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

Names and origin

Protein names

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 names

Name:	Ppp2r5e
Synonyms:	Kiaa4006

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Traceable author statement PubMed 10781942. Source: MGI intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara protein phosphatase type 2A complex Inferred from electronic annotation. Source: InterPro
Molecular_function	protein phosphatase type 2A regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform		PRO_0000071455
Amino acid modifications
	Modified residue	30	1	Phosphoserine By similarity
	Modified residue	32	1	Phosphoserine By similarity
	Modified residue	34	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	74	1	F → C in AAB37234. Ref.4
	Sequence conflict	162	1	L → W in AAB37234. Ref.4
	Sequence conflict	388	1	F → S in AAB37234. Ref.4
	Sequence conflict	409	1	N → T in AAB37234. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q61151 [UniParc]. Last modified July 19, 2005. Version 3. Checksum: 77DA129F9A4EC6AC	FASTA	467	54,713
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00224697.
RefSeq	NP_036154.1. NM_012024.2.
UniGene	Mm.259626. Mm.440646.
3D structure databases
ProteinModelPortal	Q61151.
SMR	Q61151. Positions 51-423.
ModBase	Search...
PTM databases
PhosphoSite	Q61151.
Proteomic databases
PaxDb	Q61151.
PRIDE	Q61151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021447; ENSMUSP00000021447; ENSMUSG00000021051.
GeneID	26932.
KEGG	mmu:26932.
UCSC	uc007nxe.1. mouse.
Organism-specific databases
CTD	5529.
MGI	MGI:1349473. Ppp2r5e.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG264925.
GeneTree	ENSGT00550000074525.
HOGENOM	HOG000067326.
HOVERGEN	HBG000009.
InParanoid	Q61151.
KO	K11584.
OMA	VSRGYLT.
Gene expression databases
Bgee	Q61151.
Genevestigator	Q61151.
GermOnline	ENSMUSG00000021051. Mus musculus.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR002554. PP2A_B56. [Graphical view]
PANTHER	PTHR10257. PTHR10257. 1 hit.
Pfam	PF01603. B56. 1 hit. [Graphical view]
PIRSF	PIRSF028043. PP2A_B56. 1 hit.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	304835.
SOURCE	Search...

Entry information

Entry name

2A5E_MOUSE

Accession

Primary (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 3, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program