ID PHC2_HUMAN Reviewed; 858 AA. AC Q8IXK0; A1L4Q1; A8KA40; D3DPR2; Q2TAL3; Q5T0C1; Q6NUJ6; Q6ZQR1; Q8N306; AC Q8TAG8; Q96BL4; Q9Y4Y7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 183. DE RecName: Full=Polyhomeotic-like protein 2; DE Short=hPH2; DE AltName: Full=Early development regulatory protein 2; GN Name=PHC2; Synonyms=EDR2, PH2; 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 [MRNA] (ISOFORM 1). RX PubMed=12384788; DOI=10.1007/s00439-002-0814-3; RA Tonkin E., Hagan D.-M., Li W., Strachan T.; RT "Identification and characterisation of novel mammalian homologues of RT Drosophila polyhomeotic permits new insights into relationships between RT members of the polyhomeotic family."; RL Hum. Genet. 111:435-442(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). RC TISSUE=Testis, and Trachea; 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] (ISOFORMS 2; 4 AND 5), AND VARIANT RP MET-475. RC TISSUE=Cerebellum, Hypothalamus, Placenta, Prostate, and Retina; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-266 (ISOFORM 1), AND INTERACTION WITH SP1. RC TISSUE=Colon carcinoma; 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 INTERACTION WITH BMI1 AND PHC1. RX PubMed=9121482; DOI=10.1128/mcb.17.4.2326; RA Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L., de Bruijn D., RA Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.; RT "Identification and characterization of interactions between the vertebrate RT polycomb-group protein BMI1 and human homologs of polyhomeotic."; RL Mol. Cell. Biol. 17:2326-2335(1997). RN [8] RP INTERACTION WITH RING1; PHC1 AND BMI1. RX PubMed=9199346; DOI=10.1128/mcb.17.7.4105; RA Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., RA Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.; RT "RING1 is associated with the polycomb group protein complex and acts as a RT transcriptional repressor."; RL Mol. Cell. Biol. 17:4105-4113(1997). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE RP HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; CBX8; PHC1; PHC3; RING1 AND RNF2. RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002; RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., RA Kingston R.E.; RT "The core of the polycomb repressive complex is compositionally and RT functionally conserved in flies and humans."; RL Mol. Cell. Biol. 22:6070-6078(2002). RN [10] RP INTERACTION WITH MAPKAPK2. RX PubMed=15094067; DOI=10.1016/s0014-5793(04)00351-5; RA Yannoni Y.M., Gaestel M., Lin L.L.; RT "P66(ShcA) interacts with MAPKAP kinase 2 and regulates its activity."; RL FEBS Lett. 564:205-211(2004). RN [11] RP IDENTIFICATION IN A PRC1-LIKE COMPLEX. RX PubMed=15386022; DOI=10.1038/nature02985; RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., RA Zhang Y.; RT "Role of histone H2A ubiquitination in Polycomb silencing."; RL Nature 431:873-878(2004). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] 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 [14] RP IDENTIFICATION IN A PRC1-LIKE COMPLEX. RX PubMed=19636380; DOI=10.1371/journal.pone.0006380; RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., RA Rodriguez-Niedenfuhr M., Gil J., Peters G.; RT "Several distinct polycomb complexes regulate and co-localize on the INK4a RT tumor suppressor locus."; RL PLoS ONE 4:E6380-E6380(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY RP 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 [16] 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 [17] RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4, AND RP SUBCELLULAR LOCATION. RX PubMed=21282530; DOI=10.1074/mcp.m110.002642; RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.; RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 RT Complexes in mammalian cells."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619; SER-621 AND SER-751, 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-598; LYS-600; LYS-632; LYS-702 RP AND LYS-847, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like CC complex, a complex class required to maintain the transcriptionally CC repressive state of many genes, including Hox genes, throughout CC development. PcG PRC1 complex acts via chromatin remodeling and CC modification of histones; it mediates monoubiquitination of histone H2A CC 'Lys-119', rendering chromatin heritably changed in its expressibility. CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:12167701, CC PubMed:15386022, PubMed:19636380, PubMed:21282530). Interacts with CBX4 CC (PubMed:21282530). Interacts with BMI1, PCGF2, PHC1 and RNF2 CC (PubMed:9121482, PubMed:9199346, PubMed:12167701). Interacts with CHTOP CC (By similarity). Interacts with the N-terminal region of the SP1 CC transcription factor and with MAPKAPK2 (PubMed:10976766, CC PubMed:15094067). {ECO:0000250|UniProtKB:Q9QWH1, CC ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:12167701, CC ECO:0000269|PubMed:15094067, ECO:0000269|PubMed:15386022, CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530, CC ECO:0000269|PubMed:9121482, ECO:0000269|PubMed:9199346}. CC -!- INTERACTION: CC Q8IXK0; Q8WTP8: AEN; NbExp=3; IntAct=EBI-713786, EBI-8637627; CC Q8IXK0; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-713786, EBI-8643161; CC Q8IXK0; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-713786, EBI-541426; CC Q8IXK0; P35226: BMI1; NbExp=9; IntAct=EBI-713786, EBI-2341576; CC Q8IXK0; Q13895: BYSL; NbExp=6; IntAct=EBI-713786, EBI-358049; CC Q8IXK0; Q9H257: CARD9; NbExp=3; IntAct=EBI-713786, EBI-751319; CC Q8IXK0; Q9HC52: CBX8; NbExp=8; IntAct=EBI-713786, EBI-712912; CC Q8IXK0; Q9Y295: DRG1; NbExp=4; IntAct=EBI-713786, EBI-719554; CC Q8IXK0; Q9H0I2: ENKD1; NbExp=4; IntAct=EBI-713786, EBI-744099; CC Q8IXK0; Q86V42: FAM124A; NbExp=3; IntAct=EBI-713786, EBI-744506; CC Q8IXK0; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-713786, EBI-751248; CC Q8IXK0; Q3B820: FAM161A; NbExp=3; IntAct=EBI-713786, EBI-719941; CC Q8IXK0; Q5RGS3: FAM74A1; NbExp=3; IntAct=EBI-713786, EBI-10244822; CC Q8IXK0; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-713786, EBI-10247271; CC Q8IXK0; Q92993: KAT5; NbExp=3; IntAct=EBI-713786, EBI-399080; CC Q8IXK0; Q8WVZ9: KBTBD7; NbExp=3; IntAct=EBI-713786, EBI-473695; CC Q8IXK0; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-713786, EBI-2125614; CC Q8IXK0; Q96JM7: L3MBTL3; NbExp=6; IntAct=EBI-713786, EBI-2686809; CC Q8IXK0; P25800: LMO1; NbExp=3; IntAct=EBI-713786, EBI-8639312; CC Q8IXK0; P25791: LMO2; NbExp=4; IntAct=EBI-713786, EBI-739696; CC