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Q16831 (UPP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uridine phosphorylase 1

Short name=UPase 1
Short name=UrdPase 1
EC=2.4.2.3
Gene names
Name:UPP1
Synonyms:UP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.

Catalytic activity

Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1.

Subunit structure

Homodimer. Ref.6 Ref.7

Induction

By vitamin D3 and a mixture of inflammatory cytokines: TNF, IL1/interleukin-1 and IFNG/IFN-gamma.

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16831-1)

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: Q16831-2)

Also known as: Truncated;

The sequence of this isoform differs from the canonical sequence as follows:
     15-36: NDCPVRLLNPNIAKMKEDILYH → KSGARHCGHNRAGSGYLLQGRV
     37-310: Missing.
Note: Inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Uridine phosphorylase 1
PRO_0000063191

Sites

Binding site2171Substrate
Binding site2191Substrate

Natural variations

Alternative sequence15 – 3622NDCPV…DILYH → KSGARHCGHNRAGSGYLLQG RV in isoform 2.
VSP_001279
Alternative sequence37 – 310274Missing in isoform 2.
VSP_001280

Secondary structure

................................................... 310
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 1.
Checksum: 110CF678561E53F3

FASTA31033,934
        10         20         30         40         50         60 
MAATGANAEK AESHNDCPVR LLNPNIAKMK EDILYHFNLT TSRHNFPALF GDVKFVCVGG 

        70         80         90        100        110        120 
SPSRMKAFIR CVGAELGLDC PGRDYPNICA GTDRYAMYKV GPVLSVSHGM GIPSISIMLH 

       130        140        150        160        170        180 
ELIKLLYYAR CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT 

       190        200        210        220        230        240 
DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY 

       250        260        270        280        290        300 
AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ ISSPRNVLSE YQQRPQRLVS 

       310 
YFIKKKLSKA 

« Hide

Isoform 2 (Truncated) [UniParc].

Checksum: 5D38DC6FA1548616
Show »

FASTA363,694

References

« Hide 'large scale' references
[1]"Cloning and expression of human uridine phosphorylase."
Watanabe S., Uchida T.
Biochem. Biophys. Res. Commun. 216:265-272(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Colon.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Ovary, Placenta and Skin.
[5]"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].
[6]"Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy."
Roosild T.P., Castronovo S., Fabbiani M., Pizzorno G.
BMC Struct. Biol. 9:14-14(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) ALONE AND IN COMPLEX WITH INHIBITOR, SUBUNIT.
[7]"Active site conformational dynamics in human uridine phosphorylase 1."
Roosild T.P., Castronovo S.
PLoS ONE 5:E12741-E12741(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH 5-FLUOROURACIL, SUBSTRATE-BINDING SITES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X90858 mRNA. Translation: CAA62369.1.
X90858 mRNA. Translation: CAA62370.1.
BT006699 mRNA. Translation: AAP35345.1.
CH471128 Genomic DNA. Translation: EAW60994.1.
CH471128 Genomic DNA. Translation: EAW60995.1.
BC001405 mRNA. Translation: AAH01405.1.
BC007348 mRNA. Translation: AAH07348.1.
BC053592 mRNA. Translation: AAH53592.1. Sequence problems.
PIRJC4343.
RefSeqNP_001274355.1. NM_001287426.1.
NP_001274357.1. NM_001287428.1.
NP_001274358.1. NM_001287429.1.
NP_001274359.1. NM_001287430.1.
NP_003355.1. NM_003364.3.
UniGeneHs.488240.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EUEX-ray2.30A1-310[»]
3EUFX-ray1.90A/B/C/D1-310[»]
3NBQX-ray2.30A/B/C/D1-310[»]
ProteinModelPortalQ16831.
SMRQ16831. Positions 16-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113224. 10 interactions.
IntActQ16831. 1 interaction.
STRING9606.ENSP00000330032.

Chemistry

BindingDBQ16831.
ChEMBLCHEMBL4811.

PTM databases

PhosphoSiteQ16831.

Polymorphism databases

DMDM2494059.

Proteomic databases

PaxDbQ16831.
PeptideAtlasQ16831.
PRIDEQ16831.

Protocols and materials databases

DNASU7378.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331803; ENSP00000330032; ENSG00000183696. [Q16831-1]
ENST00000341253; ENSP00000342878; ENSG00000183696. [Q16831-1]
ENST00000395560; ENSP00000378927; ENSG00000183696. [Q16831-2]
ENST00000395564; ENSP00000378931; ENSG00000183696. [Q16831-1]
ENST00000417464; ENSP00000413611; ENSG00000183696. [Q16831-2]
ENST00000457596; ENSP00000408899; ENSG00000183696. [Q16831-2]
GeneID7378.
KEGGhsa:7378.
UCSCuc003toj.3. human. [Q16831-1]

Organism-specific databases

CTD7378.
GeneCardsGC07P048094.
HGNCHGNC:12576. UPP1.
HPAHPA055394.
MIM191730. gene.
neXtProtNX_Q16831.
PharmGKBPA365.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2820.
HOGENOMHOG000231747.
HOVERGENHBG047725.
InParanoidQ16831.
KOK00757.
OMALGTGTHD.
PhylomeDBQ16831.
TreeFamTF314310.

Enzyme and pathway databases

BioCycMetaCyc:HS00053-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ16831.
SignaLinkQ16831.
UniPathwayUPA00574; UER00633.

Gene expression databases

ArrayExpressQ16831.
BgeeQ16831.
CleanExHS_UPP1.
GenevestigatorQ16831.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
InterProIPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010059. Uridine_phosphorylase_euk.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PTHR21234:SF4. PTHR21234:SF4. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01719. euk_UDPppase. 1 hit.
PROSITEPS01232. PNP_UDP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUPP1. human.
EvolutionaryTraceQ16831.
GeneWikiUPP1.
GenomeRNAi7378.
NextBio28890.
PROQ16831.
SOURCESearch...

Entry information

Entry nameUPP1_HUMAN
AccessionPrimary (citable) accession number: Q16831
Secondary accession number(s): D3DVM4, Q15362
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 119 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM