Reviewed, UniProtKB/Swiss-Prot P22102 (PUR2_HUMAN)

Names and origin

Protein names

Recommended name:
    Trifunctional purine biosynthetic protein adenosine-3
Including the following 3 domains:
    1- Recommended name:
            Phosphoribosylamine--glycine ligase
              EC=6.3.4.13
        Alternative name(s):
            Glycinamide ribonucleotide synthetase
              Short name=GARS
            Phosphoribosylglycinamide synthetase
    2- Recommended name:
            Phosphoribosylformylglycinamidine cyclo-ligase
              EC=6.3.3.1
        Alternative name(s):
            Phosphoribosyl-aminoimidazole synthetase
            AIR synthase
              Short name=AIRS
    3- Recommended name:
            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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 Phosphoprotein
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from Experiment. Source: Reactome purine base biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARF6	P62330	1	EBI-356297,EBI-638181

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

Initiator methionine

1

1

Removed

Chain

2 – 1010

1009

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

2

1

N-acetylalanine Ref.10

Modified residue

348

1

Phosphotyrosine Ref.7 Ref.8

Modified residue

350

1

N6-acetyllysine Ref.11

Natural variations

Alternative sequence

434 – 1010

577

Missing in isoform Short.

VSP_005517

Natural variant

21

1

L → F: dbSNP rs1804387.

VAR_011817

Natural variant

421

1

V → I: dbSNP rs8788. Ref.2 Ref.5

VAR_011818

Natural variant

510

1

D → G: dbSNP rs35927582.

VAR_051882

Natural variant

641

1

P → A: dbSNP rs34588874.

VAR_051883

Natural variant

752

1

D → G: dbSNP rs8971.

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

Beta strand

476 – 486

11

Beta strand

488 – 499

12

Helix

500 – 505

6

Beta strand

506 – 511

6

Helix

512 – 524

13

Beta strand

525 – 529

5

Beta strand

532 – 544

13

Helix

545 – 561

17

Beta strand

562 – 573

12

Beta strand

575 – 578

4

Beta strand

580 – 599

20

Beta strand

601 – 623

23

Helix

624 – 631

8

Beta strand

632 – 641

10

Beta strand

644 – 650

7

Helix

651 – 655

5

Beta strand

659 – 666

8

Helix

667 – 670

4

Beta strand

671 – 684

14

Helix

685 – 689

5

Beta strand

690 – 694

5

Beta strand

696 – 709

14

Helix

712 – 719

8

Beta strand

720 – 723

4

Helix

724 – 730

7

Beta strand

731 – 745

15

Helix

746 – 755

10

Beta strand

756 – 768

13

Beta strand

775 – 780

6

Helix

781 – 785

5

Beta strand

786 – 791

6

Beta strand

810 – 816

7

Helix

819 – 828

10

Beta strand

835 – 844

10

Helix

848 – 854

7

Turn

855 – 857

3

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 – 917

8

Helix

927 – 934

8

Beta strand

937 – 945

9

Helix

950 – 952

3

Beta strand

955 – 962

8

Helix

969 – 992

24

Beta strand

995 – 998

4

Beta strand

1004 – 1006

3

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. 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: 2147474] [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: 14702039] [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: 15489334] [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: 9224613] [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: 2183217] [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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348, MASS SPECTROMETRY.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350, MASS SPECTROMETRY.
[12]	"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: 12450384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 808-1010 IN COMPLEX WITH SUBSTRATE.
[13]	"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: 12755606] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 808-1010 IN COMPLEX WITH FORMYLTETRAHYDROFOLATE ANALOG.
[14]	"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: 16026156] [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.
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.
NP_001129477.1.
NP_001129478.1.
NP_780294.1.

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	[»]

SMR

P22102. Positions 446-768.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22102. 2 interactions.

STRING

P22102.

PTM databases

PhosphoSite

P22102.

Proteomic databases

PeptideAtlas

P22102.

PRIDE

P22102.

Genome annotation databases

Ensembl

ENST00000381815; ENSP00000371236; ENSG00000159131; Homo sapiens. [Genome view]
ENST00000381831; ENSP00000371253; ENSG00000159131; Homo sapiens. [Genome view]
ENST00000381839; ENSP00000371261; ENSG00000159131; Homo sapiens. [Genome view]

GeneID

2618.

KEGG

hsa:2618.

NMPDR

fig|9606.3.peg.20899.

UCSC

uc002yrx.1. human.

Organism-specific databases

CTD

2618.

GeneCards

GC21M033798.

H-InvDB

HIX0027779.

HGNC

HGNC:4163. GART.

HPA

HPA002119.
HPA005779.

MIM

138440. gene.

PharmGKB

PA28576.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18265.

HOVERGEN

P22102.

InParanoid

P22102.

OMA

GETSEMP.

OrthoDB

EOG908QTM.

PhylomeDB

P22102.

Enzyme and pathway databases

BRENDA

2.1.2.2. 247.
6.3.3.1. 247.
6.3.4.13. 247.

Reactome

REACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpress

P22102.

Bgee

P22102.

CleanEx

HS_GART.

Genevestigator

P22102.

GermOnline

ENSG00000159131. Homo sapiens.

Family and domain databases

InterPro

IPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
IPR000115. PRibGlycinamide_synth.
IPR020560. PRibGlycinamide_synth_C-dom.
IPR020559. PRibGlycinamide_synth_CS.
IPR020562. PRibGlycinamide_synth_N-dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
IPR004607. PurN_trans.
IPR011054. Rudment_hybrid_motif.
[Graphical view]

Gene3D

G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.

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]

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 Resources

BindingDB

P22102.

DrugBank

DB00642. Pemetrexed.

NextBio

10307.

SOURCE

Search...

Entry information

Entry name

PUR2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	February 9, 2010
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.