ID SCMH1_HUMAN Reviewed; 660 AA. AC Q96GD3; Q5VT76; Q6IAJ4; Q8WU48; Q9UKM5; Q9UKM6; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 05-OCT-2010, entry version 75. DE RecName: Full=Polycomb protein SCMH1; DE AltName: Full=Sex comb on midleg homolog 1; GN Name=SCMH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), AND TISSUE SPECIFICITY. RC TISSUE=Heart, and Skeletal muscle; RX MEDLINE=99453774; PubMed=10524249; DOI=10.1016/S0378-1119(99)00285-1; RA Berger J., Kurahashi H., Takihara Y., Shimada K., Brock H.W., RA Randazzo F.; RT "The human homolog of Sex comb on midleg (SCMH1) maps to chromosome RT 1p34."; RL Gene 237:185-191(1999). RN [2] 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 [3] 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Eye, and Muscle; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE PRC1 RP COMPLEX WITH PCGF2; BMI1; CBX2; CBX4; CBX8; PHC1; PHC2; PHC3; RING1 RP AND RNF2. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). CC -!- FUNCTION: Component of the Polycomb group (PcG) multiprotein PRC1 CC complex, a complex 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 CC histone H2A 'Lys-119', rendering chromatin heritably changed in CC its expressibility. CC -!- SUBUNIT: Interacts with the SAM domain of PHC1 via its SAM domain CC in vitro (By similarity). Component of chromatin-associated class CC II PcG repressive complex 1 (PRC1/hPRC-H) at least composed of CC PCGF2/RNF110, BMI1/PCGF4, CBX2/M33, CBX4/PC2, CBX8/PC3, PHC1, CC PHC2, PHC3, SCMH1, RING1 and RNF2/RING2. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q96GD3-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; CC IsoId=Q96GD3-2; Sequence=VSP_051676, VSP_051679; CC Note=Gene prediction confirmed by EST data; CC Name=3; CC IsoId=Q96GD3-3; Sequence=VSP_051678; CC Name=4; CC IsoId=Q96GD3-4; Sequence=VSP_051677, VSP_051679; CC Name=5; CC IsoId=Q96GD3-5; Sequence=VSP_051678, VSP_051679; CC Note=May be due to intron retention; CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, muscle and CC pancreas. Weakly expressed in brain, placenta, lung, liver and CC kidney. CC -!- SIMILARITY: Belongs to the SCM family. CC -!- SIMILARITY: Contains 2 MBT repeats. CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF149045; AAF01150.1; -; mRNA. DR EMBL; AF149046; AAF01151.1; -; 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 IPI; IPI00187110; -. DR IPI; IPI00396653; -. DR IPI; IPI00479699; -. DR IPI; IPI00552451; -. DR IPI; IPI00552650; -. DR RefSeq; NP_001026864.1; -. DR RefSeq; NP_001165689.1; -. DR RefSeq; NP_001165690.1; -. DR RefSeq; NP_001165691.1; -. DR RefSeq; NP_001165692.1; -. DR RefSeq; NP_001165693.1; -. DR RefSeq; NP_036368.1; -. DR UniGene; Hs.571874; -. DR PDB; 2P0K; X-ray; 1.75 A; A=27-238. DR PDBsum; 2P0K; -. DR ProteinModelPortal; Q96GD3; -. DR SMR; Q96GD3; 590-655. DR IntAct; Q96GD3; 9. DR MINT; MINT-1422768; -. DR STRING; Q96GD3; -. DR PhosphoSite; Q96GD3; -. DR PRIDE; Q96GD3; -. DR Ensembl; ENST00000326197; ENSP00000318094; ENSG00000010803. DR Ensembl; ENST00000397174; ENSP00000380359; ENSG00000010803. DR GeneID; 22955; -. DR KEGG; hsa:22955; -. DR UCSC; uc001cgo.1; human. DR UCSC; uc001cgp.1; human. DR UCSC; uc001cgq.1; human. DR CTD; 22955; -. DR GeneCards; GC01M041527; -. DR HGNC; HGNC:19003; SCMH1. DR PharmGKB; PA134870272; -. DR eggNOG; prNOG10632; -. DR HOGENOM; HBG443740; -. DR HOVERGEN; HBG056406; -. DR InParanoid; Q96GD3; -. DR OMA; TATEYSH; -. DR PhylomeDB; Q96GD3; -. DR NextBio; 43747; -. DR ArrayExpress; Q96GD3; -. DR Bgee; Q96GD3; -. DR CleanEx; HS_SCMH1; -. DR Genevestigator; Q96GD3; -. DR GermOnline; ENSG00000010803; Homo sapiens. DR GO; GO:0005634; C:nucleus; IC:UniProtKB. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0016564; F:transcription repressor activity; IC:UniProtKB. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0016458; P:gene silencing; ISS:UniProtKB. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR021987; DUF3588. DR InterPro; IPR004092; Mbt. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM_type. DR InterPro; IPR021129; SAM_type1. DR InterPro; IPR010993; Sterile_alpha_motif_homology. DR Gene3D; G3DSA:1.10.150.50; SAM_type; 1. DR Pfam; PF12140; DUF3588; 1. DR Pfam; PF02820; MBT; 2. DR Pfam; PF00536; SAM_1; 1. DR SMART; SM00561; MBT; 2. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SAM_homology; 1. DR PROSITE; PS51079; MBT; 2. DR PROSITE; PS50105; SAM_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Developmental protein; Nucleus; Phosphoprotein; Repeat; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 660 Polycomb protein SCMH1. FT /FTId=PRO_0000114334. FT REPEAT 28 126 MBT 1. FT REPEAT 134 235 MBT 2. FT DOMAIN 593 658 SAM. FT MOD_RES 649 649 Phosphoserine. FT VAR_SEQ 1 61 Missing (in isoform 3 and isoform 5). FT /FTId=VSP_051678. FT VAR_SEQ 1 48 MLVCYSVLACEILWDLPCSIMGSPLGHFTWDKYLKETCSVP FT APVHCFK -> M (in isoform 4). FT /FTId=VSP_051677. FT VAR_SEQ 1 24 MLVCYSVLACEILWDLPCSIMGSP -> MQPNVIDWSDVRK FT HKYGHLSESASQYQEAADILD (in isoform 2). FT /FTId=VSP_051676. FT VAR_SEQ 550 571 Missing (in isoform 2, isoform 4 and FT isoform 5). FT /FTId=VSP_051679. FT CONFLICT 463 463 F -> L (in Ref. 2). FT HELIX 30 36 FT HELIX 44 46 FT STRAND 47 49 FT STRAND 63 68 FT STRAND 71 84 FT STRAND 87 92 FT STRAND 101 104 FT HELIX 115 118 FT HELIX 133 135 FT HELIX 136 144 FT HELIX 152 154 FT STRAND 172 176 FT STRAND 184 193 FT STRAND 196 201 FT TURN 205 208 FT STRAND 210 213 FT HELIX 224 228 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 //