 Ref.8
	Modified residue	438	1	N6-acetyllysine Ref.5
Natural variations
	Alternative sequence	1 – 11	11	Missing in isoform 2.		VSP_012834
	Natural variant	268	1	M → I. Ref.1 Ref.2 Corresponds to variant rs1130982 [ dbSNP | Ensembl ].		VAR_033042
Experimental info
	Mutagenesis	123	1	C → S: No significant loss of activity.
	Mutagenesis	218	1	W → S: No significant loss of activity.
	Mutagenesis	266	1	H → R: No significant loss of activity.
	Mutagenesis	333	1	W → S: Loss of activity; possibly due to folding defect.
	Mutagenesis	389	1	R → H: No significant loss of activity.
	Mutagenesis	391	1	R → H: Loss of activity; possibly due to folding defect.
	Mutagenesis	422	1	R → H: No significant loss of activity.
	Mutagenesis	445	1	R → H: No significant loss of activity.
	Sequence conflict	25	1	R → L Ref.1
	Sequence conflict	44	1	S → T Ref.1
	Sequence conflict	48	1	F → Y Ref.1
	Sequence conflict	62	1	F → Y Ref.1
	Sequence conflict	152	1	T → S Ref.1
	Sequence conflict	202	1	L → R Ref.1
	Sequence conflict	202	1	L → R in AAB05640. Ref.2
	Sequence conflict	210	1	Y → S Ref.1
	Sequence conflict	214	1	N → S Ref.1
	Sequence conflict	240 – 241	2	IG → LE Ref.1
	Sequence conflict	356	1	A → P Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 60E54806807AB470	FASTA	508	56,940
	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
	Isoform 2 [UniParc]. Checksum: 2B3FD9731E371E47	FASTA	497	55,677
	10 20 30 40 50 60 MSQDGASQFQ EVIRQELELS VKKELEKILT TASSHEFEHT KKDLDGFRKL FHRFLQEKGP 70 80 90 100 110 120 SVDWGKIQRP PEDSIQPYEK IKARGLPDNI SSVLNKLVVV KLNGGLGTSM GCKGPKSLIG 130 140 150 160 170 180 VRNENTFLDL TVQQIEHLNK TYNTDVPLVL MNSFNTDEDT KKILQKYNHC RVKIYTFNQS 190 200 210 220 230 240 RYPRINKESL LPVAKDVSYS GENTEAWYPP GHGDIYASFY NSGLLDTFIG EGKEYIFVSN 250 260 270 280 290 300 IDNLGATVDL YILNHLMNPP NGKRCEFVME VTNKTRADVK GGTLTQYEGK LRLVEIAQVP 310 320 330 340 350 360 KAHVDEFKSV SKFKIFNTNN LWISLAAVKR LQEQNAIDME IIVNAKTLDG GLNVIQLETA 370 380 390 400 410 420 VGAAIKSFEN SLGINVPRSR FLPVKTTSDL LLVMSNLYSL NAGSLTMSEK REFPTVPLVK 430 440 450 460 470 480 LGSSFTKVQD YLRRFESIPD MLELDHLTVS GDVTFGKNVS LKGTVIIIAN HGDRIDIPPG 490 AVLENKIVSG NLRILDH

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.

IPI

IPI00329331.
IPI00395676.

PIR

S35692.

RefSeq

NP_001001521.1. NM_001001521.1.
NP_006750.3. NM_006759.3.

UniGene

Hs.516217.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16851.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16851. 6 interactions.

MINT

MINT-1468909.

STRING

9606.ENSP00000338703.

PTM databases

PhosphoSite

Q16851.

Polymorphism databases

DMDM

59803098.

2D gel databases

REPRODUCTION-2DPAGE

IPI00395676.

UCD-2DPAGE

Q16851.

Proteomic databases

PaxDb

Q16851.

PRIDE

Q16851.

Protocols and materials databases

DNASU

7360.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337130; ENSP00000338703; ENSG00000169764.
ENST00000394417; ENSP00000377939; ENSG00000169764.
ENST00000467648; ENSP00000420793; ENSG00000169764.

GeneID

7360.

KEGG

hsa:7360.

UCSC

uc002scl.3. human.

Organism-specific databases

CTD

7360.

GeneCards

GC02P063979.

HGNC

HGNC:12527. UGP2.

HPA

HPA034696.

MIM

191750. gene.
191760. gene.

neXtProt

NX_Q16851.

PharmGKB

PA37172.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4284.

HOGENOM

HOG000113618.

HOVERGEN

HBG055396.

InParanoid

Q16851.

KO

K00963.

PhylomeDB

Q16851.

Enzyme and pathway databases

BioCyc

MetaCyc:HS10006-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q16851.

Gene expression databases

ArrayExpress

Q16851.

Bgee

Q16851.

CleanEx

HS_UGP2.

Genevestigator

Q16851.

GermOnline

ENSG00000169764. Homo sapiens.

Family and domain databases

InterPro

IPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]

PANTHER

PTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.

Pfam

PF01704. UDPGP. 1 hit.
[Graphical view]

PIRSF

PIRSF000806. UDPGP. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

UGP2. human.

GenomeRNAi

7360.

NextBio

28818.

SOURCE

Search...

Entry information

Entry name

UGPA_HUMAN

Accession

Primary (citable) accession number: Q16851
Secondary accession number(s): Q07131 , Q0P6K2, Q86Y81, Q9BU15

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 114 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.