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Q61151

- 2A5E_MOUSE

UniProt

Q61151 - 2A5E_MOUSE

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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform

Gene

Ppp2r5e

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Interacts with cyclin G in vitro.

GO - Molecular functioni

  1. protein phosphatase type 2A regulator activity Source: InterPro

GO - Biological processi

  1. signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_207679. Separation of Sister Chromatids.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_230286. APC truncation mutants have impaired AXIN binding.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_250714. truncations of AMER1 destabilize the destruction complex.
REACT_252458. AXIN missense mutants destabilize the destruction complex.
REACT_256756. Mitotic Prometaphase.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261568. CTLA4 inhibitory signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
Alternative name(s):
PP2A B subunit isoform B'-epsilon
PP2A B subunit isoform B56-epsilon
PP2A B subunit isoform PR61-epsilon
PP2A B subunit isoform R5-epsilon
Gene namesi
Name:Ppp2r5e
Synonyms:Kiaa4006
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1349473. Ppp2r5e.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. protein phosphatase type 2A complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 467466Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoformPRO_0000071455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61151.
PaxDbiQ61151.
PRIDEiQ61151.

PTM databases

PhosphoSiteiQ61151.

Expressioni

Gene expression databases

BgeeiQ61151.
GenevestigatoriQ61151.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGOL1. Found in a complex with at least ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity).By similarity

Protein-protein interaction databases

IntActiQ61151. 3 interactions.
MINTiMINT-4114181.

Structurei

3D structure databases

ProteinModelPortaliQ61151.
SMRiQ61151. Positions 51-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG264925.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ61151.
KOiK11584.
OMAiTEQAYPE.
OrthoDBiEOG7C2R2S.
PhylomeDBiQ61151.
TreeFamiTF105556.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61151-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL
60 70 80 90 100
LKDVPTSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI
110 120 130 140 150
TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH
160 170 180 190 200
LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK
210 220 230 240 250
TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN
260 270 280 290 300
GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
310 320 330 340 350
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK
360 370 380 390 400
CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN
410 420 430 440 450
PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL
460
EDLELKRGLR RDGIIPT
Length:467
Mass (Da):54,713
Last modified:July 19, 2005 - v3
Checksum:i77DA129F9A4EC6AC
GO

Sequence cautioni

The sequence AAB37234.1 differs from that shown. Reason: Frameshift at positions 162, 180 and 185. Curated
The sequence BAD90335.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741F → C in AAB37234. (PubMed:8887688)Curated
Sequence conflicti162 – 1621L → W in AAB37234. (PubMed:8887688)Curated
Sequence conflicti388 – 3881F → S in AAB37234. (PubMed:8887688)Curated
Sequence conflicti409 – 4091N → T in AAB37234. (PubMed:8887688)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088366 mRNA. Translation: BAC40306.1.
AK132432 mRNA. Translation: BAE21166.1.
BC085149 mRNA. Translation: AAH85149.1.
AK220163 mRNA. Translation: BAD90335.1. Different initiation.
U49728 mRNA. Translation: AAB37234.1. Frameshift.
CCDSiCCDS25983.1.
RefSeqiNP_036154.1. NM_012024.2.
XP_006515988.1. XM_006515925.1.
UniGeneiMm.259626.
Mm.440646.

Genome annotation databases

EnsembliENSMUST00000021447; ENSMUSP00000021447; ENSMUSG00000021051.
GeneIDi26932.
KEGGimmu:26932.
UCSCiuc007nxe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088366 mRNA. Translation: BAC40306.1 .
AK132432 mRNA. Translation: BAE21166.1 .
BC085149 mRNA. Translation: AAH85149.1 .
AK220163 mRNA. Translation: BAD90335.1 . Different initiation.
U49728 mRNA. Translation: AAB37234.1 . Frameshift.
CCDSi CCDS25983.1.
RefSeqi NP_036154.1. NM_012024.2.
XP_006515988.1. XM_006515925.1.
UniGenei Mm.259626.
Mm.440646.

3D structure databases

ProteinModelPortali Q61151.
SMRi Q61151. Positions 51-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61151. 3 interactions.
MINTi MINT-4114181.

PTM databases

PhosphoSitei Q61151.

Proteomic databases

MaxQBi Q61151.
PaxDbi Q61151.
PRIDEi Q61151.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021447 ; ENSMUSP00000021447 ; ENSMUSG00000021051 .
GeneIDi 26932.
KEGGi mmu:26932.
UCSCi uc007nxe.1. mouse.

Organism-specific databases

CTDi 5529.
MGIi MGI:1349473. Ppp2r5e.
Rougei Search...

Phylogenomic databases

eggNOGi NOG264925.
GeneTreei ENSGT00550000074525.
HOGENOMi HOG000067326.
HOVERGENi HBG000009.
InParanoidi Q61151.
KOi K11584.
OMAi TEQAYPE.
OrthoDBi EOG7C2R2S.
PhylomeDBi Q61151.
TreeFami TF105556.

Enzyme and pathway databases

Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_207679. Separation of Sister Chromatids.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_230286. APC truncation mutants have impaired AXIN binding.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_250714. truncations of AMER1 destabilize the destruction complex.
REACT_252458. AXIN missense mutants destabilize the destruction complex.
REACT_256756. Mitotic Prometaphase.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261568. CTLA4 inhibitory signaling.

Miscellaneous databases

ChiTaRSi Ppp2r5e. mouse.
NextBioi 304835.
PROi Q61151.
SOURCEi Search...

Gene expression databases

Bgeei Q61151.
Genevestigatori Q61151.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view ]
PANTHERi PTHR10257. PTHR10257. 1 hit.
Pfami PF01603. B56. 1 hit.
[Graphical view ]
PIRSFi PIRSF028043. PP2A_B56. 1 hit.
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 and NOD.
    Tissue: Skin and Thymus.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-436.
    Tissue: Embryonic tail.
  4. "p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A."
    Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., Beach D.
    Mol. Cell. Biol. 16:6593-6602(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-437.
    Tissue: Embryonic fibroblast.

Entry informationi

Entry namei2A5E_MOUSE
AccessioniPrimary (citable) accession number: Q61151
Secondary accession number(s): Q3V1I5, Q571M6, Q8C2M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 19, 2005
Last modified: November 26, 2014
This is version 103 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, Reference proteome

Documents

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

External Data

Dasty 3