PWP2A_HUMAN
ID PWP2A_HUMAN Reviewed; 755 AA.
AC Q96N64; G5EA07; Q2HJJ2; Q8IYR3; Q96PV3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=PWWP domain-containing protein 2A;
GN Name=PWWP2A; Synonyms=KIAA1935, MST101;
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 MRNA] OF 1-435.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 241-755.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-116 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-208, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH H2AZ1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28645917; DOI=10.15252/embj.201695757;
RA Puenzeler S., Link S., Wagner G., Keilhauer E.C., Kronbeck N.,
RA Spitzer R.M., Leidescher S., Markaki Y., Mentele E., Regnard C.,
RA Schneider K., Takahashi D., Kusakabe M., Vardabasso C., Zink L.M.,
RA Straub T., Bernstein E., Harata M., Leonhardt H., Mann M., Rupp R.A.,
RA Hake S.B.;
RT "Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest
RT differentiation.";
RL EMBO J. 36:2263-2279(2017).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-208, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP FUNCTION, INTERACTION WITH MTA1 AND HDAC1 (ISOFORMS 1 AND 3), INTERACTION
RP WITH H3K36ME3, ABSENCE OF INTERACTION WITH CHD4 AND MBD3, AND
RP IDENTIFICATION IN A MTA1-SPECIFIC SUBCOMPLEX OF THE NURD COMPLEX.
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 [17]
RP FUNCTION, INTERACTION WITH MTA1; H2AZ1 AND H3K36ME3, ABSENCE OF INTERACTION
RP WITH MBD3, IDENTIFICATION IN A MTA1-SPECIFIC SUBCOMPLEX OF THE NURD
RP COMPLEX, AND MUTAGENESIS OF PHE-666; TRP-669 AND TRP-695.
RX PubMed=30327463; DOI=10.1038/s41467-018-06665-5;
RA Link S., Spitzer R.M.M., Sana M., Torrado M., Voelker-Albert M.C.,
RA Keilhauer E.C., Burgold T., Puenzeler S., Low J.K.K., Lindstroem I.,
RA Nist A., Regnard C., Stiewe T., Hendrich B., Imhof A., Mann M.,
RA Mackay J.P., Bartkuhn M., Hake S.B.;
RT "PWWP2A binds distinct chromatin moieties and interacts with an MTA1-
RT specific core NuRD complex.";
RL Nat. Commun. 9:4300-4300(2018).
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 PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1
CC to form a NuRD subcomplex, preventing the formation of full NuRD
CC complex (containing CHD4 and MBD3), leading to recruitment of HDACs to
CC gene promoters resulting in turn in the deacetylation of nearby H3K27
CC and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in
CC facilitating transcriptional elongation and repression of spurious
CC transcription initiation through regulation of histone acetylation (By
CC similarity). Essential for proper mitosis progression
CC (PubMed:28645917). {ECO:0000250|UniProtKB:Q69Z61,
CC ECO:0000269|PubMed:28645917, ECO:0000269|PubMed:30228260,
CC ECO:0000269|PubMed:30327463}.
CC -!- SUBUNIT: Component of a MTA1-specific subcomplex of the NuRD complex
CC (M1HR), composed of PWWP2A, MTA1/2, HDAC1/2, and RBBP4/7 but does not
CC contain CHD4 and MBD3 (PubMed:30228260, PubMed:30327463). Interacts
CC with MTA1; the interaction mediates the association of PWWP2A with the
CC M1HR complex (PubMed:30228260, PubMed:30327463). Interacts with
CC H2A.Z/H2AZ1 (PubMed:28645917, PubMed:30327463). Interacts (via PWWP
CC domain) with histone H3 trimethylated at 'Lys-36' (H3K36me3)
CC (PubMed:30228260, PubMed:30327463). Does not interact with CHD4 and
CC MBD3 (PubMed:30228260, PubMed:30327463). {ECO:0000269|PubMed:28645917,
CC ECO:0000269|PubMed:30228260, ECO:0000269|PubMed:30327463}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with MTA1 and with HDAC1 in a MTA1-
CC dependent manner (PubMed:30228260). Does not interact with CHD4 and
CC MBD3 (PubMed:30228260). {ECO:0000269|PubMed:30228260}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with MTA1 and with HDAC1 in a MTA1-
CC dependent manner (PubMed:30228260). Does not interact with CHD4 and
CC MBD3 (PubMed:30228260). {ECO:0000269|PubMed:30228260}.
