Full text data of SFMBT2
SFMBT2
(KIAA1617)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Scm-like with four MBT domains protein 2; Scm-like with 4 MBT domains protein 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Scm-like with four MBT domains protein 2; Scm-like with 4 MBT domains protein 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00010970
IPI00010970 KIAA1617 protein KIAA1617 protein membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00010970 KIAA1617 protein KIAA1617 protein membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q5VUG0
ID SMBT2_HUMAN Reviewed; 894 AA.
AC Q5VUG0; A7MD09; Q9HCF5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 87.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH YY1; HISTONE H3K9ME2 AND HISTONE H4K20ME2,
RP AND 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
RT mbt 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
RT protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor of HOXB13 gene.
CC -!- SUBUNIT: Interacts with YY1. Interacts with methylated histones
CC H3K9me2 and H4K20me2, but not with H3K4me2, nor H3K9Ac.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Contains 4 MBT repeats.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13443.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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; AB046837; BAB13443.1; ALT_INIT; mRNA.
DR EMBL; AL590095; CAH73318.1; -; Genomic_DNA.
DR EMBL; AL139125; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL138771; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI19142.1; -; Genomic_DNA.
DR EMBL; AL138771; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL139125; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL139125; CAI18944.1; -; Genomic_DNA.
DR EMBL; AL138771; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL138771; CAI21746.1; -; Genomic_DNA.
DR EMBL; AL139125; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW86385.1; -; Genomic_DNA.
DR EMBL; BC152430; AAI52431.1; -; mRNA.
DR RefSeq; NP_001018049.1; NM_001018039.1.
DR RefSeq; NP_001025051.1; NM_001029880.2.
DR RefSeq; XP_005252607.1; XM_005252550.1.
DR UniGene; Hs.407983; -.
DR PDB; 1WJR; NMR; -; A=181-295.
DR PDBsum; 1WJR; -.
DR ProteinModelPortal; Q5VUG0; -.
DR SMR; Q5VUG0; 43-477, 824-885.
DR STRING; 9606.ENSP00000355109; -.
DR PhosphoSite; Q5VUG0; -.
DR DMDM; 67461560; -.
DR PaxDb; Q5VUG0; -.
DR PRIDE; Q5VUG0; -.
DR DNASU; 57713; -.
DR Ensembl; ENST00000361972; ENSP00000355109; ENSG00000198879.
DR Ensembl; ENST00000397167; ENSP00000380353; ENSG00000198879.
DR GeneID; 57713; -.
DR KEGG; hsa:57713; -.
DR UCSC; uc001ijn.2; human.
DR CTD; 57713; -.
DR GeneCards; GC10M007244; -.
DR H-InvDB; HIX0008624; -.
DR HGNC; HGNC:20256; SFMBT2.
DR HPA; HPA035448; -.
DR MIM; 615392; gene.
DR neXtProt; NX_Q5VUG0; -.
DR PharmGKB; PA134866013; -.
DR eggNOG; NOG316861; -.
DR HOGENOM; HOG000004859; -.
DR HOVERGEN; HBG085238; -.
DR InParanoid; Q5VUG0; -.
DR OMA; NFCRRVC; -.
DR OrthoDB; EOG780RKN; -.
DR EvolutionaryTrace; Q5VUG0; -.
DR GenomeRNAi; 57713; -.
DR NextBio; 64624; -.
DR PRO; PR:Q5VUG0; -.
DR ArrayExpress; Q5VUG0; -.
DR Bgee; Q5VUG0; -.
DR CleanEx; HS_SFMBT2; -.
DR Genevestigator; Q5VUG0; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR021987; DUF3588.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
DR Pfam; PF12140; DUF3588; 1.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Nucleus; Polymorphism;
KW Reference proteome; Repeat; Repressor.
FT CHAIN 1 894 Scm-like with four MBT domains protein 2.
FT /FTId=PRO_0000071969.
FT REPEAT 44 144 MBT 1.
FT REPEAT 152 256 MBT 2.
FT REPEAT 266 372 MBT 3.
FT REPEAT 380 477 MBT 4.
FT DOMAIN 824 887 SAM.
FT VARIANT 675 675 P -> R (in dbSNP:rs3740212).
FT /FTId=VAR_051362.
FT HELIX 182 185
FT STRAND 191 195
FT STRAND 203 207
FT STRAND 215 218
FT STRAND 231 234
FT TURN 243 245
FT HELIX 246 249
FT TURN 257 262
FT HELIX 265 281
FT HELIX 286 289
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
//
ID SMBT2_HUMAN Reviewed; 894 AA.
AC Q5VUG0; A7MD09; Q9HCF5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 87.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH YY1; HISTONE H3K9ME2 AND HISTONE H4K20ME2,
RP AND 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
RT mbt 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
RT protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor of HOXB13 gene.
CC -!- SUBUNIT: Interacts with YY1. Interacts with methylated histones
CC H3K9me2 and H4K20me2, but not with H3K4me2, nor H3K9Ac.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Contains 4 MBT repeats.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13443.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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; AB046837; BAB13443.1; ALT_INIT; mRNA.
DR EMBL; AL590095; CAH73318.1; -; Genomic_DNA.
DR EMBL; AL139125; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL138771; CAH73318.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI19142.1; -; Genomic_DNA.
DR EMBL; AL138771; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL139125; CAI19142.1; JOINED; Genomic_DNA.
DR EMBL; AL139125; CAI18944.1; -; Genomic_DNA.
DR EMBL; AL138771; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI18944.1; JOINED; Genomic_DNA.
DR EMBL; AL138771; CAI21746.1; -; Genomic_DNA.
DR EMBL; AL139125; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; AL158046; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; AL590095; CAI21746.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW86385.1; -; Genomic_DNA.
DR EMBL; BC152430; AAI52431.1; -; mRNA.
DR RefSeq; NP_001018049.1; NM_001018039.1.
DR RefSeq; NP_001025051.1; NM_001029880.2.
DR RefSeq; XP_005252607.1; XM_005252550.1.
DR UniGene; Hs.407983; -.
DR PDB; 1WJR; NMR; -; A=181-295.
DR PDBsum; 1WJR; -.
DR ProteinModelPortal; Q5VUG0; -.
DR SMR; Q5VUG0; 43-477, 824-885.
DR STRING; 9606.ENSP00000355109; -.
DR PhosphoSite; Q5VUG0; -.
DR DMDM; 67461560; -.
DR PaxDb; Q5VUG0; -.
DR PRIDE; Q5VUG0; -.
DR DNASU; 57713; -.
DR Ensembl; ENST00000361972; ENSP00000355109; ENSG00000198879.
DR Ensembl; ENST00000397167; ENSP00000380353; ENSG00000198879.
DR GeneID; 57713; -.
DR KEGG; hsa:57713; -.
DR UCSC; uc001ijn.2; human.
DR CTD; 57713; -.
DR GeneCards; GC10M007244; -.
DR H-InvDB; HIX0008624; -.
DR HGNC; HGNC:20256; SFMBT2.
DR HPA; HPA035448; -.
DR MIM; 615392; gene.
DR neXtProt; NX_Q5VUG0; -.
DR PharmGKB; PA134866013; -.
DR eggNOG; NOG316861; -.
DR HOGENOM; HOG000004859; -.
DR HOVERGEN; HBG085238; -.
DR InParanoid; Q5VUG0; -.
DR OMA; NFCRRVC; -.
DR OrthoDB; EOG780RKN; -.
DR EvolutionaryTrace; Q5VUG0; -.
DR GenomeRNAi; 57713; -.
DR NextBio; 64624; -.
DR PRO; PR:Q5VUG0; -.
DR ArrayExpress; Q5VUG0; -.
DR Bgee; Q5VUG0; -.
DR CleanEx; HS_SFMBT2; -.
DR Genevestigator; Q5VUG0; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR021987; DUF3588.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
DR Pfam; PF12140; DUF3588; 1.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00561; MBT; 4.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Nucleus; Polymorphism;
KW Reference proteome; Repeat; Repressor.
FT CHAIN 1 894 Scm-like with four MBT domains protein 2.
FT /FTId=PRO_0000071969.
FT REPEAT 44 144 MBT 1.
FT REPEAT 152 256 MBT 2.
FT REPEAT 266 372 MBT 3.
FT REPEAT 380 477 MBT 4.
FT DOMAIN 824 887 SAM.
FT VARIANT 675 675 P -> R (in dbSNP:rs3740212).
FT /FTId=VAR_051362.
FT HELIX 182 185
FT STRAND 191 195
FT STRAND 203 207
FT STRAND 215 218
FT STRAND 231 234
FT TURN 243 245
FT HELIX 246 249
FT TURN 257 262
FT HELIX 265 281
FT HELIX 286 289
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
//
MIM
615392
*RECORD*
*FIELD* NO
615392
*FIELD* TI
*615392 SCM-LIKE PROTEIN WITH 4 MBT DOMAINS 2; SFMBT2
;;KIAA1617
*FIELD* TX
DESCRIPTION
read more
SFMBTs, such as SFMBT2, are polycomb group proteins (see 610231) that
function as transcriptional repressors by binding to methylated lysines
in histone tails and inducing formation of transcription-resistant
higher-order chromatin structures at target genes (Lee et al., 2013).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SFMBT2, which they designated
KIAA1617. The transcript contains repetitive elements in its 3-prime
end. The deduced 904-amino acid protein shares significant homology with
a fly transcriptional repressor. RT-PCR ELISA detected highest SFMBT2
expression throughout adult brain and in adult kidney and ovary, with
moderate expression in adult liver, heart, and skeletal muscle and in
fetal liver and brain. Expression was low in lung, and little to no
expression was detected in pancreas and testis.
Wu et al. (2007) reported that the SFMBT proteins, including SFMBT2,
contain 4 tandem N-terminal MBT domains and a C-terminal sterile alpha
motif (SAM) domain. The MBT repeats were predicted to fold into a
propeller-like structure required for functional activity.
Using RT-PCR, Kuzmin et al. (2008) found that mouse Sfmbt2 has 2 start
sites and 2 stop sites. A short protein isoform was predicted to be
C-terminally truncated and to lack the SAM domain and 3 of the 4 MBT
repeats found in full-length Sfmbt2. At embryonic days 7.5 and 14.5,
promoter 1 was the dominant promoter, and both long and short variants
were expressed approximately equally in extraembryonic ectoderm,
ectoplacental cone, and placenta, with weaker expression in yolk sac.
All other embryonic tissues showed much weaker Sfmbt2 expression.
Using immunohistochemical analysis, Lee et al. (2013) found that
endogenous SFMBT2 localized to the nucleus of HEK293 cells.
GENE FUNCTION
Kuzmin et al. (2008) found that Sfmbt2 was expressed from the paternal
allele in mouse blastocysts and in mouse embryonic tissues early in
development. However, Sfmbt2 was biallelically expressed later during
mouse embryonic development. Both long and short isoforms of Sfmbt2
interacted with the YY1 (600013) transcription factor in a stable
protein complex in transfected cells.
By reciprocal coimmunoprecipitation analysis of epitope-tagged proteins,
Lee et al. (2013) found that human SFMBT2 interacted with YY1. SFMBT2
also bound to histones H3 (see 602810) and H4 (see 602822) when their
lysines were modified by repressive dimethylation and trimethylation.
SFMBT2 did not interact with histones H2A (see 613499) and H2B (see
609904), nor did it interact with histones H3 and H4 when they were
modified by activating marks. Overexpression of SFMBT2 in HEK293 cells
augmented YY1-dependent dependent transcriptional repression of a HOXB13
(604607) reporter. Chromatin immunoprecipitation analysis revealed that
SFMBT2 associated with dimethylated and trimethylated H3K9 and H4K20 and
with trimethylated H3K27 at the HOXB13 promoter in DU145 prostate cancer
cells. Knockdown of SFMBT2 expression via small interfering RNA
upregulated HOXB13 expression and decreased DU145 cell growth.
MAPPING
By PCR of a human-rodent hybrid panel, Nagase et al. (2000) mapped the
SFMBT2 gene to chromosome 10.
Hartz (2013) mapped the SFMBT2 gene to chromosome 10p14 based on an
alignment of the SFMBT2 sequence(GenBank GENBANK AB046837) with the
genomic sequence (GRCh37).
Kuzmin et al. (2008) stated that the mouse Sfmbt2 gene maps to
chromosome 2A1.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/29/2013.
2. Kuzmin, A.; Han, Z.; Golding, M. C.; Mann, M. R. W.; Latham, K.
E.; Varmuza, S.: The PcG gene Sfmbt2 is paternally expressed in extraembryonic
tissues. Gene Expr. Patterns 8: 107-116, 2008.
3. Lee, K.; Na, W.; Maeng, J.-H.; Wu, H.; Ju, B.-G.: Regulation of
DU145 prostate cancer cell growth by Scm-like with four mbt domains
2. J. Biosci. 38: 105-112, 2013.
4. Nagase, T.; Kikuno, R.; Nakayama, M.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 273-281, 2000.
5. Wu, S.; Trievel, R. C.; Rice, J. C.: Human SFMBT is a transcriptional
repressor protein that selectively binds the N-terminal tail of histone
H3. FEBS Lett. 581: 3289-3296, 2007.
