SCMH1_MOUSE
ID SCMH1_MOUSE Reviewed; 706 AA.
AC Q8K214; B1AS51; Q9JME0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Polycomb protein SCMH1;
DE AltName: Full=Sex comb on midleg homolog 1;
GN Name=Scmh1 {ECO:0000312|MGI:MGI:1352762};
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] {ECO:0000305, ECO:0000312|EMBL:BAA90554.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION, AND INTERACTION WITH PHC1.
RC TISSUE=Brain {ECO:0000269|PubMed:10653359}, and
RC Neonatal brain {ECO:0000269|PubMed:10653359};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH34667.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH34667.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH34667.1};
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).
CC -!- FUNCTION: Associates with Polycomb group (PcG) multiprotein complexes;
CC the complex class is required to maintain the transcriptionally
CC repressive state of some genes. {ECO:0000250}.
CC -!- SUBUNIT: Associates with a PRC1-like complex (By similarity). Interacts
CC with the SAM domain of PHC1 via its SAM domain in vitro. {ECO:0000250,
CC ECO:0000269|PubMed:10653359}.
CC -!- INTERACTION:
CC Q8K214; O88513: Gmnn; NbExp=2; IntAct=EBI-445955, EBI-445922;
CC Q8K214; Q64028: Phc1; NbExp=2; IntAct=EBI-445955, EBI-927346;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q8K214-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10653359};
CC IsoId=Q8K214-2; Sequence=VSP_051680, VSP_051681;
CC -!- TISSUE SPECIFICITY: Most abundant in testis. Moderate levels detected
CC in heart, brain, lung, liver, skeletal muscle and kidney and lower
CC levels in spleen. {ECO:0000269|PubMed:10653359}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout embryogenesis. Expressed
CC ubiquitously in 8.5 dpc embryos. At 10.5 dpc, strongly expressed in
CC nervous system including hindbrain and spinal cord, and in the
CC pharyngeal arches and visceral organs. By 14.5 dpc, strong expression
CC is detected throughout the central nervous system, and in tongue,
CC heart, midgut and urogenital regions. {ECO:0000269|PubMed:10653359}.
CC -!- INDUCTION: By retinoic acid in F9 and F19 embryonal carcinoma cell
CC lines. {ECO:0000269|PubMed:10653359}.
CC -!- SIMILARITY: Belongs to the SCM family. {ECO:0000305}.
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DR EMBL; AB030906; BAA90554.1; -; mRNA.
DR EMBL; AL611924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034667; AAH34667.1; -; mRNA.
DR CCDS; CCDS18589.1; -. [Q8K214-2]
DR CCDS; CCDS51292.1; -. [Q8K214-1]
DR RefSeq; NP_001153102.1; NM_001159630.1. [Q8K214-1]
DR RefSeq; NP_038911.1; NM_013883.2. [Q8K214-2]
DR RefSeq; XP_011238853.1; XM_011240551.1.
DR RefSeq; XP_017175741.1; XM_017320252.1. [Q8K214-2]
DR RefSeq; XP_017175742.1; XM_017320253.1. [Q8K214-2]
DR AlphaFoldDB; Q8K214; -.
DR SMR; Q8K214; -.
DR BioGRID; 205936; 5.
DR DIP; DIP-32567N; -.
DR IntAct; Q8K214; 5.
DR STRING; 10090.ENSMUSP00000101908; -.
DR iPTMnet; Q8K214; -.
DR PhosphoSitePlus; Q8K214; -.
DR EPD; Q8K214; -.
DR MaxQB; Q8K214; -.
DR PaxDb; Q8K214; -.
DR PeptideAtlas; Q8K214; -.
DR PRIDE; Q8K214; -.
DR ProteomicsDB; 256927; -. [Q8K214-1]
DR ProteomicsDB; 256928; -. [Q8K214-2]
DR Antibodypedia; 32169; 230 antibodies from 24 providers.
DR DNASU; 29871; -.
DR Ensembl; ENSMUST00000000087; ENSMUSP00000000087; ENSMUSG00000000085. [Q8K214-2]
DR Ensembl; ENSMUST00000064991; ENSMUSP00000069813; ENSMUSG00000000085. [Q8K214-1]
DR Ensembl; ENSMUST00000106298; ENSMUSP00000101905; ENSMUSG00000000085. [Q8K214-2]
DR Ensembl; ENSMUST00000106301; ENSMUSP00000101908; ENSMUSG00000000085. [Q8K214-1]
DR GeneID; 29871; -.
DR KEGG; mmu:29871; -.
DR UCSC; uc008und.2; mouse. [Q8K214-2]
DR UCSC; uc008une.2; mouse. [Q8K214-1]
DR CTD; 22955; -.
DR MGI; MGI:1352762; Scmh1.
DR VEuPathDB; HostDB:ENSMUSG00000000085; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000157999; -.
DR HOGENOM; CLU_015000_1_1_1; -.
DR InParanoid; Q8K214; -.
DR OMA; AMFDREQ; -.
DR OrthoDB; 229086at2759; -.
DR PhylomeDB; Q8K214; -.
DR TreeFam; TF106488; -.
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 BioGRID-ORCS; 29871; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Scmh1; mouse.
DR PRO; PR:Q8K214; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K214; protein.
DR Bgee; ENSMUSG00000000085; Expressed in saccule of membranous labyrinth and 248 other tissues.
DR ExpressionAtlas; Q8K214; baseline and differential.
DR Genevisible; Q8K214; MM.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR033763; SCML2_RBR.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
DR Pfam; PF02820; MBT; 2.
DR Pfam; PF17208; RBR; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF12140; SLED; 1.
DR SMART; SM00561; MBT; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..706
FT /note="Polycomb protein SCMH1"
FT /id="PRO_0000114335"
FT REPEAT 28..126
FT /note="MBT 1"
FT REPEAT 134..235
FT /note="MBT 2"
FT DOMAIN 597..662
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 233..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 662..664
FT /note="VFW -> GKF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10653359"
FT /id="VSP_051680"
FT VAR_SEQ 665..706
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10653359"
FT /id="VSP_051681"
SQ SEQUENCE 706 AA; 78669 MW; CC7531B46A439E39 CRC64;
MLVCYSVLAC ESLWDLPCSI MGSPLGHFTW DKYLKETCSV PAPVHCFKQS YTPPSNEFKI
SMKLEAQDPR NTTSTCIATV VGLTGARLRL RLDGSDNKND FWRLVDSSEI QPIGNCEKNG
GMLQPPLGFR LNASSWPMFL LKTLNGAEMA PIKIFHKEPP SPSHNFFKMG MKLEAVDRKN
PHFICPATIG EVRGAEVLVT FDGWRGAFDY WCRFDSRDIF PVGWCSLTGD NLQPPGTKVV
IPKNPSPSSD VSTEKPSIHS TKTVLEHQPG QRGRKPGKKR GRTPKILIPH PTSTPSKSAE
PLKFPKKRGP KPGSKRKPRT LLSPPPTSPT TSTPEPDTST VPQDAATVPS SAMQAPTVCI
YLNKSGSTGP HLDKKKIQQL PDHFGPARAS VVLQQAVQAC IDCAYHQKTV FSFLKQGHGG
EVISAVFDRE QHTLNLPAVN SITYVLRFLE KLCHNLRSDN LFGNQPFTQT HLSLTATEYN
HNHDRYLPGE TFVLGNSLAR SLETHSDLMD SALKPANLVS TSQNLRTPGY RPLLPSCGLP
LSTVSAVRRL CSKGVLKGKK ERRDVESFWK LNHSPGSDRH LESRDPPRLS GRDPSSWTVE
DVMQFVREAD PQLGSHADLF RKHEIDGKAL LLLRSDMMMK YMGLKLGPAL KLSFHIDRLK
QVFWKRETIL WSREGLSREV WPISEDTALG HFFSGMDKVF GSLSKR
