RRD2

Serine/threonine-protein phosphatase 2A activator 2

457 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

51.009 kDa

MPPAALQATVSESVKDAIISKLRQPPSAVPSREWSAETRTSLTPADAGIAEARASAEDIELVDLQHHNFSEPRKRIVSPASLSRFEHSQAFAEILAFICVCNTRVVGKTLTEEIQISSACRTILEMLDQVAALRESTPPDASIGSSRFGNPAFRTFYAKIRENTDRLHRMIPGLETDSEWSRAARAELSVYFQECWGNEKRIDYGSGMELNMACWLLCLCKLRILRLPEDGACIVLRIFWTYVQVMRDIQSSYWLEPAGSHGVWGLDDYHFLPFLWGAGQLSSHRHLRPKAIHDAEIVDEFAPKYMYLACIQFINSVKTASLRWHSPMLDDISGAKSWSKVNQGMIKMYRAEVLKKLPIAQHIFFGSLLRFPEPATGELEEEDVEEDAHGHIHPAGKPHAHGTGEGQAAGWGDCCGIPIPSAFAAAEQEKKRQQGNFSSTMLGEKPFGTGVRRIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

433 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

47.937 kDa

MTSQAPPQPASSPGVAAPAAASSIPNLKDRLPKLEPRKRRSGPSNPTPIPETPALPTPPDTSSNWTFKTPSRRILSKKDHDIFLSSPTCKLVTAWVFGLAESIVDTPNSAIRDADLSALIKTILHILDETEQLVTKSPPNEQGGSRFGNKAFRGLLDLAQKNSAAWHHDIGVQNEDAINELSTYFCESFGNANRIDYGSGHELNFMIWLLCLYQLGLLKQSDFKPIVLRVFVRYLEVMRVIQMTYYLEPAGSHGVWGLDDYQFLPFLFGATQLLHHPYITPRAIHQDLTLEEFGHEYMYLGQVSFVNSTKTVKGLRWHSPMLDDISSARSWTKIDGGMRRMFVAEVLGKLPVMQHFLFGSLVPADDSMSEDTGAGDEADVEDDPHAGHDHTGKAHDGTGWGDCCGIKVPSSIAAAQEMKKRGMNQGLRRIPFD

rrd2

Serine/threonine-protein phosphatase 2A activator 2

422 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

47.322 kDa

MMPSHATMSSPPAGTKLDLSKKLSELRASRRSHSGPSPREPTPVTPPLPSPPDLSTHTYTRPVRRILSRKDHETFLASSTYTLVVSFTFSLSDSVRGRAVTDNKDQPASPNISRILSVIDTIRQLVDKHPSIDQGGSRFGNPAFRDLFDDVAAQNATWHREIIGLQNADAIEEVSSYLVHSLGSRDRLDYGSGHELNFMMWLLCLRQMQMISTADFPMIVFRVYLEYMRLMRQVQMTYYLEPAGSHGVWGLDDYHFLPFLFGAAQLVDHPYITPLAIHNTAVLDEEGDKYIYLDQVRWVDSVKTVKGLRWHSPMLDDISGAKNWLKIEGGMKKMFIKEVLGKLPIMQHFLFGSLLPADPSMGERSDDAQEDDLHDHGNGNPHARHTDHFGDCCGIKVPSTVAAGAEMRKRIGGTGLRPIPFD

rrd2

Serine/threonine-protein phosphatase 2A activator 2

422 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

47.062 kDa

MASEVSASQGVPKPKIDLSKKLSELRSNRKSQPALPSRPSREPAPVTPPLSNPPDLSSHQYARPVCRILSNHDHQLFLSSSSYSLILAFIFGLSDSVRGRATTDSKDRPVSPNVSKILAVVESIRTLLDQHPSIDQGGSRFGNPAFRDLFDDVAAQSAKWHREILGIQDSTAIEEASAYLIHSLGSRDRLDYGSGHELNFMMWLLCLRQMQLYSTADFEMIVFRVYVTYMHLMRDVQSAYYLEPAGSHGVWGLDDYHFLPFLFGAAQLVEHPYITPLAIHNNVILDEEGDRYIYLDQVRWVDSVKTVKGLRWHSPMLDDISGAKNWSKIESGMKKMFVKEVLGKLPIMQHFLFGSLIPAAPGMGEADDVQTDGHDHTHSHDHAHAQHTDHFGDCCGIKVPSTVAAGAEARKRGTGLRPIPFD

rrd2

Serine/threonine-protein phosphatase 2A activator 2

420 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

46.79 kDa

MASNTNPSPKPKIDLSQKLSELRAARAKTQSPREPAPVTPPLSKPPDLSSHSYSRPVRRILSKNDHETFLSSSTYTLVLAFIFGLSDSVRGRAAPDANAEPGYSPKISKILSVVDNIRTLVESHPSIDQGGSRFGNPAFRDLFDDVAAQSPAWLRDILGIEDAAAVNEISTYLIHSLGSRDRLDYGSGHELNFMMWLLCLRQLGLFSEPDFEAIVFHVYVRYMRLMREVQSTYYLEPAGSHGVWGLDDYHFLPFLFGAAQLVGHPYITPLAIHNTAILDEEGDRYLYLDQVRWVDSVKTVKGLRWHSPMLDDISGAKNWTKIESGMKKMFVKEVLGKLPIMQHFLFGSLLPAEPGMGEGEAEEEGEHTHAHGHSHVHDHSQQLDWFGDCCGIKVPSTVAAGQEMRKRMGGGSSLRPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

382 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

43.131 kDa

MSAPESSPSTFYTVPTKHILSKAHLAAFQRSKTHSDIFNFIEELNEDIVGKKLTEAGQGSERTRPLISILDSVREIAESTPPVDNKLSRFGNPAFKTFYDKVGDASLELHKRIPGLPEEAIQEVEVYFKESWGNKQRVDYGSGMELNFLSWLLCLAKLGVVTKEDYPFLVLGVFWRYIEVMRYLQSTYWLEPAGSHGVWGLDDYHFLPFLWGSGQLRNHKYLRPKAIHDPEILGEFSKDYMYLSCIEFINSIKTASLRWHSPMLDDISAVKTWEKVNQGMKKMFVAEVLGKLPVMQHALFGSLLPFPTPEEDPELKRALEEEDGQSATDMHGHIHDPSEKGWSMDCCGIPVPSAFAAAQDANSHKGVPTLGNRPGIKPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

382 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

43.131 kDa

MSAPESSPSTFYTVPTKHILSKAHLAAFQRSKTHSDIFNFIEELNEDIVGKKLTEAGQGSERTRPLISILDSVREIAESTPPVDNKLSRFGNPAFKTFYDKVGDASLELHKRIPGLPEEAIQEVEVYFKESWGNKQRVDYGSGMELNFLSWLLCLAKLGVVTKEDYPFLVLGVFWRYIEVMRYLQSTYWLEPAGSHGVWGLDDYHFLPFLWGSGQLRNHKYLRPKAIHDPEILGEFSKDYMYLSCIEFINSIKTASLRWHSPMLDDISAVKTWEKVNQGMKKMFVAEVLGKLPVMQHALFGSLLPFPTPEEDPELKRALEEEDGQSATDMHGHIHDPSEKGWSMDCCGIPVPSAFAAAQDANSHKGVPTLGNRPGIKPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

367 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

42.02 kDa

MTAEYTKPVRRITNTEDLEIWNGSQAYSTILDFVQDLQDSVVGLTNDAQVTVSSSSEELLKVLDKVNEIIENNPVVHEKDISRFGKIEFRDFYDEICKKSFDILKPLVEKLEDDPRIELATYFNESWGNRTRIDYGSGHELNFIAFLACLQKLGIIKHEDYPCVIVRVFTKYMTVMRALQKLYWLEPAGSHGVWGLDDYHFLPFLFGSSQLATHPHMKPKSIHNEELVESFYKQYMYLECIHFINTIKTTPANQDQKLSLRWHSPMLDDISSAKSWAKIKEGMIKMYKAEVLGKLPIVQHFMFGSIIPCPDGVSEYHEHDDDSDCGHDHGGTVNTWGDCCGIKIPSALAASEMNKINNPNNKPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

360 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

41.319 kDa

MAIKRLINEHDMELWNNSKTFEDVIGFINTLALSVRGRENNDYTQPISDNVQRVSNLLSKVTEIIGKHEVIKDANTSRFGKIEFRDFYDDISEHSNELISKIFEGIEKPDTGKLDDICTYFINSWGDRSRIDYGSGHELNFICFLYCLTESKVFDLENDSSNIVLMLFIKYLGIMRSLELKYWLEPAGSHGVWGLDDYHFLPFLFGAFQLSTHKHLKPKSIHNPEVVEMFQDRYLYFGCIAFINKVKTTASLRWHSPMLDDISGVKRWSKVAEGMVKMYKAEVLQKLPIMQHFYFGYFLKCPEGVSEPSARAQDHHEDDSCCTDGSHGHSTWADCCGIAVPSAIAASQMANKDVRLFPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

359 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

40.52 kDa

MSDGAELKMAAQKRLLTGSDLDKWKASKTFEELLRFVSSLAQSVRGRENSEHAEPVSPAIEALEALLEEMQGIAAHHPVLQDAATSRFGKVEFRDFHKEVQARAEALVLQVDPSLTDEQAQELAVYLGNAWGDCKRIDYGSGHELNFVCFLYGLWKYGVLSEHDFTNAVLRVFVKYMDVMRVLETKYWLEPAGSHGVWGLDDYHFLPFLFGAFQLATHKHLKPKSIHNPEVVELFENRYLYFGCIAFINRVKTTASLRWHSPMLDDISGVRSWTKVSEGMVKMYKAEVLGKLPIMQHFFFSRFLPVPDGVSPPRTSEEELADCSEHAHSTWGDCCGIPIPSAVAASEATRKHSKPLPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

358 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis.

