POGZ_HUMAN
ID POGZ_HUMAN Reviewed; 1410 AA.
AC Q7Z3K3; B4DTP8; B4DYL9; B7ZBY5; E9PM80; O75049; Q3LIC4; Q5SZS1; Q5SZS2;
AC Q5SZS3; Q5SZS4; Q8TDZ7; Q9Y4X7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Pogo transposable element with ZNF domain;
DE AltName: Full=Suppressor of hairy wing homolog 5;
DE AltName: Full=Zinc finger protein 280E;
DE AltName: Full=Zinc finger protein 635;
GN Name=POGZ; Synonyms=KIAA0461, SUHW5, ZNF280E, ZNF635; ORFNames=Nbla00003;
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] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
RC TISSUE=Placenta, and Testis;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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] OF 1-1107 (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-788 (ISOFORM 1), AND INTERACTION WITH SP1.
RC TISSUE=Colon;
RX PubMed=10976766; DOI=10.1023/a:1007177623283;
RA Gunther M., Laithier M., Brison O.;
RT "A set of proteins interacting with transcription factor Sp1 identified in
RT a two-hybrid screening.";
RL Mol. Cell. Biochem. 210:131-142(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363 (ISOFORM 4).
RC TISSUE=Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1410 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-425 AND SER-1338,
RP AND 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PSIP1.
RX PubMed=19244240; DOI=10.1074/jbc.m807781200;
RA Bartholomeeusen K., Christ F., Hendrix J., Rain J.C., Emiliani S.,
RA Benarous R., Debyser Z., Gijsbers R., De Rijck J.;
RT "Lens epithelium-derived growth factor/p75 interacts with the transposase-
RT derived DDE domain of PogZ.";
RL J. Biol. Chem. 284:11467-11477(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-439 AND SER-445, 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 [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHAMP1; MAD2L2; CBX1; CBX3 AND
RP CBX5.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [14]
RP FUNCTION, INTERACTION WITH CBX1; CBX3 AND CBX5, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-817; CYS-820; HIS-833 AND HIS-840.
RX PubMed=20562864; DOI=10.1038/ncb2075;
RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
RA Kimura H., Obuse C.;
RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms
RT through Aurora B activation.";
RL Nat. Cell Biol. 12:719-727(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-363; SER-425;
RP SER-445; SER-856; SER-1338; SER-1364; SER-1367 AND THR-1368, AND
RP IDENTIFICATION BY 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 [18]
RP INTERACTION WITH PSIP1.
RX PubMed=25082813; DOI=10.1158/0008-5472.can-13-3602;
RA Cermakova K., Tesina P., Demeulemeester J., El Ashkar S., Mereau H.,
RA Schwaller J., Rezacova P., Veverka V., De Rijck J.;
RT "Validation and structural characterization of the LEDGF/p75-MLL interface
RT as a new target for the treatment of MLL-dependent leukemia.";
RL Cancer Res. 74:5139-5151(2014).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-445; THR-463;
RP SER-1364 AND SER-1392, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP INVOLVEMENT IN WHSUS.
RX PubMed=25533962; DOI=10.1038/nature14135;
RG Deciphering Developmental Disorders Study;
RT "Large-scale discovery of novel genetic causes of developmental
RT disorders.";
RL Nature 519:223-228(2015).
RN [21]
RP INVOLVEMENT IN WHSUS.
RX PubMed=26739615; DOI=10.1186/s13073-015-0253-0;
RA White J., Beck C.R., Harel T., Posey J.E., Jhangiani S.N., Tang S.,
RA Farwell K.D., Powis Z., Mendelsohn N.J., Baker J.A., Pollack L.,
RA Mason K.J., Wierenga K.J., Arrington D.K., Hall M., Psychogios A.,
RA Fairbrother L., Walkiewicz M., Person R.E., Niu Z., Zhang J.,
RA Rosenfeld J.A., Muzny D.M., Eng C., Beaudet A.L., Lupski J.R.,
RA Boerwinkle E., Gibbs R.A., Yang Y., Xia F., Sutton V.R.;
RT "POGZ truncating alleles cause syndromic intellectual disability.";
RL Genome Med. 8:3-3(2016).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-319; LYS-359; LYS-422; LYS-449;
RP LYS-489; LYS-629; LYS-677; LYS-801 AND LYS-883, 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 [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HDGFL2.
RX PubMed=26721387; DOI=10.1093/nar/gkv1526;
RA Baude A., Aaes T.L., Zhai B., Al-Nakouzi N., Oo H.Z., Daugaard M.,
RA Rohde M., Jaeaettelae M.;
RT "Hepatoma-derived growth factor-related protein 2 promotes DNA repair by
RT homologous recombination.";
RL Nucleic Acids Res. 44:2214-2226(2016).
RN [24]
RP STRUCTURE BY NMR OF 352-405.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the zinc finger domain of human KIAA0461.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [25] {ECO:0007744|PDB:6EMP}
RP STRUCTURE BY NMR OF 1370-1404 IN COMPLEX WITH PSIP1, INTERACTION WITH
RP PSIP1, DOMAIN IBM MOTIF, PHOSPHORYLATION AT SER-1373; SER-1374; THR-1378;
RP SER-1392; THR-1394 AND SER-1396, AND MUTAGENESIS OF SER-1392 AND SER-1396.
RX PubMed=29997176; DOI=10.1073/pnas.1803909115;
RA Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M.,
RA El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P.,
RA Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z.,
RA Veverka V.;
RT "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-
RT dependent phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018).
RN [26]
RP VARIANT LYS-1040, AND INVOLVEMENT IN AUTISM.
RX PubMed=25694107; DOI=10.1038/jhg.2015.13;
RA Fukai R., Hiraki Y., Yofune H., Tsurusaki Y., Nakashima M., Saitsu H.,
RA Tanaka F., Miyake N., Matsumoto N.;
RT "A case of autism spectrum disorder arising from a de novo missense
RT mutation in POGZ.";
RL J. Hum. Genet. 60:277-279(2015).
CC -!- FUNCTION: Plays a role in mitotic cell cycle progression and is
CC involved in kinetochore assembly and mitotic sister chromatid cohesion.
CC Probably through its association with CBX5 plays a role in mitotic
CC chromosome segregation by regulating aurora kinase B/AURKB activation
CC and AURKB and CBX5 dissociation from chromosome arms (PubMed:20562864).
CC Promotes the repair of DNA double-strand breaks through the homologous
CC recombination pathway (PubMed:26721387). {ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:26721387}.
CC -!- SUBUNIT: Interacts with CBX1, CBX3, MAD2L2 and CHAMP1. Interacts with
CC CBX5; POGZ competes with PXVXL motif-containing proteins such as INCENP
CC and TRIM28 for interaction with CBX5. Interacts (via IBM motif) with
CC PSIP1 isoform 1 (via IBD domain); phosphorylation increases its
CC affinity for PSIP1 (PubMed:19244240, PubMed:25082813, PubMed:29997176).
CC Interacts with HDGFL2 (PubMed:26721387). {ECO:0000269|PubMed:10976766,
CC ECO:0000269|PubMed:19244240, ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:25082813,
CC ECO:0000269|PubMed:26721387, ECO:0000269|PubMed:29997176}.
CC -!- INTERACTION:
CC Q7Z3K3; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-1389308, EBI-2809489;
CC Q7Z3K3; O95994: AGR2; NbExp=3; IntAct=EBI-1389308, EBI-712648;
CC Q7Z3K3; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-1389308, EBI-12102070;
CC Q7Z3K3; P19801: AOC1; NbExp=3; IntAct=EBI-1389308, EBI-12826295;
CC Q7Z3K3; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-1389308, EBI-12015080;
CC Q7Z3K3; P54253: ATXN1; NbExp=3; IntAct=EBI-1389308, EBI-930964;
CC Q7Z3K3; B4DE54: BANP; NbExp=3; IntAct=EBI-1389308, EBI-16429313;
CC Q7Z3K3; Q8N9N5: BANP; NbExp=5; IntAct=EBI-1389308, EBI-744695;
CC Q7Z3K3; Q8N9N5-2: BANP; NbExp=10; IntAct=EBI-1389308, EBI-11524452;
CC Q7Z3K3; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-1389308, EBI-16429296;
CC Q7Z3K3; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-1389308, EBI-11983447;
CC Q7Z3K3; Q5SWW7: C10orf55; NbExp=5; IntAct=EBI-1389308, EBI-12809220;
CC Q7Z3K3; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-1389308, EBI-11976299;
CC Q7Z3K3; P45973: CBX5; NbExp=8; IntAct=EBI-1389308, EBI-78219;
CC Q7Z3K3; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-1389308, EBI-12261896;
CC Q7Z3K3; O43186: CRX; NbExp=3; IntAct=EBI-1389308, EBI-748171;
CC Q7Z3K3; O75553: DAB1; NbExp=3; IntAct=EBI-1389308, EBI-7875264;
CC Q7Z3K3; Q15038: DAZAP2; NbExp=8; IntAct=EBI-1389308, EBI-724310;
CC Q7Z3K3; B2RWN7: DMXL1; NbExp=3; IntAct=EBI-1389308, EBI-14753788;
CC Q7Z3K3; Q86UW9: DTX2; NbExp=3; IntAct=EBI-1389308, EBI-740376;
CC Q7Z3K3; Q96D98: EID2B; NbExp=3; IntAct=EBI-1389308, EBI-724968;
CC Q7Z3K3; O00303: EIF3F; NbExp=3; IntAct=EBI-1389308, EBI-711990;
CC Q7Z3K3; O00167-2: EYA2; NbExp=3; IntAct=EBI-1389308, EBI-12807776;
CC Q7Z3K3; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-1389308, EBI-12193763;
CC Q7Z3K3; Q8N0W3: FCSK; NbExp=3; IntAct=EBI-1389308, EBI-4291312;
CC Q7Z3K3; Q14192: FHL2; NbExp=3; IntAct=EBI-1389308, EBI-701903;
CC Q7Z3K3; Q53EP0-3: FNDC3B; NbExp=6; IntAct=EBI-1389308, EBI-10242151;
CC Q7Z3K3; P53539: FOSB; NbExp=3; IntAct=EBI-1389308, EBI-2806743;
CC Q7Z3K3; Q06547: GABPB1; NbExp=5; IntAct=EBI-1389308, EBI-618165;
CC Q7Z3K3; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-1389308, EBI-948296;
CC Q7Z3K3; O14964: HGS; NbExp=6; IntAct=EBI-1389308, EBI-740220;
CC Q7Z3K3; O75031: HSF2BP; NbExp=3; IntAct=EBI-1389308, EBI-7116203;
CC Q7Z3K3; Q16082: HSPB2; NbExp=3; IntAct=EBI-1389308, EBI-739395;
CC Q7Z3K3; P0C870: JMJD7; NbExp=3; IntAct=EBI-1389308, EBI-9090173;
CC Q7Z3K3; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-1389308, EBI-9478422;
CC Q7Z3K3; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-1389308, EBI-724915;
CC Q7Z3K3; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-1389308, EBI-751260;
CC Q7Z3K3; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-1389308, EBI-11962084;
CC Q7Z3K3; Q8IUC2: KRTAP8-1; NbExp=5; IntAct=EBI-1389308, EBI-10261141;
CC Q7Z3K3; Q99732: LITAF; NbExp=3; IntAct=EBI-1389308, EBI-725647;
CC Q7Z3K3; O43795: MYO1B; NbExp=3; IntAct=EBI-1389308, EBI-351119;
