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P22102

- PUR2_HUMAN

UniProt

P22102 - PUR2_HUMAN

Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene

GART

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
    ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
    10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi288 – 2881ManganeseBy similarity
    Metal bindingi290 – 2901ManganeseBy similarity
    Binding sitei871 – 871110-formyltetrahydrofolate
    Binding sitei913 – 913110-formyltetrahydrofolate
    Active sitei915 – 9151Proton donorBy similarity
    Sitei951 – 9511Raises pKa of active site HisBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 19963ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methyltransferase activity Source: InterPro
    4. phosphoribosylamine-glycine ligase activity Source: UniProtKB-EC
    5. phosphoribosylformylglycinamidine cyclo-ligase activity Source: UniProtKB-EC
    6. phosphoribosylglycinamide formyltransferase activity Source: ProtInc

    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. glycine metabolic process Source: Ensembl
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. purine nucleobase biosynthetic process Source: InterPro
    8. purine nucleobase metabolic process Source: Reactome
    9. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    10. response to inorganic substance Source: Ensembl
    11. response to organic substance Source: Ensembl
    12. small molecule metabolic process Source: Reactome
    13. tetrahydrofolate biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08358-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00125.
    UPA00074; UER00126.
    UPA00074; UER00129.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trifunctional purine biosynthetic protein adenosine-3
    Including the following 3 domains:
    Phosphoribosylamine--glycine ligase (EC:6.3.4.13)
    Alternative name(s):
    Glycinamide ribonucleotide synthetase
    Short name:
    GARS
    Phosphoribosylglycinamide synthetase
    Phosphoribosylformylglycinamidine cyclo-ligase (EC:6.3.3.1)
    Alternative name(s):
    AIR synthase
    Short name:
    AIRS
    Phosphoribosyl-aminoimidazole synthetase
    Phosphoribosylglycinamide formyltransferase (EC:2.1.2.2)
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase
    GAR transformylase
    Short name:
    GART
    Gene namesi
    Name:GART
    Synonyms:PGFT, PRGS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:4163. GART.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10101009Trifunctional purine biosynthetic protein adenosine-3PRO_0000074937Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei350 – 3501N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP22102.
    PaxDbiP22102.
    PeptideAtlasiP22102.
    PRIDEiP22102.

    PTM databases

    PhosphoSiteiP22102.

    Expressioni

    Gene expression databases

    ArrayExpressiP22102.
    BgeeiP22102.
    CleanExiHS_GART.
    GenevestigatoriP22102.

    Organism-specific databases

    HPAiHPA002119.
    HPA005779.

    Interactioni

    Protein-protein interaction databases

    BioGridi108888. 34 interactions.
    IntActiP22102. 8 interactions.
    MINTiMINT-1143007.
    STRINGi9606.ENSP00000371236.

    Structurei

    Secondary structure

    1
    1010
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Helixi12 – 2110
    Beta strandi27 – 348
    Helixi37 – 393
    Beta strandi40 – 478
    Helixi55 – 6511
    Beta strandi69 – 724
    Helixi76 – 794
    Helixi82 – 887
    Beta strandi93 – 953
    Turni98 – 1014
    Helixi102 – 1054
    Helixi107 – 11610
    Beta strandi124 – 1296
    Helixi130 – 13910
    Beta strandi144 – 1518
    Beta strandi158 – 1603
    Helixi164 – 17411
    Beta strandi187 – 1915
    Beta strandi195 – 20410
    Beta strandi209 – 2113
    Beta strandi215 – 2228
    Turni223 – 2253
    Beta strandi226 – 23813
    Helixi244 – 25310
    Helixi255 – 26410
    Beta strandi271 – 28010
    Beta strandi283 – 29210
    Turni295 – 2973
    Helixi298 – 3014
    Helixi302 – 3043
    Helixi309 – 3179
    Helixi321 – 3244
    Beta strandi333 – 3408
    Turni342 – 3454
    Helixi357 – 3626
    Beta strandi366 – 37510
    Beta strandi378 – 3814
    Beta strandi383 – 39513
    Helixi396 – 40914
    Helixi423 – 4286
    Turni479 – 4835
    Beta strandi485 – 49410
    Helixi499 – 5068
    Helixi512 – 52514
    Turni526 – 5283
    Beta strandi530 – 54213
    Helixi545 – 56218
    Beta strandi565 – 5739
    Turni575 – 5773
    Beta strandi583 – 59412
    Helixi595 – 5973
    Helixi602 – 6043
    Beta strandi610 – 6156
    Beta strandi617 – 6193
    Helixi624 – 63310
    Beta strandi648 – 6503
    Helixi651 – 6555
    Helixi663 – 6719
    Beta strandi677 – 6804
    Helixi685 – 6895
    Helixi691 – 6933
    Beta strandi698 – 7036
    Helixi704 – 7063
    Helixi711 – 72010
    Helixi724 – 7307
    Beta strandi735 – 7417
    Helixi743 – 7453
    Helixi746 – 75510
    Beta strandi760 – 7689
    Beta strandi776 – 7794
    Helixi781 – 7855
    Beta strandi810 – 8178
    Helixi821 – 8288
    Beta strandi836 – 8449
    Helixi848 – 8558
    Beta strandi860 – 8623
    Helixi865 – 8673
    Beta strandi868 – 8703
    Helixi871 – 88414
    Beta strandi889 – 8946
    Helixi901 – 9066
    Turni907 – 9104
    Beta strandi911 – 9188
    Helixi927 – 9348
    Beta strandi937 – 9459
    Beta strandi955 – 9628
    Helixi969 – 99224
    Beta strandi995 – 9984
    Beta strandi1002 – 10065

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MEJX-ray2.00A/B/C810-1010[»]
    1MENX-ray2.23A/B/C810-1010[»]
    1MEOX-ray1.72A808-1010[»]
    1NJSX-ray1.98A/B808-1010[»]
    1RBMX-ray2.30A/B808-1010[»]
    1RBQX-ray2.10A/B/C/D808-1010[»]
    1RBYX-ray2.10A/B/C/D808-1010[»]
    1RBZX-ray2.10A/B808-1010[»]
    1RC0X-ray2.05A/B808-1010[»]
    1RC1X-ray2.25A/B808-1010[»]
    1ZLXX-ray2.20A808-1010[»]
    1ZLYX-ray2.07A808-1010[»]
    2QK4X-ray2.45A/B1-430[»]
    2V9YX-ray2.10A/B467-794[»]
    4EW1X-ray1.52A810-1010[»]
    4EW2X-ray1.60A808-1010[»]
    4EW3X-ray1.70A808-1010[»]
    ProteinModelPortaliP22102.
    SMRiP22102. Positions 1-430, 475-792, 808-1010.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22102.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 318208ATP-graspAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni434 – 809376AIRSAdd
    BLAST
    Regioni810 – 1010201GARTAdd
    BLAST
    Regioni818 – 82035'-phosphoribosylglycinamide binding
    Regioni896 – 899410-formyltetrahydrofolate binding
    Regioni947 – 951510-formyltetrahydrofolate binding
    Regioni977 – 98045'-phosphoribosylglycinamide binding

    Sequence similaritiesi

    In the N-terminal section; belongs to the GARS family.Curated
    In the central section; belongs to the AIR synthase family.Curated
    In the C-terminal section; belongs to the GART family.Curated
    Contains 1 ATP-grasp domain.Curated

    Phylogenomic databases

    eggNOGiCOG0151.
    HOVERGENiHBG008333.
    InParanoidiP22102.
    KOiK11787.
    OMAiGMLFTGF.
    PhylomeDBiP22102.
    TreeFamiTF106368.

    Family and domain databases

    Gene3Di3.30.1330.10. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.170. 1 hit.
    3.40.50.20. 1 hit.
    3.90.600.10. 1 hit.
    3.90.650.10. 1 hit.
    HAMAPiMF_00138. GARS.
    MF_00741_B. AIRS_B.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR016185. PreATP-grasp_dom.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    IPR000115. PRibGlycinamide_synth.
    IPR020560. PRibGlycinamide_synth_C-dom.
    IPR020559. PRibGlycinamide_synth_CS.
    IPR020562. PRibGlycinamide_synth_N.
    IPR004733. PurM_cligase.
    IPR016188. PurM_N-like.
    IPR004607. PurN_trans.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view]
    PfamiPF00586. AIRS. 1 hit.
    PF02769. AIRS_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    PF01071. GARS_A. 1 hit.
    PF02843. GARS_C. 1 hit.
    PF02844. GARS_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF55326. SSF55326. 1 hit.
    SSF56042. SSF56042. 1 hit.
    TIGRFAMsiTIGR00877. purD. 1 hit.
    TIGR00878. purM. 1 hit.
    TIGR00639. PurN. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS00184. GARS. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P22102-1) [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

    MAARVLIIGS GGREHTLAWK LAQSHHVKQV LVAPGNAGTA CSEKISNTAI     50
    SISDHTALAQ FCKEKKIEFV VVGPEAPLAA GIVGNLRSAG VQCFGPTAEA 100
    AQLESSKRFA KEFMDRHGIP TAQWKAFTKP EEACSFILSA DFPALVVKAS 150
    GLAAGKGVIV AKSKEEACKA VQEIMQEKAF GAAGETIVIE ELLDGEEVSC 200
    LCFTDGKTVA PMPPAQDHKR LLEGDGGPNT GGMGAYCPAP QVSNDLLLKI 250
    KDTVLQRTVD GMQQEGTPYT GILYAGIMLT KNGPKVLEFN CRFGDPECQV 300
    ILPLLKSDLY EVIQSTLDGL LCTSLPVWLE NHTALTVVMA SKGYPGDYTK 350
    GVEITGFPEA QALGLEVFHA GTALKNGKVV THGGRVLAVT AIRENLISAL 400
    EEAKKGLAAI KFEGAIYRKD VGFRAIAFLQ QPRSLTYKES GVDIAAGNML 450
    VKKIQPLAKA TSRSGCKVDL GGFAGLFDLK AAGFKDPLLA SGTDGVGTKL 500
    KIAQLCNKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC GKLDLSVTEA 550
    VVAGIAKACG KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP 600
    HLERITEGDV VVGIASSGLH SNGFSLVRKI VAKSSLQYSS PAPDGCGDQT 650
    LGDLLLTPTR IYSHSLLPVL RSGHVKAFAH ITGGGLLENI PRVLPEKLGV 700
    DLDAQTWRIP RVFSWLQQEG HLSEEEMART FNCGVGAVLV VSKEQTEQIL 750
    RDIQQHKEEA WVIGSVVARA EGSPRVKVKN LIESMQINGS VLKNGSLTNH 800
    FSFEKKKARV AVLISGTGSN LQALIDSTRE PNSSAQIDIV ISNKAAVAGL 850
    DKAERAGIPT RVINHKLYKN RVEFDSAIDL VLEEFSIDIV CLAGFMRILS 900
    GPFVQKWNGK MLNIHPSLLP SFKGSNAHEQ ALETGVTVTG CTVHFVAEDV 950
    DAGQIILQEA VPVKRGDTVA TLSERVKLAE HKIFPAALQL VASGTVQLGE 1000
    NGKICWVKEE 1010
    Length:1,010
    Mass (Da):107,767
    Last modified:August 1, 1991 - v1
    Checksum:i9A4213F746EB17A2
    GO
    Isoform Short (identifier: P22102-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         434-1010: Missing.

    Show »
    Length:433
    Mass (Da):46,033
    Checksum:i45289299B5E9B397
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211L → F.
    Corresponds to variant rs1804387 [ dbSNP | Ensembl ].
    VAR_011817
    Natural varianti421 – 4211V → I.2 Publications
    Corresponds to variant rs8788 [ dbSNP | Ensembl ].
    VAR_011818
    Natural varianti510 – 5101D → G.
    Corresponds to variant rs35927582 [ dbSNP | Ensembl ].
    VAR_051882
    Natural varianti641 – 6411P → A.
    Corresponds to variant rs34588874 [ dbSNP | Ensembl ].
    VAR_051883
    Natural varianti752 – 7521D → G.
    Corresponds to variant rs8971 [ dbSNP | Ensembl ].
    VAR_011819

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei434 – 1010577Missing in isoform Short. 1 PublicationVSP_005517Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54199 mRNA. Translation: CAA38119.1.
    AK292560 mRNA. Translation: BAF85249.1.
    AK292897 mRNA. Translation: BAF85586.1.
    CH471079 Genomic DNA. Translation: EAX09826.1.
    CH471079 Genomic DNA. Translation: EAX09827.1.
    CH471079 Genomic DNA. Translation: EAX09828.1.
    CH471079 Genomic DNA. Translation: EAX09829.1.
    BC038958 mRNA. Translation: AAH38958.1.
    BC093641 mRNA. Translation: AAH93641.1.
    BC101565 mRNA. Translation: AAI01566.1.
    AF008653 Genomic DNA. Translation: AAB70812.1.
    M32082 mRNA. Translation: AAA60077.1.
    CCDSiCCDS13627.1. [P22102-1]
    CCDS13628.1. [P22102-2]
    PIRiS12616. AJHUPR.
    RefSeqiNP_000810.1. NM_000819.4. [P22102-1]
    NP_001129477.1. NM_001136005.1. [P22102-1]
    NP_001129478.1. NM_001136006.1. [P22102-1]
    NP_780294.1. NM_175085.2. [P22102-2]
    XP_005260998.1. XM_005260941.1. [P22102-1]
    XP_006724052.1. XM_006723989.1. [P22102-1]
    XP_006724053.1. XM_006723990.1. [P22102-1]
    UniGeneiHs.473648.