CC -!- INTERACTION:
CC Q96N64; Q13547: HDAC1; NbExp=5; IntAct=EBI-6597774, EBI-301834;
CC Q96N64-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-18924849, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28645917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96N64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N64-2; Sequence=VSP_029547, VSP_029548;
CC Name=3;
CC IsoId=Q96N64-3; Sequence=VSP_054064, VSP_054065;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35076.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB67828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB067522; BAB67828.1; ALT_INIT; mRNA.
DR EMBL; AK055921; BAB71045.1; ALT_INIT; mRNA.
DR EMBL; AC008706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61567.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61568.1; -; Genomic_DNA.
DR EMBL; BC035076; AAH35076.2; ALT_INIT; mRNA.
DR EMBL; BC105110; AAI05111.1; -; mRNA.
DR CCDS; CCDS47331.1; -. [Q96N64-2]
DR CCDS; CCDS47332.1; -. [Q96N64-1]
DR CCDS; CCDS58990.1; -. [Q96N64-3]
DR RefSeq; NP_001124336.1; NM_001130864.1. [Q96N64-1]
DR RefSeq; NP_001253964.1; NM_001267035.1. [Q96N64-3]
DR RefSeq; NP_443159.1; NM_052927.2. [Q96N64-2]
DR AlphaFoldDB; Q96N64; -.
DR SMR; Q96N64; -.
DR BioGRID; 125375; 66.
DR IntAct; Q96N64; 18.
DR MINT; Q96N64; -.
DR STRING; 9606.ENSP00000305151; -.
DR iPTMnet; Q96N64; -.
DR MetOSite; Q96N64; -.
DR PhosphoSitePlus; Q96N64; -.
DR BioMuta; PWWP2A; -.
DR DMDM; 160419226; -.
DR EPD; Q96N64; -.
DR jPOST; Q96N64; -.
DR MassIVE; Q96N64; -.
DR MaxQB; Q96N64; -.
DR PaxDb; Q96N64; -.
DR PeptideAtlas; Q96N64; -.
DR PRIDE; Q96N64; -.
DR ProteomicsDB; 34103; -.
DR ProteomicsDB; 77468; -. [Q96N64-1]
DR ProteomicsDB; 77469; -. [Q96N64-2]
DR Antibodypedia; 28516; 34 antibodies from 15 providers.
DR DNASU; 114825; -.
DR Ensembl; ENST00000307063.9; ENSP00000305151.7; ENSG00000170234.13. [Q96N64-1]
DR Ensembl; ENST00000456329.7; ENSP00000390462.2; ENSG00000170234.13. [Q96N64-2]
DR Ensembl; ENST00000523662.1; ENSP00000428143.1; ENSG00000170234.13. [Q96N64-3]
DR GeneID; 114825; -.
DR KEGG; hsa:114825; -.
DR MANE-Select; ENST00000307063.9; ENSP00000305151.7; NM_001130864.2; NP_001124336.1.
DR UCSC; uc003lxv.5; human. [Q96N64-1]
DR CTD; 114825; -.
DR DisGeNET; 114825; -.
DR GeneCards; PWWP2A; -.
DR HGNC; HGNC:29406; PWWP2A.
DR HPA; ENSG00000170234; Low tissue specificity.
DR MIM; 617823; gene.
DR neXtProt; NX_Q96N64; -.
DR OpenTargets; ENSG00000170234; -.
DR PharmGKB; PA162400500; -.
DR VEuPathDB; HostDB:ENSG00000170234; -.
DR eggNOG; ENOG502QU6V; Eukaryota.
DR GeneTree; ENSGT00940000157692; -.
DR HOGENOM; CLU_035885_0_0_1; -.
DR InParanoid; Q96N64; -.
DR OMA; PPCWSPK; -.
