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P11172

- UMPS_HUMAN

UniProt

P11172 - UMPS_HUMAN

Protein

Uridine 5'-monophosphate synthase

Gene

UMPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.
    Orotidine 5'-phosphate = UMP + CO2.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei312 – 3121For OMPdecase activity1 Publication
    Active sitei314 – 3141For OMPdecase activity1 Publication
    Active sitei317 – 3171For OMPdecase activity1 Publication

    GO - Molecular functioni

    1. orotate phosphoribosyltransferase activity Source: UniProtKB
    2. orotidine-5'-phosphate decarboxylase activity Source: UniProtKB

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    3. cellular response to drug Source: Ensembl
    4. female pregnancy Source: Ensembl
    5. lactation Source: Ensembl
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. pyrimidine nucleobase metabolic process Source: Reactome
    8. pyrimidine nucleoside biosynthetic process Source: Reactome
    9. small molecule metabolic process Source: Reactome
    10. UMP biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Decarboxylase, Glycosyltransferase, Lyase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Enzyme and pathway databases

    BRENDAi4.1.1.23. 2681.
    ReactomeiREACT_21376. Pyrimidine biosynthesis.
    UniPathwayiUPA00070; UER00119.
    UPA00070; UER00120.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uridine 5'-monophosphate synthase
    Short name:
    UMP synthase
    Including the following 2 domains:
    Orotate phosphoribosyltransferase (EC:2.4.2.10)
    Short name:
    OPRT
    Short name:
    OPRTase
    Orotidine 5'-phosphate decarboxylase (EC:4.1.1.23)
    Short name:
    ODC
    Alternative name(s):
    OMPdecase
    Gene namesi
    Name:UMPS
    ORF Names:OK/SW-cl.21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12563. UMPS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of pyrimidine metabolism resulting in megaloblastic anemia and orotic acid crystalluria that is frequently associated with some degree of physical and mental retardation. A minority of cases have additional features, particularly congenital malformations and immune deficiencies.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961R → G in ORAC1. 1 Publication
    VAR_006807
    Natural varianti109 – 1091V → G in ORAC1. 1 Publication
    VAR_006808
    Natural varianti429 – 4291G → R in ORAC1. 1 Publication
    VAR_006810

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi312 – 3121D → N: Loss of OMPdecase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi258900. phenotype.
    Orphaneti30. Hereditary orotic aciduria.
    PharmGKBiPA363.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 480479Uridine 5'-monophosphate synthasePRO_0000139649Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei214 – 2141Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11172.
    PaxDbiP11172.
    PeptideAtlasiP11172.
    PRIDEiP11172.

    PTM databases

    PhosphoSiteiP11172.

    Expressioni

    Gene expression databases

    ArrayExpressiP11172.
    BgeeiP11172.
    CleanExiHS_UMPS.
    GenevestigatoriP11172.

    Organism-specific databases

    HPAiHPA036178.
    HPA036179.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi113218. 13 interactions.
    DIPiDIP-29595N.
    IntActiP11172. 12 interactions.
    MINTiMINT-1397000.
    STRINGi9606.ENSP00000232607.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 169
    Turni17 – 193
    Beta strandi21 – 277
    Beta strandi33 – 386
    Helixi40 – 456
    Helixi47 – 6317
    Beta strandi69 – 735
    Turni75 – 784
    Helixi79 – 8911
    Beta strandi93 – 964
    Turni99 – 1024
    Beta strandi103 – 1053
    Beta strandi108 – 1114
    Beta strandi118 – 12912
    Helixi130 – 14112
    Beta strandi148 – 1547
    Helixi159 – 1646
    Turni165 – 1673
    Beta strandi169 – 1757
    Helixi176 – 18510
    Helixi191 – 20212
    Helixi227 – 2304
    Helixi238 – 25013
    Beta strandi254 – 2574
    Helixi263 – 27311
    Helixi274 – 2763
    Beta strandi278 – 2825
    Helixi284 – 2863
    Helixi292 – 30514
    Beta strandi308 – 3158
    Helixi319 – 3279
    Turni329 – 3313
    Helixi333 – 3353
    Beta strandi338 – 3447
    Helixi349 – 35810
    Turni359 – 3624
    Beta strandi364 – 3685
    Helixi381 – 39212
    Turni393 – 3964
    Beta strandi397 – 4015
    Beta strandi412 – 4165
    Beta strandi421 – 4255
    Beta strandi427 – 4293
    Beta strandi431 – 4333
    Helixi435 – 4395
    Turni440 – 4423
    Beta strandi445 – 4506
    Helixi451 – 4544
    Beta strandi456 – 4583
    Helixi459 – 47820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EAWX-ray2.88A/B190-480[»]
    2JGYX-ray1.95A/B224-479[»]
    2P1FX-ray1.76A190-480[»]
    2QCCX-ray1.85A/B224-480[»]
    2QCDX-ray2.03A/B224-480[»]
    2QCEX-ray1.43A224-480[»]
    2QCFX-ray1.22A224-480[»]
    2QCGX-ray1.75A/B224-480[»]
    2QCHX-ray1.95A/B224-480[»]
    2QCLX-ray1.85A/B224-480[»]
    2QCMX-ray1.67A224-480[»]
    2QCNX-ray1.85A/B224-480[»]
    2V30X-ray2.00A/B224-479[»]
    2WNSX-ray1.90A/B7-203[»]
    3BGGX-ray1.93A190-480[»]
    3BGJX-ray2.00A/B190-480[»]
    3BK0X-ray1.60A/B223-480[»]
    3BVJX-ray1.80A/B190-480[»]
    3DBPX-ray1.50A/B223-480[»]
    3EWUX-ray1.60A/B224-480[»]
    3EWWX-ray1.10A/B224-480[»]
    3EWXX-ray1.40A224-480[»]
    3EWYX-ray1.10A224-480[»]
    3EWZX-ray1.40A/B/C/D224-480[»]
    3EX1X-ray1.40A/B224-480[»]
    3EX2X-ray1.55A/B224-480[»]
    3EX3X-ray1.45A/B224-480[»]
    3EX4X-ray1.24A224-480[»]
    3EX6X-ray1.30A/B224-480[»]
    3G3DX-ray1.70A/B190-480[»]
    3G3MX-ray1.40A223-480[»]
    3L0KX-ray1.34A/B224-480[»]
    3L0NX-ray1.74A/B224-480[»]
    3MI2X-ray1.20A/B223-480[»]
    3MO7X-ray1.35A223-480[»]
    3MW7X-ray2.32A/B190-480[»]
    4HIBX-ray1.80A/B190-480[»]
    4HKPX-ray1.75A/B190-480[»]
    ProteinModelPortaliP11172.
    SMRiP11172. Positions 7-203, 224-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11172.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 214213OPRTaseAdd
    BLAST
    Regioni215 – 2206Domain linker
    Regioni221 – 480260OMPdecaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
    In the C-terminal section; belongs to the OMP decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0284.
    HOVERGENiHBG000870.
    InParanoidiP11172.
    KOiK13421.
    OMAiSMKPEFL.
    OrthoDBiEOG754HPB.
    PhylomeDBiP11172.
    TreeFamiTF314694.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.40.50.2020. 1 hit.
    HAMAPiMF_01208. PyrE.
    InterProiIPR013785. Aldolase_TIM.
    IPR014732. OMPdecase.
    IPR018089. OMPdecase_AS.
    IPR001754. OMPdeCOase_dom.
    IPR023031. OPRT.
    IPR004467. Or_phspho_trans_dom.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00215. OMPdecase. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SMARTiSM00934. OMPdecase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    SSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR00336. pyrE. 1 hit.
    TIGR01740. pyrF. 1 hit.
    PROSITEiPS00156. OMPDECASE. 1 hit.
    PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11172-1) [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

    MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL    50
    SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET 100
    KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI 150
    VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF 200
    IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK 250
    ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT 300
    LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV 350
    VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF 400
    ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG 450
    RGIISAADRL EAAEMYRKAA WEAYLSRLGV 480
    Length:480
    Mass (Da):52,222
    Last modified:July 1, 1989 - v1
    Checksum:iD985CD566B72F5CA
    GO
    Isoform 2 (identifier: P11172-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-178: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:302
    Mass (Da):33,051
    Checksum:i4B88EE5A8DC6FA65
    GO
    Isoform 3 (identifier: P11172-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-92: Missing.

    Show »
    Length:388
    Mass (Da):42,495
    Checksum:i1AA9931DE4283ABB
    GO
    Isoform 4 (identifier: P11172-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-178: Missing.
         328-424: Missing.

    Show »
    Length:205
    Mass (Da):22,922
    Checksum:i464CD94C5FDD0E5A
    GO

    Sequence cautioni

    The sequence CAB45710.3 differs from that shown. Reason: Erroneous termination at position 430. Translated as Gln.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131T → G in AAA61256. 1 PublicationCurated
    Sequence conflicti377 – 3771L → Q in AAA61256. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301S → G.1 Publication
    Corresponds to variant rs17843776 [ dbSNP | Ensembl ].
    VAR_020614
    Natural varianti96 – 961R → G in ORAC1. 1 Publication
    VAR_006807
    Natural varianti109 – 1091V → G in ORAC1. 1 Publication
    VAR_006808
    Natural varianti213 – 2131G → A.2 Publications
    Corresponds to variant rs1801019 [ dbSNP | Ensembl ].
    VAR_006809
    Natural varianti429 – 4291G → R in ORAC1. 1 Publication
    VAR_006810
    Natural varianti446 – 4461I → V.1 Publication
    Corresponds to variant rs3772809 [ dbSNP | Ensembl ].
    VAR_020615

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 178178Missing in isoform 2 and isoform 4. 2 PublicationsVSP_009273Add
    BLAST
    Alternative sequencei1 – 9292Missing in isoform 3. 1 PublicationVSP_047611Add
    BLAST
    Alternative sequencei328 – 42497Missing in isoform 4. 1 PublicationVSP_047612Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03626 mRNA. Translation: AAA61255.1.
    D86227 mRNA. Translation: BAA19920.1.
    D86228 mRNA. Translation: BAA19921.1.
    D86230 mRNA. Translation: BAA19923.1.
    AB041359 Genomic DNA. Translation: BAB20663.1.
    EU921891 mRNA. Translation: ACH48229.1.
    EU921895 mRNA. Translation: ACH48233.1.
    AB062285 mRNA. Translation: BAB93468.1.
    CR456787 mRNA. Translation: CAG33068.1.
    AL080099 mRNA. Translation: CAB45710.3. Sequence problems.
    AY691629 Genomic DNA. Translation: AAT85801.1.
    AC022336 Genomic DNA. No translation available.
    BC000364 mRNA. Translation: AAH00364.1.
    BC007511 mRNA. Translation: AAH07511.1.
    M36661 mRNA. Translation: AAA61256.1.
    CCDSiCCDS3029.1. [P11172-1]
    PIRiA30148.
    RefSeqiNP_000364.1. NM_000373.3. [P11172-1]
    UniGeneiHs.2057.

    Genome annotation databases

    EnsembliENST00000232607; ENSP00000232607; ENSG00000114491. [P11172-1]
    GeneIDi7372.
    KEGGihsa:7372.
    UCSCiuc003ehl.4. human. [P11172-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03626 mRNA. Translation: AAA61255.1 .
    D86227 mRNA. Translation: BAA19920.1 .
    D86228 mRNA. Translation: BAA19921.1 .
    D86230 mRNA. Translation: BAA19923.1 .
    AB041359 Genomic DNA. Translation: BAB20663.1 .
    EU921891 mRNA. Translation: ACH48229.1 .
    EU921895 mRNA. Translation: ACH48233.1 .
    AB062285 mRNA. Translation: BAB93468.1 .
    CR456787 mRNA. Translation: CAG33068.1 .
    AL080099 mRNA. Translation: CAB45710.3 . Sequence problems.
    AY691629 Genomic DNA. Translation: AAT85801.1 .
    AC022336 Genomic DNA. No translation available.
    BC000364 mRNA. Translation: AAH00364.1 .
    BC007511 mRNA. Translation: AAH07511.1 .
    M36661 mRNA. Translation: AAA61256.1 .
    CCDSi CCDS3029.1. [P11172-1 ]
    PIRi A30148.
    RefSeqi NP_000364.1. NM_000373.3. [P11172-1 ]
    UniGenei Hs.2057.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EAW X-ray 2.88 A/B 190-480 [» ]
    2JGY X-ray 1.95 A/B 224-479 [» ]
    2P1F X-ray 1.76 A 190-480 [» ]
    2QCC X-ray 1.85 A/B 224-480 [» ]
    2QCD X-ray 2.03 A/B 224-480 [» ]
    2QCE X-ray 1.43 A 224-480 [» ]
    2QCF X-ray 1.22 A 224-480 [» ]
    2QCG X-ray 1.75 A/B 224-480 [» ]
    2QCH X-ray 1.95 A/B 224-480 [» ]
    2QCL X-ray 1.85 A/B 224-480 [» ]
    2QCM X-ray 1.67 A 224-480 [» ]
    2QCN X-ray 1.85 A/B 224-480 [» ]
    2V30 X-ray 2.00 A/B 224-479 [» ]
    2WNS X-ray 1.90 A/B 7-203 [» ]
    3BGG X-ray 1.93 A 190-480 [» ]
    3BGJ X-ray 2.00 A/B 190-480 [» ]
    3BK0 X-ray 1.60 A/B 223-480 [» ]
    3BVJ X-ray 1.80 A/B 190-480 [» ]
    3DBP X-ray 1.50 A/B 223-480 [» ]
    3EWU X-ray 1.60 A/B 224-480 [» ]
    3EWW X-ray 1.10 A/B 224-480 [» ]
    3EWX X-ray 1.40 A 224-480 [» ]
    3EWY X-ray 1.10 A 224-480 [» ]
    3EWZ X-ray 1.40 A/B/C/D 224-480 [» ]
    3EX1 X-ray 1.40 A/B 224-480 [» ]
    3EX2 X-ray 1.55 A/B 224-480 [» ]
    3EX3 X-ray 1.45 A/B 224-480 [» ]
    3EX4 X-ray 1.24 A 224-480 [» ]
    3EX6 X-ray 1.30 A/B 224-480 [» ]
    3G3D X-ray 1.70 A/B 190-480 [» ]
    3G3M X-ray 1.40 A 223-480 [» ]
    3L0K X-ray 1.34 A/B 224-480 [» ]
    3L0N X-ray 1.74 A/B 224-480 [» ]
    3MI2 X-ray 1.20 A/B 223-480 [» ]
    3MO7 X-ray 1.35 A 223-480 [» ]
    3MW7 X-ray 2.32 A/B 190-480 [» ]
    4HIB X-ray 1.80 A/B 190-480 [» ]
    4HKP X-ray 1.75 A/B 190-480 [» ]
    ProteinModelPortali P11172.
    SMRi P11172. Positions 7-203, 224-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113218. 13 interactions.
    DIPi DIP-29595N.
    IntActi P11172. 12 interactions.
    MINTi MINT-1397000.
    STRINGi 9606.ENSP00000232607.

    Chemistry

    BindingDBi P11172.
    ChEMBLi CHEMBL5216.

    PTM databases

    PhosphoSitei P11172.

    Proteomic databases

    MaxQBi P11172.
    PaxDbi P11172.
    PeptideAtlasi P11172.
    PRIDEi P11172.

    Protocols and materials databases

    DNASUi 7372.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232607 ; ENSP00000232607 ; ENSG00000114491 . [P11172-1 ]
    GeneIDi 7372.
    KEGGi hsa:7372.
    UCSCi uc003ehl.4. human. [P11172-1 ]

    Organism-specific databases

    CTDi 7372.
    GeneCardsi GC03P124449.
    HGNCi HGNC:12563. UMPS.
    HPAi HPA036178.
    HPA036179.
    MIMi 258900. phenotype.
    613891. gene.
    neXtProti NX_P11172.
    Orphaneti 30. Hereditary orotic aciduria.
    PharmGKBi PA363.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0284.
    HOVERGENi HBG000870.
    InParanoidi P11172.
    KOi K13421.
    OMAi SMKPEFL.
    OrthoDBi EOG754HPB.
    PhylomeDBi P11172.
    TreeFami TF314694.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00119 .
    UPA00070 ; UER00120 .
    BRENDAi 4.1.1.23. 2681.
    Reactomei REACT_21376. Pyrimidine biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P11172.
    GeneWikii Uridine_monophosphate_synthetase.
    GenomeRNAii 7372.
    NextBioi 28866.
    PROi P11172.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11172.
    Bgeei P11172.
    CleanExi HS_UMPS.
    Genevestigatori P11172.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.40.50.2020. 1 hit.
    HAMAPi MF_01208. PyrE.
    InterProi IPR013785. Aldolase_TIM.
    IPR014732. OMPdecase.
    IPR018089. OMPdecase_AS.
    IPR001754. OMPdeCOase_dom.
    IPR023031. OPRT.
    IPR004467. Or_phspho_trans_dom.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00215. OMPdecase. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SMARTi SM00934. OMPdecase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR00336. pyrE. 1 hit.
    TIGR01740. pyrF. 1 hit.
    PROSITEi PS00156. OMPDECASE. 1 hit.
    PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence for the complete coding region of human UMP synthase."
      Suttle D.P., Bugg B.Y., Winkler J.K., Kanalas J.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:1754-1758(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning of human UMP synthase."
      Suchi M., Harada N., Tsuboi T., Asai K., Okajima K., Wada Y., Takagi Y.
      Adv. Exp. Med. Biol. 253A:511-518(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning of the human UMP synthase gene and characterization of point mutations in two hereditary orotic aciduria families."
      Suchi M., Mizuno H., Kawai Y., Tsuboi T., Sumi S., Okajima K., Hodgson M.E., Ogawa H., Wada Y.
      Am. J. Hum. Genet. 60:525-539(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ORAC1 GLY-96; GLY-109 AND ARG-429, VARIANT ALA-213.
      Tissue: Leukocyte.
    4. "Genomic analysis of UMPS expression and sequence reveals novel isoforms and sequence polymorphisms associated with 5-FU resistance."
      Griffith M., Pugh T.J., Tang M.J., Asano J.K., Ally A., Chan S.Y., Taylor G., Morin G.B., Tai I.T., Marra M.A.
      Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    5. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    8. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-30; ALA-213 AND VAL-446.
    9. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Muscle.
    11. "Molecular genetic studies on hereditary orotic aciduria: I. Purification of human orotidine 5'-monophosphate decarboxylase and cloning of its cDNA."
      Suchi M.
      Nagoya Med. J. 32:207-220(1988)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-480 (ISOFORM 1).
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "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-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design."
      Wittmann J.G., Heinrich D., Gasow K., Frey A., Diederichsen U., Rudolph M.G.
      Structure 16:82-92(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 224-480 IN COMPLEX WITH SUBSTRATE, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-312.

    Entry informationi

    Entry nameiUMPS_HUMAN
    AccessioniPrimary (citable) accession number: P11172
    Secondary accession number(s): B5LY68
    , B5LY72, O00758, O00759, O00760, Q16862, Q9H3Q2, Q9UG49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 172 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3