ID SCMH1_HUMAN Reviewed; 660 AA. AC Q96GD3; B4DRQ8; Q5VT76; Q6IAJ4; Q8WU48; Q9UKM5; Q9UKM6; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 191. DE RecName: Full=Polycomb protein SCMH1; DE AltName: Full=Sex comb on midleg homolog 1; GN Name=SCMH1 {ECO:0000312|EMBL:CAH72793.1}; 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] {ECO:0000305, ECO:0000312|EMBL:AAF01150.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), AND TISSUE SPECIFICITY. RC TISSUE=Heart {ECO:0000312|EMBL:AAF01150.1}, and Skeletal muscle RC {ECO:0000269|PubMed:10524249}; RX PubMed=10524249; DOI=10.1016/s0378-1119(99)00285-1; RA Berger J., Kurahashi H., Takihara Y., Shimada K., Brock H.W., Randazzo F.; RT "The human homolog of Sex comb on midleg (SCMH1) maps to chromosome 1p34."; RL Gene 237:185-191(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Tongue; 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 [3] {ECO:0000305, ECO:0000312|EMBL:CAG33442.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Fetal brain; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2). RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH21252.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Eye {ECO:0000312|EMBL:AAH21252.1}, and Muscle RC {ECO:0000312|EMBL:AAH09752.1}; 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). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH A PRC1-LIKE RP COMPLEX. 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). 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: Interacts with the SAM domain of PHC1 via its SAM domain in CC vitro (By similarity). Associates with a PRC1-like complex. CC {ECO:0000250}. CC -!- INTERACTION: CC Q96GD3; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-713793, EBI-744820; CC Q96GD3; P43365: MAGEA12; NbExp=3; IntAct=EBI-713793, EBI-749530; CC Q96GD3; Q9UHJ3: SFMBT1; NbExp=3; IntAct=EBI-713793, EBI-747398; CC Q96GD3; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-713793, EBI-12025260; CC Q96GD3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-713793, EBI-741480; CC Q96GD3; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-713793, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q96GD3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96GD3-2; Sequence=VSP_051676, VSP_051679; CC Name=3; CC IsoId=Q96GD3-3; Sequence=VSP_051678; CC Name=4 {ECO:0000269|PubMed:10524249}; CC IsoId=Q96GD3-4; Sequence=VSP_051677, VSP_051679; CC Name=5 {ECO:0000269|PubMed:10524249}; CC IsoId=Q96GD3-5; Sequence=VSP_051678, VSP_051679; CC Name=6; CC IsoId=Q96GD3-6; Sequence=VSP_051677, VSP_043395, VSP_051679; CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, muscle and pancreas. CC Weakly expressed in brain, placenta, lung, liver and kidney. CC {ECO:0000269|PubMed:10524249}. CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention. CC {ECO:0000303|PubMed:10524249}. CC -!- SIMILARITY: Belongs to the SCM family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF149045; AAF01150.1; -; mRNA. DR EMBL; AF149046; AAF01151.1; -; mRNA. DR EMBL; AK299383; BAG61370.1; -; mRNA. DR EMBL; CR457161; CAG33442.1; -; mRNA. DR EMBL; BX640721; CAE45840.1; -; mRNA. DR EMBL; AL110502; CAI22109.1; -; Genomic_DNA. DR EMBL; AL391730; CAI22109.1; JOINED; Genomic_DNA. DR EMBL; AL110502; CAI22110.1; -; Genomic_DNA. DR EMBL; AL391730; CAI22110.1; JOINED; Genomic_DNA. DR EMBL; AL110502; CAI22111.1; -; Genomic_DNA. DR EMBL; AL391730; CAI22111.1; JOINED; Genomic_DNA. DR EMBL; AL606484; CAI22111.1; JOINED; Genomic_DNA. DR EMBL; AL110502; CAI22112.1; -; Genomic_DNA. DR EMBL; AL391730; CAI22112.1; JOINED; Genomic_DNA. DR EMBL; AL110502; CAI22113.1; -; Genomic_DNA. DR EMBL; AL391730; CAI22113.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72791.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72791.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72793.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72793.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72794.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72794.1; JOINED; Genomic_DNA. DR EMBL; AL606484; CAH72794.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72795.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72795.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72796.