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Q16537 (2A5E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

Subunit structure

Found in a complex with at least ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and TBCD By similarity. 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. Ref.6

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylated on serine residues.

Sequence similarities

Belongs to the phosphatase 2A regulatory subunit B56 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16537-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16537-2)

The sequence of this isoform differs from the canonical sequence as follows:
     430-435: KSDRQR → N
Note: No experimental confirmation available.
Isoform 3 (identifier: Q16537-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 467466Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
PRO_0000071454

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue301Phosphoserine Ref.10
Modified residue321Phosphoserine Ref.10
Modified residue341Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 7676Missing in isoform 3.
VSP_055163
Alternative sequence430 – 4356KSDRQR → N in isoform 2.
VSP_054588

Experimental info

Sequence conflict1941R → W in BAH14801. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DD9CE11433F499CF

FASTA46754,699
        10         20         30         40         50         60 
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP 

        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

Isoform 2 [UniParc].

Checksum: C37302CC366D270C
Show »

FASTA46254,043
Isoform 3 [UniParc].

Checksum: 076E305A94E9F54B
Show »

FASTA39146,180

References

« Hide 'large scale' references
[1]"The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 449-455.
Tissue: Fetal retina.
[2]"The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
McCright B., Rivers A.M., Audlin S., Virshup D.M.
J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Testis.
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Brain.
[6]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGOL1.
[7]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32 AND SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z69029 mRNA. Translation: CAA93153.1.
L76703 mRNA. Translation: AAB69752.1.
AK316430 mRNA. Translation: BAH14801.1.
AL118555 Genomic DNA. No translation available.
AL132992 Genomic DNA. No translation available.
AL136038 Genomic DNA. No translation available.
BC093766 mRNA. Translation: AAH93766.1.
BC101479 mRNA. Translation: AAI01480.1.
BC143231 mRNA. Translation: AAI43232.1.
BC143234 mRNA. Translation: AAI43235.1.
CCDSCCDS9758.1.
RefSeqNP_001269108.1. NM_001282179.1. [Q16537-1]
NP_001269109.1. NM_001282180.1. [Q16537-2]
NP_001269110.1. NM_001282181.1.
NP_001269111.1. NM_001282182.1.
NP_006237.1. NM_006246.3. [Q16537-1]
UniGeneHs.334868.
Hs.594347.

3D structure databases

ProteinModelPortalQ16537.
SMRQ16537. Positions 51-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111521. 23 interactions.
IntActQ16537. 32 interactions.
MINTMINT-1198703.
STRING9606.ENSP00000337641.

PTM databases

PhosphoSiteQ16537.

Polymorphism databases

DMDM7387498.

Proteomic databases

MaxQBQ16537.
PaxDbQ16537.
PRIDEQ16537.

Protocols and materials databases

DNASU5529.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337537; ENSP00000337641; ENSG00000154001.
ENST00000422769; ENSP00000404632; ENSG00000154001.
ENST00000555899; ENSP00000452396; ENSG00000154001.
GeneID5529.
KEGGhsa:5529.
UCSCuc001xgd.1. human. [Q16537-1]

Organism-specific databases

CTD5529.
GeneCardsGC14M063838.
HGNCHGNC:9313. PPP2R5E.
HPAHPA006034.
MIM601647. gene.
neXtProtNX_Q16537.
PharmGKBPA33677.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264925.
HOGENOMHOG000067326.
HOVERGENHBG000009.
InParanoidQ16537.
KOK11584.
OMATEQAYPE.
OrthoDBEOG7C2R2S.
PhylomeDBQ16537.
TreeFamTF105556.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ16537.

Gene expression databases

ArrayExpressQ16537.
BgeeQ16537.
CleanExHS_PPP2R5E.
GenevestigatorQ16537.

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

ChiTaRSPPP2R5E. human.
GeneWikiPPP2R5E.
GenomeRNAi5529.
NextBio21418.
PROQ16537.
SOURCESearch...

Entry information

Entry name2A5E_HUMAN
AccessionPrimary (citable) accession number: Q16537
Secondary accession number(s): A4FU37 expand/collapse secondary AC list , B7ZAW5, B7ZKK8, B7ZKK9, J3KQN6, Q52LW4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM