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P63151 (2ABA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 55 kDa regulatory subunit B alpha isoform
Alternative name(s):
PP2A subunit B isoform B55-alpha
PP2A subunit B isoform PR55-alpha
PP2A subunit B isoform R2-alpha
PP2A subunit B isoform alpha
Gene names
Name:PPP2R2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length447 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 TP53. Ref.6

Tissue specificity

Expressed in all tissues examined. Ref.1

Sequence similarities

Belongs to the phosphatase 2A regulatory subunit B family.

Contains 7 WD repeats.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope reassembly

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

protein dephosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

response to morphine

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

protein phosphatase type 2A complex

Inferred from direct assay Ref.6Ref.1. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6PubMed 9847399. Source: UniProtKB

protein phosphatase type 2A regulator activity

Traceable author statement Ref.1. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP2R1AP301538EBI-1048931,EBI-302388
PPP2R1BP301542EBI-1048931,EBI-357094

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63151-1)

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: P63151-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MFPKFSLRSMFH
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 447446Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
PRO_0000071415

Regions

Repeat26 – 6540WD 1
Repeat91 – 13242WD 2
Repeat175 – 21339WD 3
Repeat224 – 26441WD 4
Repeat283 – 32139WD 5
Repeat338 – 37942WD 6
Repeat414 – 44633WD 7

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.9

Natural variations

Alternative sequence1 – 22MA → MFPKFSLRSMFH in isoform 2.
VSP_043100

Secondary structure

............................................................................... 447
Helix Strand Turn

Details...

Sequences

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

Last modified September 27, 2004. Version 1.
Checksum: F4D407FF7ADA4ED6

FASTA44751,692
        10         20         30         40         50         60 
MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE 

        70         80         90        100        110        120 
NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK 

       130        140        150        160        170        180 
LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI 

       190        200        210        220        230        240 
NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN 

       250        260        270        280        290        300 
TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM 

       310        320        330        340        350        360 
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG 

       370        380        390        400        410        420 
SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL 

       430        440 
HTAWHPKENI IAVATTNNLY IFQDKVN 

« Hide

Isoform 2 [UniParc].

Checksum: 242C50314171EDDE
Show »

FASTA45753,000

References

« Hide 'large scale' references
[1]"Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform."
Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.
Biochemistry 30:3589-3597(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Lung fibroblast.
[2]"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] (ISOFORMS 1 AND 2).
Tissue: Brain and Trachea.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Blood.
[6]"A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64929 mRNA. Translation: AAA36490.1.
AK303981 mRNA. Translation: BAG64899.1.
AK314823 mRNA. Translation: BAG37345.1.
AC022911 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63578.1.
BC041071 mRNA. Translation: AAH41071.1.
CCDSCCDS34867.1. [P63151-1]
CCDS55213.1. [P63151-2]
PIRA38351.
RefSeqNP_001171062.1. NM_001177591.1. [P63151-2]
NP_002708.1. NM_002717.3. [P63151-1]
UniGeneHs.146339.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DW8X-ray2.85B/E1-447[»]
ProteinModelPortalP63151.
SMRP63151. Positions 8-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111512. 57 interactions.
DIPDIP-29398N.
IntActP63151. 18 interactions.
MINTMINT-2835351.
STRING9606.ENSP00000370113.

Chemistry

BindingDBP63151.
ChEMBLCHEMBL4284.

PTM databases

PhosphoSiteP63151.

Polymorphism databases

DMDM52783535.

Proteomic databases

MaxQBP63151.
PaxDbP63151.
PeptideAtlasP63151.
PRIDEP63151.

Protocols and materials databases

DNASU5520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315985; ENSP00000325074; ENSG00000221914. [P63151-2]
ENST00000380737; ENSP00000370113; ENSG00000221914. [P63151-1]
GeneID5520.
KEGGhsa:5520.
UCSCuc003xeu.3. human. [P63151-1]
uc011laf.2. human. [P63151-2]

Organism-specific databases

CTD5520.
GeneCardsGC08P026204.
HGNCHGNC:9304. PPP2R2A.
HPAHPA042122.
HPA042770.
MIM604941. gene.
neXtProtNX_P63151.
PharmGKBPA33668.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5170.
HOGENOMHOG000089745.
HOVERGENHBG000012.
InParanoidP63151.
KOK04354.
OMAQRNMAGA.
OrthoDBEOG7Q5HCZ.
PhylomeDBP63151.
TreeFamTF105553.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.
SignaLinkP63151.

Gene expression databases

ArrayExpressP63151.
BgeeP63151.
CleanExHS_PPP2R2A.
GenevestigatorP63151.

Family and domain databases

Gene3D2.130.10.10. 3 hits.
InterProIPR000009. PP2A_PR55.
IPR018067. PP2A_PR55_CS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR11871. PTHR11871. 1 hit.
PIRSFPIRSF037309. PP2A_PR55. 1 hit.
PRINTSPR00600. PP2APR55.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 3 hits.
PROSITEPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP2R2A. human.
EvolutionaryTraceP63151.
GeneWikiPPP2R2A.
GenomeRNAi5520.
NextBio21352.
PROP63151.
SOURCESearch...

Entry information

Entry name2ABA_HUMAN
AccessionPrimary (citable) accession number: P63151
Secondary accession number(s): B2RBU8 expand/collapse secondary AC list , B4E1T7, P50409, Q00007
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM