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Q64737

- PUR2_MOUSE

UniProt

Q64737 - PUR2_MOUSE

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Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene

Gart

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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-formyltetrahydrofolateBy similarity
Binding sitei913 – 913110-formyltetrahydrofolateBy similarity
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: UniProtKB-EC

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. purine nucleobase biosynthetic process Source: InterPro
  7. response to inorganic substance Source: Ensembl
  8. response to organic substance Source: Ensembl
  9. 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

SABIO-RKQ64737.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:95654. Gart.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10101009Trifunctional purine biosynthetic protein adenosine-3PRO_0000074938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei350 – 3501N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ64737.
PaxDbiQ64737.
PRIDEiQ64737.

PTM databases

PhosphoSiteiQ64737.

Expressioni

Tissue specificityi

Detected in liver, kidney and brain.1 Publication

Gene expression databases

BgeeiQ64737.
CleanExiMM_GART.
ExpressionAtlasiQ64737. baseline and differential.
GenevestigatoriQ64737.

Interactioni

Protein-protein interaction databases

BioGridi199831. 1 interaction.
IntActiQ64737. 1 interaction.
MINTiMINT-1852011.

Structurei

3D structure databases

ProteinModelPortaliQ64737.
SMRiQ64737. Positions 1-430, 475-785, 808-1006.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni434 – 807374AIRSAdd
BLAST
Regioni808 – 1010203GARTAdd
BLAST
Regioni818 – 82035'-phosphoribosylglycinamide bindingBy similarity
Regioni896 – 899410-formyltetrahydrofolate bindingBy similarity
Regioni947 – 951510-formyltetrahydrofolate bindingBy similarity
Regioni977 – 98045'-phosphoribosylglycinamide bindingBy similarity

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.
HOGENOMiHOG000030315.
HOVERGENiHBG008333.
InParanoidiQ64737.
KOiK11787.
OMAiTARYESF.
OrthoDBiEOG7RBZ7H.
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: Q64737-1) [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
MAARVLVIGS GGREHTLAWK LAQSPQVKQV LVAPGNAGTA CAGKISNAAV
60 70 80 90 100
SVNDHSALAQ FCKDEKIELV VVGPEAPLAA GIVGDLTSAG VRCFGPTAQA
110 120 130 140 150
AQLESSKKFA KEFMDRHEIP TAQWRAFTNP EDACSFITSA NFPALVVKAS
160 170 180 190 200
GLAAGKGVIV AKSQAEACRA VQEIMQEKSF GAAGETVVVE EFLEGEEVSC
210 220 230 240 250
LCFTDGKTVA EMPPAQDHKR LLDGDEGPNT GGMGAYCPAP QVSKDLLVKI
260 270 280 290 300
KNTILQRAVD GMQQEGAPYT GILYAGIMLT KDGPKVLEFN CRFGDPECQV
310 320 330 340 350
ILPLLKSDLY EVMQSTLDGL LSASLPVWLE NHSAVTVVMA SKGYPGAYTK
360 370 380 390 400
GVEITGFPEA QALGLQVFHA GTALKDGKVV TSGGRVLTVT AVQENLMSAL
410 420 430 440 450
AEARKGLAAL KFEGAIYRKD IGFRAVAFLQ RPRGLTYKDS GVDIAAGNML
460 470 480 490 500
VKKIQPLAKA TSRPGCSVDL GGFAGLFDLK AAGFKDPLLA SGTDGVGTKL
510 520 530 540 550
KIAQLCNKHD SIGQDLVAMC VNDILAQGAE PLFFLDYFSC GKLDLSTTEA
560 570 580 590 600
VIAGIAAACQ QAGCALLGGE TAEMPNMYPP GEYDLAGFAV GAMERHQKLP
610 620 630 640 650
QLERITEGDA VIGVASSGLH SNGFSLVRKI VERSSLQYSS PAPGGCGDQT
660 670 680 690 700
LGDLLLTPTR IYSHSLLPII RSGRVKAFAH ITGGGLLENI PRVLPQKFGV
710 720 730 740 750
DLDASTWRVP KVFSWLQQEG ELSEEEMART FNCGIGAALV VSKDQAEQVL
760 770 780 790 800
HDVRRRQEEA WVIGSVVACP EDSPRVRVKN LIETIQTNGS LVANGFLKSN
810 820 830 840 850
FPVQQKKARV AVLISGTGSN LQALIDSTRD PKSSSHIVLV ISNKAAVAGL
860 870 880 890 900
DRAERAGIPT RVINHKLYKN RVEFDNAVDH VLEEFSVDIV CLAGFMRILS
910 920 930 940 950
GPFVRKWDGK MLNIHPSLLP SFKGSNAHEQ VLEAGVTITG CTVHFVAEDV
960 970 980 990 1000
DAGQIILQEA VPVRRGDTVA TLSERVKVAE HKIFPAALQL VASGAVQLRE
1010
DGKIHWAKEQ
Length:1,010
Mass (Da):107,503
Last modified:July 27, 2011 - v3
Checksum:i894D7D07D3C258B2
GO
Isoform Short (identifier: Q64737-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:433
Mass (Da):45,698
Checksum:iC6B2789DB78932D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411C → G in AAA19012. (PubMed:8299947)Curated
Sequence conflicti41 – 411C → G in AAA19013. (PubMed:8299947)Curated
Sequence conflicti41 – 411C → G in AAC53250. (PubMed:7829519)Curated
Sequence conflicti41 – 411C → G in AAC53251. (PubMed:7829519)Curated
Sequence conflicti318 – 3181D → G in AAC53250. (PubMed:7829519)Curated
Sequence conflicti318 – 3181D → G in AAC53251. (PubMed:7829519)Curated
Sequence conflicti563 – 5631G → A in AAA19013. (PubMed:8299947)Curated
Sequence conflicti690 – 6901I → T in AAA19013. (PubMed:8299947)Curated
Sequence conflicti868 – 8681Y → S in AAA19013. (PubMed:8299947)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei434 – 1010577Missing in isoform Short. 1 PublicationVSP_005518Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01023 mRNA. Translation: AAA19012.1.
U01024 mRNA. Translation: AAA19013.1.
U20886
, U20875, U20876, U20877, U20879, U20880, U20881, U20882, U20883 Genomic DNA. Translation: AAC53250.1.
U20892
, U20875, U20876, U20877, U20879, U20880, U20881, U20882, U20883, U20886, U20884, U20887, U20885, U20889, U20890, U20891 Genomic DNA. Translation: AAC53251.1.
AK168501 mRNA. Translation: BAE40386.1.
AK168724 mRNA. Translation: BAE40565.1.
AK168796 mRNA. Translation: BAE40629.1.
AK168864 mRNA. Translation: BAE40683.1.
AK168876 mRNA. Translation: BAE40694.1.
CH466602 Genomic DNA. Translation: EDL03819.1.
BC070465 mRNA. Translation: AAH70465.1.
CCDSiCCDS28329.1. [Q64737-1]
PIRiI67805.
RefSeqiNP_034386.2. NM_010256.2. [Q64737-1]
XP_006522973.1. XM_006522910.1. [Q64737-1]
XP_006522974.1. XM_006522911.1. [Q64737-1]
XP_006522975.1. XM_006522912.1. [Q64737-1]
UniGeneiMm.4505.

Genome annotation databases

EnsembliENSMUST00000023684; ENSMUSP00000023684; ENSMUSG00000022962. [Q64737-1]
ENSMUST00000120450; ENSMUSP00000114034; ENSMUSG00000022962. [Q64737-2]
GeneIDi14450.
KEGGimmu:14450.
UCSCiuc007zxu.1. mouse. [Q64737-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01023 mRNA. Translation: AAA19012.1 .
U01024 mRNA. Translation: AAA19013.1 .
U20886
, U20875 , U20876 , U20877 , U20879 , U20880 , U20881 , U20882 , U20883 Genomic DNA. Translation: AAC53250.1 .
U20892
, U20875 , U20876 , U20877 , U20879 , U20880 , U20881 , U20882 , U20883 , U20886 , U20884 , U20887 , U20885 , U20889 , U20890 , U20891 Genomic DNA. Translation: AAC53251.1 .
AK168501 mRNA. Translation: BAE40386.1 .
AK168724 mRNA. Translation: BAE40565.1 .
AK168796 mRNA. Translation: BAE40629.1 .
AK168864 mRNA. Translation: BAE40683.1 .
AK168876 mRNA. Translation: BAE40694.1 .
CH466602 Genomic DNA. Translation: EDL03819.1 .
BC070465 mRNA. Translation: AAH70465.1 .
CCDSi CCDS28329.1. [Q64737-1 ]
PIRi I67805.
RefSeqi NP_034386.2. NM_010256.2. [Q64737-1 ]
XP_006522973.1. XM_006522910.1. [Q64737-1 ]
XP_006522974.1. XM_006522911.1. [Q64737-1 ]
XP_006522975.1. XM_006522912.1. [Q64737-1 ]
UniGenei Mm.4505.

3D structure databases

ProteinModelPortali Q64737.
SMRi Q64737. Positions 1-430, 475-785, 808-1006.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199831. 1 interaction.
IntActi Q64737. 1 interaction.
MINTi MINT-1852011.

Chemistry

BindingDBi Q64737.
ChEMBLi CHEMBL3690.
GuidetoPHARMACOLOGYi 2612.

PTM databases

PhosphoSitei Q64737.

Proteomic databases

MaxQBi Q64737.
PaxDbi Q64737.
PRIDEi Q64737.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023684 ; ENSMUSP00000023684 ; ENSMUSG00000022962 . [Q64737-1 ]
ENSMUST00000120450 ; ENSMUSP00000114034 ; ENSMUSG00000022962 . [Q64737-2 ]
GeneIDi 14450.
KEGGi mmu:14450.
UCSCi uc007zxu.1. mouse. [Q64737-1 ]

Organism-specific databases

CTDi 2618.
MGIi MGI:95654. Gart.

Phylogenomic databases

eggNOGi COG0151.
GeneTreei ENSGT00390000000292.
HOGENOMi HOG000030315.
HOVERGENi HBG008333.
InParanoidi Q64737.
KOi K11787.
OMAi TARYESF.
OrthoDBi EOG7RBZ7H.
TreeFami TF106368.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00125 .
UPA00074 ; UER00126 .
UPA00074 ; UER00129 .
SABIO-RK Q64737.

Miscellaneous databases

ChiTaRSi GART. mouse.
NextBioi 286065.
PROi Q64737.
SOURCEi Search...

Gene expression databases

Bgeei Q64737.
CleanExi MM_GART.
ExpressionAtlasi Q64737. baseline and differential.
Genevestigatori Q64737.

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. "Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase."
    Kan J.L., Jannatipour M., Taylor S.M., Moran R.G.
    Gene 137:195-202(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Strain: C57BL/6 X CBA.
    Tissue: Spleen.
  2. "Analysis of a mouse gene encoding three steps of purine synthesis reveals use of an intronic polyadenylation signal without alternative exon usage."
    Kan J.L., Moran R.G.
    J. Biol. Chem. 270:1823-1832(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney, Liver and Stomach.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 LONG).
    Strain: C57BL/6.
    Tissue: Eye.

Entry informationi

Entry nameiPUR2_MOUSE
AccessioniPrimary (citable) accession number: Q64737
Secondary accession number(s): Q3TGI3, Q6NS48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3