Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22102 (PUR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trifunctional purine biosynthetic protein adenosine-3

Including the following 3 domains:

  1. Phosphoribosylamine--glycine ligase
    EC=6.3.4.13
    Alternative name(s):
    Glycinamide ribonucleotide synthetase
    Short name=GARS
    Phosphoribosylglycinamide synthetase
  2. Phosphoribosylformylglycinamidine cyclo-ligase
    EC=6.3.3.1
    Alternative name(s):
    AIR synthase
    Short name=AIRS
    Phosphoribosyl-aminoimidazole synthetase
  3. Phosphoribosylglycinamide formyltransferase
    EC=2.1.2.2
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase
    GAR transformylase
    Short name=GART
Gene names
Name:GART
Synonyms:PGFT, PRGS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1010 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP-Rule MF_00138

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00138

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP-Rule MF_00138

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP-Rule MF_00138

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.

Sequence similarities

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.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

brainstem development

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

glycine metabolic process

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

response to inorganic substance

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

phosphoribosylamine-glycine ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoribosylglycinamide formyltransferase activity

Traceable author statement PubMed 2050105. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P22102-1)

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.
Isoform Short (identifier: P22102-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 10101009Trifunctional purine biosynthetic protein adenosine-3 HAMAP-Rule MF_00138
PRO_0000074937

Regions

Domain111 – 318208ATP-grasp
Nucleotide binding137 – 19963ATP By similarity
Region434 – 809376AIRS HAMAP-Rule MF_00138
Region810 – 1010201GART HAMAP-Rule MF_00138
Region818 – 82035'-phosphoribosylglycinamide binding HAMAP-Rule MF_00138
Region896 – 899410-formyltetrahydrofolate binding HAMAP-Rule MF_00138
Region947 – 951510-formyltetrahydrofolate binding HAMAP-Rule MF_00138
Region977 – 98045'-phosphoribosylglycinamide binding HAMAP-Rule MF_00138

Sites

Active site9151Proton donor By similarity
Metal binding2881Manganese By similarity
Metal binding2901Manganese By similarity
Binding site871110-formyltetrahydrofolate
Binding site913110-formyltetrahydrofolate
Site9511Raises pKa of active site His By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue3501N6-acetyllysine Ref.9

Natural variations

Alternative sequence434 – 1010577Missing in isoform Short.
VSP_005517
Natural variant211L → F.
Corresponds to variant rs1804387 [ dbSNP | Ensembl ].
VAR_011817
Natural variant4211V → I. Ref.2 Ref.5
Corresponds to variant rs8788 [ dbSNP | Ensembl ].
VAR_011818
Natural variant5101D → G.
Corresponds to variant rs35927582 [ dbSNP | Ensembl ].
VAR_051882
Natural variant6411P → A.
Corresponds to variant rs34588874 [ dbSNP | Ensembl ].
VAR_051883
Natural variant7521D → G.
Corresponds to variant rs8971 [ dbSNP | Ensembl ].
VAR_011819

Secondary structure

.................................................................................................................................................................... 1010
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 9A4213F746EB17A2

FASTA1,010107,767
        10         20         30         40         50         60 
MAARVLIIGS GGREHTLAWK LAQSHHVKQV LVAPGNAGTA CSEKISNTAI SISDHTALAQ 

        70         80         90        100        110        120 
FCKEKKIEFV VVGPEAPLAA GIVGNLRSAG VQCFGPTAEA AQLESSKRFA KEFMDRHGIP 

       130        140        150        160        170        180 
TAQWKAFTKP EEACSFILSA DFPALVVKAS GLAAGKGVIV AKSKEEACKA VQEIMQEKAF 

       190        200        210        220        230        240 
GAAGETIVIE ELLDGEEVSC LCFTDGKTVA PMPPAQDHKR LLEGDGGPNT GGMGAYCPAP 

       250        260        270        280        290        300 
QVSNDLLLKI KDTVLQRTVD GMQQEGTPYT GILYAGIMLT KNGPKVLEFN CRFGDPECQV 

       310        320        330        340        350        360 
ILPLLKSDLY EVIQSTLDGL LCTSLPVWLE NHTALTVVMA SKGYPGDYTK GVEITGFPEA 

       370        380        390        400        410        420 
QALGLEVFHA GTALKNGKVV THGGRVLAVT AIRENLISAL EEAKKGLAAI KFEGAIYRKD 

       430        440        450        460        470        480 
VGFRAIAFLQ QPRSLTYKES GVDIAAGNML VKKIQPLAKA TSRSGCKVDL GGFAGLFDLK 

       490        500        510        520        530        540 
AAGFKDPLLA SGTDGVGTKL KIAQLCNKHD TIGQDLVAMC VNDILAQGAE PLFFLDYFSC 

       550        560        570        580        590        600 
GKLDLSVTEA VVAGIAKACG KAGCALLGGE TAEMPDMYPP GEYDLAGFAV GAMERDQKLP 

       610        620        630        640        650        660 
HLERITEGDV VVGIASSGLH SNGFSLVRKI VAKSSLQYSS PAPDGCGDQT LGDLLLTPTR 

       670        680        690        700        710        720 
IYSHSLLPVL RSGHVKAFAH ITGGGLLENI PRVLPEKLGV DLDAQTWRIP RVFSWLQQEG 

       730        740        750        760        770        780 
HLSEEEMART FNCGVGAVLV VSKEQTEQIL RDIQQHKEEA WVIGSVVARA EGSPRVKVKN 

       790        800        810        820        830        840 
LIESMQINGS VLKNGSLTNH FSFEKKKARV AVLISGTGSN LQALIDSTRE PNSSAQIDIV 

       850        860        870        880        890        900 
ISNKAAVAGL DKAERAGIPT RVINHKLYKN RVEFDSAIDL VLEEFSIDIV CLAGFMRILS 

       910        920        930        940        950        960 
GPFVQKWNGK MLNIHPSLLP SFKGSNAHEQ ALETGVTVTG CTVHFVAEDV DAGQIILQEA 

       970        980        990       1000       1010 
VPVKRGDTVA TLSERVKLAE HKIFPAALQL VASGTVQLGE NGKICWVKEE 

« Hide

Isoform Short [UniParc].

Checksum: 45289299B5E9B397
Show »

FASTA43346,033

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13627.1. [P22102-1]
CCDS13628.1. [P22102-2]
PIRAJHUPR. S12616.
RefSeqNP_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]
UniGeneHs.473648.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP22102.
SMRP22102. Positions 1-430, 475-792, 808-1010.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108888. 33 interactions.
IntActP22102. 8 interactions.
MINTMINT-1143007.
STRING9606.ENSP00000371236.

Chemistry

BindingDBP22102.
ChEMBLCHEMBL3972.
DrugBankDB00642. Pemetrexed.

PTM databases

PhosphoSiteP22102.

Polymorphism databases

DMDM131616.

Proteomic databases

MaxQBP22102.
PaxDbP22102.
PeptideAtlasP22102.
PRIDEP22102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361093; 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]
GeneID2618.
KEGGhsa:2618.
UCSCuc002yrx.3. human. [P22102-1]
uc002ysa.2. human. [P22102-2]

Organism-specific databases

CTD2618.
GeneCardsGC21M034870.
HGNCHGNC:4163. GART.
HPAHPA002119.
HPA005779.
MIM138440. gene.
neXtProtNX_P22102.
PharmGKBPA28576.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0151.
HOVERGENHBG008333.
InParanoidP22102.
KOK11787.
OMAGMLFTGF.
PhylomeDBP22102.
TreeFamTF106368.

Enzyme and pathway databases

BioCycMetaCyc:HS08358-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Gene expression databases

ArrayExpressP22102.
BgeeP22102.
CleanExHS_GART.
GenevestigatorP22102.

Family and domain databases

Gene3D3.30.1330.10. 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.
HAMAPMF_00138. GARS.
MF_00741_B. AIRS_B.
InterProIPR010918. 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]
PfamPF00586. 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]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF53328. SSF53328. 1 hit.
SSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00877. purD. 1 hit.
TIGR00878. purM. 1 hit.
TIGR00639. PurN. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGART. human.
EvolutionaryTraceP22102.
GenomeRNAi2618.
NextBio10307.
PROP22102.
SOURCESearch...

Entry information

Entry namePUR2_HUMAN
AccessionPrimary (citable) accession number: P22102
Secondary accession number(s): A8K945 expand/collapse secondary AC list , A8KA32, D3DSF3, D3DSF4, O14659, Q52M77
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM