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P22102

- PUR2_HUMAN

UniProt

P22102 - PUR2_HUMAN

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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

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
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, UP000005640: Unplaced

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-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

BgeeiP22102.
CleanExiHS_GART.
ExpressionAtlasiP22102. baseline and differential.
GenevestigatoriP22102.

Organism-specific databases

HPAiHPA002119.
HPA005779.

Interactioni

Protein-protein interaction databases

BioGridi108888. 36 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 – 98Combined sources
Helixi12 – 2110Combined sources
Beta strandi27 – 348Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 478Combined sources
Helixi55 – 6511Combined sources
Beta strandi69 – 724Combined sources
Helixi76 – 794Combined sources
Helixi82 – 887Combined sources
Beta strandi93 – 953Combined sources
Turni98 – 1014Combined sources
Helixi102 – 1054Combined sources
Helixi107 – 11610Combined sources
Beta strandi124 – 1296Combined sources
Helixi130 – 13910Combined sources
Beta strandi144 – 1518Combined sources
Beta strandi158 – 1603Combined sources
Helixi164 – 17411Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi195 – 20410Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi215 – 2228Combined sources
Turni223 – 2253Combined sources
Beta strandi226 – 23813Combined sources
Helixi244 – 25310Combined sources
Helixi255 – 26410Combined sources
Beta strandi271 – 28010Combined sources
Beta strandi283 – 29210Combined sources
Turni295 – 2973Combined sources
Helixi298 – 3014Combined sources
Helixi302 – 3043Combined sources
Helixi309 – 3179Combined sources
Helixi321 – 3244Combined sources
Beta strandi333 – 3408Combined sources
Turni342 – 3454Combined sources
Helixi357 – 3626Combined sources
Beta strandi366 – 37510Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi383 – 39513Combined sources
Helixi396 – 40914Combined sources
Helixi423 – 4286Combined sources
Turni479 – 4835Combined sources
Beta strandi485 – 49410Combined sources
Helixi499 – 5068Combined sources
Helixi512 – 52514Combined sources
Turni526 – 5283Combined sources
Beta strandi530 – 54213Combined sources
Helixi545 – 56218Combined sources
Beta strandi565 – 5739Combined sources
Turni575 – 5773Combined sources
Beta strandi583 – 59412Combined sources
Helixi595 – 5973Combined sources
Helixi602 – 6043Combined sources
Beta strandi610 – 6156Combined sources
Beta strandi617 – 6193Combined sources
Helixi624 – 63310Combined sources
Beta strandi648 – 6503Combined sources
Helixi651 – 6555Combined sources
Helixi663 – 6719Combined sources
Beta strandi677 – 6804Combined sources
Helixi685 – 6895Combined sources
Helixi691 – 6933Combined sources
Beta strandi698 – 7036Combined sources
Helixi704 – 7063Combined sources
Helixi711 – 72010Combined sources
Helixi724 – 7307Combined sources
Beta strandi735 – 7417Combined sources
Helixi743 – 7453Combined sources
Helixi746 – 75510Combined sources
Beta strandi760 – 7689Combined sources
Beta strandi776 – 7794Combined sources
Helixi781 – 7855Combined sources
Beta strandi810 – 8178Combined sources
Helixi821 – 8288Combined sources
Beta strandi836 – 8449Combined sources
Helixi848 – 8558Combined sources
Beta strandi860 – 8623Combined sources
Helixi865 – 8673Combined sources
Beta strandi868 – 8703Combined sources
Helixi871 – 88414Combined sources
Beta strandi889 – 8946Combined sources
Helixi901 – 9066Combined sources
Turni907 – 9104Combined sources
Beta strandi911 – 9188Combined sources
Helixi927 – 9348Combined sources
Beta strandi937 – 9459Combined sources
Beta strandi955 – 9628Combined sources
Helixi969 – 99224Combined sources
Beta strandi995 – 9984Combined sources
Beta strandi1002 – 10065Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000292.
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. AIRS.
MF_01930. PurN.
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

        10         20         30         40         50
MAARVLIIGS GGREHTLAWK LAQSHHVKQV LVAPGNAGTA CSEKISNTAI
60 70 80 90 100
SISDHTALAQ FCKEKKIEFV VVGPEAPLAA GIVGNLRSAG VQCFGPTAEA
110 120 130 140 150
AQLESSKRFA KEFMDRHGIP TAQWKAFTKP EEACSFILSA DFPALVVKAS
160 170 180 190 200
GLAAGKGVIV AKSKEEACKA VQEIMQEKAF GAAGETIVIE ELLDGEEVSC
210 220 230 240 250
LCFTDGKTVA PMPPAQDHKR LLEGDGGPNT GGMGAYCPAP QVSNDLLLKI
260 270 280 290 300
KDTVLQRTVD GMQQEGTPYT GILYAGIMLT KNGPKVLEFN CRFGDPECQV
310 320 330 340 350
ILPLLKSDLY EVIQSTLDGL LCTSLPVWLE NHTALTVVMA SKGYPGDYTK
360 370 380 390 400
GVEITGFPEA QALGLEVFHA GTALKNGKVV THGGRVLAVT AIRENLISAL
410 420 430 440 450
EEAKKGLAAI KFEGAIYRKD VGFRAIAFLQ QPRSLTYKES GVDIAAGNML
460 470 480 490 500
VKKIQPLAKA TSRSGCKVDL GGFAGLFDLK AAGFKDPLLA SGTDGVGTKL
510 520 530 540 550
KIAQLCNKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC GKLDLSVTEA
560 570 580 590 600
VVAGIAKACG KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP
610 620 630 640 650
HLERITEGDV VVGIASSGLH SNGFSLVRKI VAKSSLQYSS PAPDGCGDQT
660 670 680 690 700
LGDLLLTPTR IYSHSLLPVL RSGHVKAFAH ITGGGLLENI PRVLPEKLGV
710 720 730 740 750
DLDAQTWRIP RVFSWLQQEG HLSEEEMART FNCGVGAVLV VSKEQTEQIL
760 770 780 790 800
RDIQQHKEEA WVIGSVVARA EGSPRVKVKN LIESMQINGS VLKNGSLTNH
810 820 830 840 850
FSFEKKKARV AVLISGTGSN LQALIDSTRE PNSSAQIDIV ISNKAAVAGL
860 870 880 890 900
DKAERAGIPT RVINHKLYKN RVEFDSAIDL VLEEFSIDIV CLAGFMRILS
910 920 930 940 950
GPFVQKWNGK MLNIHPSLLP SFKGSNAHEQ ALETGVTVTG CTVHFVAEDV
960 970 980 990 1000
DAGQIILQEA VPVKRGDTVA TLSERVKLAE HKIFPAALQL VASGTVQLGE
1010
NGKICWVKEE
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000573055; ENSP00000459391; ENSG00000262473.
ENST00000575273; ENSP00000461700; ENSG00000262473.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 36 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 .
ENST00000573055 ; ENSP00000459391 ; ENSG00000262473 .
ENST00000575273 ; ENSP00000461700 ; ENSG00000262473 .
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.
GeneTreei ENSGT00390000000292.
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

Bgeei P22102.
CleanExi HS_GART.
ExpressionAtlasi P22102. baseline and differential.
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. AIRS.
MF_01930. PurN.
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: November 26, 2014
This is version 167 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