*FIELD* CD
Patricia A. Hartz: 8/29/2013
*FIELD* ED
mgross: 08/30/2013
mgross: 8/29/2013
*RECORD*
*FIELD* NO
615392
*FIELD* TI
*615392 SCM-LIKE PROTEIN WITH 4 MBT DOMAINS 2; SFMBT2
;;KIAA1617
*FIELD* TX
DESCRIPTION
read more
SFMBTs, such as SFMBT2, are polycomb group proteins (see 610231) that
function as transcriptional repressors by binding to methylated lysines
in histone tails and inducing formation of transcription-resistant
higher-order chromatin structures at target genes (Lee et al., 2013).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned SFMBT2, which they designated
KIAA1617. The transcript contains repetitive elements in its 3-prime
end. The deduced 904-amino acid protein shares significant homology with
a fly transcriptional repressor. RT-PCR ELISA detected highest SFMBT2
expression throughout adult brain and in adult kidney and ovary, with
moderate expression in adult liver, heart, and skeletal muscle and in
fetal liver and brain. Expression was low in lung, and little to no
expression was detected in pancreas and testis.
Wu et al. (2007) reported that the SFMBT proteins, including SFMBT2,
contain 4 tandem N-terminal MBT domains and a C-terminal sterile alpha
motif (SAM) domain. The MBT repeats were predicted to fold into a
propeller-like structure required for functional activity.
Using RT-PCR, Kuzmin et al. (2008) found that mouse Sfmbt2 has 2 start
sites and 2 stop sites. A short protein isoform was predicted to be
C-terminally truncated and to lack the SAM domain and 3 of the 4 MBT
repeats found in full-length Sfmbt2. At embryonic days 7.5 and 14.5,
promoter 1 was the dominant promoter, and both long and short variants
were expressed approximately equally in extraembryonic ectoderm,
ectoplacental cone, and placenta, with weaker expression in yolk sac.
All other embryonic tissues showed much weaker Sfmbt2 expression.
Using immunohistochemical analysis, Lee et al. (2013) found that
endogenous SFMBT2 localized to the nucleus of HEK293 cells.
GENE FUNCTION
Kuzmin et al. (2008) found that Sfmbt2 was expressed from the paternal
allele in mouse blastocysts and in mouse embryonic tissues early in
development. However, Sfmbt2 was biallelically expressed later during
mouse embryonic development. Both long and short isoforms of Sfmbt2
interacted with the YY1 (600013) transcription factor in a stable
protein complex in transfected cells.
By reciprocal coimmunoprecipitation analysis of epitope-tagged proteins,
Lee et al. (2013) found that human SFMBT2 interacted with YY1. SFMBT2
also bound to histones H3 (see 602810) and H4 (see 602822) when their
lysines were modified by repressive dimethylation and trimethylation.
SFMBT2 did not interact with histones H2A (see 613499) and H2B (see
609904), nor did it interact with histones H3 and H4 when they were
modified by activating marks. Overexpression of SFMBT2 in HEK293 cells
augmented YY1-dependent dependent transcriptional repression of a HOXB13
(604607) reporter. Chromatin immunoprecipitation analysis revealed that
SFMBT2 associated with dimethylated and trimethylated H3K9 and H4K20 and
with trimethylated H3K27 at the HOXB13 promoter in DU145 prostate cancer
cells. Knockdown of SFMBT2 expression via small interfering RNA
upregulated HOXB13 expression and decreased DU145 cell growth.
MAPPING
By PCR of a human-rodent hybrid panel, Nagase et al. (2000) mapped the
SFMBT2 gene to chromosome 10.
Hartz (2013) mapped the SFMBT2 gene to chromosome 10p14 based on an
alignment of the SFMBT2 sequence(GenBank GENBANK AB046837) with the
genomic sequence (GRCh37).
Kuzmin et al. (2008) stated that the mouse Sfmbt2 gene maps to
chromosome 2A1.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/29/2013.
2. Kuzmin, A.; Han, Z.; Golding, M. C.; Mann, M. R. W.; Latham, K.
E.; Varmuza, S.: The PcG gene Sfmbt2 is paternally expressed in extraembryonic
tissues. Gene Expr. Patterns 8: 107-116, 2008.
3. Lee, K.; Na, W.; Maeng, J.-H.; Wu, H.; Ju, B.-G.: Regulation of
DU145 prostate cancer cell growth by Scm-like with four mbt domains
2. J. Biosci. 38: 105-112, 2013.
4. Nagase, T.; Kikuno, R.; Nakayama, M.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 273-281, 2000.
5. Wu, S.; Trievel, R. C.; Rice, J. C.: Human SFMBT is a transcriptional
repressor protein that selectively binds the N-terminal tail of histone
H3. FEBS Lett. 581: 3289-3296, 2007.
*FIELD* CD
Patricia A. Hartz: 8/29/2013
*FIELD* ED
mgross: 08/30/2013
mgross: 8/29/2013