PHC2_HUMAN
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 03-AUG-2022, entry version 174.
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; 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; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-713786, EBI-8643161;
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};
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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 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; 150.
DR CORUM; Q8IXK0; -.
DR DIP; DIP-34464N; -.
DR IntAct; Q8IXK0; 104.
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 BioMuta; PHC2; -.
DR DMDM; 74750731; -.
DR EPD; Q8IXK0; -.
DR jPOST; Q8IXK0; -.
DR MassIVE; Q8IXK0; -.
DR MaxQB; Q8IXK0; -.
DR PaxDb; Q8IXK0; -.
DR PeptideAtlas; Q8IXK0; -.
DR PRIDE; 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 Antibodypedia; 31416; 112 antibodies from 22 providers.
DR DNASU; 1912; -.
DR Ensembl; ENST00000257118.5; ENSP00000257118.5; ENSG00000134686.20. [Q8IXK0-1]
DR Ensembl; ENST00000373418.7; ENSP00000362517.3; ENSG00000134686.20. [Q8IXK0-2]
DR Ensembl; ENST00000683057.1; ENSP00000507877.1; ENSG00000134686.20. [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 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; PTPNQVQ; -.
DR OrthoDB; 298184at2759; -.
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; 14 hits in 1083 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 195 other tissues.
DR ExpressionAtlas; Q8IXK0; baseline and differential.
DR Genevisible; Q8IXK0; HS.
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 transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
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
