Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P31939

- PUR9_HUMAN

UniProt

P31939 - PUR9_HUMAN

Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (10 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.1 Publication

    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 oxygen1 Publication
    Binding sitei339 – 3391AICAR1 Publication
    Binding sitei431 – 4311AICAR; shared with dimeric partner1 Publication
    Binding sitei451 – 4511AICAR; shared with dimeric partner1 Publication
    Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partner1 Publication
    Binding sitei588 – 5881AICAR; shared with dimeric partner1 Publication

    Regions

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

    GO - Molecular functioni

    1. IMP cyclohydrolase activity Source: Reactome
    2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: Reactome
    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. nucleobase-containing compound metabolic process Source: ProtInc
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. nucleoside metabolic process Source: Ensembl
    9. organ regeneration Source: Ensembl
    10. purine nucleobase metabolic process Source: Reactome
    11. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    12. response to inorganic substance Source: Ensembl
    13. small molecule metabolic process Source: Reactome
    14. tetrahydrofolate biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06490-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP31939.
    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
    ORF Names:OK/SW-cl.86
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:794. ATIC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti426 – 4261K → R in AICAR; loss of transformylase activity. 1 Publication
    VAR_019307

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi608688. phenotype.
    Orphaneti250977. AICA-ribosiduria.
    PharmGKBiPA25094.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000192156Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP31939.
    PaxDbiP31939.
    PeptideAtlasiP31939.
    PRIDEiP31939.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00289499.
    UCD-2DPAGEP31939.

    PTM databases

    PhosphoSiteiP31939.

    Expressioni

    Gene expression databases

    ArrayExpressiP31939.
    BgeeiP31939.
    CleanExiHS_ATIC.
    GenevestigatoriP31939.

    Organism-specific databases

    HPAiCAB013462.
    HPA021012.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi106961. 48 interactions.
    IntActiP31939. 4 interactions.
    MINTiMINT-4999053.
    STRINGi9606.ENSP00000236959.

    Structurei

    Secondary structure

    1
    592
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi17 – 259
    Turni26 – 283
    Beta strandi30 – 334
    Helixi35 – 428
    Turni43 – 453
    Helixi51 – 555
    Turni61 – 644
    Beta strandi65 – 673
    Helixi70 – 778
    Helixi82 – 9110
    Beta strandi96 – 1016
    Helixi106 – 1116
    Helixi117 – 1226
    Helixi127 – 13711
    Turni138 – 1414
    Beta strandi143 – 1453
    Helixi148 – 1503
    Helixi151 – 16010
    Beta strandi161 – 1655
    Helixi168 – 19730
    Turni200 – 2023
    Beta strandi203 – 2075
    Beta strandi209 – 2113
    Beta strandi217 – 2204
    Beta strandi222 – 2254
    Beta strandi227 – 2337
    Helixi237 – 25721
    Beta strandi261 – 2666
    Beta strandi269 – 2757
    Helixi281 – 2866
    Helixi290 – 2956
    Helixi298 – 30811
    Turni311 – 3166
    Beta strandi317 – 3237
    Helixi327 – 3348
    Beta strandi338 – 3447
    Helixi348 – 36013
    Beta strandi363 – 3675
    Beta strandi375 – 3817
    Beta strandi384 – 3896
    Helixi397 – 4004
    Helixi412 – 42615
    Beta strandi433 – 4375
    Beta strandi440 – 4456
    Helixi451 – 46717
    Helixi471 – 4744
    Helixi486 – 49611
    Helixi503 – 5097
    Beta strandi512 – 5143
    Helixi521 – 5288
    Beta strandi534 – 5407
    Beta strandi543 – 5453
    Helixi546 – 5527
    Turni553 – 5553
    Beta strandi556 – 5627
    Helixi568 – 57811
    Beta strandi581 – 5866

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P4RX-ray2.55A/B1-592[»]
    1PKXX-ray1.90A/B/C/D1-592[»]
    1PL0X-ray2.60A/B/C/D1-592[»]
    ProteinModelPortaliP31939.
    SMRiP31939. Positions 4-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31939.

