PHC1_MOUSE
ID PHC1_MOUSE Reviewed; 1012 AA.
AC Q64028; P70359; Q64307; Q8BZ80;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Polyhomeotic-like protein 1;
DE Short=mPH1;
DE AltName: Full=Early development regulatory protein 1;
DE AltName: Full=RAE-28;
GN Name=Phc1; Synonyms=Edr, Edr1, Rae28;
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] (ISOFORMS 1; 2 AND 3), AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=8070621; DOI=10.1046/j.1432-0436.1994.5710039.x;
RA Nomura M., Takihara Y., Shimada K.;
RT "Isolation and characterization of retinoic acid-inducible cDNA clones in
RT F9 cells: one of the early inducible clones encodes a novel protein sharing
RT several highly homologous regions with a Drosophila polyhomeotic protein.";
RL Differentiation 57:39-50(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), AND INTERACTION WITH BMI1.
RC TISSUE=Embryo;
RX PubMed=9009205; DOI=10.1101/gad.11.2.226;
RA Alkema M.J., Bronk M., Verhoeven E., Otte A., van't Veer L.J., Berns A.,
RA van Lohuizen M.;
RT "Identification of Bmi1-interacting proteins as constituents of a
RT multimeric mammalian polycomb complex.";
RL Genes Dev. 11:226-240(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [5]
RP FUNCTION.
RX PubMed=9367423; DOI=10.1242/dev.124.19.3673;
RA Takihara Y., Tomotsune D., Shirai M., Katoh-Fukui Y., Nishii K.,
RA Motaleb M.A., Nomura M., Tsuchiya R., Fujita Y., Shibata Y.,
RA Higashinakagawa T., Shimada K.;
RT "Targeted disruption of the mouse homologue of the Drosophila polyhomeotic
RT gene leads to altered anteroposterior patterning and neural crest
RT defects.";
RL Development 124:3673-3682(1997).
RN [6]
RP DEVELOPMENTAL STAGE, AND INTERACTION WITH SCMH1.
RX PubMed=10653359; DOI=10.1046/j.1432-0436.1999.6540229.x;
RA Tomotsune D., Takihara Y., Berger J., Duhl D., Joo S., Kyba M., Shirai M.,
RA Ohta H., Matsuda Y., Honda B.M., Simon J., Shimada K., Brock H.W.,
RA Randazzo F.;
RT "A novel member of murine polycomb-group proteins, Sex comb on midleg
RT homolog protein, is highly conserved, and interacts with RAE28/mph1 in
RT vitro.";
RL Differentiation 65:229-239(1999).
RN [7]
RP INTERACTION WITH PHC2.
RX PubMed=16024804; DOI=10.1128/mcb.25.15.6694-6706.2005;
RA Isono K., Fujimura Y., Shinga J., Yamaki M., O-Wang J., Takihara Y.,
RA Murahashi Y., Takada Y., Mizutani-Koseki Y., Koseki H.;
RT "Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate
RT polycomb repression of Hox genes.";
RL Mol. Cell. Biol. 25:6694-6706(2005).
RN [8]
RP INTERACTION WITH RNF2 AND CBX7, AND TISSUE SPECIFICITY.
RX PubMed=22226355; DOI=10.1016/j.stem.2011.12.006;
RA Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A.,
RA Di Croce L.;
RT "Nonoverlapping functions of the Polycomb group Cbx family of proteins in
RT embryonic stem cells.";
RL Cell Stem Cell 10:47-62(2012).
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 Required for proper control of cellular levels of GMNN expression (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9367423}.
CC -!- SUBUNIT: Homodimer. Component of a PRC1-like complex (By similarity).
CC Interacts with the SAM domain of SCMH1 via its SAM domain in vitro
CC (PubMed:10653359). Interacts with RNF2 and CBX7 (PubMed:22226355).
CC Interacts with PHC2 (PubMed:16024804). Interacts with BMI1
CC (PubMed:9009205). {ECO:0000250|UniProtKB:P78364,
CC ECO:0000269|PubMed:10653359, ECO:0000269|PubMed:16024804,
CC ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:9009205}.
CC -!- INTERACTION:
CC Q64028; P49138: Mapkapk2; NbExp=2; IntAct=EBI-927346, EBI-298776;
CC Q64028; P23798: Pcgf2; NbExp=4; IntAct=EBI-927346, EBI-926857;
CC Q64028; Q9QWH1: Phc2; NbExp=2; IntAct=EBI-927346, EBI-642357;
CC Q64028; Q9CQJ4: Rnf2; NbExp=7; IntAct=EBI-927346, EBI-927321;
CC Q64028; Q8K214: Scmh1; NbExp=2; IntAct=EBI-927346, EBI-445955;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q64028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64028-2; Sequence=VSP_004040;
CC Name=3;
CC IsoId=Q64028-3; Sequence=VSP_004041;
CC Name=4;
CC IsoId=Q64028-4; Sequence=VSP_004038, VSP_004039;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis with lower levels in
CC most other tissues. Expressed in embryonic stem cells
CC (PubMed:22226355). {ECO:0000269|PubMed:22226355}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously in 8.5 dpc embryos. At 10.5
CC dpc, strongly expressed in pharyngeal arches and weakly expressed in
CC heart. By 14.5 dpc, expression is detected throughout the central
CC nervous system. {ECO:0000269|PubMed:10653359}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8070621}.
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DR EMBL; S73882; AAB31766.1; -; mRNA.
DR EMBL; S73883; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S73884; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U63386; AAC28974.1; -; mRNA.
DR EMBL; BC046535; AAH46535.1; -; mRNA.
DR EMBL; AK036370; BAC29400.1; -; mRNA.
DR RefSeq; NP_001258508.1; NM_001271579.1.
DR AlphaFoldDB; Q64028; -.
DR SMR; Q64028; -.
DR BioGRID; 199382; 13.
DR CORUM; Q64028; -.
DR DIP; DIP-456N; -.
DR IntAct; Q64028; 11.
DR MINT; Q64028; -.
DR STRING; 10090.ENSMUSP00000125580; -.
DR iPTMnet; Q64028; -.
DR PhosphoSitePlus; Q64028; -.
DR MaxQB; Q64028; -.
DR PaxDb; Q64028; -.
DR PRIDE; Q64028; -.
DR ProteomicsDB; 287923; -. [Q64028-1]
DR ProteomicsDB; 287924; -. [Q64028-2]
DR ProteomicsDB; 287925; -. [Q64028-3]
DR ProteomicsDB; 287926; -. [Q64028-4]
DR DNASU; 13619; -.
DR GeneID; 13619; -.
DR KEGG; mmu:13619; -.
DR CTD; 1911; -.
DR MGI; MGI:103248; Phc1.
DR eggNOG; ENOG502QUTP; Eukaryota.
DR InParanoid; Q64028; -.
DR OrthoDB; 298184at2759; -.
DR PhylomeDB; Q64028; -.
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; 13619; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Phc1; mouse.
DR PRO; PR:Q64028; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64028; protein.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0001739; C:sex chromatin; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
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:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI.
DR GO; GO:0016574; P:histone ubiquitination; ISS:UniProtKB.
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..1012
FT /note="Polyhomeotic-like protein 1"
FT /id="PRO_0000058376"
FT DOMAIN 948..1012
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 799..833
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78364"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78364"
FT MOD_RES 930
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78364"
FT CROSSLNK 771
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78364"
FT VAR_SEQ 76
FT /note="A -> V (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9009205"
FT /id="VSP_004038"
FT VAR_SEQ 77..1012
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9009205"
FT /id="VSP_004039"
FT VAR_SEQ 153..204
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8070621"
FT /id="VSP_004041"
FT VAR_SEQ 153..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8070621"
FT /id="VSP_004040"
FT CONFLICT 127
FT /note="T -> A (in Ref. 2; AAC28974)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="S -> W (in Ref. 2; AAC28974)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="I -> Y (in Ref. 1; AAB31766)"
FT /evidence="ECO:0000305"
FT CONFLICT 425..426
FT /note="Missing (in Ref. 4; BAC29400)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="E -> K (in Ref. 4; BAC29400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 106317 MW; 5DA12A87D0B5FDDB CRC64;
METESEQNSS STNGSSSSGA SSRPQIAQMS LYERQAVQAL QALQRQPNAA QYFHQFMLQQ
QLSNAQLHSL AAVQQATIAA SRQASSPNSS TAQQQTATTQ ASMNLATTSA AQLISRSQSV
SSPSATTLTQ SVLLGNTTSP PLNQSQAQMY LRPQLGNLLQ VNRTLGRNVP LASQLILMPN
GAVAAVQQEV PPAQSPGVHA DADQVQNLAV RNQQASAQGP QMPGSTQKAI PPGASPVSGL
SQTSSQALAV AQASSGASGQ SLNLSQAGGG SGNSLPGSMG PGGGGQAPGG LGQLPSSGLT
GGSCPRKGTG VVQPLPAAQT VTVSQGSQTE AESAAAKKAE ADGSGQQSVG MNLTRTATPA
PSQTLISSAT YTQIQPHSLI QQQQQIHLQQ KQVVIQQQIA IHHQQQFQHR QSQLLHTATH
LQLAQQQQQQ QQQQQQQQQQ QQQQQQQQGT TLTAPQPPQV PPTQQVPPSQ SQQQAQTLVV
QPMLQSSPLT LPPEPTSKPP IPIQSKPPVA PIKPPQLGAA KMSATQQPPP HIPVQVVGTR
QPGSAQAQAL GLAQLAAAVP TPRGITGAVQ PGQAHLASSP PSSQAAPGAL QECPPALAAG
MTLAPVQGTA HVVKGGPTAS SPVVAQVPAA FYMQSVHLPG KAQTLAVKRK AESEEERDDL
SALASVLPTK ASPAAESPKV IEEKNSLGEK AEPVASLNAN PPNSDLVALA PTPSAPPPTL
ALVSRQMGDS KPPQAIVKPQ ILTHIIEGFV IQEGAEPFPV GCSQFLKETE KPLQAGLPTG
LNESQPSGPL GGDSPSVELE KKANLLKCEY CGKYAPAEQF RGSKRFCSMT CAKRYNVSCS
HQFRLKRKKM KEFQEASYAR VRRRGPRRSS SDIARAKIQG KRHRGQEDSS RGSDNSSYDE
ALSPTSPGPL SVRAGHGERD LGNTITTPST PELQGINPVF LSSNPSQWSV EEVYEFIASL
QGCQEIAEEF RSQEIDGQAL LLLKEEHLMS AMNIKLGPAL KICAKINVLK ET
