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Q9Y5P8

- P2R3B_HUMAN

UniProt

Q9Y5P8 - P2R3B_HUMAN

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Protein
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
Gene
PPP2R3B, PPP2R3L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi401 – 41212 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphoprotein phosphatase activity Source: Reactome
  3. protein binding Source: UniProtKB
  4. protein phosphatase type 2A regulator activity Source: ProtInc
  5. protein serine/threonine phosphatase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: Reactome
  2. cell cycle arrest Source: ProtInc
  3. mitotic cell cycle Source: Reactome
  4. protein dephosphorylation Source: UniProtKB
  5. regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_821. Cyclin D associated events in G1.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PPP2R3B
Synonyms:PPP2R3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:13417. PPP2R3B.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: ProtInc
  3. protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134878872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
PRO_0000071444Add
BLAST

Proteomic databases

MaxQBiQ9Y5P8.
PaxDbiQ9Y5P8.
PRIDEiQ9Y5P8.

PTM databases

PhosphoSiteiQ9Y5P8.

Expressioni

Gene expression databases

ArrayExpressiQ9Y5P8.
BgeeiQ9Y5P8.
CleanExiHS_PPP2R3B.
GenevestigatoriQ9Y5P8.

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. Interacts with N-terminal region of CDC6.1 Publication

Protein-protein interaction databases

BioGridi118179. 6 interactions.
IntActiQ9Y5P8. 6 interactions.
STRINGi9606.ENSP00000375080.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni122 – 1243
Helixi141 – 15212
Helixi156 – 1583
Beta strandi159 – 1613
Helixi162 – 1643
Helixi165 – 1717
Helixi176 – 1783
Helixi179 – 1857
Turni186 – 1927
Helixi196 – 20914
Helixi213 – 2219
Turni224 – 2263
Helixi231 – 2344
Helixi235 – 24410
Helixi246 – 2516
Beta strandi253 – 2553
Helixi256 – 27318
Helixi283 – 2886
Helixi291 – 2977
Turni298 – 3003
Helixi304 – 3063
Turni308 – 3114
Helixi313 – 32412
Beta strandi331 – 3355
Helixi336 – 34510
Helixi349 – 3557
Turni356 – 3583
Beta strandi359 – 3646
Helixi365 – 3695
Beta strandi371 – 3733
Helixi374 – 38512
Helixi390 – 40011
Beta strandi405 – 4084
Helixi410 – 42516
Turni426 – 4283
Helixi434 – 44512
Beta strandi448 – 4514
Helixi455 – 4617
Helixi464 – 4729
Helixi474 – 4774

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I5LX-ray2.43B/E122-490[»]
4I5NX-ray2.80B/E122-490[»]
ProteinModelPortaliQ9Y5P8.
SMRiQ9Y5P8. Positions 121-478.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini388 – 42336EF-hand
Add
BLAST

Sequence similaritiesi

Contains 1 EF-hand domain.

Phylogenomic databases

eggNOGiNOG271066.
HOGENOMiHOG000265086.
HOVERGENiHBG000010.
InParanoidiQ9Y5P8.
KOiK11583.
OMAiEMPSHLA.
OrthoDBiEOG7XWPN3.
PhylomeDBiQ9Y5P8.
TreeFamiTF105554.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5P8-1) [UniParc]FASTAAdd to Basket

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

MPPGKVLQPV LKMKVDELFL YWLSEASTQR MLQDCLRRIK APGRDQPTPG    50
DGEQPGAWPT APLAAPRPSG LEPPGTPGPG PALPLGAASS PRNAPHVRGT 100
RRSAGTRVVQ TRKEEPLPPA TSQSIPTFYF PRGRPQDSVN VDAVISKIES 150
TFARFPHERA TMDDMGLVAK ACGCPLYWKG PLFYGAGGER TGSVSVHKFV 200
AMWRKILQNC HDDAAKFVHL LMSPGCNYLV QEDFVPFLQD VVNTHPGLSF 250
LKEASEFHSR YITTVIQRIF YAVNRSWSGR ITCAELRRSS FLQNVALLEE 300
EADINQLTEF FSYEHFYVIY CKFWELDTDH DLLIDADDLA RHNDHALSTK 350
MIDRIFSGAV TRGRKVQKEG KISYADFVWF LISEEDKKTP TSIEYWFRCM 400
DLDGDGALSM FELEYFYEEQ CRRLDSMAIE ALPFQDCLCQ MLDLVKPRTE 450
GKITLQDLKR CKLANVFFDT FFNIEKYLDH EQKEQISLLR DGDSGGPELS 500
DWEKYAAEEY DILVAEETAG EPWEDGFEAE LSPVEQKLSA LRSPLAQRPF 550
FEAPSPLGAV DLYEYACGDE DLEPL 575
Length:575
Mass (Da):65,061
Last modified:September 11, 2007 - v2
Checksum:i9FDE046345C1F85F
GO
Isoform 2 (identifier: Q9Y5P8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:176
Mass (Da):20,111
Checksum:i6B819D28EBF3AE5F
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631D → E.
Corresponds to variant rs3813594 [ dbSNP | Ensembl ].
VAR_035109
Natural varianti519 – 5191A → V.1 Publication
Corresponds to variant rs1133520 [ dbSNP | Ensembl ].
VAR_055356

