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P31939 (PUR9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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:
Bifunctional purine biosynthesis protein PURH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:ATIC
Synonyms:PURH
ORF Names:OK/SW-cl.86
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. Ref.16

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Subunit structure

Homodimer. Ref.15 Ref.16

Domain

The IMP cyclohydrolase activity resides in the N-terminal region.

Involvement in disease

AICAR transformylase/IMP cyclohydrolase deficiency (AICAR) [MIM:608688]: A neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICAR causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17

Sequence similarities

Belongs to the PurH family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
   Molecular functionHydrolase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

brainstem development

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

dihydrofolate metabolic process

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing compound metabolic process

Traceable author statement Ref.1. Source: ProtInc

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleoside metabolic process

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

response to inorganic substance

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionIMP cyclohydrolase activity

Traceable author statement. Source: Reactome

phosphoribosylaminoimidazolecarboxamide formyltransferase activity

Traceable author statement. Source: Reactome

protein homodimerization activity

Inferred from physical interaction Ref.15Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31939-1)

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: P31939-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAPGQL → MSSLS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000192156

Regions

Nucleotide binding12 – 143IMP
Nucleotide binding34 – 374IMP
Nucleotide binding64 – 674IMP
Nucleotide binding101 – 1044IMP
Nucleotide binding125 – 1273IMP
Region207 – 2082AICAR binding

Sites

Active site1371Proton acceptor Potential
Active site2671Proton acceptor Probable
Binding site3161AICAR; via carbonyl oxygen
Binding site3391AICAR
Binding site4311AICAR; shared with dimeric partner
Binding site4511AICAR; shared with dimeric partner
Binding site5411AICAR; via carbonyl oxygen; shared with dimeric partner
Binding site5881AICAR; shared with dimeric partner
Site2661Transition state stabilizer Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue1991N6-acetyllysine Ref.12

Natural variations

Alternative sequence1 – 66MAPGQL → MSSLS in isoform 2.
VSP_053495
Natural variant1161T → S. Ref.5 Ref.7
Corresponds to variant rs2372536 [ dbSNP | Ensembl ].
VAR_019306
Natural variant4261K → R in AICAR; loss of transformylase activity. Ref.17
VAR_019307

Experimental info

Sequence conflict1651D → G in AAA97405. Ref.1

Secondary structure

.......................................................................................................... 592
Helix Strand Turn

Details...

Sequences

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

Last modified October 10, 2002. Version 3.
Checksum: AD778892021F0888

FASTA59264,616
        10         20         30         40         50         60 
MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA CNLYPFVKTV ASPGVTVEEA 

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YVVVSTEMQS SESKDTSLET RRQLALKAFT 

       190        200        210        220        230        240 
HTAQYDEAIS DYFRKQYSKG VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL 

       250        260        270        280        290        300 
CDALNAWQLV KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 

       310        320        330        340        350        360 
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA LTILSKKKNG 

       370        380        390        400        410        420 
NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF SNVVTKNKDL PESALRDLIV 

       430        440        450        460        470        480 
ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PQVLSMKFKT 

       490        500        510        520        530        540 
GVKRAEISNA IDQYVTGTIG EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 

« Hide

Isoform 2 [UniParc].

Checksum: 372861CF93D74887
Show »

