PHC3_MOUSE
ID PHC3_MOUSE Reviewed; 981 AA.
AC Q8CHP6; A2RTJ9; Q3TLV5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Polyhomeotic-like protein 3;
GN Name=Phc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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] (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND SER-614, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; THR-607; SER-614 AND
RP SER-760, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a PRC1-like complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHP6-2; Sequence=VSP_016772, VSP_016773, VSP_016774,
CC VSP_016775;
CC -!- TISSUE SPECIFICITY: Ubiquitous expression.
CC {ECO:0000269|PubMed:12384788}.
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DR EMBL; AJ414610; CAC93885.1; -; mRNA.
DR EMBL; AK166296; BAE38687.1; -; mRNA.
DR EMBL; BC132533; AAI32534.1; -; mRNA.
DR CCDS; CCDS17288.1; -. [Q8CHP6-1]
DR RefSeq; NP_001159426.1; NM_001165954.1.
DR RefSeq; NP_700470.2; NM_153421.2. [Q8CHP6-1]
DR AlphaFoldDB; Q8CHP6; -.
DR SMR; Q8CHP6; -.
DR BioGRID; 232356; 6.
DR IntAct; Q8CHP6; 2.
DR STRING; 10090.ENSMUSP00000130142; -.
DR iPTMnet; Q8CHP6; -.
DR PhosphoSitePlus; Q8CHP6; -.
DR EPD; Q8CHP6; -.
DR jPOST; Q8CHP6; -.
DR MaxQB; Q8CHP6; -.
DR PaxDb; Q8CHP6; -.
DR PRIDE; Q8CHP6; -.
DR ProteomicsDB; 287697; -. [Q8CHP6-1]
DR ProteomicsDB; 287698; -. [Q8CHP6-2]
DR Antibodypedia; 33708; 112 antibodies from 23 providers.
DR DNASU; 241915; -.
DR Ensembl; ENSMUST00000129817; ENSMUSP00000114916; ENSMUSG00000037652. [Q8CHP6-1]
DR Ensembl; ENSMUST00000168645; ENSMUSP00000130142; ENSMUSG00000037652. [Q8CHP6-1]
DR GeneID; 241915; -.
DR KEGG; mmu:241915; -.
DR UCSC; uc008ovl.2; mouse. [Q8CHP6-1]
DR CTD; 80012; -.
DR MGI; MGI:2181434; Phc3.
DR VEuPathDB; HostDB:ENSMUSG00000037652; -.
DR eggNOG; ENOG502QS5Q; Eukaryota.
DR GeneTree; ENSGT00940000154964; -.
DR InParanoid; Q8CHP6; -.
DR OMA; XCQDIAD; -.
DR OrthoDB; 298184at2759; -.
DR PhylomeDB; Q8CHP6; -.
DR TreeFam; TF331299; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 241915; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Phc3; mouse.
DR PRO; PR:Q8CHP6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CHP6; protein.
DR Bgee; ENSMUSG00000037652; Expressed in otolith organ and 225 other tissues.
DR ExpressionAtlas; Q8CHP6; baseline and differential.
DR Genevisible; Q8CHP6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISS: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 Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..981
FT /note="Polyhomeotic-like protein 3"
FT /id="PRO_0000076291"
FT DOMAIN 917..981
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 774..808
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 689..718
FT /note="HD1"
FT COMPBIAS 224..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT CROSSLNK 730
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDX5"
FT VAR_SEQ 1
FT /note="M -> MAEAEFKDHSTAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016772"
FT VAR_SEQ 178..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016773"
FT VAR_SEQ 720..736
FT /note="RSSLLIEQPVKKRPLLD -> QKLICVFKIIFSDTTLS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016774"
FT VAR_SEQ 737..981
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016775"
FT CONFLICT 147
FT /note="S -> I (in Ref. 1; CAC93885)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="N -> T (in Ref. 2; BAE38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> T (in Ref. 2; BAE38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="V -> G (in Ref. 2; BAE38687)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="S -> F (in Ref. 1; CAC93885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 105353 MW; 6FB97F04595ED7E3 CRC64;
MDSEPSSGTS VSTTASSTTT TTITTSSSRM QQPQISVYSG SDRHAVQVIQ QALHRPPSSA
AQYLQQMYAA QQQHLMLHTA ALQQQHLSSS QLQSLAAVQA SLSSGRPSTS PTGSVTQQSS
MSQTSILSAS PAPAQLMNRS QTSSSTSGSI TQQTMLLGST SPTLTASQAQ MYLRAQMLIF
TPATTVAAVQ SDIPVVSSSP SPSCQSAAAQ VQNLTLRSQK LGVLSSSQNG SPKSAGQTQS
LTICHNKTTV TSSKISQRDP SPESKKGGSP GLESRSTAVT RTSSIHQLIA PASYSPIQPH
SLIKHQQIPL HSPPPKVSHH QLLLQQQQQQ IQPITLQSPS QDPPPSQHCI PLPNHGLSPA
PSNAQPQHCS PVQSHPPPLT VSPNQAQSAQ QSVVVSPPPP HSPSQSPTII IHPQALIQPH
PLVSSALQTG PNLQQAAADQ VQSTAQLNLP SHLPLPASPV VHIGPVQQSA LVSPGQQMVS
PTSHQQYSAL QSSPIPIATP PQMSASPPAQ LPPLPLQSMQ SLQVQPEILS QGQVLVQNAL
VSEEELPAAE ALVQLPFQTL PPPQTVAVNL QVQPPAPVDP PVVYQVEDVC EEEMPEESDE
CARMDRTPPP PTLSPAAVTV GRGEDLTSEH PLLEQVELPA VASVSASVIK SPSDPTHASA
PAPPLLIPAA STRSSSTSLA SSTPSLENKP PQAIVKPQIL THVIEGFVIQ EGLEPFPVSR
SSLLIEQPVK KRPLLDNQVV NSVCVQPELQ NNTKHADNSS DTEIEDMMAE ETLEEMDSEL
LKCEFCGKMG YPNEFLRSKR FCTMSCAKRY NVSCSKKFAL SRWNRKPDNQ SLGHRGRRPS
GPEGAAREHI LRQLPITYPS AEEDVASHED PVPSAMTTRL RRQSERERER ELRDVRIRKM
PENSDLLPVA QTEPSIWTVD DVWAFIHSLP GCQDVADEFR AQEIDGQALL LLKEDHLMSA
MNMKLGPALK ICARINSLKD S
