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Protein

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform

Gene

Ppp2r2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity. Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
Alternative name(s):
PP2A subunit B isoform B55-beta
PP2A subunit B isoform PR55-beta
PP2A subunit B isoform R2-beta
PP2A subunit B isoform beta
Gene namesi
Name:Ppp2r2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1920180. Ppp2r2b.

Subcellular locationi

Isoform 2 :
  • Cytoplasm By similarity
  • Mitochondrion By similarity
  • Mitochondrion outer membrane By similarity

  • Note: Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoformPRO_0000071423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei295 – 2951PhosphotyrosineBy similarity
Modified residuei298 – 2981PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6ZWR4.
MaxQBiQ6ZWR4.
PaxDbiQ6ZWR4.
PeptideAtlasiQ6ZWR4.
PRIDEiQ6ZWR4.

PTM databases

iPTMnetiQ6ZWR4.
PhosphoSiteiQ6ZWR4.

Expressioni

Tissue specificityi

Expressed in brain, testis, lung and spleen. In the brain, expressed in the cortex, hippocampus and cerebellum (at protein level).1 Publication

Developmental stagei

Expressed in embryo at 14 and 17 dpc.1 Publication

Gene expression databases

BgeeiQ6ZWR4.
GenevisibleiQ6ZWR4. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi215651. 2 interactions.
IntActiQ6ZWR4. 1 interaction.
STRINGi10090.ENSMUSP00000025377.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWR4.
SMRiQ6ZWR4. Positions 23-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6140WD 1Add
BLAST
Repeati87 – 12842WD 2Add
BLAST
Repeati171 – 20939WD 3Add
BLAST
Repeati220 – 26041WD 4Add
BLAST
Repeati279 – 31739WD 5Add
BLAST
Repeati334 – 37542WD 6Add
BLAST
Repeati410 – 44233WD 7Add
BLAST

Domaini

The N-terminal 26 residues of isoform 2 constitute a cryptic mitochondrial matrix import signal with critical basic and hydrophobic residues, that is necessary and sufficient for targeting the PP2A holoenzyme to the outer mitochondrial membrane (OMM) and does not affect holoenzyme formation or catalytic activity.By similarity
The last WD repeat of isoform 2 constitutes a mitochondrial stop-transfer domain that confers resistance to the unfolding step process required for import and therefore prevents PPP2R2B matrix translocation and signal sequence cleavage.By similarity

Sequence similaritiesi

Contains 7 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1354. Eukaryota.
COG5170. LUCA.
GeneTreeiENSGT00390000006311.
HOGENOMiHOG000089745.
HOVERGENiHBG000012.
InParanoidiQ6ZWR4.
KOiK04354.
OMAiPIPPRTF.
OrthoDBiEOG7Q5HCZ.
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.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR11871. PTHR11871. 1 hit.
PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
PRINTSiPR00600. PP2APR55.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZWR4-1) [UniParc]FASTAAdd to basket

Also known as: Bbeta

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

        10         20         30         40         50
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI
60 70 80 90 100
FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ
110 120 130 140 150
QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV
160 170 180 190 200
PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN
210 220 230 240 250
FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC
260 270 280 290 300
DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD
310 320 330 340 350
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD
360 370 380 390 400
SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR
410 420 430 440
KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN
Length:443
Mass (Da):51,710
Last modified:July 5, 2004 - v1
Checksum:iC383C834B2852B8F
GO
Isoform 2 (identifier: Q6ZWR4-2) [UniParc]FASTAAdd to basket

Also known as: Bbeta2

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEEDIDTRKINNSFLRDHSYA → MKCFSRYLPYIFRPPNTILSSSCH

Note: Contains a cryptic mitochondrial transit peptide at positions 1-26.By similarity
Show »
Length:446
Mass (Da):52,017
Checksum:iD5BDD8D10F79CF0B
GO
Isoform 3 (identifier: Q6ZWR4-3) [UniParc]FASTAAdd to basket

Also known as: Bbeta1

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MEEDIDTRKINNSFLRDHSYATEA → MKPFTA

