APR2 - 5'adenylylphosphosulfate reductase 2-BMKCloudï½ç¾è¿å®¢äº

例如："NBL1", "4681", "drought"

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842514 APR2

基因描述

Type	Description
Definition	5'adenylylphosphosulfate reductase 2

研究结论

Date	Results	Publications
2015-10-31 10:34:00	The frequency of APR2 alleles in the global Arabidopsis population.Variation in sulfur and selenium accumulation is controlled by naturally occurring isoforms of APR2.	25245030
2012-03-10 10:26:00	HY5 plays an important role in regulation of APR1 and APR2 gene expression and plant sulfate assimilation	21623972
2011-10-08 11:25:00	A mutant Arabidopsis line (apr2-1) was studied to determine whether APR2 has a role in selenium tolerance and metabolism.	21585336
2010-01-21 00:00:00	APR2 is a key enzyme of the assimilatory sulfate reduction pathway responsible for a decrease in enzyme activity, leading to sulfate accumulation in the plant.	17589509

名称对应

Type	IDs
Synonymous	3'-PHOSPHOADENOSINE-5'-PHOSPHOSULFATE (PAPS) REDUCTASE HOMOLOG 43, 5'adenylylphosphosulfate reductase 2, ADENOSINE-5'-PHOSPHOSULFATE REDUCTASE, APS REDUCTASE, APSR, ATAPR2, F19K23.11, F19K23_11, PRH, PRH43
Gene	UniProtKB-ID: APR2_ARATH, F4HX50_ARATH UniprotKB: P92981, F4HX50 UniParc: UPI00000483E1, UPI0001E92B9F EMBL: AF360192, U53866, AY040005, AY088665, AC000375, CP002684, AF016283, U56921, AF023167, U96045 EnsemblGenome: AT1G62180 KO: ath:AT1G62180
Nucleutide sequences	EMBL-CDS: AAK64082.1, AAM66987.1, AAC49563.1, AAC26977.1, AAC26980.1, AAK25902.1, AAB57688.1, AEE33931.1, AAB80957.1, AAB60764.1, AEE33932.1 Gene_ORFName: F19K23.11, F19K23.11, F19K23_11 EnsemblGenome_TRS: AT1G62180.1
Protein sequencees	EnsemblGenome_PRO: AT1G62180.1 RefSeq: NP_176409.1, NP_001185293.1
Others	UniRef100: UniRef100_F4HX50, UniRef100_P92981 UniRef90: UniRef90_P92981 UniRef50: UniRef50_P92981 UniGene: At.25368, At.74995

