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P11172

- UMPS_HUMAN

UniProt

P11172 - UMPS_HUMAN

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Protein

Uridine 5'-monophosphate synthase

Gene

UMPS

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP11172.
CleanExiHS_UMPS.
ExpressionAtlasiP11172. baseline and differential.
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.
GeneTreeiENSGT00390000001856.
HOVERGENiHBG000870.
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

        10         20         30         40         50
MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL
60 70 80 90 100
SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET
110 120 130 140 150
KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI
160 170 180 190 200
VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF
210 220 230 240 250
IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK
260 270 280 290 300
ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT
310 320 330 340 350
LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV
360 370 380 390 400
VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF
410 420 430 440 450
ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG
460 470 480
RGIISAADRL EAAEMYRKAA WEAYLSRLGV
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]
uc011bkd.2. human.

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.
DrugBanki DB00544. Fluorouracil.

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 ]
uc011bkd.2. human.

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.
GeneTreei ENSGT00390000001856.
HOVERGENi HBG000870.
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

Bgeei P11172.
CleanExi HS_UMPS.
ExpressionAtlasi P11172. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 173 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