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P63151

- 2ABA_HUMAN

UniProt

P63151 - 2ABA_HUMAN

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Protein
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
Gene
PPP2R2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein phosphatase type 2A regulator activity Source: UniProtKB
  3. protein serine/threonine phosphatase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: Reactome
  2. RNA metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear envelope reassembly Source: Reactome
  7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  8. protein dephosphorylation Source: UniProtKB
  9. regulation of catalytic activity Source: GOC
  10. response to morphine Source: Ensembl
  11. signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinkiP63151.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PPP2R2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9304. PPP2R2A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
  3. protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 447446Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
PRO_0000071415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP63151.
PaxDbiP63151.
PeptideAtlasiP63151.
PRIDEiP63151.

PTM databases

PhosphoSiteiP63151.

Expressioni

Tissue specificityi

Expressed in all tissues examined.1 Publication

Gene expression databases

ArrayExpressiP63151.
BgeeiP63151.
CleanExiHS_PPP2R2A.
GenevestigatoriP63151.

Organism-specific databases

HPAiHPA042122.
HPA042770.

Interactioni

Subunit structurei

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 TP53.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP2R1AP301538EBI-1048931,EBI-302388
PPP2R1BP301542EBI-1048931,EBI-357094

Protein-protein interaction databases

BioGridi111512. 53 interactions.
DIPiDIP-29398N.
IntActiP63151. 18 interactions.
MINTiMINT-2835351.
STRINGi9606.ENSP00000370113.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 164
Beta strandi21 – 233
Helixi27 – 293
Beta strandi30 – 367
Beta strandi38 – 4710
Beta strandi50 – 578
Beta strandi71 – 788
Beta strandi83 – 853
Helixi86 – 883
Beta strandi90 – 923
Beta strandi98 – 1014
Beta strandi106 – 1149
Beta strandi119 – 13214
Beta strandi156 – 17217
Beta strandi182 – 1854
Beta strandi189 – 1957
Beta strandi197 – 2048
Beta strandi207 – 21610
Helixi222 – 2243
Beta strandi229 – 2346
Beta strandi241 – 2466
Beta strandi251 – 2555
Turni256 – 2583
Beta strandi260 – 2623
Beta strandi267 – 2693
Helixi280 – 2845
Beta strandi288 – 2936
Beta strandi297 – 31216
Beta strandi323 – 3253
Helixi327 – 3293
Turni330 – 3323
Helixi333 – 3386
Helixi341 – 3433
Beta strandi348 – 3503
Beta strandi354 – 3607
Beta strandi365 – 3706
Turni371 – 3733
Beta strandi376 – 3805
Helixi410 – 4123
Beta strandi421 – 4244
Beta strandi426 – 4349
Beta strandi439 – 4435

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DW8X-ray2.85B/E1-447[»]
ProteinModelPortaliP63151.
SMRiP63151. Positions 8-446.

Miscellaneous databases

EvolutionaryTraceiP63151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati26 – 6540WD 1
Add
BLAST
Repeati91 – 13242WD 2
Add
BLAST
Repeati175 – 21339WD 3
Add
BLAST
Repeati224 – 26441WD 4
Add
BLAST
Repeati283 – 32139WD 5
Add
BLAST
Repeati338 – 37942WD 6
Add
BLAST
Repeati414 – 44633WD 7
Add
BLAST

Sequence similaritiesi

Contains 7 WD repeats.

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG5170.
HOGENOMiHOG000089745.
HOVERGENiHBG000012.
InParanoidiP63151.
KOiK04354.
OMAiQRNMAGA.
OrthoDBiEOG7Q5HCZ.
PhylomeDBiP63151.
TreeFamiTF105553.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR000009. PP2A_PR55.
IPR018067. PP2A_PR55_CS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR11871. PTHR11871. 1 hit.
PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
PRINTSiPR00600. PP2APR55.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P63151-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG    50
RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR 100
WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT 150
TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI 200
NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT 250
IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM 300
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW 350
NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS 400
GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN 447
Length:447
Mass (Da):51,692
Last modified:September 27, 2004 - v1
Checksum:iF4D407FF7ADA4ED6
GO
Isoform 2 (identifier: P63151-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MFPKFSLRSMFH

Note: No experimental confirmation available.

