P2R3B_HUMAN
ID P2R3B_HUMAN Reviewed; 575 AA.
AC Q9Y5P8; Q6P4G9; Q7RTT1; Q96H01;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta;
DE AltName: Full=PP2A subunit B isoform PR48;
DE AltName: Full=Protein phosphatase 2A 48 kDa regulatory subunit;
GN Name=PPP2R3B; Synonyms=PPP2R3L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-519.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-475, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CDC6.
RC TISSUE=Placenta;
RX PubMed=10629059; DOI=10.1128/mcb.20.3.1021-1029.2000;
RA Yan Z., Fedorov S.A., Mumby M.C., Williams R.S.;
RT "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with
RT cdc6 and modulates DNA replication in human cells.";
RL Mol. Cell. Biol. 20:1021-1029(2000).
RN [4]
RP IDENTIFICATION OF MISSING N-TERMINAL SEQUENCE.
RX PubMed=12605688; DOI=10.1046/j.1432-1033.2003.03398.x;
RA Stevens I., Janssens V., Martens E., Dilworth S., Goris J., Van Hoof C.;
RT "Identification and characterization of B''-subunits of protein phosphatase
RT 2 A in Xenopus laevis oocytes and adult tissues.";
RL Eur. J. Biochem. 270:376-387(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP INTERACTION WITH NOD2.
RX PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT Interacting Proteins.";
RL PLoS ONE 11:E0165420-E0165420(2016).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include three families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules.
CC Interacts with N-terminal region of CDC6. Interacts with NOD2
CC (PubMed:27812135). {ECO:0000269|PubMed:10629059,
CC ECO:0000269|PubMed:27812135}.
CC -!- INTERACTION:
CC Q9Y5P8; Q9UNI6: DUSP12; NbExp=4; IntAct=EBI-2479826, EBI-715161;
CC Q9Y5P8; O14964: HGS; NbExp=3; IntAct=EBI-2479826, EBI-740220;
CC Q9Y5P8; P41227: NAA10; NbExp=3; IntAct=EBI-2479826, EBI-747693;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10629059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5P8-2; Sequence=VSP_037310;
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL954664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009032; AAH09032.1; -; mRNA.
DR EMBL; BC063429; AAH63429.1; -; mRNA.
DR EMBL; AF135016; AAD38515.1; ALT_INIT; mRNA.
DR EMBL; BK000521; DAA00385.1; -; mRNA.
DR CCDS; CCDS14104.1; -. [Q9Y5P8-1]
DR RefSeq; NP_037371.2; NM_013239.4. [Q9Y5P8-1]
DR PDB; 4I5L; X-ray; 2.43 A; B/E=122-490.
DR PDB; 4I5N; X-ray; 2.80 A; B/E=122-490.
DR PDB; 4MEW; X-ray; 1.99 A; A=130-483.
DR PDBsum; 4I5L; -.
DR PDBsum; 4I5N; -.
DR PDBsum; 4MEW; -.
DR AlphaFoldDB; Q9Y5P8; -.
DR SMR; Q9Y5P8; -.
DR BioGRID; 118179; 28.
DR CORUM; Q9Y5P8; -.
DR IntAct; Q9Y5P8; 22.
DR MINT; Q9Y5P8; -.
DR STRING; 9606.ENSP00000375080; -.
DR iPTMnet; Q9Y5P8; -.
DR PhosphoSitePlus; Q9Y5P8; -.
DR BioMuta; PPP2R3B; -.
DR DMDM; 158523346; -.
DR EPD; Q9Y5P8; -.
DR MassIVE; Q9Y5P8; -.
DR MaxQB; Q9Y5P8; -.
DR PaxDb; Q9Y5P8; -.
DR PeptideAtlas; Q9Y5P8; -.
DR PRIDE; Q9Y5P8; -.
DR ProteomicsDB; 86468; -. [Q9Y5P8-1]
DR ProteomicsDB; 86469; -. [Q9Y5P8-2]
DR Antibodypedia; 23305; 226 antibodies from 29 providers.
DR DNASU; 28227; -.
DR Ensembl; ENST00000390665.9; ENSP00000375080.3; ENSG00000167393.18. [Q9Y5P8-1]
DR GeneID; 28227; -.
DR KEGG; hsa:28227; -.
DR MANE-Select; ENST00000390665.9; ENSP00000375080.3; NM_013239.5; NP_037371.2.
DR UCSC; uc004cpg.4; human. [Q9Y5P8-1]
DR CTD; 28227; -.
DR DisGeNET; 28227; -.
DR GeneCards; PPP2R3B; -.
DR HGNC; HGNC:13417; PPP2R3B.
DR HPA; ENSG00000167393; Group enriched (heart muscle, skeletal muscle).
DR MIM; 300339; gene.
DR neXtProt; NX_Q9Y5P8; -.
DR OpenTargets; ENSG00000167393; -.
DR PharmGKB; PA134878872; -.
DR VEuPathDB; HostDB:ENSG00000167393; -.
DR eggNOG; KOG2562; Eukaryota.
DR GeneTree; ENSGT00940000154659; -.
DR HOGENOM; CLU_019589_2_0_1; -.
DR OMA; DYWINDN; -.
DR OrthoDB; 255081at2759; -.
DR PhylomeDB; Q9Y5P8; -.
DR TreeFam; TF105554; -.
DR PathwayCommons; Q9Y5P8; -.
DR Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR SignaLink; Q9Y5P8; -.
DR BioGRID-ORCS; 28227; 13 hits in 578 CRISPR screens.
DR ChiTaRS; PPP2R3B; human.
DR GeneWiki; PPP2R3B; -.
DR GenomeRNAi; 28227; -.
DR Pharos; Q9Y5P8; Tbio.
DR PRO; PR:Q9Y5P8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y5P8; protein.
DR Bgee; ENSG00000167393; Expressed in apex of heart and 95 other tissues.
DR ExpressionAtlas; Q9Y5P8; baseline and differential.
DR Genevisible; Q9Y5P8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:ProtInc.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR041534; EF-hand_13.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF17958; EF-hand_13; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..575
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit B'' subunit beta"
FT /id="PRO_0000071444"
FT DOMAIN 388..423
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 41..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037310"
FT VARIANT 163
FT /note="D -> E (in dbSNP:rs3813594)"
FT /id="VAR_035109"
FT VARIANT 519
FT /note="A -> V (in dbSNP:rs1133520)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055356"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4I5L"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4I5N"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4I5N"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:4I5L"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:4I5L"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4I5L"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:4MEW"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:4MEW"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:4I5N"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:4MEW"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4MEW"
SQ SEQUENCE 575 AA; 65061 MW; 9FDE046345C1F85F CRC64;
MPPGKVLQPV LKMKVDELFL YWLSEASTQR MLQDCLRRIK APGRDQPTPG DGEQPGAWPT
APLAAPRPSG LEPPGTPGPG PALPLGAASS PRNAPHVRGT RRSAGTRVVQ TRKEEPLPPA
TSQSIPTFYF PRGRPQDSVN VDAVISKIES TFARFPHERA TMDDMGLVAK ACGCPLYWKG
PLFYGAGGER TGSVSVHKFV AMWRKILQNC HDDAAKFVHL LMSPGCNYLV QEDFVPFLQD
VVNTHPGLSF LKEASEFHSR YITTVIQRIF YAVNRSWSGR ITCAELRRSS FLQNVALLEE
EADINQLTEF FSYEHFYVIY CKFWELDTDH DLLIDADDLA RHNDHALSTK MIDRIFSGAV
TRGRKVQKEG KISYADFVWF LISEEDKKTP TSIEYWFRCM DLDGDGALSM FELEYFYEEQ
CRRLDSMAIE ALPFQDCLCQ MLDLVKPRTE GKITLQDLKR CKLANVFFDT FFNIEKYLDH
EQKEQISLLR DGDSGGPELS DWEKYAAEEY DILVAEETAG EPWEDGFEAE LSPVEQKLSA
LRSPLAQRPF FEAPSPLGAV DLYEYACGDE DLEPL
