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Q61151 (2A5E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ppp2r5e
Synonyms:Kiaa4006
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphatase 2A regulatory subunit B56 family.

Sequence caution

The sequence AAB37234.1 differs from that shown. Reason: Frameshift at positions 162, 180 and 185.

The sequence BAD90335.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 467466Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
PRO_0000071455

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue301Phosphoserine By similarity
Modified residue321Phosphoserine By similarity
Modified residue341Phosphoserine By similarity

Experimental info

Sequence conflict741F → C in AAB37234. Ref.4
Sequence conflict1621L → W in AAB37234. Ref.4
Sequence conflict3881F → S in AAB37234. Ref.4
Sequence conflict4091N → T in AAB37234. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q61151 [UniParc].

Last modified July 19, 2005. Version 3.
Checksum: 77DA129F9A4EC6AC

FASTA46754,713
        10         20         30         40         50         60 
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPTSEQP 

        70         80         90        100        110        120 
ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS 

       130        140        150        160        170        180 
CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF 

       190        200        210        220        230        240 
VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE 

       250        260        270        280        290        300 
LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE 

       310        320        330        340        350        360 
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA 

       370        380        390        400        410        420 
ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST 

       430        440        450        460 
MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_036154.1. NM_012024.2.
XP_006515988.1. XM_006515925.1.
UniGeneMm.259626.
Mm.440646.

3D structure databases

ProteinModelPortalQ61151.
SMRQ61151. Positions 51-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61151. 2 interactions.
MINTMINT-4114181.

PTM databases

PhosphoSiteQ61151.

Proteomic databases

PaxDbQ61151.
PRIDEQ61151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021447; ENSMUSP00000021447; ENSMUSG00000021051.
GeneID26932.
KEGGmmu:26932.
UCSCuc007nxe.1. mouse.

Organism-specific databases

CTD5529.
MGIMGI:1349473. Ppp2r5e.
RougeSearch...

Phylogenomic databases

eggNOGNOG264925.
GeneTreeENSGT00550000074525.
HOGENOMHOG000067326.
HOVERGENHBG000009.
InParanoidQ61151.
KOK11584.
OMATEQAYPE.
OrthoDBEOG7C2R2S.
PhylomeDBQ61151.
TreeFamTF105556.

Gene expression databases

BgeeQ61151.
GenevestigatorQ61151.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERPTHR10257. PTHR10257. 1 hit.
PfamPF01603. B56. 1 hit.
[Graphical view]
PIRSFPIRSF028043. PP2A_B56. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio304835.
PROQ61151.
SOURCESearch...

Entry information

Entry name2A5E_MOUSE
AccessionPrimary (citable) accession number: Q61151
Secondary accession number(s): Q3V1I5, Q571M6, Q8C2M2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot