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Protein

Polycomb protein Sfmbt

Gene

Sfmbt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polycomb group (PcG) protein that binds to the Polycomb response elements (PREs) found in the regulatory regions of many genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility. Necessary but not sufficient to recruit a functional PcG repressive complex that represses target genes, suggesting that the recruitment of the distinct PRC1 complex is also required to allow a subsequent repression.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri322 – 35736FCS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • DNA binding Source: UniProtKB-KW
  • methylated histone binding Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • chromatin silencing Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • negative regulation of gene expression Source: FlyBase
  • oogenesis Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9VK33.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb protein Sfmbt
Alternative name(s):
Scm-like with four MBT domain-containing protein 1
dSfmbt
Gene namesi
Name:Sfmbt1 Publication
ORF Names:CG16975
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032475. Sfmbt.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: FlyBase
  • PcG protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12201220Polycomb protein SfmbtPRO_0000306371Add
BLAST

Proteomic databases

PaxDbiQ9VK33.

Expressioni

Gene expression databases

BgeeiQ9VK33.
ExpressionAtlasiQ9VK33. differential.
GenevisibleiQ9VK33. DM.

Interactioni

Subunit structurei

Interacts with pho as a component of the pho-repressive complex (PhoRC).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
H3F3BP8424315EBI-117801,EBI-120658From a different organism.
HIST2H4BP6280510EBI-117801,EBI-302023From a different organism.
phoQ8ST836EBI-117801,EBI-125201
pholQ9VSZ32EBI-117801,EBI-176113

GO - Molecular functioni

  • methylated histone binding Source: FlyBase

Protein-protein interaction databases

BioGridi60747. 11 interactions.
IntActiQ9VK33. 8 interactions.
MINTiMINT-291178.
STRINGi7227.FBpp0288419.

Structurei

Secondary structure

1
1220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi539 – 5424Combined sources
Helixi552 – 5543Combined sources
Helixi561 – 5666Combined sources
Beta strandi572 – 5765Combined sources
Beta strandi595 – 60410Combined sources
Beta strandi607 – 6126Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi622 – 6254Combined sources
Turni626 – 6283Combined sources
Beta strandi629 – 6335Combined sources
Helixi636 – 6394Combined sources
Turni648 – 6525Combined sources
Helixi658 – 6658Combined sources
Helixi675 – 6817Combined sources
Beta strandi692 – 6976Combined sources
Beta strandi700 – 71314Combined sources
Beta strandi716 – 7216Combined sources
Beta strandi727 – 7315Combined sources
Helixi742 – 7465Combined sources
Beta strandi749 – 7513Combined sources
Helixi754 – 7618Combined sources
Turni762 – 7665Combined sources
Helixi777 – 7793Combined sources
Helixi786 – 7883Combined sources
Beta strandi803 – 8086Combined sources
Beta strandi811 – 82313Combined sources
Beta strandi828 – 8336Combined sources
Turni841 – 8444Combined sources
Beta strandi846 – 8494Combined sources
Helixi860 – 8634Combined sources
Turni876 – 8783Combined sources
Helixi881 – 8888Combined sources
Helixi895 – 8973Combined sources
Beta strandi912 – 9165Combined sources
Beta strandi924 – 93310Combined sources
Beta strandi936 – 9416Combined sources
Helixi946 – 9483Combined sources
Beta strandi950 – 9534Combined sources
Helixi964 – 9685Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H6ZX-ray2.80A/B535-977[»]
4C5EX-ray1.95A/B/C/D531-980[»]
4C5GX-ray2.10A531-980[»]
4C5HX-ray3.20A531-980[»]
5J8YX-ray1.98C/D1137-1220[»]
ProteinModelPortaliQ9VK33.
SMRiQ9VK33. Positions 533-977.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VK33.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati536 – 647112MBT 1Sequence analysisAdd
BLAST
Repeati655 – 75399MBT 2Sequence analysisAdd
BLAST
Repeati761 – 871111MBT 3Sequence analysisAdd
BLAST
Repeati879 – 97597MBT 4Sequence analysisAdd
BLAST
Domaini1140 – 120364SAMPROSITE-ProRule annotationAdd
BLAST

Domaini

MBT repeats have unique discriminatory binding activity for methylated Lys residues in H3 and H4; the MBT repeats bind mono- and dimethylated H3K9Me1, H3K9Me2, H4K20Me1 and H4K20Me2 but fail to interact with these residues if they are unmodified or trimethylated.

Sequence similaritiesi

Contains 1 FCS-type zinc finger.PROSITE-ProRule annotation
Contains 4 MBT repeats.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri322 – 35736FCS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IMEY. Eukaryota.
ENOG410ZCJZ. LUCA.
GeneTreeiENSGT00760000119024.
InParanoidiQ9VK33.
OrthoDBiEOG7K6PTF.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
[Graphical view]
PfamiPF02820. MBT. 4 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 4 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 4 hits.
PS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B1 Publication (identifier: Q9VK33-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNPSELRMMW MSSQYNSERI TLEDAATLLG HPTVGLSVME DLSAHQPTLD
60 70 80 90 100
MNPMMSLMGG DFTGQAAATA AALGVQPGTL IATNSNNLYG FAHMGGLQQQ
110 120 130 140 150
LLQQSAAAAV FQNYAEAMDN DVENGMVGMA MEAVVDDDDQ VYGQRDNNFD
160 170 180 190 200
DNGSELEPKQ EIINIDDFVM MNEDNNSYDG TDFMTSSDKD ISQSSSSCMA
210 220 230 240 250
QMPGSLGVPG VEHDLLVPLP DGLLHHKLLG TTLVPAMGTL NGNAFGNIMV
260 270 280 290 300
STENTSSKQM QRTYSTAKGA NSTATTATCS ASTSSALRSQ RKTRKIEPVN
310 320 330 340 350
RPGLVLKTPI AYRGNIDPSV IPIQKDGMAV CKRCGAIGVK HTFYTKSRRF
360 370 380 390 400
CSMACARGEL YSLVLNTKME GDQATTSSPD PGAGSESADL PGDQQQSQSD
410 420 430 440 450
IELDLHAAHI KNANYRFRIT DQSKITQLNS FGEPMSMGGD AAANNVQMAA
460 470 480 490 500
DETIAALNGG AVGDATAPGS TEEGASTPNS YLSAAPTPKA LRLFKDIYPQ
510 520 530 540 550
DDLPQIPKYE RLPVPCPQME KIISIRRRMY DPTHSYDWLP RLSKENFNAA
560 570 580 590 600
PVTCFPHAPG CEVWDNLGVG MKVEVENTDC DSIEVIQPGQ TPTSFWVATI
610 620 630 640 650
LEIKGYKALM SYEGFDTDSH DFWVNLCNAE VHSVGWCATR GKPLIPPRTI
660 670 680 690 700
EHKYKDWKDF LVGRLSGART LPSNFYNKIN DSLQSRFRLG LNLECVDKDR
710 720 730 740 750
ISQVRLATVT KIVGKRLFLR YFDSDDGFWC HEDSPIIHPV GWATTVGHNL
760 770 780 790 800
AAPQDYLERM LAGREAMIEV HEDDATIELF KMNFTFDEYY SDGKTNSFVE
810 820 830 840 850
GMKLEAVDPL NLSSICPATV MAVLKFGYMM IRIDSYQPDA SGSDWFCYHE
860 870 880 890 900
KSPCIFPAGF CSVNNISVTP PNGYDSRTFT WEGYLRDTGA VAAGQHLFHR
910 920 930 940 950
IIPDHGFEVG MSLECADLMD PRLVCVATVA RVVGRLLKVH FDGWTDEYDQ
960 970 980 990 1000
WLDCESADIY PVGWCVLVNH KLEGPPRVAH QQAPKPAPKP KIQRKRKPKK
1010 1020 1030 1040 1050
GAAGGKTPTD NNTQSVKSRT IALKTTPHLP KLSIKLELKP EHHNAAFYEN
1060 1070 1080 1090 1100
NQPEEEGDEE DPDADGDGDG STSHISEQST TQSSSDLIAG SGSGSGSASL
1110 1120 1130 1140 1150
VTLATGSNKT NSSATNNKYI PRLADIDSSE PHLELVPDTW NVYDVSQFLR
1160 1170 1180 1190 1200
VNDCTAHCDT FSRNKIDGKR LLQLTKDDIM PLLGMKVGPA LKISDLIAQL
1210 1220
KCKVNPGRAR SHKTNKSPFL
Note: No experimental confirmation available.Curated
Length:1,220
Mass (Da):133,666
Last modified:June 1, 2003 - v2
Checksum:i2BE2785144CA051F
GO
Isoform A1 Publication (identifier: Q9VK33-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-352: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:868
Mass (Da):95,867
Checksum:iA8D56440315A78E4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 352352Missing in isoform A. 1 PublicationVSP_052548Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53249.2.
AE014134 Genomic DNA. Translation: AAF53250.2.
BT006011 mRNA. Translation: AAO74694.1.
RefSeqiNP_001260432.1. NM_001273503.1. [Q9VK33-1]
NP_609606.2. NM_135762.3. [Q9VK33-1]
NP_723786.1. NM_165026.2. [Q9VK33-2]
UniGeneiDm.11543.

Genome annotation databases

EnsemblMetazoaiFBtr0080492; FBpp0080070; FBgn0032475. [Q9VK33-1]
FBtr0333236; FBpp0305438; FBgn0032475. [Q9VK33-1]
GeneIDi34709.
KEGGidme:Dmel_CG16975.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53249.2.
AE014134 Genomic DNA. Translation: AAF53250.2.
BT006011 mRNA. Translation: AAO74694.1.
RefSeqiNP_001260432.1. NM_001273503.1. [Q9VK33-1]
NP_609606.2. NM_135762.3. [Q9VK33-1]
NP_723786.1. NM_165026.2. [Q9VK33-2]
UniGeneiDm.11543.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H6ZX-ray2.80A/B535-977[»]
4C5EX-ray1.95A/B/C/D531-980[»]
4C5GX-ray2.10A531-980[»]
4C5HX-ray3.20A531-980[»]
5J8YX-ray1.98C/D1137-1220[»]
ProteinModelPortaliQ9VK33.
SMRiQ9VK33. Positions 533-977.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60747. 11 interactions.
IntActiQ9VK33. 8 interactions.
MINTiMINT-291178.
STRINGi7227.FBpp0288419.

Proteomic databases

PaxDbiQ9VK33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080492; FBpp0080070; FBgn0032475. [Q9VK33-1]
FBtr0333236; FBpp0305438; FBgn0032475. [Q9VK33-1]
GeneIDi34709.
KEGGidme:Dmel_CG16975.

Organism-specific databases

CTDi34709.
FlyBaseiFBgn0032475. Sfmbt.

Phylogenomic databases

eggNOGiENOG410IMEY. Eukaryota.
ENOG410ZCJZ. LUCA.
GeneTreeiENSGT00760000119024.
InParanoidiQ9VK33.
OrthoDBiEOG7K6PTF.

Enzyme and pathway databases

SignaLinkiQ9VK33.

Miscellaneous databases

EvolutionaryTraceiQ9VK33.
GenomeRNAii34709.
PROiQ9VK33.

Gene expression databases

BgeeiQ9VK33.
ExpressionAtlasiQ9VK33. differential.
GenevisibleiQ9VK33. DM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR012313. Znf_FCS.
[Graphical view]
PfamiPF02820. MBT. 4 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 4 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 4 hits.
PS50105. SAM_DOMAIN. 1 hit.
PS51024. ZF_FCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: BerkeleyImported.
    Tissue: Embryo.
  4. "A Polycomb group protein complex with sequence-specific DNA-binding and selective methyl-lysine-binding activities."
    Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C., Wild B., Wilm M., Mueller J.
    Genes Dev. 20:1110-1122(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHO, SUBCELLULAR LOCATION.
    Tissue: Embryo1 Publication.

Entry informationi

Entry nameiSMBT_DROME
AccessioniPrimary (citable) accession number: Q9VK33
Secondary accession number(s): Q7KTB5, Q9VK32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.