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P11611 (PP2AB_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform

Short name=PP2A-beta
EC=3.1.3.16
Gene names
Name:PPP2CB
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

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. Binds PPME1 By similarity. May indirectly interact with SGOL1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD By similarity. Interacts with CTTNBP2NL By similarity.

Subcellular location

Cytoplasm. Nucleus By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles By similarity.

Post-translational modification

Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly. Demethylated by PME1 (in vitro) By similarity.

Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation By similarity.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
PRO_0000058848

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Amino acid modifications

Modified residue3071Phosphotyrosine Ref.2
Modified residue3091Leucine methyl ester By similarity

Sequences

Sequence LengthMass (Da)Tools
P11611 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: BE76EEB6B0EAC19E

FASTA30935,605
        10         20         30         40         50         60 
MDDKTFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI 

       190        200        210        220        230        240 
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA 

       250        260        270        280        290        300 
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 


TRRTPDYFL 

« Hide

References

[1]"A second catalytic subunit of type-2A protein phosphatase from rabbit skeletal muscle."
da Cruz e Silva O.B., Cohen P.T.W.
FEBS Lett. 226:176-178(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Skeletal muscle.
[2]"Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation."
Chen J., Martin B.L., Brautigan D.L.
Science 257:1261-1264(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00763 mRNA. Translation: CAA68732.1.
PIRPARB2B. S00220.
RefSeqNP_001095177.1. NM_001101707.1.
UniGeneOcu.2088.

3D structure databases

ProteinModelPortalP11611.
SMRP11611. Positions 2-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000004530.

Proteomic databases

PRIDEP11611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000005228; ENSOCUP00000004530; ENSOCUG00000005230.
GeneID100009300.

Organism-specific databases

CTD5516.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
HOGENOMHOG000172696.
HOVERGENHBG000216.
OMAVENDIFC.
OrthoDBEOG74N5H2.
TreeFamTF105559.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP2AB_RABIT
AccessionPrimary (citable) accession number: P11611
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families