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Q9UHJ3 (SMBT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Scm-like with four MBT domains protein 1

Short name=hSFMBT
Alternative name(s):
Renal ubiquitous protein 1
Gene names
Name:SFMBT1
Synonyms:RU1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length866 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis. Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with MYOD1 By similarity. Component of the SLC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and RCOR1/CoREST. Ref.8 Ref.10 Ref.11

Subcellular location

Nucleus Ref.8.

Tissue specificity

Expressed in all cell lines and normal tissues tested, including the thymus. Ref.1

Domain

The MBT repeats mediate binding to histones tails; however, in contrast to other MBT repeats, does not bind specific histone lysine modifications. The MBT repeats lack the conserved Asp and aromatic cage at conserved positions (Ref.10).

Sequence similarities

Contains 4 MBT repeats.

Contains 1 SAM (sterile alpha motif) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST3H3Q166954EBI-747398,EBI-358900

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHJ3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UHJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     778-820: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 866866Scm-like with four MBT domains protein 1
PRO_0000071966

Regions

Repeat20 – 120101MBT 1
Repeat128 – 232105MBT 2
Repeat242 – 348107MBT 3
Repeat356 – 45398MBT 4
Domain796 – 86469SAM
Region34 – 429Antigenic epitope

Amino acid modifications

Modified residue7751Phosphoserine Ref.9

Natural variations

Alternative sequence778 – 82043Missing in isoform 2.
VSP_013857

Experimental info

Mutagenesis1731F → A: Reduced histone-binding. Ref.10
Mutagenesis1801W → A: Abolishes histone-binding. Ref.10
Mutagenesis1961Y → A: Reduced histone-binding. Ref.10
Sequence conflict6421K → R in AAF19794. Ref.1
Sequence conflict7671S → F in AAF19794. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: DCE67BF35C413EB7

FASTA86698,141
        10         20         30         40         50         60 
MNGEQQLDAD AGSGMEEVEL SWEDYLEETG STAVPYGSFK HVDTRLQNGF APGMKLEVAV 

        70         80         90        100        110        120 
RTDPETYWVA TVITTCEQLL LLRYDGYGED RRADFWCDIR KADLYPIGWC EQNKKTLEAP 

       130        140        150        160        170        180 
EGIRDKVSDW DEFLRQTLIG ACSPPVPLLE GLRNGRNPLD LIAPGSRLEC QAFQDSLSTW 

       190        200        210        220        230        240 
IVTVVENIGG RLKLRYEGLE SSDNYEHWLY YLDPFLHHVG WAAQQGYELQ PPSAIRHLKN 

       250        260        270        280        290        300 
EAEWQEILAK VKEEEEEPLP SYLFKDKQVI GIHTFSVNMK LEAVDPWSPF GISPATVVKV 

       310        320        330        340        350        360 
FDEKYFLVEM DDLRPENHAR RSFVCHADSP GIFPVQWSLK NGLHISPPPG YPSQDFDWAD 

       370        380        390        400        410        420 
YLKQCGAEAA PQRCFPPLIS EHEFKENMKL EAVNPILPEE VCVATITAVR GSYLWLQLEG 

       430        440        450        460        470        480 
SKKPIPECIV SVESMDIFPL GWCETNGHPL STPRRARVYK QRKIAVVQPE KQVPSSRTVH 

       490        500        510        520        530        540 
EGLRNQELNS TESVMINGKY CCPKIYFNHR CFSGPYLNKG RIAELPQCVG PGNCVLVLRE 

       550        560        570        580        590        600 
VLTLLINAAY KPSRVLRELQ LDKDSVWHGC GEVLKAKYKG KSYRATVEIV KTADRVTEFC 

       610        620        630        640        650        660 
RQTCIKLECC PNLFGPRMVL DKCSENCSVL TKTKYTHYYG KKKNKRIGRP PGGHSNLACA 

       670        680        690        700        710        720 
LKKASKRRKR RKNVFVHKKK RSSASVDNTP AGSPQGSGGE DEDDPDEGDD DSLSEGSTSE 

       730        740        750        760        770        780 
QQDELQEESE MSEKKSCSSS PTQSEISTSL PPDRQRRKRE LRTFSFSDDE NKPPSPKEIR 

       790        800        810        820        830        840 
IEVAERLHLD SNPLKWSVAD VVRFIRSTDC APLARIFLDQ EIDGQALLLL TLPTVQECMD 

       850        860 
LKLGPAIKLC HHIERIKFAF YEQFAN 

« Hide

Isoform 2 [UniParc].

Checksum: 896FEF37B9FCCECF
Show »

FASTA82393,166

References

« Hide 'large scale' references
[1]"Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells."
Morel S., Levy F., Burlet-Schiltz O., Brasseur F., Probst-Kepper M., Peitrequin A.L., Monsarrat B., Van Velthoven R., Cerottini J.C., Boon T., Gairin J.E., Van den Eynde B.J.
Immunity 12:107-117(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"SFMBT and H-L(3)MBT interact with each other and regulate HOX expression and cell proliferation."
Usui H., Ichikawa T., Kobayashi K., Kumanishi T.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-866 (ISOFORM 2).
Tissue: Testis.
[8]"Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3."
Wu S., Trievel R.C., Rice J.C.
FEBS Lett. 581:3289-3296(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"SFMBT1 functions with LSD1 to regulate expression of canonical histone genes and chromatin-related factors."
Zhang J., Bonasio R., Strino F., Kluger Y., Holloway J.K., Modzelewski A.J., Cohen P.E., Reinberg D.
Genes Dev. 27:749-766(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KDM1A AND RCOR1, IDENTIFICATION IN THE SLC COMPLEX, MUTAGENESIS OF PHE-173; TRP-180 AND TYR-196.
[11]"Proteomic and functional analyses reveal the role of chromatin reader SFMBT1 in regulating epigenetic silencing and the myogenic gene program."
Lin S., Shen H., Li J.L., Tang S., Gu Y., Chen Z., Hu C., Rice J.C., Lu J., Wu L.
J. Biol. Chem. 288:6238-6247(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN VARIOUS COREPRESSOR COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF168132 mRNA. Translation: AAF19794.1.
AB189472 mRNA. Translation: BAE43835.1.
AK313965 mRNA. Translation: BAG36680.1.
AC099667 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65272.1.
BC014614 mRNA. Translation: AAH14614.1.
AL080140 mRNA. Translation: CAB45734.1.
PIRT12525.
RefSeqNP_057413.2. NM_016329.3.
XP_005265278.1. XM_005265221.1.
UniGeneHs.343679.

3D structure databases

ProteinModelPortalQ9UHJ3.
SMRQ9UHJ3. Positions 14-530, 796-857.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119553. 8 interactions.
IntActQ9UHJ3. 10 interactions.
MINTMINT-1448033.
STRING9606.ENSP00000350789.

Chemistry

ChEMBLCHEMBL1764944.

PTM databases

PhosphoSiteQ9UHJ3.

Polymorphism databases

DMDM67461585.

Proteomic databases

PaxDbQ9UHJ3.
PRIDEQ9UHJ3.

Protocols and materials databases

DNASU51460.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296295; ENSP00000296295; ENSG00000163935. [Q9UHJ3-2]
ENST00000358080; ENSP00000350789; ENSG00000163935. [Q9UHJ3-1]
ENST00000394750; ENSP00000378233; ENSG00000163935. [Q9UHJ3-1]
ENST00000394752; ENSP00000378235; ENSG00000163935. [Q9UHJ3-1]
GeneID51460.
KEGGhsa:51460.
UCSCuc003dgh.3. human. [Q9UHJ3-1]
uc010hmr.3. human. [Q9UHJ3-2]

Organism-specific databases

CTD51460.
GeneCardsGC03M052913.
HGNCHGNC:20255. SFMBT1.
HPAHPA036153.
MIM607319. gene.
neXtProtNX_Q9UHJ3.
PharmGKBPA134898464.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316861.
HOGENOMHOG000004859.
HOVERGENHBG085238.
InParanoidQ9UHJ3.
OMAKCSENCS.
OrthoDBEOG780RKN.
PhylomeDBQ9UHJ3.
TreeFamTF316498.

Gene expression databases

ArrayExpressQ9UHJ3.
BgeeQ9UHJ3.
CleanExHS_SFMBT1.
GenevestigatorQ9UHJ3.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR021987. DUF3588.
IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamPF12140. DUF3588. 1 hit.
PF02820. MBT. 4 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTSM00561. MBT. 4 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS51079. MBT. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSFMBT1. human.
GenomeRNAi51460.
NextBio55079.
PROQ9UHJ3.
SOURCESearch...

Entry information

Entry nameSMBT1_HUMAN
AccessionPrimary (citable) accession number: Q9UHJ3
Secondary accession number(s): Q402F7, Q96C73, Q9Y4Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM