MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Genome-wide biochemical analysis of Arabidopsis protein phosphatase using a wheat cell-free system. Genome-wide biochemical analysis of Arabidopsis protein phosphatase using a wheat cell-free system. FEBS Lett. (0014-5793) 2012 Takahashi H., Ozawa A., Nemoto K., Nozawa A., Seki M., Shinozaki K., Takeda H., Endo Y., Sawasaki T. in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Takahashi H., Ozawa A., Nemoto K., Nozawa A., Seki M., Shinozaki K., Takeda H., Endo Y., Sawasaki T. FEBS Lett. (0014-5793) 2012 p2c32_arath Protein phosphatase 2C 32 POL Protein POLTERGEIST Protein phosphatase 2C POL F14M4.25 At2g46920 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGNGTSRVVGCFVPSNDKNGVDLEFLEPLDEGLGHSFCYVRPSIFESPDITPSNSERFTIDSSTIDSETLTGSFRNDIVDDPSFLNRHNSKGLAETTFKAISGASVSANVSTARTGNQMALCSSDVLEPAASFESTSSFASIPLQPLPRGGSGPLNGFMSGPLERGFASGPLDRNNGFMSGPIEKGVMSGPLDVSDRSNFSAPLSFRRKKPRFQRFMRSVSGPMKSTLARTFSRRSGGLSWMHRFFLHPETRVSWAVGKDGKLHGEDPESCLESNRNLQWAHGKAGEDRVHVVLSEEQGWLFIGIYDGFSGPDAPDFVMSHLYKAIDKELEGLLWDYEEPSEDNQLQPDQEPPTEENMCDPESISEQHSKSVVAESEEVMIDDISSLGNTDTQIADGPPGDSAGPGKKSMRLYELLQLEQWEGEEIGLKRYGGNVALNNMTNQVENPSTSGGGAGNDPCTTDRSALDGIPNSGQRHGTKKSQISSKIRRMYQKQKSLRKKLFPWSYDWHREEGICVEEKIVESSGPIRRRWSGTVDHDAVLRAMARALESTEEAYMDMVEKSLDINPELALMGSCVLVMLMKDQDVYVMNVGDSRAILAQERLHDRHSNPGFGNDEGIGHKSRSRESLVRIELDRISEESPIHNQATPISVSNKNRDVTSYRLKMRAVQLSSDHSTSVEEEIWRIRSEHPEDDQSILKDRVKGQLKVTRAFGAGFLKKPNFNEALLEMFQVEYIGTDPYITCEPCTVHHRLTSSDRFMVLSSDGLYEYFSNEEVVAHVTWFIENVPEGDPAQYLIAELLSRAATKNGMEFHDLLDIPQGDRRKYHDDVSVMVVSLEGRIWRSSGQYYPERKQKFNR mint 95BDFC8DEB5DE4F2 p2c71_arath Probable protein phosphatase 2C 71 F6A4.150 At5g24940 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGYMDLALSYSNQMRIVEAPASGGGLSQNGKFSYGYASSAGKRSSMEDFFETRIDGIDGEIVGLFGVFDGHGGSRAAEYVKRHLFSNLITHPKFISDTKSAIADAYTHTDSELLKSENSHTRDAGSTASTAILVGDRLLVANVGDSRAVICRGGNAFAVSRDHKPDQSDERERIENAGGFVMWAGTWRVGGVLAVSRAFGDRLLKQYVVADPEIQEEKIDDSLEFLILASDGLWDVFSNEEAVAVVKEVEDPEESTKKLVGEAIKRGSADNITCVVVRFLESKSANNNGSSSSEEANQVPTAVRNDSDHKISAKETNQDHTTVNKDLDRNTDSQSLNQKPIAARSADNSNQKPIATTATGHSVSSEQSGLTGEKSQMPIKIRSDSEPKSSAKVPNQTQSTVHNDLDSSTAKKPAATEQSGSTGERNRKPIKVHSDSAARKTTPSIFN mint B3BB13D43A2A6939 p2c69_arath Probable protein phosphatase 2C 69 MAJ23.3 T30N20.10 At5g10740 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGYLDLALSYSNQPQTVEAPASGGGLSQNGKFSYGYASSAGKRSSMEDFFETRIDGINGEIVGLFGVFDGHGGARAAEYVKRHLFSNLITHPKFISDTKSAITDAYNHTDSELLKSENSHNRDAGSTASTAILVGDRLVVANVGDSRAVISRGGKAIAVSRDHKPDQSDERERIENAGGFVMWAGTWRVGGVLAVSRAFGDRLLKQYVVADPEIQEEKIDDTLEFLILASDGLWDVFSNEAAVAMVKEVEDPEDSAKKLVGEAIKRGSADNITCVVVRFLEKKSASSSHISSSSSKEAKEMPPLGDLAISSNEAKQVQIGSGNKPENVTNRKPDTASRSTDTLTLERNSVTDKV mint 87DA535B561C9D68 p2c35_arath Probable protein phosphatase 2C 35 F28L1.21 At3g06270 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGCVQCKCCSRYPSSSSDGDSRGPLEANGVLKGKDQKPLGSIHVPSPNFDMVYSVLSQRGYYPDSPDKENQDTYCIKTELQGNPNVHFFGVFDGHGVLGTQCSNFVKERVVEMLSEDPTLLEDPEKAYKSAFLRVNEELHDSEIDDSMSGTTAITVLVVGDKIYVANVGDSRAVLAVKDRNRILAEDLSYDQTPFRKDECERVKACGARVLSVDQVEGLKDPNIQTWANEESEGGDPPRLWVQNGMYPGTAFTRSVGDFTAESIGVIAEPEVSMVHLSPNHLFFVVASDGIFEFLPSQAVVDMVGRYADPRDGCAAAAAESYKLWLEHENRTDDITIIIVQIKKLSNE mint 2F20E79DC63515B0 p2c21_arath Probable protein phosphatase 2C 21 PPC4-2 AtPPC4;2 F13D4.1 F27C12 At2g25070 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGTYLSSPKTEKLSEDGENDKLRFGLSSMQGWRATMEDAHAAILDLDDKTSFFGVYDGHGGKVVAKFCAKYLHQQVISNEAYKTGDVETSLRRAFFRMDDMMQGQRGWRELAVLGDKMNKFSGMIEGFIWSPRSGDTNNQPDSWPLEDGPHSDFTGPTSGCTACVALIKDKKLFVANAGDSRCVISRKSQAYNLSKDHKPDLEVEKERILKAGGFIHAGRINGSLNLTRAIGDMEFKQNKFLPSEKQMVTADPDINTIDLCDDDDFLVVACDGIWDCMSSQELVDFIHEQLKSETKLSTVCEKVVDRCLAPDTATGEGCDNMTIILVQFKKPNPSETEPEDSKPEPSEDEPSSSS mint CAD638796203C746 ptp1_arath Protein-tyrosine-phosphatase PTP1 PTP1 Protein tyrosine phosphatase 1 F14O23.24 At1g71860 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATGKTSSAANLFTGSTRFDLSSADSPPSKLSLSSDQLNHCHQALGVFRGKIQNPDSIAHEFTGLQANRMWPSELLLNSTVAMNSVNVEKNRYSDVVPFDKNRIVLNPCKDSSAKGYVNASLIKTSESESISQFIATQGPLPHTMEDFWEMVIQQHCPIIVMLTRLVDNNRTVKCGDYFQDEDGPREFGNISLTTKWIKTTDTSLMLRNLEVNYKETEDQPMSVLHIQYPEWPDHGVPKDTVAVREILKRLYQVPPSLGPIIVHCSAGIGRTGTYCAIHNTIQRILAGDMSALDLAKTVALFRKQRIGMVQTMDQYFFCYNAIVDELEDLTAGTNAGTSS mint 7885C03A664CA02D p2c18_arath Probable protein phosphatase 2C 18 F20B17.6 At1g79630 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGLCYSVDRTTGKEPGEASSTATTAETVEERSGSGRWRRPRDLKGGGDIEGIPQVLGRLVSNGSSKIACLYTQQGKKGTNQDAMLVFENFCSRDDTVFCGVFDGHGPFGHMVAKKVRDTLPFTLLTQLKMTSESDQSSLVGANGFQIKCTEEEEVQTTESEQVQKTESVTTMDEQWCELNPNVNNDELPEMYLPLKHAMLKSCQQIDKELKMHPTIDCFCSGTTSVTLIKQGEDLVVGNIGDSRAVLATRDEDNALLAVQLTIDLKPDLPGESARIQKCKGRVFALQDEPEVARVWLPNSDSPGLAMARAFGDFCLKDYGLISVPDINYRRLTERDQFIILASDGVWDVLSNKEAVDIVASAPSRSTAARALVDTAVRSWRIKYPTSKNDDCTVVCLFLQDSSVAMEVSTNVKKDSPKEESIESVTNSTSKEEDEIVPVKDEKIPESCGIESKMMTMTLAECISVAQDDEEWSALEGLTRVNSLLSIPRFLSGELRSTSWRKWL mint 71B511B182D7B86E p2c11_arath Probable protein phosphatase 2C 11 F28H19.16 F9C16.6 At1g43900 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MKKTRNVASSPIECVHLQTKPTTTLVRSFFFFLFNSQTISSFIIFYLFLCSFFWFCQSPNLTNPSPPPLSVAPLRGDANSPPPESSSSPATKSSLMISSRDPNALFSGGGISFLAGVRTVKFSYGYSSLKGKRATMEDYFETRISDVNGQMVAFFGVFDGHGGARTAEYLKNNLFKNLVSHDDFISDTKKAIVEVFKQTDEEYLIEEAGQPKNAGSTAATAFLIGDKLIVANVGDSRVVASRNGSAVPLSDDHKPDRSDERQRIEDAGGFIIWAGTWRVGGILAVSRAFGDKQLKPYVIAEPEIQEEDISTLEFIVVASDGLWNVLSNKDAVAIVRDISDAETAARKLVQEGYARGSCDNITCIVVRFEVS mint 5579D3D23F1805E8 p2c26_arath Probable protein phosphatase 2C 26 T27E13.9 At2g30170 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MAIPVTRMMVPHAIPSLRLSHPNPSRVDFLCRCAPSEIQPLRPELSLSVGIHAIPHPDKVEKGGEDAFFVSSYRGGVMAVADGVSGWAEQDVDPSLFSKELMANASRLVDDQEVRYDPGFLIDKAHTATTSRGSATIILAMLEEVGILKIGNVGDCGLKLLREGQIIFATAPQEHYFDCPYQLSSEGSAQTYLDASFSIVEVQKGDVIVMGSDGLFDNVFDHEIVSIVTKHTDVAESSRLLAEVASSHSRDTEFESPYALEARAKGFDVPLWKKVLGKKLTGGKLDDVTVIVAKVVSS mint 52327F83126D89F5 p2c60_arath Probable protein phosphatase 2C 60 F11C18.60 At4g31860 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGIYLSTPKTDKFSEDGENHKLRYGLSSMQGWRASMEDAHAAILDLDDNTSFLGVYDGHGGKVVSKFCAKYLHQQVLSDEAYAAGDVGTSLQKAFFRMDEMMQGQRGWRELAVLGDKINKFSGMIEGLIWSPRSGDSANKPDAWAFEEGPHSDFAGPNSGSTACVAVVRDKQLFVANAGDSRCVISRKNQAYNLSRDHKPDLEAEKERILKAGGFIHAGRVNGSLNLSRAIGDMEFKQNKFLPSEKQIVTASPDVNTVELCDDDDFLVLACDGIWDCMTSQQLVDFIHEQLNSETKLSVVCEKVLDRCLAPNTSGGEGCDNMTMILVRFKNPTPSETELKPEASQAEGNHDEPSSSN 98EE1A09818CA0D3 p2c58_arath Probable protein phosphatase 2C 58 F20O9.80 At4g28400 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MAGSNILHKIKLKAGFCGSAPDMGRGKSKMWKNITHGFHCVKGKSSHPMEDYVVSEFKKLEGHELGLFAIFDGHLGHDVAKYLQTNLFDNILKEKDFWTDTENAIRNAYRSTDAVILQQSLKLGKGGSTAVTGILIDGKKLVVANVGDSRAVMSKNGVAHQLSVDHEPSKEKKEIESRGGFVSNIPGDVPRVDGQLAVARAFGDKSLKLHLSSEPDITHQTIDDHTEFILFASDGIWKVLSNQEAVDAIKSIKDPHAAAKHLIEEAISRKSKDDISCIVVKFH mint 0F885E060AA68BE7 p2c79_arath Probable protein phosphatase 2C 79 K2A18.16 At5g66080 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MLSLFFNFLTSCLWPSSSTTSHTYSDSKGKQDGLLWYKDSAHHLFGDFSMAVVQANNLLEDQSQVESGPLTTLSSSGPYGTFVGVYDGHGGPETSRFVNDHLFHHLKRFAAEQDSMSVDVIRKAYEATEEGFLGVVAKQWAVKPHIAAVGSCCLIGVVCDGKLYVANVGDSRAVLGKVIKATGEVNALQLSAEHNVSIESVRQEMHSLHPDDSHIVVLKHNVWRVKGIIQVSRSIGDVYLKKSEFNKEPLYTKYRLREPMKRPILSWEPSITVHDLQPDDQFLIFASDGLWEQLSNQEAVEIVQNHPRNGIARRLVKAALQEAAKKREMRYSDLNKIERGVRRHFHDDITVVVLFLDTNLLSRASSLKTPSVSIRGGGITLPKKL mint C28A2ABB7F243B2D p2c43_arath Probable protein phosphatase 2C 43 MGD8.13 MGD8.8 At3g17250 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRTSKASVTQTWLLYTQLCLWKDLIIRYVRQIIRRAKSMLFSQNMVADSAEISVIDVKSHLSVAKDPSNFQIAEIRIHDSICIDIPSSEETPLLESIKSCSATTIEEHVTEFVPNISSGSYADKGDYREYMEDEHICIDDLSDHLGSSFYRFPVPMAFYGVFDGHGGSDASQYIKENAMSLFFEDAVFRQSPSVVDSLFLKELETSHREAYRLADLAMEDERIVSSSCGTTALTALVIGRHLMVANVGDCRAVLCRKGKAVDMSFDHKSTFEPERRRVEDLGGYFEGEYLYGDLAVTRALGDWSIKRFSPLGESLSPLISDPDIQQMILTEEDEFLIMGCDGVWDVMTSQYAVTFVRQGLRRHGDPRRCAMELGREALRLDSSDNVTVVVICFSSSPAPQRRRIRFCVSDEARARLQTMLEG mint 63B7B3E7DD69FCE4 p2c77_arath Protein phosphatase 2C 77 Protein ABSCISIC ACID-INSENSITIVE 2 ABI2 At5g57050 MHM17.19 Protein phosphatase 2C ABI2 PP2C77 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDEVSPAVAVPFRPFTDPHAGLRGYCNGESRVTLPESSCSGDGAMKDSSFEINTRQDSLTSSSSAMAGVDISAGDEINGSDEFDPRSMNQSEKKVLSRTESRSLFEFKCVPLYGVTSICGRRPEMEDSVSTIPRFLQVSSSSLLDGRVTNGFNPHLSAHFFGVYDGHGGSQVANYCRERMHLALTEEIVKEKPEFCDGDTWQEKWKKALFNSFMRVDSEIETVAHAPETVGSTSVVAVVFPTHIFVANCGDSRAVLCRGKTPLALSVDHKPDRDDEAARIEAAGGKVIRWNGARVFGVLAMSRSIGDRYLKPSVIPDPEVTSVRRVKEDDCLILASDGLWDVMTNEEVCDLARKRILLWHKKNAMAGEALLPAEKRGEGKDPAAMSAAEYLSKMALQKGSKDNISVVVVDLKGIRKFKSKSLN 67CAAC76DA531A71 p2c68_arath Probable protein phosphatase 2C 68 MPH15.11 At5g06750 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MFSWLARMALFCLRPMRRYGRMNRDDDDDDDHDGDSSSSGDSLLWSRELERHSFGDFSIAVVQANEVIEDHSQVETGNGAVFVGVYDGHGGPEASRYISDHLFSHLMRVSRERSCISEEALRAAFSATEEGFLTLVRRTCGLKPLIAAVGSCCLVGVIWKGTLLIANVGDSRAVLGSMGSNNNRSNKIVAEQLTSDHNAALEEVRQELRSLHPDDSHIVVLKHGVWRIKGIIQVSRSIGDAYLKRPEFSLDPSFPRFHLAEELQRPVLSAEPCVYTRVLQTSDKFVIFASDGLWEQMTNQQAVEIVNKHPRPGIARRLVRRAITIAAKKREMNYDDLKKVERGVRRFFHDDITVVVIFIDNELLMVEKATVPELSIKGFSHTVGPSKFSIFLS mint CAB959A38511D7B8 pp18_arath Serine/threonine-protein phosphatase PP1 isozyme 8 TOPP8 Type one protein phosphatase 8 T1G16.170 At5g27840 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MMTSMEGMVEKGVLDDIIRRLLEGKGGKQVQLSESEIRQLCFNARQIFLSQPNLLDLHAPIRICGDIHGQYQDLLRLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLLAYKIRYPSKIYLLRGNHEDAKINRIYGFYDECKRRFNVRLWKVFTDCFNCLPVAALIDEKILCMHGGLSPDLDNLNQIREIQRPIEIPDSGLLCDLLWSDPDQKIEGWADSDRGISCTFGADKVAEFLDKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEIMKPAPASSSHPLKKDFHNRTLGYNLSA AD6ECB37F8FBBFE0 p2c56_arath Protein phosphatase 2C 56 Protein ABSCISIC ACID-INSENSITIVE 1 ABI1 At4g26080 F20B18.190 Protein phosphatase 2C ABI1 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEEVSPAIAGPFRPFSETQMDFTGIRLGKGYCNNQYSNQDSENGDLMVSLPETSSCSVSGSHGSESRKVLISRINSPNLNMKESAAADIVVVDISAGDEINGSDITSEKKMISRTESRSLFEFKSVPLYGFTSICGRRPEMEDAVSTIPRFLQSSSGSMLDGRFDPQSAAHFFGVYDGHGGSQVANYCRERMHLALAEEIAKEKPMLCDGDTWLEKWKKALFNSFLRVDSEIESVAPETVGSTSVVAVVFPSHIFVANCGDSRAVLCRGKTALPLSVDHKPDREDEAARIEAAGGKVIQWNGARVFGVLAMSRSIGDRYLKPSIIPDPEVTAVKRVKEDDCLILASDGVWDVMTDEEACEMARKRILLWHKKNAVAGDASLLADERRKEGKDPAAMSAAEYLSKLAIQRGSKDNISVVVVDLKPRRKLKSKPLN DIP protein P49597 original sequence version: 104 DIP protein P49597 original sequence version: 101 DIP protein P49597 original sequence version: 106 DIP protein P49597 original sequence version: 102 DIP protein P49597 original sequence version: 116 DIP protein P49597 original sequence version: 107 DIP protein P49597 original sequence version: 124 DIP protein P49597 original sequence version: 161 4A4C54F04195F572 p2c08_arath Probable protein phosphatase 2C 8 T10F20.4 At1g18030 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MLEKESDLTAMEKPNNKHAADSFSSEDLVSPVKKAKKSEEVSGGGEAVAAVGNREAEEDKPSFVSEEKKEFLVEADVAEDKGARHTMEDVWVVLPDASLDFPGTLRCAHFAIYDGHGGRLAAEFAKKHLHLNVLSAGLPRELLDVKVAKKAILEGFRKTDELLLQKSVSGGWQDGATAVCVWILDQKVFVANIGDAKAVLARSSTTNELGNHTEAGNPLKAIVLTREHKAIYPQERSRIQKSGGVISSNGRLQGRLEVSRAFGDRHFKKFGVSATPDIHAFELTERENFMILGCDGLWEVFGPSDAVGFVQKLLKEGLHVSTVSRRLVKEAVKERRCKDNCTAIVIVFKRV mint 0A6808FD713CCB7E p2c76_arath Probable protein phosphatase 2C 76 MFH8.8 At5g53140 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MVCSSFIRSFIVQAGCRIGVLAQGRHQFIHIKKTLSVGFGFRTSVIGFRTTSGIGFRTSAKMMVDTSAGEKRISLVDMPPEKVDDGGYIGGGWKNDDGSLSCGYCSFRGKRSTMEDFYDIKASTIEGQAVCMFGIFDGHGGSRAAEYLKEHLFNNLMKHPQFLTDTKLALNETYKQTDVAFLESEKDTYRDDGSTASAAVLVGNHLYVANVGDSRTIVSKAGKAIALSDDHKPNRSDERKRIESAGGVIMWAGTWRVGGVLAMSRAFGNRMLKQFVVAEPEIQDLEIDHEAELLVLASDGLWDVVPNEDAVALAQSEEEPEAAARKLTDTAFSRGSADNITCIVVKFRHDKTESPKIETNAMAESEPELNPTTELEPESNPSTALETESIPKAELESEPDAIPDPKPETEPETKGEKAGE mint C312D84D35159052 mbp_bovin Myelin basic protein MBP Myelin A1 protein 20 kDa microtubule-stabilizing protein protein protein bovin Bos taurus (Bovine) Bovine AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR DIP protein P02687 original sequence version: 75 8E1157B7A1978484 p2c16_arath Protein phosphatase 2C 16 HAB1 P2C-HA Protein phosphatase 2C HAB1 AtP2C-HA Protein HYPERSENSITIVE TO ABA 1 F28P22.4 At1g72770 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT DIP protein Q9CAJ0 original sequence version: 64 DIP protein Q9CAJ0-1 original sequence version: 62 DIP protein Q9CAJ0-1 original sequence version: 77 DIP protein Q9CAJ0 original sequence version: 62 DIP protein Q9CAJ0 original sequence version: 65 DIP protein Q9CAJ0-1 original sequence version: 66 DIP protein Q9CAJ0 original sequence version: 81 DIP protein Q9CAJ0-1 original sequence version: 86 DIP protein Q9CAJ0-1 original sequence version: 108 DIP protein Q9CAJ0 original sequence version: 112 DIP protein Q9CAJ0-1 original sequence version: 81 B001BAF0DD8333E1 p2c64_arath Probable protein phosphatase 2C 64 F20M13.80 At4g38520 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MLSGLMNFLNACLWPRSDQQARSASDSGGRQEGLLWFRDSGQHVFGDFSMAVVQANSLLEDQSQLESGSLSSHDSGPFGTFVGVYDGHGGPETSRFINDHMFHHLKRFTAEQQCMSSEVIKKAFQATEEGFLSIVTNQFQTRPQIATVGSCCLVSVICDGKLYVANAGDSRAVLGQVMRVTGEAHATQLSAEHNASIESVRRELQALHPDHPDIVVLKHNVWRVKGIIQVSRSIGDVYLKRSEFNREPLYAKFRLRSPFSKPLLSAEPAITVHTLEPHDQFIICASDGLWEHMSNQEAVDIVQNHPRNGIAKRLVKVALQEAAKKREMRYSDLKKIDRGVRRHFHDDITVIVVFFDTNLVSRGSMLRGPAVSVRGAGVNLPHNTLAPCTTPTQAAAAGAS mint 66AA091D20562CE3 p2c10_arath Probable protein phosphatase 2C 10 F21H2.4 At1g34750 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MAKLCCFGSSDYDLVVGRASTSSGKGRNNDGEIKFGYSLVKGKANHPMEDYHVSKFVKIDGNELGLFAIYDGHLGERVPAYLQKHLFSNILKEEQFRYDPQRSIIAAYEKTDQAILSHSSDLGRGGSTAVTAILMNGRRLWVANVGDSRAVLSQGGQAIQMTIDHEPHTERLSIEGKGGFVSNMPGDVPRVNGQLAVSRAFGDKSLKTHLRSDPDVKDSSIDDHTDVLVLASDGLWKVMANQEAIDIARRIKDPLKAAKELTTEALRRDSKDDISCIVVRLR mint 36404709FB03DA8D p2c37_arath Protein phosphatase 2C 37 F24K9.8 At3g11410 PP2CA AHG3 Protein ABA-HYPERSENSITIVE GERMINATION 3 Protein phosphatase 2C A protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MAGICCGVVGETEPAAPVDSTSRASLRRRLDLLPSIKIVADSAVAPPLENCRKRQKRETVVLSTLPGNLDLDSNVRSENKKARSAVTNSNSVTEAESFFSDVPKIGTTSVCGRRRDMEDAVSIHPSFLQRNSENHHFYGVFDGHGCSHVAEKCRERLHDIVKKEVEVMASDEWTETMVKSFQKMDKEVSQRECNLVVNGATRSMKNSCRCELQSPQCDAVGSTAVVSVVTPEKIIVSNCGDSRAVLCRNGVAIPLSVDHKPDRPDELIRIQQAGGRVIYWDGARVLGVLAMSRAIGDNYLKPYVIPDPEVTVTDRTDEDECLILASDGLWDVVPNETACGVARMCLRGAGAGDDSDAAHNACSDAALLLTKLALARQSSDNVSVVVVDLRKRRNNQASS DIP protein P49598 original sequence version: 79 DIP protein P49598 original sequence version: 80 DIP protein P49598 original sequence version: 95 DIP protein P49598 original sequence version: 130 83B82E32FEC71D4D p2c34_arath Probable protein phosphatase 2C 34 F18C1.9 At3g05640 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGHFSSMFNGIARSFSIKKAKNINSSKSYAKEATDEMAREAKKKELILRSSGCINADGSNNLASVFSRRGEKGVNQDCAIVWEGYGCQEDMIFCGIFDGHGPWGHFVSKQVRNSMPISLLCNWKETLSQTTIAEPDKELQRFAIWKYSFLKTCEAVDLELEHHRKIDSFNSGTTALTIVRQGDVIYIANVGDSRAVLATVSDEGSLVAVQLTVDFKPNLPQEEERIIGCNGRVFCLQDEPGVHRVWQPVDESPGLAMSRAFGDYCIKDYGLVSVPEVTQRHISIRDQFIILATDGVWDVISNQEAIDIVSSTAERAKAAKRLVQQAVRAWNRKRRGIAMDDISAVCLFFHSSSSSPSL 3B11400CD38E254A p2c39_arath Probable protein phosphatase 2C 39 K7L4.6 At3g15260 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MTGREILHKMKESVKEKVGLGASASSADSGKGKSKMLKQITHGFHLVKGKAFHEMEDYVVAKFKEVDDNELGLFAIFDGHLSHEIPDYLCSHLFENILKEPNFWQEPEKAIKKAYYITDTTILDKADDLGKGGSTAVTAILINCQKLVVANVGDSRAVICQNGVAKPLSVDHEPNMEKDEIENRGGFVSNFPGDVPRVDGQLAVARAFGDKSLKMHLSSEPYVTVEIIDDDAEFLILASDGLWKVMSNQEAVDSIKGIKDAKAAAKHLAEEAVARKSSDDISVVVVKFQ mint D37C3DE3BF2F481B p2c33_arath Probable protein phosphatase 2C 33 PPC6-1 AtPPC6;1 F13E7.31 At3g02750 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGSCLSAESRSPRPGSPCSPAFSVRKRKNSKKRPGSRNSSFDYRREEPLNQVPGRMFLNGSTEVACIYTQQGKKGPNQDAMVVWENFGSRTDTIFCGVFDGHGPYGHMVAKRVRDNLPLKLSAYWEAKVPVEGVLKAITTDTVNNVTNINNPEDAAAAAAFVTAEEEPRTSADMEEENTETQPELFQTLKESFLKAFKVMDRELKFHGSVDCFCSGTTAVTLIKQGQYLVVGNVGDSRAVMGTRDSENTLVAVQLTVDLKPNLPAEAERIRKCRGRVFALRDEPEVCRVWLPNCDSPGLAMARAFGDFCLKDFGLISVPDVSFRQLTEKDEFIVLATDGIWDVLSNEDVVAIVASAPSRSSAARALVESAVRAWRYKYPTSKVDDCAAVCLYLDSSNTNAISTASSISKLEDGEEEELKATTEDDDASGPSGLGRSSTVRSGKEIALDESETEKLIKEADNLDSEPGTEYSALEGVARVNTLLNLPRFVPGK mint D021BD5ACE735CF2 mbp-topp8 1 MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified TOPP8 17 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). abi1-mbp 1 MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified at4g26080 18 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). abi2-mbp 1 MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified ABI2 15 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). hab1-mbp 1 MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified HAB1 22 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-pp2ca 1 AtPP2C 25 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-pol 1 POLTE 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c64 1 At4g38520 23 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c79 1 At5g66080 13 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c68 1 At5g06750 16 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c34 1 At3g05640 26 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-ppc6_1 1 At3g02750 28 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c18 1 At1g79630 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c11 1 At1g43900 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c58 1 At4g28400 12 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c76 1 At5g53140 20 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c10 1 At1g34750 24 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c39 1 At3g15260 27 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c69 1 At5g10740 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c71 1 At5g24940 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c43 1 At3g17250 14 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-ppc4_2 1 At2g25070 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c60 1 MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified At4g31860 11 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c08 1 At1g18030 19 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c35 1 At3g06270 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-p2c26 1 At2g30170 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3a mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A). mbp-ptp1 1 PTP1 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined MBP 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified dephosphorylation dephosphorylation reaction dephosphorylation f3b mint Ser/Thr- (A) and Tyr- (B) phosphatase activity of AtPPases were measured comprehensively by using 32P-Ser/Thr-MBP and 32P-Tyr-MBP proteins as model substrates, respectively. The assay was carried out in presence of magnesium ion (gray bars) or manganese ion (black bars), and the result was obtained from single experiment. We comprehensively investigated the activity of all 82 recombinant AtPPases. The amount of free 32Pi released from 32P-labelled MBP was determined using liquid scintillation counter in 96-well plate format. Each streptavidin-AtPPase was bound to the surface of biotin-conjugated magnetic beads, and the beads were then mixed with either 32P-Ser/Thr-MBP or 32P-Tyr-MBP. 26 PPases exhibited Ser/Thr-PPase activity (Fig. 3A).