PWP2B_MOUSE
ID PWP2B_MOUSE Reviewed; 600 AA.
AC E9Q9M8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=PWWP domain-containing protein 2B;
GN Name=Pwwp2b; Synonyms=Pwwp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION.
RX PubMed=30228260; DOI=10.1038/s41467-018-06235-9;
RA Zhang T., Wei G., Millard C.J., Fischer R., Konietzny R., Kessler B.M.,
RA Schwabe J.W.R., Brockdorff N.;
RT "A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate
RT transcription at active genes.";
RL Nat. Commun. 9:3798-3798(2018).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH MTA1; MTA2; MTA3; HDAC1; HDAC2; RBBP4; RBBP7; BRCC3 AND ZNF516, AND
RP DEUBIQUITINATION.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
CC -!- FUNCTION: Chromatin-binding protein that acts as an adapter between
CC distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-
CC modifying complexes, contributing to the regulation of the levels of
CC histone acetylation at actively transcribed genes (PubMed:30228260).
CC Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD
CC subcomplex, preventing the formation of full NuRD complex (containing
CC CHD4 and MBD3), leading to recruitment of HDACs to gene promoters
CC resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (By
CC similarity). Plays a role in facilitating transcriptional elongation
CC through regulation of histone acetylation (PubMed:30228260). Negatively
CC regulates brown adipocyte thermogenesis by interacting with and
CC stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone
CC deacetylation at the promoter leading to the repression of UCP1
CC expression (PubMed:34180153). {ECO:0000250|UniProtKB:Q6NUJ5,
CC ECO:0000269|PubMed:30228260, ECO:0000269|PubMed:34180153}.
CC -!- SUBUNIT: Component of a MTA1-specific subcomplex of the NuRD complex
CC composed of PWWP2B, MTA1 and HDAC1 but does not contain CHD4 and MBD3
CC (By similarity). Interacts with MTA1, MTA2, MTA3, HDAC1, HDAC2, RBBP4,
CC RBBP7, BRCC3 and ZNF516 (PubMed:34180153). Does not interact with CHD4
CC and MBD3 (By similarity). {ECO:0000250|UniProtKB:Q6NUJ5,
CC ECO:0000269|PubMed:34180153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34180153}.
CC -!- TISSUE SPECIFICITY: Expressed in the brown adipose tissue.
CC {ECO:0000269|PubMed:34180153}.
CC -!- INDUCTION: Induced in response to cold. {ECO:0000269|PubMed:34180153}.
CC -!- PTM: Deubiquitinated by BRCC3; leading to its stabilization.
CC {ECO:0000269|PubMed:34180153}.
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DR EMBL; AC093363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52427.1; -.
DR RefSeq; NP_001092106.1; NM_001098636.1.
DR AlphaFoldDB; E9Q9M8; -.
DR SMR; E9Q9M8; -.
DR STRING; 10090.ENSMUSP00000130888; -.
DR iPTMnet; E9Q9M8; -.
DR PhosphoSitePlus; E9Q9M8; -.
DR MaxQB; E9Q9M8; -.
DR PaxDb; E9Q9M8; -.
DR PRIDE; E9Q9M8; -.
DR ProteomicsDB; 328310; -.
DR Antibodypedia; 46422; 83 antibodies from 22 providers.
DR Ensembl; ENSMUST00000172136; ENSMUSP00000130888; ENSMUSG00000060260.
DR GeneID; 101631; -.
DR UCSC; uc009kfo.1; mouse.
DR CTD; 170394; -.
DR MGI; MGI:2142008; Pwwp2b.
DR VEuPathDB; HostDB:ENSMUSG00000060260; -.
DR eggNOG; ENOG502QQ5Q; Eukaryota.
DR GeneTree; ENSGT00940000160735; -.
DR HOGENOM; CLU_020678_0_0_1; -.
DR InParanoid; E9Q9M8; -.
DR OMA; TSPEMCD; -.
DR OrthoDB; 326248at2759; -.
DR PhylomeDB; E9Q9M8; -.
DR TreeFam; TF331271; -.
DR BioGRID-ORCS; 101631; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pwwp2b; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9Q9M8; protein.
DR Bgee; ENSMUSG00000060260; Expressed in testis and 60 other tissues.
DR ExpressionAtlas; E9Q9M8; baseline and differential.
DR Genevisible; E9Q9M8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0120325; F:NuRD complex binding; ISS:UniProtKB.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:1901675; P:negative regulation of histone H3-K27 acetylation; IMP:UniProtKB.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0120161; P:regulation of cold-induced thermogenesis; IMP:UniProtKB.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..600
FT /note="PWWP domain-containing protein 2B"
FT /id="PRO_0000454860"
FT DOMAIN 500..560
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 81..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUJ5"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUJ5"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUJ5"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NUJ5"
SQ SEQUENCE 600 AA; 65434 MW; C225DF8DAD894D30 CRC64;
MEPRAGCRLP VRVEQVVNGA LVVTVSCGER SFAGILLDCT KKSGLFGLSP STLLPLADNS
SAVSCHGQAP EEGTGEVMQL ETGPLHPHHK DPEKDQPPKT AVSEPPPPLI PPVPAGNLPP
FPPYFEGAPF PHPLWLRNTY QQWVPQPPPR TIKRTRRRLS RNRDPGRLIL STIRLRPRQV
LCEKCKSTVS PQEASPSPLN TPKPRRRLGS GPDSEHRKPE EPEDSAVIAT AAPRRSKREK
REEDRVAGER VPRSPVIKIS YSTPQGKGEV VKIPSRVHGS VEPFCPQQSL QNGSQDSEVS
RDVEPRGGGD RPPSGSSASI PKLKLTRPVP PISDLPPPKI RLKPHRLGDG EHEPLYRAEL
VEELNGCPRG PLVSSPALFA DGSSHGLEDL SSGSSGEDDD LKRFPQGKHG RDGLAFLVDC
PGRRTDCTSE SVCSTDSLDE LKSSGSEVTS PDTGDLSSGD SASVPSSSAD TRQTVPPLTV
RLHTQSVSRC VTEDGRTVAV GDIVWGKIHG FPWWPARVLD ISLGQKEDGE PSWQEAKVSW
FGSPTTSFLS ISKLSPFSEF FKLRFNRKKK GMYRKAITEA ANATQHVAPE IRELLTQFEM