    Genome annotation databases

    EnsembliENST00000361093; ENSP00000354388; ENSG00000159131. [P22102-2]
    ENST00000381815; ENSP00000371236; ENSG00000159131. [P22102-1]
    ENST00000381831; ENSP00000371253; ENSG00000159131. [P22102-1]
    ENST00000381839; ENSP00000371261; ENSG00000159131. [P22102-1]
    ENST00000571089; ENSP00000459532; ENSG00000262473. [P22102-1]
    ENST00000573055; ENSP00000459391; ENSG00000262473. [P22102-1]
    ENST00000575273; ENSP00000461700; ENSG00000262473. [P22102-1]
    GeneIDi2618.
    KEGGihsa:2618.
    UCSCiuc002yrx.3. human. [P22102-1]
    uc002ysa.2. human. [P22102-2]

    Polymorphism databases

    DMDMi131616.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54199 mRNA. Translation: CAA38119.1 .
    AK292560 mRNA. Translation: BAF85249.1 .
    AK292897 mRNA. Translation: BAF85586.1 .
    CH471079 Genomic DNA. Translation: EAX09826.1 .
    CH471079 Genomic DNA. Translation: EAX09827.1 .
    CH471079 Genomic DNA. Translation: EAX09828.1 .
    CH471079 Genomic DNA. Translation: EAX09829.1 .
    BC038958 mRNA. Translation: AAH38958.1 .
    BC093641 mRNA. Translation: AAH93641.1 .
    BC101565 mRNA. Translation: AAI01566.1 .
    AF008653 Genomic DNA. Translation: AAB70812.1 .
    M32082 mRNA. Translation: AAA60077.1 .
    CCDSi CCDS13627.1. [P22102-1 ]
    CCDS13628.1. [P22102-2 ]
    PIRi S12616. AJHUPR.
    RefSeqi NP_000810.1. NM_000819.4. [P22102-1 ]
    NP_001129477.1. NM_001136005.1. [P22102-1 ]
    NP_001129478.1. NM_001136006.1. [P22102-1 ]
    NP_780294.1. NM_175085.2. [P22102-2 ]
    XP_005260998.1. XM_005260941.1. [P22102-1 ]
    XP_006724052.1. XM_006723989.1. [P22102-1 ]
    XP_006724053.1. XM_006723990.1. [P22102-1 ]
    UniGenei Hs.473648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MEJ X-ray 2.00 A/B/C 810-1010 [» ]
    1MEN X-ray 2.23 A/B/C 810-1010 [» ]
    1MEO X-ray 1.72 A 808-1010 [» ]
    1NJS X-ray 1.98 A/B 808-1010 [» ]
    1RBM X-ray 2.30 A/B 808-1010 [» ]
    1RBQ X-ray 2.10 A/B/C/D 808-1010 [» ]
    1RBY X-ray 2.10 A/B/C/D 808-1010 [» ]
    1RBZ X-ray 2.10 A/B 808-1010 [» ]
    1RC0 X-ray 2.05 A/B 808-1010 [» ]
    1RC1 X-ray 2.25 A/B 808-1010 [» ]
    1ZLX X-ray 2.20 A 808-1010 [» ]
    1ZLY X-ray 2.07 A 808-1010 [» ]
    2QK4 X-ray 2.45 A/B 1-430 [» ]
    2V9Y X-ray 2.10 A/B 467-794 [» ]
    4EW1 X-ray 1.52 A 810-1010 [» ]
    4EW2 X-ray 1.60 A 808-1010 [» ]
    4EW3 X-ray 1.70 A 808-1010 [» ]
    ProteinModelPortali P22102.
    SMRi P22102. Positions 1-430, 475-792, 808-1010.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108888. 34 interactions.
    IntActi P22102. 8 interactions.
    MINTi MINT-1143007.
    STRINGi 9606.ENSP00000371236.

    Chemistry

    BindingDBi P22102.
    ChEMBLi CHEMBL3972.
    DrugBanki DB00642. Pemetrexed.

    PTM databases

    PhosphoSitei P22102.

    Polymorphism databases

    DMDMi 131616.

    Proteomic databases

    MaxQBi P22102.
    PaxDbi P22102.
    PeptideAtlasi P22102.
    PRIDEi P22102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361093 ; ENSP00000354388 ; ENSG00000159131 . [P22102-2 ]
    ENST00000381815 ; ENSP00000371236 ; ENSG00000159131 . [P22102-1 ]
    ENST00000381831 ; ENSP00000371253 ; ENSG00000159131 . [P22102-1 ]
    ENST00000381839 ; ENSP00000371261 ; ENSG00000159131 . [P22102-1 ]
    ENST00000571089 ; ENSP00000459532 ; ENSG00000262473 . [P22102-1 ]
    ENST00000573055 ; ENSP00000459391 ; ENSG00000262473 . [P22102-1 ]
    ENST00000575273 ; ENSP00000461700 ; ENSG00000262473 . [P22102-1 ]
    GeneIDi 2618.
    KEGGi hsa:2618.
    UCSCi uc002yrx.3. human. [P22102-1 ]
    uc002ysa.2. human. [P22102-2 ]

    Organism-specific databases

    CTDi 2618.
    GeneCardsi GC21M034870.
    HGNCi HGNC:4163. GART.
    HPAi HPA002119.
    HPA005779.
    MIMi 138440. gene.
    neXtProti NX_P22102.
    PharmGKBi PA28576.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0151.
    HOVERGENi HBG008333.
    InParanoidi P22102.
    KOi K11787.
    OMAi GMLFTGF.
    PhylomeDBi P22102.
    TreeFami TF106368.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00125 .
    UPA00074 ; UER00126 .
    UPA00074 ; UER00129 .
    BioCyci MetaCyc:HS08358-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    ChiTaRSi GART. human.
    EvolutionaryTracei P22102.
    GenomeRNAii 2618.
    NextBioi 10307.
    PROi P22102.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22102.
    Bgeei P22102.
    CleanExi HS_GART.
    Genevestigatori P22102.

    Family and domain databases

    Gene3Di 3.30.1330.10. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.170. 1 hit.
    3.40.50.20. 1 hit.
    3.90.600.10. 1 hit.
    3.90.650.10. 1 hit.
    HAMAPi MF_00138. GARS.
    MF_00741_B. AIRS_B.
    InterProi IPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR016185. PreATP-grasp_dom.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    IPR000115. PRibGlycinamide_synth.
    IPR020560. PRibGlycinamide_synth_C-dom.
    IPR020559. PRibGlycinamide_synth_CS.
    IPR020562. PRibGlycinamide_synth_N.
    IPR004733. PurM_cligase.
    IPR016188. PurM_N-like.
    IPR004607. PurN_trans.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view ]
    Pfami PF00586. AIRS. 1 hit.
    PF02769. AIRS_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    PF01071. GARS_A. 1 hit.
    PF02843. GARS_C. 1 hit.
    PF02844. GARS_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF53328. SSF53328. 1 hit.
    SSF55326. SSF55326. 1 hit.
    SSF56042. SSF56042. 1 hit.
    TIGRFAMsi TIGR00877. purD. 1 hit.
    TIGR00878. purM. 1 hit.
    TIGR00639. PurN. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS00184. GARS. 1 hit.
    PS00373. GART. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli."
      Aimi J., Qiu H., Williams J., Zalkin H., Dixon J.E.
      Nucleic Acids Res. 18:6665-6672(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    2. "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 LONG), VARIANT ILE-421.
      Tissue: Testis and Trachea.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 SHORT).
      Tissue: Brain and Testis.
    5. "Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene."
      Kan J.L.C., Moran R.G.
      Nucleic Acids Res. 25:3118-3123(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-432, VARIANT ILE-421.
    6. "Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations."
      Schild D., Brake A.J., Kiefer M.C., Young D., Barr P.J.
      Proc. Natl. Acad. Sci. U.S.A. 87:2916-2920(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 709-1010.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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].
    9. "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-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR."
      Zhang Y., Desharnais J., Greasley S.E., Beardsley G.P., Boger D.L., Wilson I.A.
      Biochemistry 41:14206-14215(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 808-1010 IN COMPLEX WITH SUBSTRATE.
    12. "Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid."
      Zhang Y., Desharnais J., Marsilje T.H., Li C., Hedrick M.P., Gooljarsingh L.T., Tavassoli A., Benkovic S.J., Olson A.J., Boger D.L., Wilson I.A.
      Biochemistry 42:6043-6056(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 808-1010 IN COMPLEX WITH FORMYLTETRAHYDROFOLATE ANALOG.
    13. "The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase."
      Dahms T.E., Sainz G., Giroux E.L., Caperelli C.A., Smith J.L.
      Biochemistry 44:9841-9850(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 808-1010 IN COMPLEX WITH SUBSTRATE ANALOGS.

    Entry informationi

    Entry nameiPUR2_HUMAN
    AccessioniPrimary (citable) accession number: P22102
    Secondary accession number(s): A8K945
    , A8KA32, D3DSF3, D3DSF4, O14659, Q52M77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 165 of the entry and version 1 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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