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Q9CWJ9

- PUR9_MOUSE

UniProt

Q9CWJ9 - PUR9_MOUSE

Protein

Bifunctional purine biosynthesis protein PURH

Gene

Atic

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    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 acceptorSequence Analysis
    Sitei266 – 2661Transition state stabilizerSequence Analysis
    Active sitei267 – 2671Proton acceptorCurated
    Binding sitei316 – 3161AICAR; via carbonyl oxygenBy similarity
    Binding sitei339 – 3391AICARBy similarity
    Binding sitei431 – 4311AICAR; shared with dimeric partnerBy similarity
    Binding sitei451 – 4511AICAR; shared with dimeric partnerBy similarity
    Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity
    Binding sitei588 – 5881AICAR; shared with dimeric partnerBy similarity

    Regions

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

    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

    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-acetylmethionineBy similarity
    Modified residuei199 – 1991N6-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the PurH family.Curated

    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.
    HAMAPiMF_00139. PurH.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221R → K in BAB26949. (PubMed:16141072)Curated
    Sequence conflicti183 – 1831A → T in BAE23927. (PubMed:16141072)Curated
    Sequence conflicti219 – 2191L → S in AAH39925. (PubMed:15489334)Curated
    Sequence conflicti371 – 3711Y → C in BAB27060. (PubMed:16141072)Curated

    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.
    HAMAPi MF_00139. PurH.
    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

    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: October 1, 2014
    This is version 110 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