Show »
Length:457
Mass (Da):53,000
Checksum:i242C50314171EDDE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22MA → MFPKFSLRSMFH in isoform 2.
VSP_043100

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34867.1. [P63151-1]
CCDS55213.1. [P63151-2]
PIRiA38351.
RefSeqiNP_001171062.1. NM_001177591.1. [P63151-2]
NP_002708.1. NM_002717.3. [P63151-1]
UniGeneiHs.146339.

Genome annotation databases

EnsembliENST00000315985; ENSP00000325074; ENSG00000221914. [P63151-2]
ENST00000380737; ENSP00000370113; ENSG00000221914. [P63151-1]
GeneIDi5520.
KEGGihsa:5520.
UCSCiuc003xeu.3. human. [P63151-1]
uc011laf.2. human. [P63151-2]

Polymorphism databases

DMDMi52783535.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34867.1. [P63151-1 ]
CCDS55213.1. [P63151-2 ]
PIRi A38351.
RefSeqi NP_001171062.1. NM_001177591.1. [P63151-2 ]
NP_002708.1. NM_002717.3. [P63151-1 ]
UniGenei Hs.146339.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DW8 X-ray 2.85 B/E 1-447 [» ]
ProteinModelPortali P63151.
SMRi P63151. Positions 8-446.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111512. 53 interactions.
DIPi DIP-29398N.
IntActi P63151. 18 interactions.
MINTi MINT-2835351.
STRINGi 9606.ENSP00000370113.

Chemistry

BindingDBi P63151.
ChEMBLi CHEMBL4284.

PTM databases

PhosphoSitei P63151.

Polymorphism databases

DMDMi 52783535.

Proteomic databases

MaxQBi P63151.
PaxDbi P63151.
PeptideAtlasi P63151.
PRIDEi P63151.

Protocols and materials databases

DNASUi 5520.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315985 ; ENSP00000325074 ; ENSG00000221914 . [P63151-2 ]
ENST00000380737 ; ENSP00000370113 ; ENSG00000221914 . [P63151-1 ]
GeneIDi 5520.
KEGGi hsa:5520.
UCSCi uc003xeu.3. human. [P63151-1 ]
uc011laf.2. human. [P63151-2 ]

Organism-specific databases

CTDi 5520.
GeneCardsi GC08P026204.
HGNCi HGNC:9304. PPP2R2A.
HPAi HPA042122.
HPA042770.
MIMi 604941. gene.
neXtProti NX_P63151.
PharmGKBi PA33668.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5170.
HOGENOMi HOG000089745.
HOVERGENi HBG000012.
InParanoidi P63151.
KOi K04354.
OMAi QRNMAGA.
OrthoDBi EOG7Q5HCZ.
PhylomeDBi P63151.
TreeFami TF105553.

Enzyme and pathway databases

Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinki P63151.

Miscellaneous databases

ChiTaRSi PPP2R2A. human.
EvolutionaryTracei P63151.
GeneWikii PPP2R2A.
GenomeRNAii 5520.
NextBioi 21352.
PROi P63151.
SOURCEi Search...

Gene expression databases

ArrayExpressi P63151.
Bgeei P63151.
CleanExi HS_PPP2R2A.
Genevestigatori P63151.

Family and domain databases

Gene3Di 2.130.10.10. 3 hits.
InterProi IPR000009. PP2A_PR55.
IPR018067. PP2A_PR55_CS.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
PANTHERi PTHR11871. PTHR11871. 1 hit.
PIRSFi PIRSF037309. PP2A_PR55. 1 hit.
PRINTSi PR00600. PP2APR55.
SMARTi SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 3 hits.
PROSITEi PS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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].

Entry informationi

Entry namei2ABA_HUMAN
AccessioniPrimary (citable) accession number: P63151
Secondary accession number(s): B2RBU8
, B4E1T7, P50409, Q00007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: September 3, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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