CC Q7Z3K3; P23511: NFYA; NbExp=3; IntAct=EBI-1389308, EBI-389739;
CC Q7Z3K3; P23511-2: NFYA; NbExp=3; IntAct=EBI-1389308, EBI-11061759;
CC Q7Z3K3; Q13952-2: NFYC; NbExp=3; IntAct=EBI-1389308, EBI-11956831;
CC Q7Z3K3; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-1389308, EBI-12868744;
CC Q7Z3K3; Q9BSH3: NICN1; NbExp=3; IntAct=EBI-1389308, EBI-13324229;
CC Q7Z3K3; Q16656: NRF1; NbExp=3; IntAct=EBI-1389308, EBI-2547810;
CC Q7Z3K3; Q16656-4: NRF1; NbExp=7; IntAct=EBI-1389308, EBI-11742836;
CC Q7Z3K3; A1E959: ODAM; NbExp=3; IntAct=EBI-1389308, EBI-5774125;
CC Q7Z3K3; Q99471: PFDN5; NbExp=3; IntAct=EBI-1389308, EBI-357275;
CC Q7Z3K3; Q9HB75-2: PIDD1; NbExp=3; IntAct=EBI-1389308, EBI-12326369;
CC Q7Z3K3; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-1389308, EBI-373552;
CC Q7Z3K3; Q99541: PLIN2; NbExp=3; IntAct=EBI-1389308, EBI-2115275;
CC Q7Z3K3; Q16633: POU2AF1; NbExp=3; IntAct=EBI-1389308, EBI-943588;
CC Q7Z3K3; P14859: POU2F1; NbExp=3; IntAct=EBI-1389308, EBI-624770;
CC Q7Z3K3; P86479: PRR20C; NbExp=3; IntAct=EBI-1389308, EBI-10172814;
CC Q7Z3K3; P86480: PRR20D; NbExp=3; IntAct=EBI-1389308, EBI-12754095;
CC Q7Z3K3; Q2TAL8: QRICH1; NbExp=7; IntAct=EBI-1389308, EBI-2798044;
CC Q7Z3K3; Q9NWB1-5: RBFOX1; NbExp=5; IntAct=EBI-1389308, EBI-12123390;
CC Q7Z3K3; Q93062: RBPMS; NbExp=3; IntAct=EBI-1389308, EBI-740322;
CC Q7Z3K3; Q93062-3: RBPMS; NbExp=5; IntAct=EBI-1389308, EBI-740343;
CC Q7Z3K3; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-1389308, EBI-12275818;
CC Q7Z3K3; P08047: SP1; NbExp=2; IntAct=EBI-1389308, EBI-298336;
CC Q7Z3K3; Q02447: SP3; NbExp=3; IntAct=EBI-1389308, EBI-348158;
CC Q7Z3K3; Q02446: SP4; NbExp=3; IntAct=EBI-1389308, EBI-10198587;
CC Q7Z3K3; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-1389308, EBI-10696971;
CC Q7Z3K3; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-1389308, EBI-12408727;
CC Q7Z3K3; Q8IWL8: STH; NbExp=3; IntAct=EBI-1389308, EBI-12843506;
CC Q7Z3K3; O60806: TBX19; NbExp=3; IntAct=EBI-1389308, EBI-12096770;
CC Q7Z3K3; Q13488: TCIRG1; NbExp=3; IntAct=EBI-1389308, EBI-3914669;
CC Q7Z3K3; Q7Z782: TMBIM4; NbExp=3; IntAct=EBI-1389308, EBI-12924766;
CC Q7Z3K3; Q86WV8: TSC1; NbExp=3; IntAct=EBI-1389308, EBI-12806590;
CC Q7Z3K3; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-1389308, EBI-12068150;
CC Q7Z3K3; Q14119: VEZF1; NbExp=3; IntAct=EBI-1389308, EBI-11980193;
CC Q7Z3K3; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-1389308, EBI-11957216;
CC Q7Z3K3; O43167: ZBTB24; NbExp=8; IntAct=EBI-1389308, EBI-744471;
CC Q7Z3K3; P52747: ZNF143; NbExp=3; IntAct=EBI-1389308, EBI-2849334;
CC Q7Z3K3; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-1389308, EBI-11741890;
CC Q7Z3K3; Q8N1W2: ZNF710; NbExp=3; IntAct=EBI-1389308, EBI-18096911;
CC Q7Z3K3; P36508: ZNF76; NbExp=3; IntAct=EBI-1389308, EBI-7254550;
CC Q7Z3K3; Q2QGD7: ZXDC; NbExp=4; IntAct=EBI-1389308, EBI-1538838;
CC Q7Z3K3; G4XUV3; NbExp=3; IntAct=EBI-1389308, EBI-10177989;
CC Q7Z3K3; Q9H891; NbExp=3; IntAct=EBI-1389308, EBI-10218875;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26721387}.
CC Chromosome. Cytoplasm. Note=According to some authors, it is not
CC localized to mitotic chromatin (PubMed:19244240). Recruited to
CC trimethylated 'Lys-9' of histone H3 (H3K9me3).
CC {ECO:0000269|PubMed:19244240}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q7Z3K3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3K3-2; Sequence=VSP_010185;
CC Name=3;
CC IsoId=Q7Z3K3-3; Sequence=VSP_010185, VSP_010186;
CC Name=4;
CC IsoId=Q7Z3K3-4; Sequence=VSP_010187, VSP_010188;
CC Name=5; Synonyms=CRA_e;
CC IsoId=Q7Z3K3-5; Sequence=VSP_030150;
CC Name=6;
CC IsoId=Q7Z3K3-6; Sequence=VSP_046785;
CC Name=7;
CC IsoId=Q7Z3K3-7; Sequence=VSP_010185, VSP_046785;
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000269|PubMed:29997176}.
CC -!- DISEASE: Note=Defects in POGZ may be associated with neuropsychiatric
CC disorders such as autism spectrum disorders (ASD), bipolar affective
CC disorders and early dementia onset. ASD are characterized by
CC impairments in reciprocal social interaction and communication as well
CC as restricted and stereotyped patterns of interest and activities. ASD
CC include forms with moderate to severe cognitive impairment and milder
CC forms with higher cognitive ability (Asperger syndrome).
CC {ECO:0000269|PubMed:25694107}.
CC -!- DISEASE: White-Sutton syndrome (WHSUS) [MIM:616364]: An autosomal
CC dominant syndrome characterized by developmental delay, intellectual
CC disability, hypotonia, behavioral abnormalities, and dysmorphic facial
CC features. Variable features include short stature, microcephaly,
CC strabismus and hearing loss. {ECO:0000269|PubMed:25533962,
CC ECO:0000269|PubMed:26739615}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE45744.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX537838; CAD97850.1; -; mRNA.
DR EMBL; AK300307; BAG62060.1; -; mRNA.
DR EMBL; AK302501; BAG63781.1; -; mRNA.
DR EMBL; AL589764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53440.1; -; Genomic_DNA.
DR EMBL; AB037911; BAB87117.1; -; mRNA.
DR EMBL; AB075477; BAE45744.1; ALT_INIT; mRNA.
DR EMBL; AJ242979; CAB45136.1; -; mRNA.
DR EMBL; BC057773; AAH57773.1; -; mRNA.
DR EMBL; AB007930; BAA32306.1; -; mRNA.
DR CCDS; CCDS44222.2; -. [Q7Z3K3-5]
DR CCDS; CCDS53365.1; -. [Q7Z3K3-7]
DR CCDS; CCDS53366.1; -. [Q7Z3K3-6]
DR CCDS; CCDS997.1; -. [Q7Z3K3-1]
DR CCDS; CCDS998.1; -. [Q7Z3K3-2]
DR PIR; T00075; T00075.
DR RefSeq; NP_001181866.1; NM_001194937.1. [Q7Z3K3-6]
DR RefSeq; NP_001181867.1; NM_001194938.1. [Q7Z3K3-7]
DR RefSeq; NP_055915.2; NM_015100.3. [Q7Z3K3-1]
DR RefSeq; NP_665739.3; NM_145796.3. [Q7Z3K3-5]
DR RefSeq; NP_997054.1; NM_207171.2. [Q7Z3K3-2]
DR RefSeq; XP_005245056.1; XM_005244999.2. [Q7Z3K3-1]
DR RefSeq; XP_005245057.1; XM_005245000.4. [Q7Z3K3-1]
DR RefSeq; XP_005245058.1; XM_005245001.2. [Q7Z3K3-1]
DR RefSeq; XP_005245062.1; XM_005245005.1. [Q7Z3K3-2]
DR RefSeq; XP_005245063.1; XM_005245006.4. [Q7Z3K3-2]
DR RefSeq; XP_016856234.1; XM_017000745.1. [Q7Z3K3-6]
DR RefSeq; XP_016856235.1; XM_017000746.1. [Q7Z3K3-6]
DR RefSeq; XP_016856237.1; XM_017000748.1. [Q7Z3K3-2]
DR RefSeq; XP_016856238.1; XM_017000749.1. [Q7Z3K3-2]
DR PDB; 2E72; NMR; -; A=370-405.
DR PDB; 2N3A; NMR; -; A=1389-1404.
DR PDB; 6EMP; NMR; -; A=1370-1404.
DR PDBsum; 2E72; -.
DR PDBsum; 2N3A; -.
DR PDBsum; 6EMP; -.
DR AlphaFoldDB; Q7Z3K3; -.
DR BMRB; Q7Z3K3; -.
DR SMR; Q7Z3K3; -.
DR BioGRID; 116745; 225.
DR DIP; DIP-38044N; -.
DR IntAct; Q7Z3K3; 184.
DR MINT; Q7Z3K3; -.
DR STRING; 9606.ENSP00000271715; -.
DR GlyConnect; 2865; 1 O-Linked glycan (1 site). [Q7Z3K3-2]
DR GlyGen; Q7Z3K3; 21 sites, 2 O-linked glycans (21 sites).
DR iPTMnet; Q7Z3K3; -.
DR PhosphoSitePlus; Q7Z3K3; -.
DR SwissPalm; Q7Z3K3; -.
DR BioMuta; POGZ; -.
DR DMDM; 143811442; -.
DR EPD; Q7Z3K3; -.
DR jPOST; Q7Z3K3; -.
DR MassIVE; Q7Z3K3; -.
DR MaxQB; Q7Z3K3; -.
DR PaxDb; Q7Z3K3; -.
DR PeptideAtlas; Q7Z3K3; -.
DR PRIDE; Q7Z3K3; -.
DR ProteomicsDB; 22027; -.
DR ProteomicsDB; 69059; -. [Q7Z3K3-1]
DR ProteomicsDB; 69060; -. [Q7Z3K3-2]
DR ProteomicsDB; 69061; -. [Q7Z3K3-3]
DR ProteomicsDB; 69062; -. [Q7Z3K3-4]
DR ProteomicsDB; 69063; -. [Q7Z3K3-5]
DR ProteomicsDB; 7168; -.
DR Antibodypedia; 1872; 152 antibodies from 28 providers.
DR DNASU; 23126; -.
DR Ensembl; ENST00000271715.7; ENSP00000271715.2; ENSG00000143442.22. [Q7Z3K3-1]
DR Ensembl; ENST00000368863.6; ENSP00000357856.2; ENSG00000143442.22. [Q7Z3K3-5]
DR Ensembl; ENST00000392723.5; ENSP00000376484.1; ENSG00000143442.22. [Q7Z3K3-2]
DR Ensembl; ENST00000409503.5; ENSP00000386836.1; ENSG00000143442.22. [Q7Z3K3-6]
DR Ensembl; ENST00000491586.5; ENSP00000418408.1; ENSG00000143442.22. [Q7Z3K3-3]
DR Ensembl; ENST00000531094.5; ENSP00000431259.1; ENSG00000143442.22. [Q7Z3K3-7]
DR GeneID; 23126; -.
DR KEGG; hsa:23126; -.
DR MANE-Select; ENST00000271715.7; ENSP00000271715.2; NM_015100.4; NP_055915.2.
DR UCSC; uc001eyd.2; human. [Q7Z3K3-1]
DR CTD; 23126; -.
DR DisGeNET; 23126; -.
DR GeneCards; POGZ; -.
DR GeneReviews; POGZ; -.
DR HGNC; HGNC:18801; POGZ.
DR HPA; ENSG00000143442; Low tissue specificity.
DR MalaCards; POGZ; -.
DR MIM; 614787; gene.
DR MIM; 616364; phenotype.
DR neXtProt; NX_Q7Z3K3; -.
DR OpenTargets; ENSG00000143442; -.
DR Orphanet; 468678; White-Sutton syndrome.
DR PharmGKB; PA38685; -.
DR VEuPathDB; HostDB:ENSG00000143442; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG3105; Eukaryota.
DR GeneTree; ENSGT00940000160649; -.
DR HOGENOM; CLU_002015_0_0_1; -.
DR InParanoid; Q7Z3K3; -.
DR OMA; QIMQNAN; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q7Z3K3; -.
DR TreeFam; TF331707; -.
DR PathwayCommons; Q7Z3K3; -.
DR SignaLink; Q7Z3K3; -.
DR SIGNOR; Q7Z3K3; -.
DR BioGRID-ORCS; 23126; 236 hits in 1083 CRISPR screens.
DR ChiTaRS; POGZ; human.
DR EvolutionaryTrace; Q7Z3K3; -.
DR GeneWiki; POGZ; -.
DR GenomeRNAi; 23126; -.
DR Pharos; Q7Z3K3; Tbio.
DR PRO; PR:Q7Z3K3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z3K3; protein.
DR Bgee; ENSG00000143442; Expressed in right uterine tube and 202 other tissues.
DR ExpressionAtlas; Q7Z3K3; baseline and differential.
DR Genevisible; Q7Z3K3; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; IMP:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR SMART; SM00674; CENPB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51253; HTH_CENPB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autism spectrum disorder; Cell cycle;
KW Cell division; Chromosome; Coiled coil; Cytoplasm; Disease variant;
KW DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1410
FT /note="Pogo transposable element with ZNF domain"
FT /id="PRO_0000047224"
FT DOMAIN 1015..1085
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT DOMAIN 1117..1323
FT /note="DDE-1"
FT /evidence="ECO:0000255"
FT ZN_FING 375..397
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..553
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 560..583
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 590..613
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 619..641
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 647..670
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 771..794
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 815..840
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 238..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..850
FT /note="Required for interaction with CBX5"
FT REGION 857..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1340..1360
FT /evidence="ECO:0000255"
FT MOTIF 1380..1404
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000269|PubMed:29997176"
FT COMPBIAS 238..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 1378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 1392
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:29997176,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29997176"
FT MOD_RES 1396
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:29997176"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 801
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 883
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 42..94
FT /note="Missing (in isoform 2, isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12880961,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9455484"
FT /id="VSP_010185"
FT VAR_SEQ 96..190
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_030150"
FT VAR_SEQ 287..295
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046785"
FT VAR_SEQ 360..363
FT /note="VTSS -> GTIT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010187"
FT VAR_SEQ 364..1410
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010188"
FT VAR_SEQ 593
FT /note="Q -> QPYFPSYVTQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880961"
FT /id="VSP_010186"
FT VARIANT 1040
FT /note="E -> K (probable disease-associated variant found in
FT patients with ASD)"
FT /evidence="ECO:0000269|PubMed:25694107"
FT /id="VAR_073179"
FT VARIANT 1365
FT /note="E -> D (in dbSNP:rs35198305)"
FT /id="VAR_031476"
FT MUTAGEN 817
FT /note="C->A: Diminishes interaction with CBX5 and abolishes
FT interaction with CBX1 and CBX5; when associated with A-820;
FT A-833 and A-840."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 820
FT /note="C->A: Abolishes interaction with CBX1, CBX3 and
FT CBX5; when associated with when associated with A-817; A-
FT 833 and A-840."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 833
FT /note="H->A: Abolishes interaction with CBX1, CBX3 and
FT CBX5; when associated with A-817; A-820 and A-840."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 840
FT /note="H->A: Abolishes interaction with CBX1, CBX3 and
FT CBX5; when associated with A-817; A-820 and A-833."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 1392
FT /note="S->A: Loss of phosphorylation. Loss of interaction
FT with PSIP1; when associated with A-1396."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 1392
FT /note="S->D: Phosphomimetic mutant. Significant increase in
FT interaction with PSIP1; when associated with D-1396."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 1396
FT /note="S->A: Loss of phosphorylation. Loss of interaction
FT with PSIP1; when associated with A-1392."
FT /evidence="ECO:0000269|PubMed:29997176"
FT MUTAGEN 1396
FT /note="S->D: Phosphomimetic mutant. Significant increase in
FT interaction with PSIP1; when associated with D-1392."
FT /evidence="ECO:0000269|PubMed:29997176"
FT CONFLICT 213
FT /note="R -> G (in Ref. 2; BAG63781)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="I -> F (in Ref. 2; BAG62060)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="L -> P (in Ref. 5; BAB87117/BAE45744)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="V -> A (in Ref. 2; BAG63781)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="N -> T (in Ref. 6; CAB45136)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="K -> E (in Ref. 5; BAB87117/BAE45744)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="A -> V (in Ref. 1; CAD97850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="E -> G (in Ref. 1; CAD97850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="R -> W (in Ref. 5; BAB87117/BAE45744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092..1107
FT /note="TLPKDVAENAGLFIDF -> PTLLFCLFVFSSPSTL (in Ref. 5;
FT BAB87117/BAE45744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1248
FT /note="T -> A (in Ref. 2; BAG63781)"
FT /evidence="ECO:0000305"
FT CONFLICT 1304
FT /note="W -> R (in Ref. 1; CAD97850)"
FT /evidence="ECO:0000305"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2E72"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:2E72"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2E72"
FT HELIX 1382..1388
FT /evidence="ECO:0007829|PDB:6EMP"
SQ SEQUENCE 1410 AA; 155344 MW; 58F672EDCD57CCD8 CRC64;
MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT TVSVSQQPVS APVPIAAHAS
VAGHLSTSTT VSSSGAQNSD STKKTLVTLI ANNNAGNPLV QQGGQPLILT QNPAPGLGTM
VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ
TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST
VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AVQSPGQSNQ TTNPKLAPSF PSPPAVSIAS
FVTVKRPGVT GENSNEVAKL VNTLNTIPSL GQSPGPVVVS NNSSAHGSQR TSGPESSMKV
TSSIPVFDLQ DGGRKICPRC NAQFRVTEAL RGHMCYCCPE MVEYQKKGKS LDSEPSVPSA
AKPPSPEKTA PVASTPSSTP IPALSPPTKV PEPNENVGDA VQTKLIMLVD DFYYGRDGGK
VAQLTNFPKV ATSFRCPHCT KRLKNNIRFM NHMKHHVELD QQNGEVDGHT ICQHCYRQFS
TPFQLQCHLE NVHSPYESTT KCKICEWAFE SEPLFLQHMK DTHKPGEMPY VCQVCQYRSS
LYSEVDVHFR MIHEDTRHLL CPYCLKVFKN GNAFQQHYMR HQKRNVYHCN KCRLQFLFAK
DKIEHKLQHH KTFRKPKQLE GLKPGTKVTI RASRGQPRTV PVSSNDTPPS ALQEAAPLTS
SMDPLPVFLY PPVQRSIQKR AVRKMSVMGR QTCLECSFEI PDFPNHFPTY VHCSLCRYST
CCSRAYANHM INNHVPRKSP KYLALFKNSV SGIKLACTSC TFVTSVGDAM AKHLVFNPSH
RSSSILPRGL TWIAHSRHGQ TRDRVHDRNV KNMYPPPSFP TNKAATVKSA GATPAEPEEL
LTPLAPALPS PASTATPPPT PTHPQALALP PLATEGAECL NVDDQDEGSP VTQEPELASG
GGGSGGVGKK EQLSVKKLRV VLFALCCNTE QAAEHFRNPQ RRIRRWLRRF QASQGENLEG
KYLSFEAEEK LAEWVLTQRE QQLPVNEETL FQKATKIGRS LEGGFKISYE WAVRFMLRHH
LTPHARRAVA HTLPKDVAEN AGLFIDFVQR QIHNQDLPLS MIVAIDEISL FLDTEVLSSD
DRKENALQTV GTGEPWCDVV LAILADGTVL PTLVFYRGQM DQPANMPDSI LLEAKESGYS
DDEIMELWST RVWQKHTACQ RSKGMLVMDC HRTHLSEEVL AMLSASSTLP AVVPAGCSSK
IQPLDVCIKR TVKNFLHKKW KEQAREMADT ACDSDVLLQL VLVWLGEVLG VIGDCPELVQ
RSFLVASVLP GPDGNINSPT RNADMQEELI ASLEEQLKLS GEHSESSTPR PRSSPEETIE
PESLHQLFEG ESETESFYGF EEADLDLMEI