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mRNA

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Pubmed编号	文献信息	发表日期	相关基因
25245030	Variation in sulfur and selenium accumulation is controlled by naturally occurring isoforms of the key sulfur assimilation enzyme ADENOSINE 5'-PHOSPHOSULFATE REDUCTASE2 across the Arabidopsis species range. Plant Physiol. Dai-Yin Chao , Patrycja Baraniecka , John Danku , Anna Koprivova , Brett Lahner , Hongbing Luo , Elena Yakubova , Brian Dilkes , Stanislav Kopriva , David E Salt	2014-11-01	APR2
24736607	A split-ubiquitin yeast two-hybrid screen to examine the substrate specificity of atToc159 and atToc132, two Arabidopsis chloroplast preprotein import receptors. PLoS ONE Siddhartha Dutta , Howard J Teresinski , Matthew D Smith	2014-01-01	-
21623972	The key enzyme of sulfate assimilation, adenosine 5'-phosphosulfate reductase, is regulated by HY5 in Arabidopsis. Plant J. Bok-Rye Lee , Anna Koprivova , Stanislav Kopriva	2011-09-01	APR1, HY5, APR2
21585336	Adenosine 5'-phosphosulfate reductase (APR2) mutation in Arabidopsis implicates glutathione deficiency in selenate toxicity. Biochem. J. Kevron Grant , Nicole M Carey , Miguel Mendoza , John Schulze , Marinus Pilon , Elizabeth A H Pilon-Smits , Doug van Hoewyk	2011-09-01	APR2
19259774	A novel extended family of stromal thioredoxins. Plant Mol. Biol. Peter Cain , Michael Hall , Wolfgang P SchrÃ¶der , Thomas Kieselbach , Colin Robinson	2009-06-01	-
18431481	Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS One Boris Zybailov , Heidi Rutschow , Giulia Friso , Andrea Rudella , Olof Emanuelsson , Qi Sun , Klaas J van Wijk	2008-04-23	-
17589509	Natural variation for sulfate content in Arabidopsis thaliana is highly controlled by APR2. Nat. Genet. Olivier Loudet , Vera Saliba-Colombani , Christine Camilleri , Fanny Calenge , Virginie Gaudon , Anna Koprivova , Kathryn A North , Stanislav Kopriva , FranÃ§oise Daniel-Vedele	2007-07-01	APR2
11130712	Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana. Nature A Theologis , J R Ecker , C J Palm , N A Federspiel , S Kaul , O White , J Alonso , H Altafi , R Araujo , C L Bowman , S Y Brooks , E Buehler , A Chan , Q Chao , H Chen , R F Cheuk , C W Chin , M K Chung , L Conn , A B Conway , A R Conway , T H Creasy , K Dewar , P Dunn , P Etgu , T V Feldblyum , J Feng , B Fong , C Y Fujii , J E Gill , A D Goldsmith , B Haas , N F Hansen , B Hughes , L Huizar , J L Hunter , J Jenkins , C Johnson-Hopson , S Khan , E Khaykin , C J Kim , H L Koo , I Kremenetskaia , D B Kurtz , A Kwan , B Lam , S Langin-Hooper , A Lee , J M Lee , C A Lenz , J H Li , Y Li , X Lin , S X Liu , Z A Liu , J S Luros , R Maiti , A Marziali , J Militscher , M Miranda , M Nguyen , W C Nierman , B I Osborne , G Pai , J Peterson , P K Pham , M Rizzo , T Rooney , D Rowley , H Sakano , S L Salzberg , J R Schwartz , P Shinn , A M Southwick , H Sun , L J Tallon , G Tambunga , M J Toriumi , C D Town , T Utterback , S Van Aken , M Vaysberg , V S Vysotskaia , M Walker , D Wu , G Yu , C M Fraser , J C Venter , R W Davis	2000-12-14	AT1G27045, AT1G24095, AT1G12855, AT1G63295, AT1G45163, AT1G20735, AT1G51035, AT1G55207, AT1G25145, AT1G53023, AT1G29025, AT1G19396, AT1G26515, AT1G78476, AT1G71866, AT1G36922, AT1G47578, AT1G11125, AT1G02575, AT1G25150, AT1G62914, AT1G51020, AT1G03365, AT1G53025, AT1G50732, AT1G09794, AT1G64583, AT1G05675, AT1G33612, AT1G03103, AT1G03106, AT1G05085, AT1G06135, AT1G06475, DSI-1VOC, AT1G07730, AT1G07985, AT1G08125, AT1G12805, AT1G13635, AT1G16515, AT1G17285, AT1G18265, AT1G19394, AT1G19397, AT1G21395, AT1G23465, AT1G23935, AT1G24580, AT1G26798, AT1G26799, AT1G28695, AT1G30475, AT1G31835, AT1G43666, AT1G45165, AT1G48195, AT1G48325, ATHAL3B, AT1G52315, CDT1, AT1G52855, AT1G52905, AT1G53285, AT1G53785, AT1G53815, AT1G54217, AT1G54575, AT1G55475, AT1G55675, AT1G56045, AT1G56415, AT1G58242, AT1G59865, SCRL5, AT1G61097, AT1G61105, BRD4, AT1G62085, AT1G63055, AT1G64065, AT1G64235, AT1G64255, AT1G72645, AT1G76955, AT1G77885, GL22, AT1G03495, AT1G03982, AT1G04625, AT1G05894, AT1G06645, AT1G06923, YAB2, SCRL3, AT1G09157, AT1G10417, AT1G10850, AT1G12064
9653199	Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase. Proc. Natl. Acad. Sci. U.S.A. J A Bick , F Aslund , Y Chen , T Leustek	1998-07-07	-
8917599	Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity. Proc. Natl. Acad. Sci. U.S.A. J F Gutierrez-Marcos , M A Roberts , E I Campbell , J L Wray	1996-11-12	-

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