    Family & Domainsi

    Region

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the PurH family.Curated

    Phylogenomic databases

    eggNOGiCOG0138.
    HOGENOMiHOG000230372.
    HOVERGENiHBG006912.
    InParanoidiP31939.
    KOiK00602.
    OMAiAGDKANC.
    OrthoDBiEOG74N5GD.
    PhylomeDBiP31939.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31939-1) [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

    MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD    50
    VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA 100
    CNLYPFVKTV ASPGVTVEEA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED 150
    YVVVSTEMQS SESKDTSLET RRQLALKAFT HTAQYDEAIS DYFRKQYSKG 200
    VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL CDALNAWQLV 250
    KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 300
    AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA 350
    LTILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF 400
    SNVVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS 450
    RIHCTRLAGD KANYWWLRHH PQVLSMKFKT GVKRAEISNA IDQYVTGTIG 500
    EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA FFPFRDNVDR 550
    AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 592
    Length:592
    Mass (Da):64,616
    Last modified:October 10, 2002 - v3
    Checksum:iAD778892021F0888
    GO
    Isoform 2 (identifier: P31939-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:591
    Mass (Da):64,524
    Checksum:i372861CF93D74887
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti165 – 1651D → G in AAA97405. (PubMed:8567683)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161T → S.2 Publications
    Corresponds to variant rs2372536 [ dbSNP | Ensembl ].
    VAR_019306
    Natural varianti426 – 4261K → R in AICAR; loss of transformylase activity. 1 Publication
    VAR_019307

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MAPGQL → MSSLS in isoform 2. 2 PublicationsVSP_053495

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2398.1. [P31939-1]
    PIRiJC4642.
    RefSeqiNP_004035.2. NM_004044.6. [P31939-1]
    UniGeneiHs.90280.

    Genome annotation databases

    EnsembliENST00000236959; ENSP00000236959; ENSG00000138363. [P31939-1]
    ENST00000435675; ENSP00000415935; ENSG00000138363. [P31939-2]
    GeneIDi471.
    KEGGihsa:471.
    UCSCiuc002vex.4. human. [P31939-1]

    Polymorphism databases

    DMDMi23831360.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2398.1. [P31939-1 ]
    PIRi JC4642.
    RefSeqi NP_004035.2. NM_004044.6. [P31939-1 ]
    UniGenei Hs.90280.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P4R X-ray 2.55 A/B 1-592 [» ]
    1PKX X-ray 1.90 A/B/C/D 1-592 [» ]
    1PL0 X-ray 2.60 A/B/C/D 1-592 [» ]
    ProteinModelPortali P31939.
    SMRi P31939. Positions 4-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106961. 48 interactions.
    IntActi P31939. 4 interactions.
    MINTi MINT-4999053.
    STRINGi 9606.ENSP00000236959.

    Chemistry

    BindingDBi P31939.
    ChEMBLi CHEMBL2518.
    DrugBanki DB00116. Tetrahydrofolic acid.

    PTM databases

    PhosphoSitei P31939.

    Polymorphism databases

    DMDMi 23831360.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00289499.
    UCD-2DPAGE P31939.

    Proteomic databases

    MaxQBi P31939.
    PaxDbi P31939.
    PeptideAtlasi P31939.
    PRIDEi P31939.

    Protocols and materials databases

    DNASUi 471.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236959 ; ENSP00000236959 ; ENSG00000138363 . [P31939-1 ]
    ENST00000435675 ; ENSP00000415935 ; ENSG00000138363 . [P31939-2 ]
    GeneIDi 471.
    KEGGi hsa:471.
    UCSCi uc002vex.4. human. [P31939-1 ]

    Organism-specific databases

    CTDi 471.
    GeneCardsi GC02P216176.
    HGNCi HGNC:794. ATIC.
    HPAi CAB013462.
    HPA021012.
    MIMi 601731. gene.
    608688. phenotype.
    neXtProti NX_P31939.
    Orphaneti 250977. AICA-ribosiduria.
    PharmGKBi PA25094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0138.
    HOGENOMi HOG000230372.
    HOVERGENi HBG006912.
    InParanoidi P31939.
    KOi K00602.
    OMAi AGDKANC.
    OrthoDBi EOG74N5GD.
    PhylomeDBi P31939.
    TreeFami TF105642.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    BioCyci MetaCyc:HS06490-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RK P31939.

    Miscellaneous databases

    ChiTaRSi ATIC. human.
    EvolutionaryTracei P31939.
    GeneWikii Inosine_monophosphate_synthase.
    GenomeRNAii 471.
    NextBioi 1945.
    PROi P31939.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31939.
    Bgeei P31939.
    CleanExi HS_ATIC.
    Genevestigatori P31939.

    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 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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. 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.

    Entry informationi

    Entry nameiPUR9_HUMAN
    AccessioniPrimary (citable) accession number: P31939
    Secondary accession number(s): A8K202
    , E9PBU3, Q13856, Q53S28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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