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O95045 (UPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uridine phosphorylase 2

Short name=UPase 2
Short name=UrdPase 2
EC=2.4.2.3
Gene names
Name:UPP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 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. Shows substrate specificity and accept uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates.

Catalytic activity

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

Enzyme regulation

A conditional disulfide bridge can form within the protein that dislocates a critical phosphate-coordinating arginine Arg-100 away from the active site, disabling the enzyme. Ref.5

Pathway

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

Tissue specificity

Predominantly expressed in kidney. Ref.1

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Sequence caution

The sequence AAH33529.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95045-1)

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: O95045-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLAPGCELDPDQEVVRTRPEDVPASPSTSTMIVSVLRPPSHASCTACGTVTFHIVERM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Uridine phosphorylase 2
PRO_0000063193

Amino acid modifications

Disulfide bond95 ↔ 102Redox-active Ref.5

Natural variations

Alternative sequence11M → MLAPGCELDPDQEVVRTRPE DVPASPSTSTMIVSVLRPPS HASCTACGTVTFHIVERM in isoform 2.
VSP_043756
Natural variant101R → S.
Corresponds to variant rs6710480 [ dbSNP | Ensembl ].
VAR_024431
Natural variant781M → L.
Corresponds to variant rs7561584 [ dbSNP | Ensembl ].
VAR_034580

Experimental info

Sequence conflict1531I → M in AAO61681. Ref.1
Sequence conflict1571T → R in AAO61681. Ref.1
Sequence conflict256 – 2627ESTVFAA → GIYSVCS in AAO61681. Ref.1

Secondary structure

.................................................. 317
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: 69F6BA1DC44977A3

FASTA31735,527
        10         20         30         40         50         60 
MASVIPASNR SMRSDRNTYV GKRFVHVKNP YLDLMDEDIL YHLDLGTKTH NLPAMFGDVK 

        70         80         90        100        110        120 
FVCVGGSPNR MKAFALFMHK ELGFEEAEED IKDICAGTDR YCMYKTGPVL AISHGMGIPS 

       130        140        150        160        170        180 
ISIMLHELIK LLHHARCCDV TIIRIGTSGG IGIAPGTVVI TDIAVDSFFK PRFEQVILDN 

       190        200        210        220        230        240 
IVTRSTELDK ELSEELFNCS KEIPNFPTLV GHTMCTYDFY EGQGRLDGAL CSFSREKKLD 

       250        260        270        280        290        300 
YLKRAFKAGV RNIEMESTVF AAMCGLCGLK AAVVCVTLLD RLDCDQINLP HDVLVEYQQR 

       310 
PQLLISNFIR RRLGLCD 

« Hide

Isoform 2 [UniParc].

Checksum: F1FF70496CD41D8F
Show »

FASTA37441,602

References

« Hide 'large scale' references
[1]"Identification of a novel human uridine phosphorylase."
Johansson M.
Biochem. Biophys. Res. Commun. 307:41-46(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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 2).
Tissue: Brain.
[5]"A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity."
Roosild T.P., Castronovo S., Villoso A., Ziemba A., Pizzorno G.
J. Struct. Biol. 176:229-237(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-314, ENZYME REGULATION, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY225131 mRNA. Translation: AAO61681.1.
AK122743 mRNA. Translation: BAG53699.1.
AC005539 Genomic DNA. Translation: AAD12227.1.
BC033529 mRNA. Translation: AAH33529.1. Different initiation.
CCDSCCDS2207.1. [O95045-1]
CCDS46435.1. [O95045-2]
RefSeqNP_001128570.1. NM_001135098.1. [O95045-2]
NP_775491.1. NM_173355.3. [O95045-1]
UniGeneHs.128427.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRFX-ray2.30A/B/C23-317[»]
3P0EX-ray2.00A/B/C/D/E/F21-314[»]
3P0FX-ray1.54A21-314[»]
ProteinModelPortalO95045.
SMRO95045. Positions 22-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127387. 1 interaction.
STRING9606.ENSP00000387230.

Chemistry

BindingDBO95045.

PTM databases

PhosphoSiteO95045.

Proteomic databases

PaxDbO95045.
PRIDEO95045.

Protocols and materials databases

DNASU151531.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000005756; ENSP00000005756; ENSG00000007001. [O95045-1]
ENST00000409859; ENSP00000387230; ENSG00000007001. [O95045-2]
ENST00000605860; ENSP00000474090; ENSG00000007001. [O95045-2]
GeneID151531.
KEGGhsa:151531.
UCSCuc002tzo.3. human. [O95045-2]
uc002tzp.3. human. [O95045-1]

Organism-specific databases

CTD151531.
GeneCardsGC02P158677.
HGNCHGNC:23061. UPP2.
HPAHPA035225.
HPA035226.
neXtProtNX_O95045.
PharmGKBPA134866434.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2820.
HOGENOMHOG000231747.
HOVERGENHBG047725.
InParanoidO95045.
KOK00757.
OMACMYKTGP.
OrthoDBEOG79W961.
PhylomeDBO95045.
TreeFamTF314310.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKO95045.
SignaLinkO95045.
UniPathwayUPA00574; UER00633.

Gene expression databases

BgeeO95045.
CleanExHS_UPP2.
GenevestigatorO95045.

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.
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

EvolutionaryTraceO95045.
GenomeRNAi151531.
NextBio86721.
PROO95045.

Entry information

Entry nameUPP2_HUMAN
AccessionPrimary (citable) accession number: O95045
Secondary accession number(s): B3KV87
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 110 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

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