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P22102

- PUR2_HUMAN

UniProt

P22102 - PUR2_HUMAN

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Protein
Trifunctional purine biosynthetic protein adenosine-3
Gene
GART, PGFT, PRGS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 19963ATP By similarity
Add
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
Complete GO annotation...

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
Complete GO annotation...

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-3UniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP22102.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni434 – 809376AIRSUniRule annotation
Add
BLAST
Regioni810 – 1010201GARTUniRule annotation
Add
BLAST
Regioni818 – 82035'-phosphoribosylglycinamide bindingUniRule annotation
Regioni896 – 899410-formyltetrahydrofolate bindingUniRule annotation
Regioni947 – 951510-formyltetrahydrofolate bindingUniRule annotation
Regioni977 – 98045'-phosphoribosylglycinamide bindingUniRule annotation

Sequence similaritiesi

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

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.
VSP_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]
ENST00000574893; ENSP00000460497; ENSG00000262473. [P22102-2]
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 ]
ENST00000574893 ; ENSP00000460497 ; ENSG00000262473 . [P22102-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 164 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

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