Q8IXK0; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-713786, EBI-10268010; CC Q8IXK0; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-713786, EBI-6447163; CC Q8IXK0; Q96EZ8: MCRS1; NbExp=2; IntAct=EBI-713786, EBI-348259; CC Q8IXK0; P55081: MFAP1; NbExp=3; IntAct=EBI-713786, EBI-1048159; CC Q8IXK0; Q15014: MORF4L2; NbExp=3; IntAct=EBI-713786, EBI-399257; CC Q8IXK0; P35227: PCGF2; NbExp=8; IntAct=EBI-713786, EBI-2129767; CC Q8IXK0; Q3KNV8: PCGF3; NbExp=3; IntAct=EBI-713786, EBI-2339807; CC Q8IXK0; Q86SE9: PCGF5; NbExp=3; IntAct=EBI-713786, EBI-2827999; CC Q8IXK0; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-713786, EBI-713786; CC Q8IXK0; P53350: PLK1; NbExp=2; IntAct=EBI-713786, EBI-476768; CC Q8IXK0; P62875: POLR2L; NbExp=3; IntAct=EBI-713786, EBI-359527; CC Q8IXK0; Q96T49: PPP1R16B; NbExp=4; IntAct=EBI-713786, EBI-10293968; CC Q8IXK0; Q13131: PRKAA1; NbExp=3; IntAct=EBI-713786, EBI-1181405; CC Q8IXK0; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-713786, EBI-1567797; CC Q8IXK0; Q14498: RBM39; NbExp=3; IntAct=EBI-713786, EBI-395290; CC Q8IXK0; Q14498-3: RBM39; NbExp=3; IntAct=EBI-713786, EBI-6654703; CC Q8IXK0; P57060: RWDD2B; NbExp=3; IntAct=EBI-713786, EBI-724442; CC Q8IXK0; O00560: SDCBP; NbExp=3; IntAct=EBI-713786, EBI-727004; CC Q8IXK0; Q9UHJ3: SFMBT1; NbExp=4; IntAct=EBI-713786, EBI-747398; CC Q8IXK0; Q8IUQ4: SIAH1; NbExp=5; IntAct=EBI-713786, EBI-747107; CC Q8IXK0; P84022: SMAD3; NbExp=3; IntAct=EBI-713786, EBI-347161; CC Q8IXK0; P08047: SP1; NbExp=2; IntAct=EBI-713786, EBI-298336; CC Q8IXK0; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-713786, EBI-2212028; CC Q8IXK0; Q17RD7: SYT16; NbExp=3; IntAct=EBI-713786, EBI-10238936; CC Q8IXK0; Q9BT49: THAP7; NbExp=3; IntAct=EBI-713786, EBI-741350; CC Q8IXK0; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-713786, EBI-725997; CC Q8IXK0; O43167: ZBTB24; NbExp=3; IntAct=EBI-713786, EBI-744471; CC Q8IXK0; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-713786, EBI-3439227; CC Q8IXK0; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-713786, EBI-10183064; CC Q8IXK0; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-713786, EBI-2682299; CC Q8IXK0; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-713786, EBI-740727; CC Q8IXK0; P25916: Bmi1; Xeno; NbExp=2; IntAct=EBI-713786, EBI-927401; CC Q8IXK0-4; Q9H0A9: SPATC1L; NbExp=3; IntAct=EBI-10304199, EBI-372911; CC Q8IXK0-5; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-11527347, EBI-21553822; CC Q8IXK0-5; O14901: KLF11; NbExp=3; IntAct=EBI-11527347, EBI-948266; CC Q8IXK0-5; O43395: PRPF3; NbExp=3; IntAct=EBI-11527347, EBI-744322; CC Q8IXK0-5; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-11527347, EBI-1567797; CC Q8IXK0-5; P84022: SMAD3; NbExp=3; IntAct=EBI-11527347, EBI-347161; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8IXK0-1; Sequence=Displayed; CC Name=2; Synonyms=isoform b; CC IsoId=Q8IXK0-2; Sequence=VSP_016915; CC Name=3; CC IsoId=Q8IXK0-3; Sequence=VSP_016914, VSP_016916, VSP_016917, CC VSP_016918; CC Name=4; CC IsoId=Q8IXK0-4; Sequence=VSP_027217; CC Name=5; CC IsoId=Q8IXK0-5; Sequence=VSP_039755; CC -!- DOMAIN: HD1 motif interacts with SAM domain of PHC1. CC -!- MISCELLANEOUS: The hPRC-H complex purification reported by CC PubMed:12167701 probably presents a mixture of different PRC1-like CC complexes. CC -!- SEQUENCE CAUTION: CC Sequence=AAH68573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH92492.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ419231; CAD11673.1; -; mRNA. DR EMBL; AK128821; BAC87622.1; -; mRNA. DR EMBL; AK292905; BAF85594.1; -; mRNA. DR EMBL; AL513327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07457.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07458.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07459.1; -; Genomic_DNA. DR EMBL; BC015450; AAH15450.1; -; mRNA. DR EMBL; BC028396; AAH28396.3; -; mRNA. DR EMBL; BC029269; AAH29269.1; -; mRNA. DR EMBL; BC068573; AAH68573.1; ALT_INIT; mRNA. DR EMBL; BC092492; AAH92492.1; ALT_INIT; mRNA. DR EMBL; BC110863; AAI10864.2; -; mRNA. DR EMBL; BC130630; AAI30631.1; -; mRNA. DR EMBL; AJ242730; CAB44779.1; -; mRNA. DR CCDS; CCDS378.1; -. [Q8IXK0-1] DR CCDS; CCDS379.1; -. [Q8IXK0-2] DR CCDS; CCDS90911.1; -. [Q8IXK0-5] DR RefSeq; NP_004418.2; NM_004427.3. [Q8IXK0-2] DR RefSeq; NP_932157.1; NM_198040.2. [Q8IXK0-1] DR RefSeq; XP_005270627.1; XM_005270570.1. DR RefSeq; XP_016856005.1; XM_017000516.1. DR RefSeq; XP_016856006.1; XM_017000517.1. DR RefSeq; XP_016856007.1; XM_017000518.1. DR AlphaFoldDB; Q8IXK0; -. DR SMR; Q8IXK0; -. DR BioGRID; 108234; 159. DR ComplexPortal; CPX-2601; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC2 variant. DR ComplexPortal; CPX-2609; Polycomb repressive complex 1, RING1-PCGF2-CBX2-PHC2 variant. DR ComplexPortal; CPX-2613; Polycomb repressive complex 1, RING1-PCGF2-CBX4-PHC2 variant. DR ComplexPortal; CPX-2617; Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC2 variant. DR ComplexPortal; CPX-2622; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-7502; Polycomb repressive complex 1, RING1-PCGF4-CBX2-PHC2 variant. DR ComplexPortal; CPX-7506; Polycomb repressive complex 1, RING1-PCGF4-CBX4-PHC2 variant. DR ComplexPortal; CPX-7510; Polycomb repressive complex 1, RING1-PCGF4-CBX6-PHC2 variant. DR ComplexPortal; CPX-7514; Polycomb repressive complex 1, RING1-PCGF4-CBX7-PHC2 variant. DR ComplexPortal; CPX-7517; Polycomb repressive complex 1, RING1-PCGF4-CBX8-PHC2 variant. DR ComplexPortal; CPX-7522; Polycomb repressive complex 1, RING2-PCGF2-CBX2-PHC2 variant. DR ComplexPortal; CPX-7526; Polycomb repressive complex 1, RING2-PCGF2-CBX4-PHC2 variant. DR ComplexPortal; CPX-7528; Polycomb repressive complex 1, RING2-PCGF2-CBX6-PHC2 variant. DR ComplexPortal; CPX-7531; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC2 variant. DR ComplexPortal; CPX-7534; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-7542; Polycomb repressive complex 1, RING2-PCGF4-CBX2-PHC2 variant. DR ComplexPortal; CPX-7546; Polycomb repressive complex 1, RING2-PCGF4-CBX4-PHC2 variant. DR ComplexPortal; CPX-7549; Polycomb repressive complex 1, RING2-PCGF4-CBX6-PHC2 variant. DR ComplexPortal; CPX-7552; Polycomb repressive complex 1, RING2-PCGF4-CBX7-PHC2 variant. DR ComplexPortal; CPX-7555; Polycomb repressive complex 1, RING2-PCGF4-CBX8-PHC2 variant. DR CORUM; Q8IXK0; -. DR DIP; DIP-34464N; -. DR IntAct; Q8IXK0; 106. DR MINT; Q8IXK0; -. DR STRING; 9606.ENSP00000257118; -. DR MoonDB; Q8IXK0; Predicted. DR GlyGen; Q8IXK0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IXK0; -. DR PhosphoSitePlus; Q8IXK0; -. DR SwissPalm; Q8IXK0; -. DR BioMuta; PHC2; -. DR DMDM; 74750731; -. DR EPD; Q8IXK0; -. DR jPOST; Q8IXK0; -. DR MassIVE; Q8IXK0; -. DR MaxQB; Q8IXK0; -. DR PaxDb; 9606-ENSP00000257118; -. DR PeptideAtlas; Q8IXK0; -. DR ProteomicsDB; 71014; -. [Q8IXK0-1] DR ProteomicsDB; 71015; -. [Q8IXK0-2] DR ProteomicsDB; 71016; -. [Q8IXK0-3] DR ProteomicsDB; 71017; -. [Q8IXK0-4] DR ProteomicsDB; 71018; -. [Q8IXK0-5] DR Pumba; Q8IXK0; -. DR Antibodypedia; 31416; 138 antibodies from 22 providers. DR DNASU; 1912; -. DR Ensembl; ENST00000257118.5; ENSP00000257118.5; ENSG00000134686.21. [Q8IXK0-1] DR Ensembl; ENST00000373418.7; ENSP00000362517.3; ENSG00000134686.21. [Q8IXK0-2] DR Ensembl; ENST00000683057.1; ENSP00000507877.1; ENSG00000134686.21. [Q8IXK0-5] DR GeneID; 1912; -. DR KEGG; hsa:1912; -. DR MANE-Select; ENST00000683057.1; ENSP00000507877.1; NM_001385109.1; NP_001372038.1. [Q8IXK0-5] DR UCSC; uc001bxe.2; human. [Q8IXK0-1] DR AGR; HGNC:3183; -. DR CTD; 1912; -. DR DisGeNET; 1912; -. DR GeneCards; PHC2; -. DR HGNC; HGNC:3183; PHC2. DR HPA; ENSG00000134686; Low tissue specificity. DR MIM; 602979; gene. DR neXtProt; NX_Q8IXK0; -. DR OpenTargets; ENSG00000134686; -. DR PharmGKB; PA27620; -. DR VEuPathDB; HostDB:ENSG00000134686; -. DR eggNOG; ENOG502QS5Q; Eukaryota. DR GeneTree; ENSGT00940000160840; -. DR HOGENOM; CLU_047131_0_0_1; -. DR InParanoid; Q8IXK0; -. DR OMA; HSPAHET; -. DR OrthoDB; 5399754at2759; -. DR PhylomeDB; Q8IXK0; -. DR TreeFam; TF331299; -. DR PathwayCommons; Q8IXK0; -. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR SignaLink; Q8IXK0; -. DR SIGNOR; Q8IXK0; -. DR BioGRID-ORCS; 1912; 19 hits in 1160 CRISPR screens. DR ChiTaRS; PHC2; human. DR GeneWiki; PHC2; -. DR GenomeRNAi; 1912; -. DR Pharos; Q8IXK0; Tbio. DR PRO; PR:Q8IXK0; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8IXK0; Protein. DR Bgee; ENSG00000134686; Expressed in right lung and 197 other cell types or tissues. DR ExpressionAtlas; Q8IXK0; baseline and differential. DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB. DR GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd09577; SAM_Ph1_2_3; 1. DR Gene3D; 3.30.60.160; -; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR012313; Znf_FCS. DR InterPro; IPR038603; Znf_FCS_sf. DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR12247:SF86; POLYHOMEOTIC-LIKE PROTEIN 2; 1. DR Pfam; PF16616; PHC2_SAM_assoc; 1. DR Pfam; PF00536; SAM_1; 1. DR Pfam; PF21319; zf-FCS_1; 1. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS51024; ZF_FCS; 1. DR Genevisible; Q8IXK0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..858 FT /note="Polyhomeotic-like protein 2" FT /id="PRO_0000076286" FT DOMAIN 794..858 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT ZN_FING 633..667 FT /note="FCS-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000250|UniProtKB:Q9QWH1" FT REGION 33..53 FT /note="Interaction with BMI1" FT /evidence="ECO:0000250|UniProtKB:Q9QWH1" FT REGION 230..307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 337..388 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 407..444 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 473..493 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..561 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 688..720 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 732..768 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 558..587 FT /note="HD1" FT COMPBIAS 230..245 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..429 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..557 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 732..762 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 642 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 645 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 661 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 665 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT MOD_RES 619 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 621 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 751 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 598 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 600 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 632 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 702 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 847 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..585 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016914" FT VAR_SEQ 1..535 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016915" FT VAR_SEQ 193..221 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027217" FT VAR_SEQ 463 FT /note="P -> PV (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_039755" FT VAR_SEQ 586 FT /note="P -> M (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016916" FT VAR_SEQ 809..852 FT /note="CQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARI -> LPSS FT FPKGHETSIYSLSKHLRHSRFPQSPSGSCLWPVLRPRPHL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016917" FT VAR_SEQ 853..858 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016918" FT VARIANT 254 FT /note="P -> S (in dbSNP:rs10914692)" FT /id="VAR_051276" FT VARIANT 475 FT /note="V -> M (in dbSNP:rs12026290)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_051277" FT CONFLICT 745 FT /note="S -> N (in Ref. 2; BAC87622)" FT /evidence="ECO:0000305" FT CONFLICT 778 FT /note="D -> E (in Ref. 2; BAC87622)" FT /evidence="ECO:0000305" FT CONFLICT 813 FT /note="A -> E (in Ref. 5; AAH28396)" FT /evidence="ECO:0000305" SQ SEQUENCE 858 AA; 90713 MW; 2E3FD3898CFD702B CRC64; MENELPVPHT SSSACATSST SGASSSSGCN NSSSGGSGRP TGPQISVYSG IPDRQTVQVI QQALHRQPST AAQYLQQMYA AQQQHLMLQT AALQQQHLSS AQLQSLAAVQ QASLVSNRQG STSGSNVSAQ APAQSSSINL AASPAAAQLL NRAQSVNSAA ASGIAQQAVL LGNTSSPALT ASQAQMYLRA QMLIFTPTAT VATVQPELGT GSPARPPTPA QVQNLTLRTQ QTPAAAASGP TPTQPVLPSL ALKPTPGGSQ PLPTPAQSRN TAQASPAGAK PGIADSVMEP HKKGDGNSSV PGSMEGRAGL SRTVPAVAAH PLIAPAYAQL QPHQLLPQPS SKHLQPQFVI QQQPQPQQQQ PPPQQSRPVL QAEPHPQLAS VSPSVALQPS SEAHAMPLGP VTPALPLQCP TANLHKPGGS QQCHPPTPDT GPQNGHPEGV PHTPQRRFQH TSAVILQLQP ASPPQQCVPD DWKEVAPGEK SVPETRSGPS PHQQAIVTAM PGGLPVPTSP NIQPSPAHET GQGIVHALTD LSSPGMTSGN GNSASSIAGT APQNGENKPP QAIVKPQILT HVIEGFVIQE GAEPFPVGRS SLLVGNLKKK YAQGFLPEKL PQQDHTTTTD SEMEEPYLQE SKEEGAPLKL KCELCGRVDF AYKFKRSKRF CSMACAKRYN VGCTKRVGLF HSDRSKLQKA GAATHNRRRA SKASLPPLTK DTKKQPTGTV PLSVTAALQL THSQEDSSRC SDNSSYEEPL SPISASSSTS RRRQGQRDLE LPDMHMRDLV GMGHHFLPSE PTKWNVEDVY EFIRSLPGCQ EIAEEFRAQE IDGQALLLLK EDHLMSAMNI KLGPALKIYA RISMLKDS //