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 399399Missing in isoform 2.
VSP_037310Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14104.1. [Q9Y5P8-1]
RefSeqiNP_037371.2. NM_013239.4. [Q9Y5P8-1]
XP_005274485.1. XM_005274428.2.
XP_005274834.1. XM_005274777.2.
XP_006724505.1. XM_006724442.1.
XP_006724926.1. XM_006724863.1.
XP_006725712.1. XM_006725649.1.
UniGeneiHs.124942.

Genome annotation databases

EnsembliENST00000390665; ENSP00000375080; ENSG00000167393. [Q9Y5P8-1]
GeneIDi102725016.
28227.
KEGGihsa:102725016.
hsa:28227.
UCSCiuc004cpf.3. human. [Q9Y5P8-2]
uc004cpg.3. human. [Q9Y5P8-1]

Polymorphism databases

DMDMi158523346.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14104.1. [Q9Y5P8-1 ]
RefSeqi NP_037371.2. NM_013239.4. [Q9Y5P8-1 ]
XP_005274485.1. XM_005274428.2.
XP_005274834.1. XM_005274777.2.
XP_006724505.1. XM_006724442.1.
XP_006724926.1. XM_006724863.1.
XP_006725712.1. XM_006725649.1.
UniGenei Hs.124942.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4I5L X-ray 2.43 B/E 122-490 [» ]
4I5N X-ray 2.80 B/E 122-490 [» ]
ProteinModelPortali Q9Y5P8.
SMRi Q9Y5P8. Positions 121-478.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118179. 6 interactions.
IntActi Q9Y5P8. 6 interactions.
STRINGi 9606.ENSP00000375080.

PTM databases

PhosphoSitei Q9Y5P8.

Polymorphism databases

DMDMi 158523346.

Proteomic databases

MaxQBi Q9Y5P8.
PaxDbi Q9Y5P8.
PRIDEi Q9Y5P8.

Protocols and materials databases

DNASUi 28227.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000390665 ; ENSP00000375080 ; ENSG00000167393 . [Q9Y5P8-1 ]
GeneIDi 102725016.
28227.
KEGGi hsa:102725016.
hsa:28227.
UCSCi uc004cpf.3. human. [Q9Y5P8-2 ]
uc004cpg.3. human. [Q9Y5P8-1 ]

Organism-specific databases

CTDi 28227.
GeneCardsi GC0XM000264.
H-InvDB HIX0038850.
HIX0176522.
HIX0177602.
HGNCi HGNC:13417. PPP2R3B.
MIMi 300339. gene.
neXtProti NX_Q9Y5P8.
PharmGKBi PA134878872.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271066.
HOGENOMi HOG000265086.
HOVERGENi HBG000010.
InParanoidi Q9Y5P8.
KOi K11583.
OMAi EMPSHLA.
OrthoDBi EOG7XWPN3.
PhylomeDBi Q9Y5P8.
TreeFami TF105554.

Enzyme and pathway databases

Reactomei REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_821. Cyclin D associated events in G1.

Miscellaneous databases

GeneWikii PPP2R3B.
GenomeRNAii 28227.
NextBioi 50538.
PROi Q9Y5P8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5P8.
Bgeei Q9Y5P8.
CleanExi HS_PPP2R3B.
Genevestigatori Q9Y5P8.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 1 hit.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiP2R3B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5P8
Secondary accession number(s): Q6P4G9, Q7RTT1, Q96H01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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