41.452 kDa

MLPEKRLLTPDDMKLWEESPTRAHFTKFIIDLAESVKGHENSQYKEPISESINSMMNLLSQIKDITQKHPVIKDADSSRFGKVEFRDFYDEVSRNSRKILRSEFPSLTDEQLEQLSIYLDESWGNKRRIDYGSGHELNFMCLLYGLYSYGIFNLSNDSTNLVLKVFIEYLKIMRILETKYWLEPAGSHGVWGLDDYHFLPFLFGAFQLTTHKHLKPISIHNNELVEMFAHRYLYFGCIAFINKVKSSASLRWHSPMLDDISGVKTWSKVAEGMIKMYKAEVLSKLPIMQHFYFSEFLPCPDGVSPPRGHIHDGTDKDDECNFEGHVHTTWGDCCGIKLPSAIAATEMNKKHHKPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

358 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

40.71 kDa

MSYITPTKRIFTPEDLSKWVGSPTYNTVLDFIVELQSSVTGKSNDSSYETSSIIDKLSKLLSKVDNLITLHPAHDSVSRFGKIEFRDFYSDLSSKAEEYISEITATAIQETSAYFIESWGNSTRIDYGSGHELNFICFLLCLKELGQITSADYEGLVLKVFTQYMSIMRKLQKEYWLEPAGSHGVWGLDDYHFLPFLFGAAQLSTHPHMKPKSIHNDELVEMYSTKYMYFECINFINKIKTIPNHQGKLSLRWHSPMLDDISAAKNWDKIREGMVKMYKVEVLGKLPIMQHFMFGSLLKCPEGIPEHTDENGHGENPEDHCGHAHVNTWGDCCGIKIPSGIAASESLKHERKGNIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

358 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

41.231 kDa

MIPSKRILTDKDVKIWEESETREDILSFIESLAKAVEGFENDQVSEPVSDSVQSTIAVLTEIDKLIKLHPVIQDKNTSRFGKVEFRDFYDDVCEKADDLLSSHFPALTSEQIEQLSIYLQESWGNKRRIDYGSGHELNFICFLYGLTHYKIFDLQRDARNLVLVLFIEYLKIMREIETLYWLEPAGSHGVWGLDDYHFLPFLFGAFQLAPHKHLKPKSIHNEELVEMFADKYLYFGCIAFINSVKTSTSLRWHSPMLDDISGVKKWSKVAEGMIKMYKAEVLGKLPIMQHFYFSEFLVCPEGISEPRTHIHNGDEDDDQCCQDGAAHNTWGDCCGIKIPSLYAANAMEKQSHKPIPFD

RRD2

Serine/threonine-protein phosphatase 2A activator 2

354 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

40.029 kDa

MSHSHPVRRILSPKDLEIFGASDTKKQVFGFVKVLNYYVVGKGNSYETLKHPIIGKLVAILDKVIDLVAKYPPEDATSSRFGKPEFRDFHQALEENAKDWISDLGELEDWQLVELCTYFAASFGDRTRIDFGSGHELNFICFLFCLRQLGLLDTDSSAAVLTVFVQYLKTMRAVQASYWLEPAGSHGVWGLDDYHFLPFMFGSAQLACHKYLRPLSIHDMEMLDMWKHEYLYMGCIHFINSVKTTASLRWHSPMLDDISGVKTWAKVNQGMVKMYDAEVLSKLPILQHFMFGQLIKAPEGVSPPPDPNAEVQHIHNHWADCCGIKVPSAIAASEMSQKPGDLRKLRGSGVLPFD

rrd2

Serine/threonine-protein phosphatase 2A activator 2

352 amino acids

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).

Belongs to the PTPA-type PPIase family.

40.288 kDa

MLSREEQNRCFVPVRRILDNEDLKLFKEGDAYKLIDSFICDLDEAVKDKPISASIPQSSSIEHVLNILDRVGEIKQENPAIDNMGSRFGNPAFQSFYDQVYIETPKLHQVFGIEHNAAMEAGRYFYESFGNRKRIDYGSGHELYFMSWLLILKQLGIFTKNDYPALVVRVFVKYVELMRSLQIFYTLEPAGSHGVWGLDDFHFLPFLFGAAQLVNHKYLRPKHVRDPEILEMCRADYMYLGYVYFLNKLKPSVSLRFHSPMIDDISAVKTWSKVNEGMIKMYRAEVLGKLPIMQHYLFGHLIPASPGMSPAPQDGDDSEVTHVHSHYADCCGIKIPSAISAAKNNGSRIPFD