PHC3_HUMAN
ID PHC3_HUMAN Reviewed; 983 AA.
AC Q8NDX5; A2RRP9; Q5HYF0; Q6NSG2; Q8NFT7; Q8NFZ1; Q8TBM2; Q9H971; Q9H9I4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Polyhomeotic-like protein 3;
DE AltName: Full=Early development regulatory protein 3;
DE AltName: Full=Homolog of polyhomeotic 3;
DE Short=hPH3;
GN Name=PHC3; Synonyms=EDR3, PH3;
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 [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH
RP BMI1; CBX2; CBX4; CBX8; PHC1; PHC2; RING1 AND RNF2, AND SUBCELLULAR
RP LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hansen M.F., Deshpande A.M., Nellissery M.J., Reveles X., Naylor S.L.,
RA Jackson L.G., Leach R.J.;
RT "EDR3 is a candidate gene for the Cornelia de Lange Syndrome locus.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
RC TISSUE=Adipose tissue, and Amygdala;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6).
RC TISSUE=Testis;
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; THR-609; SER-616;
RP SER-761 AND SER-762, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609; SER-616 AND SER-762, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-272; THR-609 AND
RP SER-616, AND 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 [15]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-272; SER-315;
RP THR-609 AND SER-616, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609; THR-614; SER-761 AND
RP SER-762, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-691; LYS-732 AND LYS-810, AND
RP IDENTIFICATION BY MASS 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).
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 {ECO:0000269|PubMed:12167701}.
CC -!- SUBUNIT: Component of a PRC1-like complex.
CC {ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:19636380,
CC ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC Q8NDX5; O15294: OGT; NbExp=3; IntAct=EBI-1223801, EBI-539828;
CC Q8NDX5; Q93009: USP7; NbExp=3; IntAct=EBI-1223801, EBI-302474;
CC Q8NDX5-7; O95994: AGR2; NbExp=5; IntAct=EBI-12910528, EBI-712648;
CC Q8NDX5-7; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-12910528, EBI-10188461;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167701,
CC ECO:0000269|PubMed:21282530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8NDX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDX5-2; Sequence=VSP_016765;
CC Name=3;
CC IsoId=Q8NDX5-3; Sequence=VSP_016763, VSP_016770, VSP_016771;
CC Name=4;
CC IsoId=Q8NDX5-4; Sequence=VSP_016764, VSP_016768, VSP_016769;
CC Name=5;
CC IsoId=Q8NDX5-5; Sequence=VSP_016763, VSP_016766, VSP_016767;
CC Name=6;
CC IsoId=Q8NDX5-6; Sequence=VSP_016764, VSP_016766, VSP_016767;
CC Name=7;
CC IsoId=Q8NDX5-7; Sequence=VSP_016763;
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: [Isoform 5]:
CC Sequence=BAB14245.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ320486; CAC86587.2; -; mRNA.
DR EMBL; AF444193; AAM51781.1; -; mRNA.
DR EMBL; AF380154; AAM46139.1; -; mRNA.
DR EMBL; AK022791; BAB14245.1; ALT_FRAME; mRNA.
DR EMBL; AK023029; BAB14365.1; -; mRNA.
DR EMBL; BX647868; CAI46090.1; -; mRNA.
DR EMBL; EF560717; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78519.1; -; Genomic_DNA.
DR EMBL; BC022325; AAH22325.1; -; mRNA.
DR EMBL; BC070164; AAH70164.1; -; mRNA.
DR EMBL; BC131772; AAI31773.1; -; mRNA.
DR CCDS; CCDS46952.1; -. [Q8NDX5-7]
DR CCDS; CCDS77858.1; -. [Q8NDX5-1]
DR RefSeq; NP_001295045.1; NM_001308116.1. [Q8NDX5-1]
DR RefSeq; NP_079223.3; NM_024947.3. [Q8NDX5-7]
DR PDB; 4PZN; X-ray; 2.30 A; A/B/C/D/E=914-983.
DR PDB; 4PZO; X-ray; 2.25 A; A/B/C/D/E/F=914-983.
DR PDBsum; 4PZN; -.
DR PDBsum; 4PZO; -.
