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O95045

- UPP2_HUMAN

UniProt

O95045 - UPP2_HUMAN

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Protein

Uridine phosphorylase 2

Gene

UPP2

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

Functioni

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 activityi

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

Enzyme regulationi

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.1 Publication

Pathwayi

GO - Molecular functioni

  1. uridine phosphorylase activity Source: UniProtKB

GO - Biological processi

  1. nucleobase-containing small molecule metabolic process Source: Reactome
  2. nucleoside metabolic process Source: UniProtKB
  3. nucleotide catabolic process Source: InterPro
  4. pyrimidine nucleobase metabolic process Source: Reactome
  5. pyrimidine nucleoside catabolic process Source: Reactome
  6. pyrimidine nucleoside salvage Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. UMP salvage Source: UniProtKB-UniPathway
  9. uridine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_1023. Pyrimidine catabolism.
REACT_655. Pyrimidine salvage reactions.
SABIO-RKO95045.
SignaLinkiO95045.
UniPathwayiUPA00574; UER00633.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridine phosphorylase 2 (EC:2.4.2.3)
Short name:
UPase 2
Short name:
UrdPase 2
Gene namesi
Name:UPP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:23061. UPP2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. type III intermediate filament Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134866434.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Uridine phosphorylase 2PRO_0000063193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 102Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO95045.
PRIDEiO95045.

PTM databases

PhosphoSiteiO95045.

Expressioni

Tissue specificityi

Predominantly expressed in kidney.1 Publication

Gene expression databases

BgeeiO95045.
CleanExiHS_UPP2.
GenevestigatoriO95045.

Organism-specific databases

HPAiHPA035225.
HPA035226.

Interactioni

Protein-protein interaction databases

BioGridi127387. 1 interaction.
STRINGi9606.ENSP00000387230.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343
Helixi41 – 433
Turni47 – 493
Helixi52 – 565
Beta strandi61 – 666
Helixi68 – 8215
Turni94 – 974
Beta strandi98 – 1003
Beta strandi103 – 1064
Beta strandi109 – 1135
Helixi118 – 13417
Beta strandi141 – 15313
Beta strandi158 – 1658
Beta strandi171 – 1777
Beta strandi180 – 1856
Helixi190 – 20112
Beta strandi208 – 2158
Helixi221 – 2233
Beta strandi226 – 2294
Helixi235 – 24814
Beta strandi250 – 2567
Helixi257 – 26610
Beta strandi270 – 28011
Turni281 – 2833
Helixi291 – 2988
Helixi300 – 31314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRFX-ray2.30A/B/C23-317[»]
3P0EX-ray2.00A/B/C/D/E/F21-314[»]
3P0FX-ray1.54A21-314[»]
ProteinModelPortaliO95045.
SMRiO95045. Positions 22-314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95045.

Family & Domainsi

Sequence similaritiesi

Belongs to the PNP/UDP phosphorylase family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG2820.
GeneTreeiENSGT00390000004400.
HOGENOMiHOG000231747.
HOVERGENiHBG047725.
InParanoidiO95045.
KOiK00757.
OMAiCMYKTGP.
OrthoDBiEOG79W961.
PhylomeDBiO95045.
TreeFamiTF314310.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010059. Uridine_phosphorylase_euk.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01719. euk_UDPppase. 1 hit.
PROSITEiPS01232. PNP_UDP_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95045-1) [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
MASVIPASNR SMRSDRNTYV GKRFVHVKNP YLDLMDEDIL YHLDLGTKTH
60 70 80 90 100
NLPAMFGDVK FVCVGGSPNR MKAFALFMHK ELGFEEAEED IKDICAGTDR
110 120 130 140 150
YCMYKTGPVL AISHGMGIPS ISIMLHELIK LLHHARCCDV TIIRIGTSGG
160 170 180 190 200
IGIAPGTVVI TDIAVDSFFK PRFEQVILDN IVTRSTELDK ELSEELFNCS
210 220 230 240 250
KEIPNFPTLV GHTMCTYDFY EGQGRLDGAL CSFSREKKLD YLKRAFKAGV
260 270 280 290 300
RNIEMESTVF AAMCGLCGLK AAVVCVTLLD RLDCDQINLP HDVLVEYQQR
310
PQLLISNFIR RRLGLCD
Length:317
Mass (Da):35,527
Last modified:May 1, 1999 - v1
Checksum:i69F6BA1DC44977A3
GO
Isoform 2 (identifier: O95045-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLAPGCELDPDQEVVRTRPEDVPASPSTSTMIVSVLRPPSHASCTACGTVTFHIVERM

Note: No experimental confirmation available.

Show »
Length:374
Mass (Da):41,602
Checksum:iF1FF70496CD41D8F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531I → M in AAO61681. (PubMed:12849978)Curated
Sequence conflicti157 – 1571T → R in AAO61681. (PubMed:12849978)Curated
Sequence conflicti256 – 2627ESTVFAA → GIYSVCS in AAO61681. (PubMed:12849978)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101R → S.
Corresponds to variant rs6710480 [ dbSNP | Ensembl ].
VAR_024431
Natural varianti78 – 781M → L.
Corresponds to variant rs7561584 [ dbSNP | Ensembl ].
VAR_034580

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLAPGCELDPDQEVVRTRPE DVPASPSTSTMIVSVLRPPS HASCTACGTVTFHIVERM in isoform 2. 1 PublicationVSP_043756

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY225131 mRNA. Translation: AAO61681.1.
AK122743 mRNA. Translation: BAG53699.1.
AC005539 Genomic DNA. Translation: AAD12227.1.
BC033529 mRNA. Translation: AAH33529.1. Different initiation.
CCDSiCCDS2207.1. [O95045-1]
CCDS46435.1. [O95045-2]
RefSeqiNP_001128570.1. NM_001135098.1. [O95045-2]
NP_775491.1. NM_173355.3. [O95045-1]
UniGeneiHs.128427.

Genome annotation databases

EnsembliENST00000005756; ENSP00000005756; ENSG00000007001. [O95045-1]
ENST00000605860; ENSP00000474090; ENSG00000007001. [O95045-2]
GeneIDi151531.
KEGGihsa:151531.
UCSCiuc002tzo.3. human. [O95045-2]
uc002tzp.3. human. [O95045-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY225131 mRNA. Translation: AAO61681.1 .
AK122743 mRNA. Translation: BAG53699.1 .
AC005539 Genomic DNA. Translation: AAD12227.1 .
BC033529 mRNA. Translation: AAH33529.1 . Different initiation.
CCDSi CCDS2207.1. [O95045-1 ]
CCDS46435.1. [O95045-2 ]
RefSeqi NP_001128570.1. NM_001135098.1. [O95045-2 ]
NP_775491.1. NM_173355.3. [O95045-1 ]
UniGenei Hs.128427.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XRF X-ray 2.30 A/B/C 23-317 [» ]
3P0E X-ray 2.00 A/B/C/D/E/F 21-314 [» ]
3P0F X-ray 1.54 A 21-314 [» ]
ProteinModelPortali O95045.
SMRi O95045. Positions 22-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127387. 1 interaction.
STRINGi 9606.ENSP00000387230.

Chemistry

BindingDBi O95045.
DrugBanki DB00544. Fluorouracil.

PTM databases

PhosphoSitei O95045.

Proteomic databases

PaxDbi O95045.
PRIDEi O95045.

Protocols and materials databases

DNASUi 151531.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000005756 ; ENSP00000005756 ; ENSG00000007001 . [O95045-1 ]
ENST00000605860 ; ENSP00000474090 ; ENSG00000007001 . [O95045-2 ]
GeneIDi 151531.
KEGGi hsa:151531.
UCSCi uc002tzo.3. human. [O95045-2 ]
uc002tzp.3. human. [O95045-1 ]

Organism-specific databases

CTDi 151531.
GeneCardsi GC02P158736.
HGNCi HGNC:23061. UPP2.
HPAi HPA035225.
HPA035226.
neXtProti NX_O95045.
PharmGKBi PA134866434.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2820.
GeneTreei ENSGT00390000004400.
HOGENOMi HOG000231747.
HOVERGENi HBG047725.
InParanoidi O95045.
KOi K00757.
OMAi CMYKTGP.
OrthoDBi EOG79W961.
PhylomeDBi O95045.
TreeFami TF314310.

Enzyme and pathway databases

UniPathwayi UPA00574 ; UER00633 .
Reactomei REACT_1023. Pyrimidine catabolism.
REACT_655. Pyrimidine salvage reactions.
SABIO-RK O95045.
SignaLinki O95045.

Miscellaneous databases

EvolutionaryTracei O95045.
GenomeRNAii 151531.
NextBioi 86721.
PROi O95045.

Gene expression databases

Bgeei O95045.
CleanExi HS_UPP2.
Genevestigatori O95045.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
InterProi IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010059. Uridine_phosphorylase_euk.
[Graphical view ]
PANTHERi PTHR21234. PTHR21234. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01719. euk_UDPppase. 1 hit.
PROSITEi PS01232. PNP_UDP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiUPP2_HUMAN
AccessioniPrimary (citable) accession number: O95045
Secondary accession number(s): B3KV87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 113 of the entry and version 1 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

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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