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Q9Y5P8 (P2R3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
Alternative name(s):
PP2A subunit B isoform PR48
Protein phosphatase 2A 48 kDa regulatory subunit
Gene names
Name:PPP2R3B
Synonyms:PPP2R3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
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

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 N-terminal region of CDC6. Ref.3

Subcellular location

Nucleus Ref.3.

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

Sequence similarities

Contains 1 EF-hand domain.

Sequence caution

The sequence AAD38515.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5P8-1)

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: Q9Y5P8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-399: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
PRO_0000071444

Regions

Domain388 – 42336EF-hand
Calcium binding401 – 41212 Potential

Natural variations

Alternative sequence1 – 399399Missing in isoform 2.
VSP_037310
Natural variant1631D → E.
Corresponds to variant rs3813594 [ dbSNP | Ensembl ].
VAR_035109
Natural variant5191A → V. Ref.2
Corresponds to variant rs1133520 [ dbSNP | Ensembl ].
VAR_055356

Secondary structure

................................................................... 575
Helix Strand Turn

Details...

Sequences

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

Last modified September 11, 2007. Version 2.
Checksum: 9FDE046345C1F85F

FASTA57565,061
        10         20         30         40         50         60 
MPPGKVLQPV LKMKVDELFL YWLSEASTQR MLQDCLRRIK APGRDQPTPG DGEQPGAWPT 

        70         80         90        100        110        120 
APLAAPRPSG LEPPGTPGPG PALPLGAASS PRNAPHVRGT RRSAGTRVVQ TRKEEPLPPA 

       130        140        150        160        170        180 
TSQSIPTFYF PRGRPQDSVN VDAVISKIES TFARFPHERA TMDDMGLVAK ACGCPLYWKG 

       190        200        210        220        230        240 
PLFYGAGGER TGSVSVHKFV AMWRKILQNC HDDAAKFVHL LMSPGCNYLV QEDFVPFLQD 

       250        260        270        280        290        300 
VVNTHPGLSF LKEASEFHSR YITTVIQRIF YAVNRSWSGR ITCAELRRSS FLQNVALLEE 

       310        320        330        340        350        360 
EADINQLTEF FSYEHFYVIY CKFWELDTDH DLLIDADDLA RHNDHALSTK MIDRIFSGAV 

       370        380        390        400        410        420 
TRGRKVQKEG KISYADFVWF LISEEDKKTP TSIEYWFRCM DLDGDGALSM FELEYFYEEQ 

       430        440        450        460        470        480 
CRRLDSMAIE ALPFQDCLCQ MLDLVKPRTE GKITLQDLKR CKLANVFFDT FFNIEKYLDH 

       490        500        510        520        530        540 
EQKEQISLLR DGDSGGPELS DWEKYAAEEY DILVAEETAG EPWEDGFEAE LSPVEQKLSA 

       550        560        570 
LRSPLAQRPF FEAPSPLGAV DLYEYACGDE DLEPL 

« Hide

Isoform 2 [UniParc].

Checksum: 6B819D28EBF3AE5F
Show »

FASTA17620,111

References

« Hide 'large scale' references
[1]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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), VARIANT VAL-519.
Tissue: Brain.
[3]"PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with cdc6 and modulates DNA replication in human cells."
Yan Z., Fedorov S.A., Mumby M.C., Williams R.S.
Mol. Cell. Biol. 20:1021-1029(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-475, SUBCELLULAR LOCATION, INTERACTION WITH CDC6.
Tissue: Placenta.
[4]"Identification and characterization of B''-subunits of protein phosphatase 2 A in Xenopus laevis oocytes and adult tissues."
Stevens I., Janssens V., Martens E., Dilworth S., Goris J., Van Hoof C.
Eur. J. Biochem. 270:376-387(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF MISSING N-TERMINAL SEQUENCE.
[5]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954664 Genomic DNA. No translation available.
BX000476 Genomic DNA. No translation available.
BC009032 mRNA. Translation: AAH09032.1.
BC063429 mRNA. Translation: AAH63429.1.
AF135016 mRNA. Translation: AAD38515.1. Different initiation.
BK000521 mRNA. Translation: DAA00385.1.
RefSeqNP_037371.2. NM_013239.4.
XP_005274485.1. XM_005274428.2.
XP_005274834.1. XM_005274777.2.
UniGeneHs.124942.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I5LX-ray2.43B/E122-490[»]
4I5NX-ray2.80B/E122-490[»]
ProteinModelPortalQ9Y5P8.
SMRQ9Y5P8. Positions 121-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118179. 6 interactions.
IntActQ9Y5P8. 6 interactions.
STRING9606.ENSP00000375080.

PTM databases

PhosphoSiteQ9Y5P8.

Polymorphism databases

DMDM158523346.

Proteomic databases

PaxDbQ9Y5P8.
PRIDEQ9Y5P8.

Protocols and materials databases

DNASU28227.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000390665; ENSP00000375080; ENSG00000167393. [Q9Y5P8-1]
GeneID28227.
KEGGhsa:28227.
UCSCuc004cpf.3. human. [Q9Y5P8-2]
uc004cpg.3. human. [Q9Y5P8-1]

Organism-specific databases

CTD28227.
GeneCardsGC0XM000264.
H-InvDBHIX0038850.
HIX0176522.
HIX0177602.
HGNCHGNC:13417. PPP2R3B.
MIM300339. gene.
neXtProtNX_Q9Y5P8.
PharmGKBPA134878872.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271066.
HOGENOMHOG000265086.
HOVERGENHBG000010.
InParanoidQ9Y5P8.
KOK11583.
OMAASATQIQ.
OrthoDBEOG7XWPN3.
PhylomeDBQ9Y5P8.
TreeFamTF105554.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ9Y5P8.
BgeeQ9Y5P8.
CleanExHS_PPP2R3B.
GenevestigatorQ9Y5P8.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPPP2R3B.
GenomeRNAi28227.
NextBio50538.
PROQ9Y5P8.
SOURCESearch...

Entry information

Entry nameP2R3B_HUMAN
AccessionPrimary (citable) accession number: Q9Y5P8
Secondary accession number(s): Q6P4G9, Q7RTT1, Q96H01
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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