Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform

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Reviewed, UniProtKB/Swiss-Prot P62714 (PP2AB_HUMAN)

Last modified February 9, 2010. Version 67. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
      Short name=PP2A-beta
    EC=3.1.3.16

Gene names

Name:

PPP2CB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Ref.7
Catalytic activity	A phosphoprotein + H₂O = a protein + 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) (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. May indirectly interact with SGOL1, most probably through regulatory B56 subunits.
Subcellular location	Cytoplasm. Nucleus. Centromere. Cytoplasm › cytoskeleton › spindle pole. Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Ref.11
Post-translational modification	Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly. It varies during the cell cycle. Demethylated by PME1 (in vitro). Ref.9 Ref.10 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.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

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Ontologies

Keywords
Cellular component	Centromere Cytoplasm Cytoskeleton Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell protein phosphatase type 2A complex Ref.9 Traceable author statement. Source: UniProtKB spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP4C	P60510	1	EBI-1044367,EBI-1046072
STK24	Q5T5B3	1	EBI-1044367,EBI-1054809

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform

PRO_0000058845

Sites

Active site

118

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

117

Manganese By similarity

Metal binding

167

Manganese By similarity

Metal binding

241

Manganese By similarity

Amino acid modifications

Modified residue

307

Phosphotyrosine By similarity

Modified residue

309

Leucine methyl ester Ref.9

Experimental info

Sequence conflict

E → D in AAB38020. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P62714-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 51DA9EB0633FC191
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FASTA

309

35,575

        10         20         30         40         50         60 
MDDKAFTKEL 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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A beta catalytic subunit." Hemmings B.A., Wernet W., Mayer R., Maurer F., Hofsteenge J., Stone S.R. Nucleic Acids Res. 16:11366-11366(1988) [PubMed: 2849765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes." Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L. Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988) [PubMed: 2837763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-309. Tissue: Liver.
[5]	"Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes." Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A. Biochemistry 30:89-97(1991) [PubMed: 1846293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[7]	"Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A." Virshup D.M., Kauffman M.G., Kelly T.J. EMBO J. 8:3891-3898(1989) [PubMed: 2555176] [Abstract] Cited for: PROTEIN SEQUENCE OF 91-97; 111-114; 122-127; 137-144 AND 207-238, FUNCTION.
[8]	"Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A." Pallas D.C., Shahrik L.K., Martin B.L., Jaspers S., Miller T.B. Jr., Brautigan D.L., Roberts T.M. Cell 60:167-176(1990) [PubMed: 2153055] [Abstract] Cited for: PROTEIN SEQUENCE OF 75-89; 215-234; 270-294 AND 303-309, INTERACTION WITH VIRAL PROTEINS.
[9]	"The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo." Favre B., Zolnierowicz S., Turowski P., Hemmings B.A. J. Biol. Chem. 269:16311-16317(1994) [PubMed: 8206937] [Abstract] Cited for: METHYLATION AT LEU-309.
[10]	"A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A." Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C. J. Biol. Chem. 274:14382-14391(1999) [PubMed: 10318862] [Abstract] Cited for: INTERACTION WITH PME1, DEMETHYLATION.
[11]	"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: 16541025] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X12656 mRNA. Translation: CAA31183.1. CR541747 mRNA. Translation: CAG46547.1. J03805 mRNA. Translation: AAB38020.1. CH471080 Genomic DNA. Translation: EAW63434.1. BC012022 mRNA. Translation: AAH12022.1. M60484 Genomic DNA. Translation: AAA36467.1.
IPI	IPI00429689.
PIR	PAHU2B. B37135.
RefSeq	NP_001009552.1. NP_004147.1.
UniGene	Hs.491440
3D structure databases
SMR	P62714. Positions 2-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62714. 53 interactions.
STRING	P62714.
PTM databases
PhosphoSite	P62714.
2-D gel databases
OGP	P62714.
REPRODUCTION-2DPAGE	IPI00429689.
Proteomic databases
PRIDE	P62714.
Genome annotation databases
Ensembl	ENST00000221138; ENSP00000221138; ENSG00000104695; Homo sapiens. [Genome view] ENST00000397308; ENSP00000380475; ENSG00000104695; Homo sapiens. [Genome view] ENST00000406655; ENSP00000384493; ENSG00000104695; Homo sapiens. [Genome view]
GeneID	5516.
KEGG	hsa:5516.
UCSC	uc003xik.1. human.
Organism-specific databases
CTD	5516.
GeneCards	GC08M030762.
H-InvDB	HIX0007439.
HGNC	HGNC:9300. PPP2CB.
HPA	CAB018600.
MIM	176916. gene.
PharmGKB	PA33664.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16980.
HOGENOM	HBG716770.
HOVERGEN	P62714.
InParanoid	P62714.
OMA	TENQVRT.
PhylomeDB	P62714.
Enzyme and pathway databases
BRENDA	3.1.3.16. 247.
Pathway_Interaction_DB	tgfbrpathway. TGF-beta receptor signaling.
Reactome	REACT_11045. Signaling by Wnt. REACT_11061. Signalling by NGF. REACT_1505. Integration of energy metabolism. REACT_152. Cell Cycle, Mitotic. REACT_15295. Opioid Signalling. REACT_6900. Signaling in Immune system.
Gene expression databases
ArrayExpress	P62714.
Bgee	P62714.
CleanEx	HS_PPP2CB.
Genevestigator	P62714.
GermOnline	ENSG00000104695. Homo sapiens.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
PANTHER	PTHR11668. T_phtase_apaH. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00163. Vitamin E.
NextBio	21334.
SOURCE	Search...

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Entry information

Entry name

PP2AB_HUMAN

Accession

Primary (citable) accession number: P62714
Secondary accession number(s): P11082, Q6FHK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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Relevant documents

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents