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O95045

- UPP2_HUMAN

UniProt

O95045 - UPP2_HUMAN

Protein

Uridine phosphorylase 2

Gene

UPP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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

    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

    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.
    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

    MASVIPASNR SMRSDRNTYV GKRFVHVKNP YLDLMDEDIL YHLDLGTKTH    50
    NLPAMFGDVK FVCVGGSPNR MKAFALFMHK ELGFEEAEED IKDICAGTDR 100
    YCMYKTGPVL AISHGMGIPS ISIMLHELIK LLHHARCCDV TIIRIGTSGG 150
    IGIAPGTVVI TDIAVDSFFK PRFEQVILDN IVTRSTELDK ELSEELFNCS 200
    KEIPNFPTLV GHTMCTYDFY EGQGRLDGAL CSFSREKKLD YLKRAFKAGV 250
    RNIEMESTVF AAMCGLCGLK AAVVCVTLLD RLDCDQINLP HDVLVEYQQR 300
    PQLLISNFIR RRLGLCD 317
    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.

    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 GC02P158677.
    HGNCi HGNC:23061. UPP2.
    HPAi HPA035225.
    HPA035226.
    neXtProti NX_O95045.
    PharmGKBi PA134866434.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2820.
    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

    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 1, 2014
    This is version 112 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