Show »
Length:425
Mass (Da):49,548
Checksum:iDC88E2624D319280
GO

Sequence cautioni

The sequence BAB31079.1 differs from that shown.Aberrant splicing.Curated
The sequence EDL10024.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351T → S in BAE28701 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MEEDI…YATEA → MKPFTA in isoform 3. 1 PublicationVSP_037982Add
BLAST
Alternative sequencei1 – 2121MEEDI…DHSYA → MKCFSRYLPYIFRPPNTILS SSCH in isoform 2. 3 PublicationsVSP_037983Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF512670 mRNA. Translation: AAM46987.1.
AF536771 mRNA. Translation: AAN05641.1.
AK013600 mRNA. Translation: BAB28921.1.
AK018119 mRNA. Translation: BAB31079.1. Sequence problems.
AK039592 mRNA. Translation: BAC30395.1.
AK148956 mRNA. Translation: BAE28701.1.
CH466528 Genomic DNA. Translation: EDL10024.1. Sequence problems.
CH466528 Genomic DNA. Translation: EDL10025.1.
BC026686 mRNA. Translation: AAH26686.1.
BC088979 mRNA. Translation: AAH88979.1.
CCDSiCCDS29216.1. [Q6ZWR4-2]
RefSeqiNP_082668.1. NM_028392.3. [Q6ZWR4-2]
XP_006526349.1. XM_006526286.2. [Q6ZWR4-3]
UniGeneiMm.26134.

Genome annotation databases

EnsembliENSMUST00000025377; ENSMUSP00000025377; ENSMUSG00000024500. [Q6ZWR4-2]
ENSMUST00000117687; ENSMUSP00000113731; ENSMUSG00000024500. [Q6ZWR4-1]
ENSMUST00000120632; ENSMUSP00000113411; ENSMUSG00000024500. [Q6ZWR4-1]
GeneIDi72930.
KEGGimmu:72930.
UCSCiuc008eub.2. mouse. [Q6ZWR4-1]
uc008euc.2. mouse. [Q6ZWR4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF512670 mRNA. Translation: AAM46987.1.
AF536771 mRNA. Translation: AAN05641.1.
AK013600 mRNA. Translation: BAB28921.1.
AK018119 mRNA. Translation: BAB31079.1. Sequence problems.
AK039592 mRNA. Translation: BAC30395.1.
AK148956 mRNA. Translation: BAE28701.1.
CH466528 Genomic DNA. Translation: EDL10024.1. Sequence problems.
CH466528 Genomic DNA. Translation: EDL10025.1.
BC026686 mRNA. Translation: AAH26686.1.
BC088979 mRNA. Translation: AAH88979.1.
CCDSiCCDS29216.1. [Q6ZWR4-2]
RefSeqiNP_082668.1. NM_028392.3. [Q6ZWR4-2]
XP_006526349.1. XM_006526286.2. [Q6ZWR4-3]
UniGeneiMm.26134.

3D structure databases

ProteinModelPortaliQ6ZWR4.
SMRiQ6ZWR4. Positions 23-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215651. 2 interactions.
IntActiQ6ZWR4. 1 interaction.
STRINGi10090.ENSMUSP00000025377.

PTM databases

iPTMnetiQ6ZWR4.
PhosphoSiteiQ6ZWR4.

Proteomic databases

EPDiQ6ZWR4.
MaxQBiQ6ZWR4.
PaxDbiQ6ZWR4.
PeptideAtlasiQ6ZWR4.
PRIDEiQ6ZWR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025377; ENSMUSP00000025377; ENSMUSG00000024500. [Q6ZWR4-2]
ENSMUST00000117687; ENSMUSP00000113731; ENSMUSG00000024500. [Q6ZWR4-1]
ENSMUST00000120632; ENSMUSP00000113411; ENSMUSG00000024500. [Q6ZWR4-1]
GeneIDi72930.
KEGGimmu:72930.
UCSCiuc008eub.2. mouse. [Q6ZWR4-1]
uc008euc.2. mouse. [Q6ZWR4-2]

Organism-specific databases

CTDi5521.
MGIiMGI:1920180. Ppp2r2b.

Phylogenomic databases

eggNOGiKOG1354. Eukaryota.
COG5170. LUCA.
GeneTreeiENSGT00390000006311.
HOGENOMiHOG000089745.
HOVERGENiHBG000012.
InParanoidiQ6ZWR4.
KOiK04354.
OMAiPIPPRTF.
OrthoDBiEOG7Q5HCZ.
TreeFamiTF105553.

Miscellaneous databases

PROiQ6ZWR4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWR4.
GenevisibleiQ6ZWR4. MM.

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.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR11871. PTHR11871. 1 hit.
PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
PRINTSiPR00600. PP2APR55.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS01024. PR55_1. 1 hit.
PS01025. PR55_2. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Diversity, developmental regulation and distribution of murine PR55/B subunits of protein phosphatase 2A."
    Schmidt K., Kins S., Schild A., Nitsch R.M., Hemmings B.A., Goetz J.
    Eur. J. Neurosci. 16:2039-2048(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: CD-1 and Czech II.
    Tissue: Lung tumor and Testis.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Hippocampus, Medulla oblongata, Spinal cord and Sympathetic ganglion.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Strain: C57BL/6J and Czech II.
    Tissue: Brain and Mammary tumor.

Entry informationi

Entry namei2ABB_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWR4
Secondary accession number(s): Q3UF60
, Q8K413, Q9D3B7, Q9D6I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.