SMBT2_HUMAN
ID SMBT2_HUMAN Reviewed; 894 AA.
AC Q5VUG0; A7MD09; Q9HCF5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Scm-like with four MBT domains protein 2;
DE Short=Scm-like with 4 MBT domains protein 2;
GN Name=SFMBT2; Synonyms=KIAA1617;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, INTERACTION WITH YY1; HISTONE H3K9ME2 AND HISTONE H4K20ME2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23385818; DOI=10.1007/s12038-012-9283-6;
RA Lee K., Na W., Maeng J.H., Wu H., Ju B.G.;
RT "Regulation of DU145 prostate cancer cell growth by Scm-like with four mbt
RT domains 2.";
RL J. Biosci. 38:105-112(2013).
RN [6]
RP STRUCTURE BY NMR OF 191-305.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 2nd MBT domain from human KIAA1617 protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor of HOXB13 gene.
CC {ECO:0000269|PubMed:23385818}.
CC -!- SUBUNIT: Interacts with YY1. Interacts with methylated histones H3K9me2
CC and H4K20me2, but not with H3K4me2, nor H3K9Ac.
CC {ECO:0000269|PubMed:23385818}.
CC -!- INTERACTION:
CC Q5VUG0; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-12025260, EBI-11985629;
CC Q5VUG0; O75608: LYPLA1; NbExp=3; IntAct=EBI-12025260, EBI-1052185;
CC Q5VUG0; P78364: PHC1; NbExp=4; IntAct=EBI-12025260, EBI-725403;
CC Q5VUG0; Q96GD3: SCMH1; NbExp=3; IntAct=EBI-12025260, EBI-713793;
CC Q5VUG0; Q9UN30-2: SCML1; NbExp=3; IntAct=EBI-12025260, EBI-12137487;
CC Q5VUG0; Q9UQR0: SCML2; NbExp=3; IntAct=EBI-12025260, EBI-2513111;
CC Q5VUG0; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-12025260, EBI-11522811;
CC Q5VUG0; Q8IX21: SLF2; NbExp=3; IntAct=EBI-12025260, EBI-2682240;
CC Q5VUG0; Q01664: TFAP4; NbExp=3; IntAct=EBI-12025260, EBI-2514218;
CC Q5VUG0; Q9C0C9: UBE2O; NbExp=8; IntAct=EBI-12025260, EBI-2339946;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23385818}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13443.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046837; BAB13443.1; ALT_INIT; mRNA.
DR EMBL; AL590095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86385.1; -; Genomic_DNA.
DR EMBL; BC152430; AAI52431.1; -; mRNA.
DR CCDS; CCDS31138.1; -.
DR RefSeq; NP_001018049.1; NM_001018039.1.
DR RefSeq; NP_001025051.1; NM_001029880.2.
DR RefSeq; XP_011517913.1; XM_011519611.1.
DR RefSeq; XP_016871955.1; XM_017016466.1.
DR PDB; 1WJR; NMR; -; A=182-295.
DR PDBsum; 1WJR; -.
DR AlphaFoldDB; Q5VUG0; -.
DR SMR; Q5VUG0; -.
DR BioGRID; 121736; 20.
DR IntAct; Q5VUG0; 16.
DR MINT; Q5VUG0; -.
DR STRING; 9606.ENSP00000380353; -.
DR iPTMnet; Q5VUG0; -.
DR PhosphoSitePlus; Q5VUG0; -.
DR BioMuta; SFMBT2; -.
DR DMDM; 67461560; -.
DR MassIVE; Q5VUG0; -.
DR MaxQB; Q5VUG0; -.
DR PaxDb; Q5VUG0; -.
DR PeptideAtlas; Q5VUG0; -.
DR PRIDE; Q5VUG0; -.
DR ProteomicsDB; 65417; -.
DR ABCD; Q5VUG0; 1 sequenced antibody.
DR Antibodypedia; 52040; 43 antibodies from 14 providers.
DR DNASU; 57713; -.
DR Ensembl; ENST00000361972.8; ENSP00000355109.4; ENSG00000198879.13.
DR Ensembl; ENST00000397167.6; ENSP00000380353.1; ENSG00000198879.13.
DR GeneID; 57713; -.
DR KEGG; hsa:57713; -.
DR MANE-Select; ENST00000397167.6; ENSP00000380353.1; NM_001387889.1; NP_001374818.1.
DR UCSC; uc001ijn.2; human.
DR CTD; 57713; -.
DR DisGeNET; 57713; -.
DR GeneCards; SFMBT2; -.
DR HGNC; HGNC:20256; SFMBT2.
DR HPA; ENSG00000198879; Tissue enhanced (brain).
DR MIM; 615392; gene.
DR neXtProt; NX_Q5VUG0; -.
DR OpenTargets; ENSG00000198879; -.
DR PharmGKB; PA134866013; -.
DR VEuPathDB; HostDB:ENSG00000198879; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000158123; -.
DR HOGENOM; CLU_005352_0_0_1; -.
DR InParanoid; Q5VUG0; -.
DR OMA; KMTSEWK; -.
DR OrthoDB; 237430at2759; -.
DR PhylomeDB; Q5VUG0; -.
DR TreeFam; TF316498; -.
DR PathwayCommons; Q5VUG0; -.
DR SignaLink; Q5VUG0; -.
DR BioGRID-ORCS; 57713; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; SFMBT2; human.
DR EvolutionaryTrace; Q5VUG0; -.
DR GenomeRNAi; 57713; -.
DR Pharos; Q5VUG0; Tdark.
DR PRO; PR:Q5VUG0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VUG0; protein.
DR Bgee; ENSG00000198879; Expressed in sural nerve and 165 other tissues.
DR ExpressionAtlas; Q5VUG0; baseline and differential.
DR Genevisible; Q5VUG0; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd09581; SAM_Scm-like-4MBT1_2; 1.
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; IPR037604; Scm-like-4MBT1/2_SAM.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF12140; SLED; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repeat; Repressor.
FT CHAIN 1..894
FT /note="Scm-like with four MBT domains protein 2"
FT /id="PRO_0000071969"
FT REPEAT 44..144
FT /note="MBT 1"
FT REPEAT 152..256
FT /note="MBT 2"
FT REPEAT 266..372
FT /note="MBT 3"
FT REPEAT 380..477
FT /note="MBT 4"
FT DOMAIN 824..887
FT /note="SAM"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..736
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 675
FT /note="P -> R (in dbSNP:rs3740212)"
FT /id="VAR_051362"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1WJR"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1WJR"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1WJR"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1WJR"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1WJR"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1WJR"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1WJR"
FT TURN 257..262
FT /evidence="ECO:0007829|PDB:1WJR"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:1WJR"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1WJR"
SQ SEQUENCE 894 AA; 100563 MW; 20EFF7F789F41787 CRC64;
MESTLSASNM QDPSSSPLEK CLGSANGNGD LDSEEGSSLE ETGFNWGEYL EETGASAAPH
TSFKHVEISI QSNFQPGMKL EVANKNNPDT YWVATIITTC GQLLLLRYCG YGEDRRADFW
CDVVIADLHP VGWCTQNNKV LMPPDAIKEK YTDWTEFLIR DLTGSRTAPA NLLEGPLRGK
GPIDLITVGS LIELQDSQNP FQYWIVSVIE NVGGRLRLRY VGLEDTESYD QWLFYLDYRL
RPVGWCQENK YRMDPPSEIY PLKMASEWKC TLEKSLIDAA KFPLPMEVFK DHADLRSHFF
TVGMKLETVN MCEPFYISPA SVTKVFNNHF FQVTIDDLRP EPSKLSMLCH ADSLGILPVQ
WCLKNGVSLT PPKGYSGQDF DWADYHKQHG AQEAPPFCFR NTSFSRGFTK NMKLEAVNPR
NPGELCVASV VSVKGRLMWL HLEGLQTPVP EVIVDVESMD IFPVGWCEAN SYPLTAPHKT
VSQKKRKIAV VQPEKQLPPT VPVKKIPHDL CLFPHLDTTG TVNGKYCCPQ LFINHRCFSG
PYLNKGRIAE LPQSVGPGKC VLVLKEVLSM IINAAYKPGR VLRELQLVED PHWNFQEETL
KAKYRGKTYR AVVKIVRTSD QVANFCRRVC AKLECCPNLF SPVLISENCP ENCSIHTKTK
YTYYYGKRKK ISKPPIGESN PDSGHPKPAR RRKRRKSIFV QKKRRSSAVD FTAGSGEESE
EEDADAMDDD TASEETGSEL RDDQTDTSSA EVPSARPRRA VTLRSGSEPV RRPPPERTRR
GRGAPAASSA EEGEKCPPTK PEGTEDTKQE EEERLVLESN PLEWTVTDVV RFIKLTDCAP
LAKIFQEQDI DGQALLLLTL PTVQECMELK LGPAIKLCHQ IERVKVAFYA QYAN
