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Q9CWJ9

- PUR9_MOUSE

UniProt

Q9CWJ9 - PUR9_MOUSE

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Protein

Bifunctional purine biosynthesis protein PURH

Gene
Atic, Purh
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis By similarity.

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371Proton acceptor Reviewed prediction
Sitei266 – 2661Transition state stabilizer Reviewed prediction
Active sitei267 – 2671Proton acceptor Inferred
Binding sitei316 – 3161AICAR; via carbonyl oxygen By similarity
Binding sitei339 – 3391AICAR By similarity
Binding sitei431 – 4311AICAR; shared with dimeric partner By similarity
Binding sitei451 – 4511AICAR; shared with dimeric partner By similarity
Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partner By similarity
Binding sitei588 – 5881AICAR; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143IMP By similarity
Nucleotide bindingi34 – 374IMP By similarity
Nucleotide bindingi64 – 674IMP By similarity
Nucleotide bindingi101 – 1044IMP By similarity
Nucleotide bindingi125 – 1273IMP By similarity

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-EC
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. brainstem development Source: Ensembl
  3. cerebellum development Source: Ensembl
  4. cerebral cortex development Source: Ensembl
  5. dihydrofolate metabolic process Source: Ensembl
  6. nucleoside metabolic process Source: Ensembl
  7. organ regeneration Source: Ensembl
  8. response to inorganic substance Source: Ensembl
  9. tetrahydrofolate biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:Atic
Synonyms:Purh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1351352. Atic.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000192157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei199 – 1991N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CWJ9.
PaxDbiQ9CWJ9.
PRIDEiQ9CWJ9.

2D gel databases

REPRODUCTION-2DPAGEQ9CWJ9.

PTM databases

PhosphoSiteiQ9CWJ9.

Expressioni

Gene expression databases

ArrayExpressiQ9CWJ9.
BgeeiQ9CWJ9.
GenevestigatoriQ9CWJ9.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi223864. 1 interaction.
IntActiQ9CWJ9. 2 interactions.
MINTiMINT-1855853.

Structurei

3D structure databases

ProteinModelPortaliQ9CWJ9.
SMRiQ9CWJ9. Positions 5-592.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 2082AICAR binding By similarity

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOVERGENiHBG006912.
InParanoidiQ9CWJ9.
KOiK00602.
OMAiRAFKTDP.
OrthoDBiEOG74N5GD.
PhylomeDBiQ9CWJ9.
TreeFamiTF105642.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CWJ9-1 [UniParc]FASTAAdd to Basket

« Hide

MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD    50
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLVRVVV 100
CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED 150
YAGVAAEMHG SDSKDTSLET RRHLALKAFT HTAQYDEAIS DYFRKQYSKG 200
ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV 250
TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA 300
VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA 350
LKILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF 400
SNIVTKNKDL PESALRDLIV ATVAVKYTQS NSVCYAKDGQ VIGIGAGQQS 450
RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEISNA IDQYVTGTIG 500
EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR 550
AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH 592
Length:592
Mass (Da):64,217
Last modified:May 1, 2007 - v2
Checksum:i8C5278040059FB5D
GO

Sequence cautioni

The sequence BAB28011.1 differs from that shown. Reason: Frameshift at position 558.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → K in BAB26949. 1 Publication
Sequence conflicti183 – 1831A → T in BAE23927. 1 Publication
Sequence conflicti219 – 2191L → S in AAH39925. 1 Publication
Sequence conflicti371 – 3711Y → C in BAB27060. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK010449 mRNA. Translation: BAB26949.3.
AK010611 mRNA. Translation: BAB27060.1.
AK012074 mRNA. Translation: BAB28011.1. Frameshift.
AK046353 mRNA. Translation: BAC32688.1.
AK076091 mRNA. Translation: BAC36175.1.
AK139235 mRNA. Translation: BAE23927.1.
BC039925 mRNA. Translation: AAH39925.2.
CCDSiCCDS15030.1.
RefSeqiNP_080471.2. NM_026195.3.
UniGeneiMm.38010.

Genome annotation databases

EnsembliENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
GeneIDi108147.
KEGGimmu:108147.
UCSCiuc007bjs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK010449 mRNA. Translation: BAB26949.3 .
AK010611 mRNA. Translation: BAB27060.1 .
AK012074 mRNA. Translation: BAB28011.1 . Frameshift.
AK046353 mRNA. Translation: BAC32688.1 .
AK076091 mRNA. Translation: BAC36175.1 .
AK139235 mRNA. Translation: BAE23927.1 .
BC039925 mRNA. Translation: AAH39925.2 .
CCDSi CCDS15030.1.
RefSeqi NP_080471.2. NM_026195.3.
UniGenei Mm.38010.

3D structure databases

ProteinModelPortali Q9CWJ9.
SMRi Q9CWJ9. Positions 5-592.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223864. 1 interaction.
IntActi Q9CWJ9. 2 interactions.
MINTi MINT-1855853.

Chemistry

BindingDBi Q9CWJ9.
ChEMBLi CHEMBL2277.

PTM databases

PhosphoSitei Q9CWJ9.

2D gel databases

REPRODUCTION-2DPAGE Q9CWJ9.

Proteomic databases

MaxQBi Q9CWJ9.
PaxDbi Q9CWJ9.
PRIDEi Q9CWJ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027384 ; ENSMUSP00000027384 ; ENSMUSG00000026192 .
GeneIDi 108147.
KEGGi mmu:108147.
UCSCi uc007bjs.2. mouse.

Organism-specific databases

CTDi 471.
MGIi MGI:1351352. Atic.

Phylogenomic databases

eggNOGi COG0138.
GeneTreei ENSGT00390000004553.
HOVERGENi HBG006912.
InParanoidi Q9CWJ9.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG74N5GD.
PhylomeDBi Q9CWJ9.
TreeFami TF105642.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

Miscellaneous databases

ChiTaRSi ATIC. mouse.
NextBioi 360158.
PROi Q9CWJ9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9CWJ9.
Bgeei Q9CWJ9.
Genevestigatori Q9CWJ9.

Family and domain databases

Gene3Di 1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProi IPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Corpora quadrigemina and Embryonic stem cell.
  2. "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].
    Strain: 129.
    Tissue: Mammary tumor.
  3. Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 98-108; 178-194 AND 531-545, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.

Entry informationi

Entry nameiPUR9_MOUSE
AccessioniPrimary (citable) accession number: Q9CWJ9
Secondary accession number(s): Q3UTQ3
, Q80UH0, Q8BPF0, Q8BQV9, Q9CRI1, Q9CZW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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