FASTA59164,524

References

« Hide 'large scale' references
[1]"The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping."
Rayl E.A., Moroson B.A., Beardsley G.P.
J. Biol. Chem. 271:2225-2233(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hepatoma.
[2]"Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript."
Yamauchi M., Seki N., Mita K., Saito T., Tsuji S., Hongo E., Morimyo M., Shiomi T., Koyama H.
DNA Res. 2:269-275(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[3]"Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase."
Sugita T., Aya H., Ueno M., Ishizuka T., Kawashima K.
J. Biochem. 122:309-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[4]"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.
[5]"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. expand/collapse author list , 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 2), VARIANT SER-116.
Tissue: Substantia nigra.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-116.
[8]"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: Pancreas.
[9]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-39; 91-97; 178-194; 208-225; 267-285 AND 417-426, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 178-189 AND 267-281.
Tissue: Keratinocyte.
[11]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor."
Wolan D.W., Cheong C.-G., Greasley S.E., Wilson I.A.
Biochemistry 43:1171-1183(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH XMP, SUBUNIT.
[16]"Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates."
Cheong C.-G., Wolan D.W., Greasley S.E., Horton P.A., Beardsley G.P., Wilson I.A.
J. Biol. Chem. 279:18034-18045(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH AICAR; XMP AND THE INHIBITORS BW1540 AND BW2315, FUNCTION, SUBUNIT.
[17]"AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC."
Marie S., Heron B., Bitoun P., Timmerman T., Van Den Berghe G., Vincent M.-F.
Am. J. Hum. Genet. 74:1276-1281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AICAR ARG-426, CHARACTERIZATION OF VARIANT AICAR ARG-426.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37436 mRNA. Translation: AAA97405.1.
D82348 mRNA. Translation: BAA11559.1.
D89976 mRNA. Translation: BAA21762.1.
AB062403 mRNA. Translation: BAB93490.1.
AK290067 mRNA. Translation: BAF82756.1.
AC073284 Genomic DNA. Translation: AAY24062.1.
CH471063 Genomic DNA. Translation: EAW70529.1.
BC008879 mRNA. Translation: AAH08879.1.
CCDSCCDS2398.1.
PIRJC4642.
RefSeqNP_004035.2. NM_004044.6. [P31939-1]
UniGeneHs.90280.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4RX-ray2.55A/B1-592[»]
1PKXX-ray1.90A/B/C/D1-592[»]
1PL0X-ray2.60A/B/C/D1-592[»]
ProteinModelPortalP31939.
SMRP31939. Positions 4-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106961. 46 interactions.
IntActP31939. 4 interactions.
MINTMINT-4999053.
STRING9606.ENSP00000236959.

Chemistry

BindingDBP31939.
ChEMBLCHEMBL2518.
DrugBankDB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSiteP31939.

Polymorphism databases

DMDM23831360.

2D gel databases

REPRODUCTION-2DPAGEIPI00289499.
UCD-2DPAGEP31939.

Proteomic databases

MaxQBP31939.
PaxDbP31939.
PeptideAtlasP31939.
PRIDEP31939.

Protocols and materials databases

DNASU471.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236959; ENSP00000236959; ENSG00000138363. [P31939-1]
ENST00000435675; ENSP00000415935; ENSG00000138363. [P31939-2]
GeneID471.
KEGGhsa:471.
UCSCuc002vex.4. human. [P31939-1]

Organism-specific databases

CTD471.
GeneCardsGC02P216176.
HGNCHGNC:794. ATIC.
HPACAB013462.
HPA021012.
MIM601731. gene.
608688. phenotype.
neXtProtNX_P31939.
Orphanet250977. AICA-ribosiduria.
PharmGKBPA25094.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
HOVERGENHBG006912.
InParanoidP31939.
KOK00602.
OMAAGDKANC.
OrthoDBEOG74N5GD.
PhylomeDBP31939.
TreeFamTF105642.

Enzyme and pathway databases

BioCycMetaCyc:HS06490-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP31939.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Gene expression databases

ArrayExpressP31939.
BgeeP31939.
CleanExHS_ATIC.
GenevestigatorP31939.

Family and domain databases

Gene3D1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATIC. human.
EvolutionaryTraceP31939.
GeneWikiInosine_monophosphate_synthase.
GenomeRNAi471.
NextBio1945.
PROP31939.
SOURCESearch...

Entry information

Entry namePUR9_HUMAN
AccessionPrimary (citable) accession number: P31939
Secondary accession number(s): A8K202 expand/collapse secondary AC list , E9PBU3, Q13856, Q53S28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 10, 2002
Last modified: July 9, 2014
This is version 150 of the entry and version 3 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 2

Human chromosome 2: entries, gene names and cross-references to MIM