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Polyhomeotic-like protein 2 (hPH2) (Early development regulatory protein 2)

 PHC2_HUMAN              Reviewed;         858 AA.
Q8IXK0; A1L4Q1; A8KA40; D3DPR2; Q2TAL3; Q5T0C1; Q6NUJ6; Q6ZQR1;
Q8N306; Q8TAG8; Q96BL4; Q9Y4Y7;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
30-AUG-2017, entry version 138.
RecName: Full=Polyhomeotic-like protein 2;
Short=hPH2;
AltName: Full=Early development regulatory protein 2;
Name=PHC2; Synonyms=EDR2, PH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12384788; DOI=10.1007/s00439-002-0814-3;
Tonkin E., Hagan D.-M., Li W., Strachan T.;
"Identification and characterisation of novel mammalian homologues of
Drosophila polyhomeotic permits new insights into relationships
between members of the polyhomeotic family.";
Hum. Genet. 111:435-442(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
TISSUE=Testis, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND
VARIANT MET-475.
TISSUE=Cerebellum, Hypothalamus, Placenta, Prostate, and Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-266 (ISOFORM 1), AND INTERACTION WITH
SP1.
TISSUE=Colon carcinoma;
PubMed=10976766; DOI=10.1023/A:1007177623283;
Gunther M., Laithier M., Brison O.;
"A set of proteins interacting with transcription factor Sp1
identified in a two-hybrid screening.";
Mol. Cell. Biochem. 210:131-142(2000).
[7]
INTERACTION WITH BMI1 AND PHC1.
PubMed=9121482; DOI=10.1128/MCB.17.4.2326;
Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L.,
de Bruijn D., Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.;
"Identification and characterization of interactions between the
vertebrate polycomb-group protein BMI1 and human homologs of
polyhomeotic.";
Mol. Cell. Biol. 17:2326-2335(1997).
[8]
INTERACTION WITH RING1; PHC1 AND BMI1.
PubMed=9199346; DOI=10.1128/MCB.17.7.4105;
Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
"RING1 is associated with the polycomb group protein complex and acts
as a transcriptional repressor.";
Mol. Cell. Biol. 17:4105-4113(1997).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; CBX8; PHC1; PHC3; RING1 AND
RNF2.
PubMed=12167701; DOI=10.1128/MCB.22.17.6070-6078.2002;
Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
Kingston R.E.;
"The core of the polycomb repressive complex is compositionally and
functionally conserved in flies and humans.";
Mol. Cell. Biol. 22:6070-6078(2002).
[10]
INTERACTION WITH MAPKAPK2.
PubMed=15094067; DOI=10.1016/S0014-5793(04)00351-5;
Yannoni Y.M., Gaestel M., Lin L.L.;
"P66(ShcA) interacts with MAPKAP kinase 2 and regulates its
activity.";
FEBS Lett. 564:205-211(2004).
[11]
IDENTIFICATION IN A PRC1-LIKE COMPLEX.
PubMed=15386022; DOI=10.1038/nature02985;
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H2A ubiquitination in Polycomb silencing.";
Nature 431:873-878(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION IN A PRC1-LIKE COMPLEX.
PubMed=19636380; DOI=10.1371/journal.pone.0006380;
Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K.,
Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.;
"Several distinct polycomb complexes regulate and co-localize on the
INK4a tumor suppressor locus.";
PLoS ONE 4:E6380-E6380(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4, AND
SUBCELLULAR LOCATION.
PubMed=21282530; DOI=10.1074/mcp.M110.002642;
Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
"Interaction proteomics analysis of polycomb proteins defines distinct
PRC1 Complexes in mammalian cells.";
Mol. Cell. Proteomics 0:0-0(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619; SER-621 AND
SER-751, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-598; LYS-600; LYS-632;
LYS-702 AND LYS-847, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-
like complex, a complex class required to maintain the
transcriptionally repressive state of many genes, including Hox
genes, throughout development. PcG PRC1 complex acts via chromatin
remodeling and modification of histones; it mediates
monoubiquitination of histone H2A 'Lys-119', rendering chromatin
heritably changed in its expressibility.
-!- SUBUNIT: Component of a PRC1-like complex. Interacts with CBX4.
Interacts with BMI1, PCGF2, PHC1 and RNF2. Interacts with CHTOP
(By similarity). Interacts with the N-terminal region of the SP1
transcription factor and with MAPKAPK2. {ECO:0000250,
ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:12167701,
ECO:0000269|PubMed:15094067, ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530,
ECO:0000269|PubMed:9121482, ECO:0000269|PubMed:9199346}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-713786, EBI-713786;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-713786, EBI-8637627;
Q9BXS5:AP1M1; NbExp=3; IntAct=EBI-713786, EBI-541426;
P35226:BMI1; NbExp=7; IntAct=EBI-713786, EBI-2341576;
P25916:Bmi1 (xeno); NbExp=2; IntAct=EBI-713786, EBI-927401;
Q13895:BYSL; NbExp=6; IntAct=EBI-713786, EBI-358049;
Q9NX04:C1orf109; NbExp=3; IntAct=EBI-713786, EBI-8643161;
Q9H257:CARD9; NbExp=3; IntAct=EBI-713786, EBI-751319;
Q9HC52:CBX8; NbExp=7; IntAct=EBI-713786, EBI-712912;
Q9Y295:DRG1; NbExp=4; IntAct=EBI-713786, EBI-719554;
Q9H0I2:ENKD1; NbExp=4; IntAct=EBI-713786, EBI-744099;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-713786, EBI-744506;
Q8NE31:FAM13C; NbExp=3; IntAct=EBI-713786, EBI-751248;
Q3B820:FAM161A; NbExp=3; IntAct=EBI-713786, EBI-719941;
Q5RGS3:FAM74A1; NbExp=3; IntAct=EBI-713786, EBI-10244822;
Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-713786, EBI-10247271;
Q92993:KAT5; NbExp=3; IntAct=EBI-713786, EBI-399080;
Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-713786, EBI-473695;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-713786, EBI-2125614;
Q96JM7:L3MBTL3; NbExp=6; IntAct=EBI-713786, EBI-2686809;
P25800:LMO1; NbExp=3; IntAct=EBI-713786, EBI-8639312;
P25791:LMO2; NbExp=4; IntAct=EBI-713786, EBI-739696;
Q8N8X9:MAB21L3; NbExp=3; IntAct=EBI-713786, EBI-10268010;
Q8N7X4:MAGEB6; NbExp=3; IntAct=EBI-713786, EBI-6447163;
Q96EZ8:MCRS1; NbExp=2; IntAct=EBI-713786, EBI-348259;
P55081:MFAP1; NbExp=3; IntAct=EBI-713786, EBI-1048159;
Q15014:MORF4L2; NbExp=3; IntAct=EBI-713786, EBI-399257;
P35227:PCGF2; NbExp=8; IntAct=EBI-713786, EBI-2129767;
Q3KNV8:PCGF3; NbExp=3; IntAct=EBI-713786, EBI-2339807;
Q86SE9:PCGF5; NbExp=3; IntAct=EBI-713786, EBI-2827999;
P53350:PLK1; NbExp=2; IntAct=EBI-713786, EBI-476768;
P62875:POLR2L; NbExp=3; IntAct=EBI-713786, EBI-359527;
Q96T49:PPP1R16B; NbExp=3; IntAct=EBI-713786, EBI-10293968;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-713786, EBI-1181405;
O43395:PRPF3; NbExp=3; IntAct=EBI-11527347, EBI-744322;
Q8WWY3:PRPF31; NbExp=3; IntAct=EBI-11527347, EBI-1567797;
Q14498:RBM39; NbExp=3; IntAct=EBI-713786, EBI-395290;
Q14498-3:RBM39; NbExp=3; IntAct=EBI-713786, EBI-6654703;
P57060:RWDD2B; NbExp=3; IntAct=EBI-713786, EBI-724442;
O00560:SDCBP; NbExp=3; IntAct=EBI-713786, EBI-727004;
Q9UHJ3:SFMBT1; NbExp=4; IntAct=EBI-713786, EBI-747398;
Q8IUQ4:SIAH1; NbExp=5; IntAct=EBI-713786, EBI-747107;
P84022:SMAD3; NbExp=3; IntAct=EBI-713786, EBI-347161;
P08047:SP1; NbExp=2; IntAct=EBI-713786, EBI-298336;
Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-10304199, EBI-372911;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-713786, EBI-2212028;
Q17RD7:SYT16; NbExp=3; IntAct=EBI-713786, EBI-10238936;
Q9BT49:THAP7; NbExp=3; IntAct=EBI-713786, EBI-741350;
Q8WV44:TRIM41; NbExp=3; IntAct=EBI-713786, EBI-725997;
O43167:ZBTB24; NbExp=3; IntAct=EBI-713786, EBI-744471;
Q8N5A5:ZGPAT; NbExp=3; IntAct=EBI-713786, EBI-3439227;
Q8N5A5-2:ZGPAT; NbExp=3; IntAct=EBI-713786, EBI-10183064;
Q96NC0:ZMAT2; NbExp=3; IntAct=EBI-713786, EBI-2682299;
Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-713786, EBI-740727;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8IXK0-1; Sequence=Displayed;
Name=2; Synonyms=isoform b;
IsoId=Q8IXK0-2; Sequence=VSP_016915;
Name=3;
IsoId=Q8IXK0-3; Sequence=VSP_016914, VSP_016916, VSP_016917,
VSP_016918;
Name=4;
IsoId=Q8IXK0-4; Sequence=VSP_027217;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8IXK0-5; Sequence=VSP_039755;
Note=No experimental confirmation available.;
-!- DOMAIN: HD1 motif interacts with SAM domain of PHC1.
-!- MISCELLANEOUS: The hPRC-H complex purification reported by
PubMed:12167701 probably presents a mixture of different PRC1-like
complexes.
-!- SEQUENCE CAUTION:
Sequence=AAH68573.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH92492.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI13956.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AJ419231; CAD11673.1; -; mRNA.
EMBL; AK128821; BAC87622.1; -; mRNA.
EMBL; AK292905; BAF85594.1; -; mRNA.
EMBL; AL513327; CAI13955.1; -; Genomic_DNA.
EMBL; AL513327; CAI13956.1; ALT_SEQ; Genomic_DNA.
EMBL; AL513327; CAI13957.1; -; Genomic_DNA.
EMBL; CH471059; EAX07457.1; -; Genomic_DNA.
EMBL; CH471059; EAX07458.1; -; Genomic_DNA.
EMBL; CH471059; EAX07459.1; -; Genomic_DNA.
EMBL; BC015450; AAH15450.1; -; mRNA.
EMBL; BC028396; AAH28396.3; -; mRNA.
EMBL; BC029269; AAH29269.1; -; mRNA.
EMBL; BC068573; AAH68573.1; ALT_INIT; mRNA.
EMBL; BC092492; AAH92492.1; ALT_INIT; mRNA.
EMBL; BC110863; AAI10864.2; -; mRNA.
EMBL; BC130630; AAI30631.1; -; mRNA.
EMBL; AJ242730; CAB44779.1; -; mRNA.
CCDS; CCDS378.1; -. [Q8IXK0-1]
CCDS; CCDS379.1; -. [Q8IXK0-2]
RefSeq; NP_004418.2; NM_004427.3. [Q8IXK0-2]
RefSeq; NP_932157.1; NM_198040.2. [Q8IXK0-1]
RefSeq; XP_005270627.1; XM_005270570.1. [Q8IXK0-2]
RefSeq; XP_016856005.1; XM_017000516.1. [Q8IXK0-5]
RefSeq; XP_016856006.1; XM_017000517.1. [Q8IXK0-5]
RefSeq; XP_016856007.1; XM_017000518.1. [Q8IXK0-5]
UniGene; Hs.524271; -.
UniGene; Hs.674410; -.
ProteinModelPortal; Q8IXK0; -.
SMR; Q8IXK0; -.
BioGrid; 108234; 95.
DIP; DIP-34464N; -.
IntAct; Q8IXK0; 92.
MINT; MINT-1369031; -.
STRING; 9606.ENSP00000257118; -.
iPTMnet; Q8IXK0; -.
PhosphoSitePlus; Q8IXK0; -.
BioMuta; PHC2; -.
DMDM; 74750731; -.
EPD; Q8IXK0; -.
MaxQB; Q8IXK0; -.
PaxDb; Q8IXK0; -.
PeptideAtlas; Q8IXK0; -.
PRIDE; Q8IXK0; -.
Ensembl; ENST00000257118; ENSP00000257118; ENSG00000134686. [Q8IXK0-1]
Ensembl; ENST00000373418; ENSP00000362517; ENSG00000134686. [Q8IXK0-2]
GeneID; 1912; -.
KEGG; hsa:1912; -.
UCSC; uc001bxe.2; human. [Q8IXK0-1]
CTD; 1912; -.
DisGeNET; 1912; -.
GeneCards; MIR3605; -.
GeneCards; PHC2; -.
HGNC; HGNC:3183; PHC2.
HPA; HPA047403; -.
MIM; 602979; gene.
neXtProt; NX_Q8IXK0; -.
OpenTargets; ENSG00000134686; -.
PharmGKB; PA27620; -.
eggNOG; ENOG410IDZN; Eukaryota.
eggNOG; ENOG4111F0Y; LUCA.
GeneTree; ENSGT00550000074459; -.
HOGENOM; HOG000236275; -.
HOVERGEN; HBG039325; -.
InParanoid; Q8IXK0; -.
KO; K11457; -.
OMA; NELPVPH; -.
OrthoDB; EOG091G02VS; -.
PhylomeDB; Q8IXK0; -.
TreeFam; TF331299; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
ChiTaRS; PHC2; human.
GeneWiki; PHC2; -.
GenomeRNAi; 1912; -.
PRO; PR:Q8IXK0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134686; -.
ExpressionAtlas; Q8IXK0; baseline and differential.
Genevisible; Q8IXK0; HS.
GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR012313; Znf_FCS.
Pfam; PF00536; SAM_1; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS51024; ZF_FCS; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 858 Polyhomeotic-like protein 2.
/FTId=PRO_0000076286.
DOMAIN 794 858 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ZN_FING 633 667 FCS-type. {ECO:0000255|PROSITE-
ProRule:PRU00367}.
MOTIF 558 587 HD1.
COMPBIAS 11 37 Ser-rich.
COMPBIAS 55 111 Gln-rich.
COMPBIAS 329 377 Gln-rich.
MOD_RES 619 619 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 751 751 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 598 598 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 600 600 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 632 632 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 702 702 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 847 847 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 585 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016914.
VAR_SEQ 1 535 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016915.
VAR_SEQ 193 221 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027217.
VAR_SEQ 463 463 P -> PV (in isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_039755.
VAR_SEQ 586 586 P -> M (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016916.
VAR_SEQ 809 852 CQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIY
ARI -> LPSSFPKGHETSIYSLSKHLRHSRFPQSPSGSCL
WPVLRPRPHL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016917.
VAR_SEQ 853 858 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016918.
VARIANT 254 254 P -> S (in dbSNP:rs10914692).
/FTId=VAR_051276.
VARIANT 475 475 V -> M (in dbSNP:rs12026290).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051277.
CONFLICT 745 745 S -> N (in Ref. 2; BAC87622).
{ECO:0000305}.
CONFLICT 778 778 D -> E (in Ref. 2; BAC87622).
{ECO:0000305}.
CONFLICT 813 813 A -> E (in Ref. 5; AAH28396).
{ECO:0000305}.
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


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