P22102 (PUR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	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.
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. 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 process	Purine biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway methylation Inferred from electronic annotation. Source: GOC 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
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP 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: EC phosphoribosylformylglycinamidine cyclo-ligase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1010

1010

Trifunctional purine biosynthetic protein adenosine-3

PRO_0000074937

Regions

Domain

111 – 318

208

ATP-grasp

Nucleotide binding

137 – 199

63

ATP By similarity

Region

434 – 809

376

AIRS

Region

810 – 1010

201

GART

Region

818 – 820

3

5'-phosphoribosylglycinamide binding

Region

896 – 899

4

10-formyltetrahydrofolate binding

Region

947 – 951

5

10-formyltetrahydrofolate binding

Region

977 – 980

4

5'-phosphoribosylglycinamide binding

Sites

Active site

915

1

Proton donor By similarity

Metal binding

288

1

Manganese By similarity

Metal binding

290

1

Manganese By similarity

Binding site

871

1

10-formyltetrahydrofolate

Binding site

913

1

10-formyltetrahydrofolate

Site

951

1

Raises pKa of active site His By similarity

Amino acid modifications

Modified residue

350

1

N6-acetyllysine Ref.8

Natural variations

Alternative sequence

434 – 1010

577

Missing in isoform Short.

VSP_005517

Natural variant

21

1

L → F.
Corresponds to variant rs1804387 [ dbSNP | Ensembl ].

VAR_011817

Natural variant

421

1

V → I. Ref.2 Ref.5
Corresponds to variant rs8788 [ dbSNP | Ensembl ].

VAR_011818

Natural variant

510

1

D → G.
Corresponds to variant rs35927582 [ dbSNP | Ensembl ].

VAR_051882

Natural variant

641

1

P → A.
Corresponds to variant rs34588874 [ dbSNP | Ensembl ].

VAR_051883

Natural variant

752

1

D → G.
Corresponds to variant rs8971 [ dbSNP | Ensembl ].

VAR_011819

Secondary structure

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1010

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Helix

12 – 21

10

Beta strand

27 – 34

8

Helix

37 – 39

3

Beta strand

40 – 47

8

Helix

55 – 65

11

Beta strand

69 – 72

4

Helix

76 – 79

4

Helix

82 – 88

7

Beta strand

93 – 95

3

Turn

98 – 101

4

Helix

102 – 105

4

Helix

107 – 116

10

Beta strand

124 – 129

6

Helix

130 – 139

10

Beta strand

144 – 151

8

Beta strand

158 – 160

3

Helix

164 – 174

11

Beta strand

187 – 191

5

Beta strand

195 – 204

10

Beta strand

209 – 211

3

Beta strand

215 – 222

8

Turn

223 – 225

3

Beta strand

226 – 238

13

Helix

244 – 253

10

Helix

255 – 264

10

Beta strand

271 – 280

10

Beta strand

283 – 292

10

Turn

295 – 297

3

Helix

298 – 301

4

Helix

302 – 304

3

Helix

309 – 317

9

Helix

321 – 324

4

Beta strand

333 – 340

8

Turn

342 – 345

4

Helix

357 – 362

6

Beta strand

366 – 375

10

Beta strand

378 – 381

4

Beta strand

383 – 395

13

Helix

396 – 409

14

Helix

423 – 428

6

Turn

479 – 483

5

Beta strand

485 – 494

10

Helix

499 – 506

8

Helix

512 – 525

14

Turn

526 – 528

3

Beta strand

530 – 542

13

Helix

545 – 562

18

Beta strand

565 – 573

9

Turn

575 – 577

3

Beta strand

583 – 594

12

Helix

595 – 597

3

Helix

602 – 604

3

Beta strand

610 – 615

6

Beta strand

617 – 619

3

Helix

624 – 633

10

Beta strand

648 – 650

3

Helix

651 – 655

5

Helix

663 – 671

9

Beta strand

677 – 680

4

Helix

685 – 689

5

Helix

691 – 693

3

Beta strand

698 – 703

6

Helix

704 – 706

3

Helix

711 – 720

10

Helix

724 – 730

7

Beta strand

735 – 741

7

Helix

743 – 745

3

Helix

746 – 755

10

Beta strand

760 – 768

9

Beta strand

776 – 779

4

Helix

781 – 785

5

Beta strand

809 – 817

9

Helix

821 – 829

9

Beta strand

836 – 844

9

Helix

848 – 855

8

Beta strand

860 – 862

3

Helix

865 – 867

3

Beta strand

868 – 870

3

Helix

871 – 884

14

Beta strand

889 – 894

6

Helix

901 – 906

6

Turn

907 – 909

3

Beta strand

910 – 918

9

Helix

927 – 934

8

Beta strand

937 – 945

9

Beta strand

955 – 962

8

Helix

969 – 992

24

Beta strand

995 – 998

4

Beta strand

1002 – 1006

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 9A4213F746EB17A2	FASTA	1,010	107,767
	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
	Isoform Short [UniParc]. Checksum: 45289299B5E9B397	FASTA	433	46,033
	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 VGFRAIAFLQ QPR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY.
[9]	"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].
[10]	"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.
[11]	"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.
[12]	"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.

IPI

IPI00025273.
IPI00218408.

PIR

AJHUPR. S12616.

RefSeq

NP_000810.1. NM_000819.4.
NP_001129477.1. NM_001136005.1.
NP_001129478.1. NM_001136006.1.
NP_780294.1. NM_175085.2.

UniGene

Hs.473648.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P22102.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22102. 8 interactions.

MINT

MINT-1143007.

STRING

9606.ENSP00000371236.

PTM databases

PhosphoSite

P22102.

Polymorphism databases

DMDM

131616.

Proteomic databases

PaxDb

P22102.

PeptideAtlas

P22102.

PRIDE

P22102.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000361093; ENSP00000354388; ENSG00000159131.
ENST00000381815; ENSP00000371236; ENSG00000159131.
ENST00000381831; ENSP00000371253; ENSG00000159131.
ENST00000381839; ENSP00000371261; ENSG00000159131.
ENST00000571089; ENSP00000459532; ENSG00000262473.
ENST00000573055; ENSP00000459391; ENSG00000262473.
ENST00000574893; ENSP00000460497; ENSG00000262473.
ENST00000575273; ENSP00000461700; ENSG00000262473.

GeneID

2618.

KEGG

hsa:2618.

UCSC

uc002yrx.3. human.
uc002ysa.2. human.

Organism-specific databases

CTD

2618.

GeneCards

GC21M034870.

HGNC

HGNC:4163. GART.

HPA

HPA002119.
HPA005779.

MIM

138440. gene.

neXtProt

NX_P22102.

PharmGKB

PA28576.

GenAtlas

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Phylogenomic databases

eggNOG

COG0151.

HOVERGEN

HBG008333.

InParanoid

P22102.

KO

K11787.

OMA

GETSEMP.

OrthoDB

EOG4FFD13.

PhylomeDB

P22102.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00074; UER00125.
UPA00074; UER00126.
UPA00074; UER00129.

Gene expression databases

ArrayExpress

P22102.

Bgee

P22102.

CleanEx

HS_GART.

Genevestigator

P22102.

GermOnline

ENSG00000159131. Homo sapiens.

Family and domain databases

Gene3D

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.

InterPro

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]

Pfam

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]

SUPFAM

SSF56042. AIR_synth_C. 1 hit.
SSF53328. formyl_transf. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF55326. PurM_N-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.

TIGRFAMs

TIGR00877. purD. 1 hit.
TIGR00878. purM. 1 hit.
TIGR00639. PurN. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
PS00184. GARS. 1 hit.
PS00373. GART. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P22102.

ChEMBL

CHEMBL3972.

ChiTaRS

GART. human.

DrugBank

DB00642. Pemetrexed.

EvolutionaryTrace

P22102.

GenomeRNAi

2618.

NextBio

10307.

SOURCE

Search...

Entry information

Entry name

PUR2_HUMAN

Accession

Primary (citable) accession number: P22102
Secondary accession number(s): A8K945 , A8KA32, D3DSF3, D3DSF4, O14659, Q52M77

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 151 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.