DR OrthoDB; 326248at2759; -.
DR PhylomeDB; Q96N64; -.
DR TreeFam; TF331271; -.
DR PathwayCommons; Q96N64; -.
DR SignaLink; Q96N64; -.
DR BioGRID-ORCS; 114825; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; PWWP2A; human.
DR GenomeRNAi; 114825; -.
DR Pharos; Q96N64; Tdark.
DR PRO; PR:Q96N64; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96N64; protein.
DR Bgee; ENSG00000170234; Expressed in ileal mucosa and 182 other tissues.
DR ExpressionAtlas; Q96N64; baseline and differential.
DR Genevisible; Q96N64; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0120325; F:NuRD complex binding; IDA: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; ISS:UniProtKB.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; ISS: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 Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..755
FT /note="PWWP domain-containing protein 2A"
FT /id="PRO_0000311363"
FT DOMAIN 655..715
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..373
FT /note="Interaction with HDAC1 and MTA1"
FT /evidence="ECO:0000269|PubMed:30228260"
FT REGION 282..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..574
FT /note="Interaction with the H2A.Z/H2AZ1"
FT /evidence="ECO:0000269|PubMed:28645917"
FT REGION 578..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 517..520
FT /note="GEAP -> AQRH (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054064"
FT VAR_SEQ 518..560
FT /note="EAPSENQSPSKGPEEASSEVQDTNEVHVPGDQDEPQTLGKKGS -> LNKWQ
FT LLHQTVTSPAAPLQCLTDHCGFRLGALKLTVKRAAQRH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029547"
FT VAR_SEQ 521..755
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054065"
FT VAR_SEQ 561..755
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029548"
FT MUTAGEN 666
FT /note="F->A: No effect on interaction with H3K36me3."
FT /evidence="ECO:0000269|PubMed:30327463"
FT MUTAGEN 669
FT /note="W->A: Loss of interaction with H3K36me3."
FT /evidence="ECO:0000269|PubMed:30327463"
FT MUTAGEN 695
FT /note="W->A: Loss of interaction with H3K36me3."
FT /evidence="ECO:0000269|PubMed:30327463"
FT CONFLICT 154
FT /note="S -> L (in Ref. 5; AAH35076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 81960 MW; 6BF89E9C8D68EAA0 CRC64;
MAAVAAEAAA TAASPGEGGA GEAEPEMEPI PGSEAGTDPL PVTATEASVP DGETDGQQSA
PQADEPPLPP PPPPPGELAR SPEAVGPELE AEEKLSVRVA ESAAAAPQGG PELPPSPASP
PEQPPAPEER EEPPLPQPVA PALVPPAGGD STVSQLIPGS EVRVTLDHII EDALVVSFRF
GEKLFSGVLM DLSKRFGPHG IPVTVFPKRE YKDKPEAMPL QSNTFQEGTE VKCEANGAVP
DDPSPVPHPE LSLAESLWTS KPPPLFHEGA PYPPPLFIRD TYNQSIPQPP PRKIKRPKRK
MYREEPTSIM NAIKLRPRQV LCDKCKNSVV AEKKEIRKGS SATDSSKYED KKRRNESVTT
VNKKLKTDHK VDGKNQNESQ KRNAVVKVSN IAHSRGRVVK VSAQANTSKA QLSTKKVLQS
KNMDHAKARE VLKIAKEKAQ KKQNETSTSK NAHSKVHFTR RYQNPSSGSL PPRVRLKPQR
YRNEENDSSL KTGLEKMRSG KMAPKPQSRC TSTRSAGEAP SENQSPSKGP EEASSEVQDT
NEVHVPGDQD EPQTLGKKGS KNNISVYMTL NQKKSDSSSA SVCSIDSTDD LKSSNSECSS
SESFDFPPGS MHAPSTSSTS SSSKEEKKLS NSLKMKVFSK NVSKCVTPDG RTICVGDIVW
AKIYGFPWWP ARILTITVSR KDNGLLVRQE ARISWFGSPT TSFLALSQLS PFLENFQSRF
NKKRKGLYRK AITEAAKAAK QLTPEVRALL TQFET
