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P11172 (UMPS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uridine 5'-monophosphate synthase

Short name=UMP synthase

Including the following 2 domains:

  1. Orotate phosphoribosyltransferase
    Short name=OPRT
    Short name=OPRTase
    EC=2.4.2.10
  2. Orotidine 5'-phosphate decarboxylase
    Short name=ODC
    EC=4.1.1.23
    Alternative name(s):
    OMPdecase
Gene names
Name:UMPS
ORF Names:OK/SW-cl.21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01208

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01208

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP-Rule MF_01208

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.

Subunit structure

Homodimer. Ref.17

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3

Sequence similarities

In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

In the C-terminal section; belongs to the OMP decarboxylase family.

Sequence caution

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

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Molecular functionDecarboxylase
Glycosyltransferase
Lyase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from direct assay PubMed 11730338PubMed 6893554. Source: UniProtKB

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleobase metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleoside biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15890648. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15890648. Source: UniProtKB

   Molecular_functionorotate phosphoribosyltransferase activity

Inferred from direct assay PubMed 11730338PubMed 6893554. Source: UniProtKB

orotidine-5'-phosphate decarboxylase activity

Inferred from direct assay PubMed 11730338PubMed 6893554. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11172-1)

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: P11172-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P11172-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
Isoform 4 (identifier: P11172-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 480479Uridine 5'-monophosphate synthase HAMAP-Rule MF_01208
PRO_0000139649

Regions

Region2 – 214213OPRTase HAMAP-Rule MF_01208
Region215 – 2206Domain linker HAMAP-Rule MF_01208
Region221 – 480260OMPdecase HAMAP-Rule MF_01208

Sites

Active site3121For OMPdecase activity Ref.17
Active site3141For OMPdecase activity Ref.17
Active site3171For OMPdecase activity Ref.17

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue2141Phosphoserine Ref.12 Ref.14

Natural variations

Alternative sequence1 – 178178Missing in isoform 2 and isoform 4.
VSP_009273
Alternative sequence1 – 9292Missing in isoform 3.
VSP_047611
Alternative sequence328 – 42497Missing in isoform 4.
VSP_047612
Natural variant301S → G. Ref.8
Corresponds to variant rs17843776 [ dbSNP | Ensembl ].
VAR_020614
Natural variant961R → G in ORAC1. Ref.3
VAR_006807
Natural variant1091V → G in ORAC1. Ref.3
VAR_006808
Natural variant2131G → A. Ref.3 Ref.8
Corresponds to variant rs1801019 [ dbSNP | Ensembl ].
VAR_006809
Natural variant4291G → R in ORAC1. Ref.3
VAR_006810
Natural variant4461I → V. Ref.8
Corresponds to variant rs3772809 [ dbSNP | Ensembl ].
VAR_020615

Experimental info

Mutagenesis3121D → N: Loss of OMPdecase activity. Ref.17
Sequence conflict131T → G in AAA61256. Ref.11
Sequence conflict3771L → Q in AAA61256. Ref.11

Secondary structure

........................................................................................ 480
Helix Strand Turn

Details...

Sequences

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

Last modified July 1, 1989. Version 1.
Checksum: D985CD566B72F5CA

FASTA48052,222
        10         20         30         40         50         60 
MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT 

        70         80         90        100        110        120 
AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL 

       130        140        150        160        170        180 
IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML 

       190        200        210        220        230        240 
EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA 

       250        260        270        280        290        300 
SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT 

       310        320        330        340        350        360 
LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP 

       370        380        390        400        410        420 
LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ 

       430        440        450        460        470        480 
LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV 

« Hide

Isoform 2 [UniParc].

Checksum: 4B88EE5A8DC6FA65
Show »

FASTA30233,051
Isoform 3 [UniParc].

Checksum: 1AA9931DE4283ABB
Show »

FASTA38842,495
Isoform 4 [UniParc].

Checksum: 464CD94C5FDD0E5A
Show »

FASTA20522,922

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA30148.
RefSeqNP_000364.1. NM_000373.3.
UniGeneHs.2057.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP11172.
SMRP11172. Positions 7-203, 224-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113218. 13 interactions.
DIPDIP-29595N.
IntActP11172. 12 interactions.
MINTMINT-1397000.
STRING9606.ENSP00000232607.

Chemistry

BindingDBP11172.
ChEMBLCHEMBL5216.

PTM databases

PhosphoSiteP11172.

Proteomic databases

PaxDbP11172.
PeptideAtlasP11172.
PRIDEP11172.

Protocols and materials databases

DNASU7372.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000232607; ENSP00000232607; ENSG00000114491. [P11172-1]
ENST00000413078; ENSP00000397965; ENSG00000114491. [P11172-4]
ENST00000536109; ENSP00000443577; ENSG00000114491. [P11172-3]
ENST00000538242; ENSP00000444988; ENSG00000114491. [P11172-2]
GeneID7372.
KEGGhsa:7372.
UCSCuc003ehl.4. human. [P11172-1]

Organism-specific databases

CTD7372.
GeneCardsGC03P124449.
HGNCHGNC:12563. UMPS.
HPAHPA036178.
HPA036179.
MIM258900. phenotype.
613891. gene.
neXtProtNX_P11172.
Orphanet30. Hereditary orotic aciduria.
PharmGKBPA363.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0284.
HOVERGENHBG000870.
InParanoidP11172.
KOK13421.
OMAMKPEFLH.
OrthoDBEOG754HPB.
PhylomeDBP11172.
TreeFamTF314694.

Enzyme and pathway databases

BRENDA4.1.1.23. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00070; UER00119.
UPA00070; UER00120.

Gene expression databases

ArrayExpressP11172.
BgeeP11172.
CleanExHS_UMPS.
GenevestigatorP11172.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01208. PyrE.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00336. pyrE. 1 hit.
TIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11172.
GeneWikiUridine_monophosphate_synthetase.
GenomeRNAi7372.
NextBio28866.
PROP11172.
SOURCESearch...

Entry information

Entry nameUMPS_HUMAN
AccessionPrimary (citable) accession number: P11172
Secondary accession number(s): B5LY68 expand/collapse secondary AC list , B5LY72, O00758, O00759, O00760, Q16862, Q9H3Q2, Q9UG49
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 167 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 3

Human chromosome 3: entries, gene names and cross-references to MIM