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72796.1; JOINED; Genomic_DNA. DR EMBL; AL606484; CAH72242.1; -; Genomic_DNA. DR EMBL; AL110502; CAH72242.1; JOINED; Genomic_DNA. DR EMBL; AL391730; CAH72242.1; JOINED; Genomic_DNA. DR EMBL; BC009752; AAH09752.1; -; mRNA. DR EMBL; BC021252; AAH21252.1; -; mRNA. DR CCDS; CCDS30688.1; -. [Q96GD3-1] DR CCDS; CCDS461.1; -. [Q96GD3-4] DR CCDS; CCDS53301.1; -. [Q96GD3-5] DR CCDS; CCDS53302.1; -. [Q96GD3-3] DR CCDS; CCDS53303.1; -. [Q96GD3-6] DR CCDS; CCDS53304.1; -. [Q96GD3-2] DR RefSeq; NP_001026864.1; NM_001031694.3. [Q96GD3-1] DR RefSeq; NP_001165689.1; NM_001172218.2. [Q96GD3-5] DR RefSeq; NP_001165690.1; NM_001172219.2. [Q96GD3-2] DR RefSeq; NP_001165691.1; NM_001172220.2. [Q96GD3-5] DR RefSeq; NP_001165692.1; NM_001172221.3. [Q96GD3-3] DR RefSeq; NP_001165693.1; NM_001172222.3. [Q96GD3-6] DR RefSeq; NP_001381229.1; NM_001394300.1. [Q96GD3-1] DR RefSeq; NP_001381230.1; NM_001394301.1. [Q96GD3-1] DR RefSeq; NP_001381231.1; NM_001394302.1. [Q96GD3-1] DR RefSeq; NP_001381232.1; NM_001394303.1. [Q96GD3-3] DR RefSeq; NP_036368.1; NM_012236.4. [Q96GD3-4] DR RefSeq; XP_047305523.1; XM_047449567.1. [Q96GD3-1] DR RefSeq; XP_047305524.1; XM_047449568.1. [Q96GD3-2] DR RefSeq; XP_047305534.1; XM_047449578.1. [Q96GD3-3] DR RefSeq; XP_047305539.1; XM_047449583.1. [Q96GD3-3] DR RefSeq; XP_054191196.1; XM_054335221.1. [Q96GD3-1] DR RefSeq; XP_054191197.1; XM_054335222.1. [Q96GD3-2] DR RefSeq; XP_054191200.1; XM_054335225.1. [Q96GD3-3] DR RefSeq; XP_054191201.1; XM_054335226.1. [Q96GD3-3] DR PDB; 2P0K; X-ray; 1.75 A; A=27-238. DR AlphaFoldDB; Q96GD3; -. DR SMR; Q96GD3; -. DR BioGRID; 116609; 57. DR CORUM; Q96GD3; -. DR FunCoup; Q96GD3; 1243. DR IntAct; Q96GD3; 47. DR MINT; Q96GD3; -. DR STRING; 9606.ENSP00000318094; -. DR DrugBank; DB03345; Mercaptoethanol. DR GlyGen; Q96GD3; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q96GD3; -. DR PhosphoSitePlus; Q96GD3; -. DR BioMuta; SCMH1; -. DR DMDM; 60390956; -. DR jPOST; Q96GD3; -. DR MassIVE; Q96GD3; -. DR PaxDb; 9606-ENSP00000318094; -. DR PeptideAtlas; Q96GD3; -. DR ProteomicsDB; 76617; -. [Q96GD3-1] DR ProteomicsDB; 76618; -. [Q96GD3-2] DR ProteomicsDB; 76619; -. [Q96GD3-3] DR ProteomicsDB; 76620; -. [Q96GD3-4] DR ProteomicsDB; 76621; -. [Q96GD3-5] DR ProteomicsDB; 76622; -. [Q96GD3-6] DR Pumba; Q96GD3; -. DR ABCD; Q96GD3; 1 sequenced antibody. DR Antibodypedia; 32169; 231 antibodies from 24 providers. DR DNASU; 22955; -. DR Ensembl; ENST00000326197.11; ENSP00000318094.7; ENSG00000010803.19. [Q96GD3-1] DR Ensembl; ENST00000337495.9; ENSP00000337352.5; ENSG00000010803.19. [Q96GD3-2] DR Ensembl; ENST00000372595.5; ENSP00000361676.1; ENSG00000010803.19. [Q96GD3-3] DR Ensembl; ENST00000372596.5; ENSP00000361677.1; ENSG00000010803.19. [Q96GD3-5] DR Ensembl; ENST00000372597.5; ENSP00000361678.1; ENSG00000010803.19. [Q96GD3-4] DR Ensembl; ENST00000456518.3; ENSP00000403974.2; ENSG00000010803.19. [Q96GD3-6] DR GeneID; 22955; -. DR KEGG; hsa:22955; -. DR UCSC; uc001cgp.4; human. [Q96GD3-1] DR AGR; HGNC:19003; -. DR ClinPGx; PA134870272; -. DR CTD; 22955; -. DR DisGeNET; 22955; -. DR GeneCards; SCMH1; -. DR HGNC; HGNC:19003; SCMH1. DR HPA; ENSG00000010803; Low tissue specificity. DR MIM; 616396; gene. DR OpenTargets; ENSG00000010803; -. DR VEuPathDB; HostDB:ENSG00000010803; -. DR eggNOG; KOG3766; Eukaryota. DR GeneTree; ENSGT00940000157999; -. DR HOGENOM; CLU_015000_1_1_1; -. DR InParanoid; Q96GD3; -. DR OMA; NKEFCSM; -. DR OrthoDB; 5912862at2759; -. DR PAN-GO; Q96GD3; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q96GD3; -. DR PathwayCommons; Q96GD3; -. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. [Q96GD3-2] DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. [Q96GD3-2] DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. [Q96GD3-2] DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. [Q96GD3-2] DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. [Q96GD3-2] DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins. [Q96GD3-2] DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. [Q96GD3-2] DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. [Q96GD3-2] DR Reactome; R-HSA-9976102; Differentiation of naive CD4+ T cells to T helper 2 cells (Th2 cells). [Q96GD3-2] DR SignaLink; Q96GD3; -. DR Agora; ENSG00000010803; -. DR BioGRID-ORCS; 22955; 16 hits in 1165 CRISPR screens. DR ChiTaRS; SCMH1; human. DR EvolutionaryTrace; Q96GD3; -. DR GeneWiki; SCMH1; -. DR GenomeRNAi; 22955; -. DR Pharos; Q96GD3; Tbio. DR PRO; PR:Q96GD3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96GD3; protein. DR Bgee; ENSG00000010803; Expressed in lower esophagus muscularis layer and 176 other cell types or tissues. DR ExpressionAtlas; Q96GD3; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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:0031507; P:heterochromatin formation; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd20105; MBT_SCMH1_rpt1; 1. DR CDD; cd20108; MBT_SCMH1_rpt2; 1. DR CDD; cd09578; SAM_Scm; 1. DR FunFam; 1.10.150.50:FF:000018; Polycomb protein scmh1 isoform 4; 1. DR FunFam; 3.90.1150.190:FF:000001; Polycomb protein scmh1 isoform 4; 1. DR FunFam; 2.30.30.140:FF:000016; polycomb protein SCMH1 isoform X1; 1. DR Gene3D; 2.30.30.140; -; 2. DR Gene3D; 3.90.1150.190; SLED domain; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR004092; Mbt. DR InterPro; IPR047279; MBT_SCMH1_rpt1. DR InterPro; IPR047280; MBT_SCMH1_rpt2. DR InterPro; IPR050548; PcG_chromatin_remod_factors. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR047531; SAM_Scm-like. DR InterPro; IPR033763; SCML2_RBR. DR InterPro; IPR021987; SLED. DR InterPro; IPR038348; SLED_sf. DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR12247:SF68; POLYCOMB PROTEIN SCMH1; 1. 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; SAM/Pointed domain; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2. DR PROSITE; PS51079; MBT; 2. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PDBsum; 2P0K; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Developmental protein; Nucleus; KW Proteomics identification; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..660 FT /note="Polycomb protein SCMH1" FT /id="PRO_0000114334" FT REPEAT 28..126 FT /note="MBT 1" FT REPEAT 134..235 FT /note="MBT 2" FT DOMAIN 593..658 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT REGION 233..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 273..284 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 305..320 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 330..343 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..61 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10524249, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.3" FT /id="VSP_051678" FT VAR_SEQ 1..48 FT /note="MLVCYSVLACEILWDLPCSIMGSPLGHFTWDKYLKETCSVPAPVHCFK -> FT M (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:10524249, FT ECO:0000303|PubMed:14702039" FT /id="VSP_051677" FT VAR_SEQ 1..24 FT /note="MLVCYSVLACEILWDLPCSIMGSP -> MQPNVIDWSDVRKHKYGHLSESAS FT QYQEAADILD (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_051676" FT VAR_SEQ 128..238 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043395" FT VAR_SEQ 550..571 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:10524249, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005" FT /id="VSP_051679" FT CONFLICT 463 FT /note="F -> L (in Ref. 3)" FT /evidence="ECO:0000305" FT HELIX 30..36 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 71..84 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 136..144 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:2P0K" FT TURN 205..208 FT /evidence="ECO:0007829|PDB:2P0K" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:2P0K" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:2P0K" SQ SEQUENCE 660 AA; 73354 MW; 6544DD484DA8D037 CRC64; MLVCYSVLAC EILWDLPCSI MGSPLGHFTW DKYLKETCSV PAPVHCFKQS YTPPSNEFKI SMKLEAQDPR NTTSTCIATV VGLTGARLRL RLDGSDNKND FWRLVDSAEI QPIGNCEKNG GMLQPPLGFR LNASSWPMFL LKTLNGAEMA PIRIFHKEPP SPSHNFFKMG MKLEAVDRKN PHFICPATIG EVRGSEVLVT FDGWRGAFDY WCRFDSRDIF PVGWCSLTGD NLQPPGTKVV IPKNPYPASD VNTEKPSIHS STKTVLEHQP GQRGRKPGKK RGRTPKTLIS HPISAPSKTA EPLKFPKKRG PKPGSKRKPR TLLNPPPASP TTSTPEPDTS TVPQDAATIP SSAMQAPTVC IYLNKNGSTG PHLDKKKVQQ LPDHFGPARA SVVLQQAVQA CIDCAYHQKT VFSFLKQGHG GEVISAVFDR EQHTLNLPAV NSITYVLRFL EKLCHNLRSD NLFGNQPFTQ THLSLTAIEY SHSHDRYLPG ETFVLGNSLA RSLEPHSDSM DSASNPTNLV STSQRHRPLL SSCGLPPSTA SAVRRLCSRG VLKGSNERRD MESFWKLNRS PGSDRYLESR DASRLSGRDP SSWTVEDVMQ FVREADPQLG PHADLFRKHE IDGKALLLLR SDMMMKYMGL KLGPALKLSY HIDRLKQGKF //