DR AlphaFoldDB; Q8NDX5; -.
DR SMR; Q8NDX5; -.
DR BioGRID; 123068; 83.
DR CORUM; Q8NDX5; -.
DR IntAct; Q8NDX5; 40.
DR MINT; Q8NDX5; -.
DR STRING; 9606.ENSP00000420294; -.
DR GlyConnect; 2863; 1 O-Linked glycan (1 site).
DR GlyGen; Q8NDX5; 14 sites, 2 O-linked glycans (14 sites).
DR iPTMnet; Q8NDX5; -.
DR PhosphoSitePlus; Q8NDX5; -.
DR BioMuta; PHC3; -.
DR DMDM; 74715388; -.
DR EPD; Q8NDX5; -.
DR jPOST; Q8NDX5; -.
DR MassIVE; Q8NDX5; -.
DR MaxQB; Q8NDX5; -.
DR PaxDb; Q8NDX5; -.
DR PeptideAtlas; Q8NDX5; -.
DR PRIDE; Q8NDX5; -.
DR ProteomicsDB; 73079; -. [Q8NDX5-1]
DR ProteomicsDB; 73080; -. [Q8NDX5-2]
DR ProteomicsDB; 73081; -. [Q8NDX5-3]
DR ProteomicsDB; 73082; -. [Q8NDX5-4]
DR ProteomicsDB; 73083; -. [Q8NDX5-5]
DR ProteomicsDB; 73084; -. [Q8NDX5-6]
DR ProteomicsDB; 73085; -. [Q8NDX5-7]
DR Antibodypedia; 33708; 112 antibodies from 23 providers.
DR DNASU; 80012; -.
DR Ensembl; ENST00000494943.5; ENSP00000420271.1; ENSG00000173889.16. [Q8NDX5-1]
DR Ensembl; ENST00000495893.7; ENSP00000420294.1; ENSG00000173889.16. [Q8NDX5-7]
DR Ensembl; ENST00000497658.5; ENSP00000420454.1; ENSG00000173889.16. [Q8NDX5-5]
DR GeneID; 80012; -.
DR KEGG; hsa:80012; -.
DR MANE-Select; ENST00000495893.7; ENSP00000420294.1; NM_024947.4; NP_079223.3. [Q8NDX5-7]
DR UCSC; uc003fgl.3; human. [Q8NDX5-1]
DR CTD; 80012; -.
DR DisGeNET; 80012; -.
DR GeneCards; PHC3; -.
DR HGNC; HGNC:15682; PHC3.
DR HPA; ENSG00000173889; Low tissue specificity.
DR neXtProt; NX_Q8NDX5; -.
DR OpenTargets; ENSG00000173889; -.
DR PharmGKB; PA134886018; -.
DR VEuPathDB; HostDB:ENSG00000173889; -.
DR eggNOG; ENOG502QS5Q; Eukaryota.
DR GeneTree; ENSGT00940000154964; -.
DR HOGENOM; CLU_012048_0_0_1; -.
DR InParanoid; Q8NDX5; -.
DR OMA; XCQDIAD; -.
DR OrthoDB; 298184at2759; -.
DR PhylomeDB; Q8NDX5; -.
DR TreeFam; TF331299; -.
DR PathwayCommons; Q8NDX5; -.
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 Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q8NDX5; -.
DR BioGRID-ORCS; 80012; 15 hits in 1087 CRISPR screens.
DR ChiTaRS; PHC3; human.
DR GeneWiki; PHC3; -.
DR GenomeRNAi; 80012; -.
DR Pharos; Q8NDX5; Tbio.
DR PRO; PR:Q8NDX5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NDX5; protein.
DR Bgee; ENSG00000173889; Expressed in endothelial cell and 190 other tissues.
DR ExpressionAtlas; Q8NDX5; baseline and differential.
DR Genevisible; Q8NDX5; HS.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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 3D-structure; Alternative splicing; Developmental protein; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..983
FT /note="Polyhomeotic-like protein 3"
FT /id="PRO_0000076290"
FT DOMAIN 919..983
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 776..810
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 691..720
FT /note="HD1"
FT COMPBIAS 225..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT CROSSLNK 691
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 810
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MAEAEFKDHSTAM (in isoform 3, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_016763"
FT VAR_SEQ 48..51
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016764"
FT VAR_SEQ 123..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_016765"
FT VAR_SEQ 127..139
FT /note="INLSTSPTPAQLI -> VSSLNFFFLDLKF (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016766"
FT VAR_SEQ 140..983
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016767"
FT VAR_SEQ 180..190
FT /note="LIFTPATTVAA -> VRYELPNFFSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016768"
FT VAR_SEQ 191..983
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016769"
FT VAR_SEQ 295..321
FT /note="ASYSPIQPHSLIKHQQIPLHSPPSKVS -> GGIKLLLKIVVLFIFLADRAK
FT QRMFMT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016770"
FT VAR_SEQ 322..983
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016771"
FT CONFLICT 50
FT /note="I -> F (in Ref. 3; AAM46139)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="A -> S (in Ref. 2; AAM51781)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="Q -> R (in Ref. 5; EF560717)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="N -> D (in Ref. 5; EF560717)"
FT /evidence="ECO:0000305"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:4PZO"
FT HELIX 921..929
FT /evidence="ECO:0007829|PDB:4PZO"
FT HELIX 935..943
FT /evidence="ECO:0007829|PDB:4PZO"
FT HELIX 948..952
FT /evidence="ECO:0007829|PDB:4PZO"
FT HELIX 956..959
FT /evidence="ECO:0007829|PDB:4PZO"
FT TURN 960..962
FT /evidence="ECO:0007829|PDB:4PZO"
FT HELIX 967..982
FT /evidence="ECO:0007829|PDB:4PZO"
SQ SEQUENCE 983 AA; 106162 MW; 05819632A1675049 CRC64;
MDTEPNPGTS SVSTTTSSTT TTTITTSSSR MQQPQISVYS GSDRHAVQVI QQALHRPPSS
AAQYLQQMYA AQQQHLMLHT AALQQQHLSS SQLQSLAAVQ ASLSSGRPST SPTGSVTQQS
SMSQTSINLS TSPTPAQLIS RSQASSSTSG SITQQTMLLG STSPTLTASQ AQMYLRAQML
IFTPATTVAA VQSDIPVVSS SSSSSCQSAA TQVQNLTLRS QKLGVLSSSQ NGPPKSTSQT
QSLTICHNKT TVTSSKISQR DPSPESNKKG ESPSLESRST AVTRTSSIHQ LIAPASYSPI
QPHSLIKHQQ IPLHSPPSKV SHHQLILQQQ QQQIQPITLQ NSTQDPPPSQ HCIPLQNHGL
PPAPSNAQSQ HCSPIQSHPS PLTVSPNQSQ SAQQSVVVSP PPPHSPSQSP TIIIHPQALI
QPHPLVSSAL QPGPNLQQST ANQVQATAQL NLPSHLPLPA SPVVHIGPVQ QSALVSPGQQ
IVSPSHQQYS SLQSSPIPIA SPPQMSTSPP AQIPPLPLQS MQSLQVQPEI LSQGQVLVQN
ALVSEEELPA AEALVQLPFQ TLPPPQTVAV NLQVQPPAPV DPPVVYQVED VCEEEMPEES
DECVRMDRTP PPPTLSPAAI TVGRGEDLTS EHPLLEQVEL PAVASVSASV IKSPSDPSHV
SVPPPPLLLP AATTRSNSTS MHSSIPSIEN KPPQAIVKPQ ILTHVIEGFV IQEGLEPFPV
SRSSLLIEQP VKKRPLLDNQ VINSVCVQPE LQNNTKHADN SSDTEMEDMI AEETLEEMDS
ELLKCEFCGK MGYANEFLRS KRFCTMSCAK RYNVSCSKKF ALSRWNRKPD NQSLGHRGRR
PSGPDGAARE HILRQLPITY PSAEEDLASH EDSVPSAMTT RLRRQSERER ERELRDVRIR
KMPENSDLLP VAQTEPSIWT VDDVWAFIHS LPGCQDIADE FRAQEIDGQA LLLLKEDHLM
SAMNIKLGPA LKICARINSL KES
