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Q6INA9 (SETB1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SETDB1

EC=2.1.1.43
Alternative name(s):
SET domain bifurcated 1
Gene names
Name:setdb1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1269 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation By similarity.

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Subcellular location

Nucleus By similarity. Chromosome By similarity. Note: Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin By similarity.

Domain

In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster By similarity.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.

Contains 1 MBD (methyl-CpG-binding) domain.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

Contains 2 Tudor domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12691269Histone-lysine N-methyltransferase SETDB1
PRO_0000281821

Regions

Domain250 – 31263Tudor 1
Domain340 – 39556Tudor 2
Domain620 – 69172MBD
Domain753 – 82674Pre-SET
Domain829 – 1244416SET
Domain1253 – 126917Post-SET
Region839 – 8413S-adenosyl-L-methionine binding By similarity
Region1201 – 12022S-adenosyl-L-methionine binding By similarity
Coiled coil9 – 6355 Potential
Compositional bias508 – 58073Gln-rich

Sites

Metal binding7551Zinc 1 By similarity
Metal binding7551Zinc 2 By similarity
Metal binding7571Zinc 1 By similarity
Metal binding7611Zinc 1 By similarity
Metal binding7611Zinc 3 By similarity
Metal binding7671Zinc 1 By similarity
Metal binding7691Zinc 2 By similarity
Metal binding8071Zinc 2 By similarity
Metal binding8071Zinc 3 By similarity
Metal binding8111Zinc 2 By similarity
Metal binding8131Zinc 3 By similarity
Metal binding8181Zinc 3 By similarity
Metal binding12041Zinc 4 By similarity
Metal binding12571Zinc 4 By similarity
Metal binding12591Zinc 4 By similarity
Metal binding12641Zinc 4 By similarity
Binding site8771S-adenosyl-L-methionine By similarity
Binding site8791S-adenosyl-L-methionine By similarity
Binding site11981S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6INA9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6241910CB4266FAC

FASTA1,269141,777
        10         20         30         40         50         60 
MELEQMVVKE LGISMDDLRE LIDRELEKIE FVKQRKAQLL EMEQLVKQKE AEVDHVDKLF 

        70         80         90        100        110        120 
DNATRAVDDC ETLVKSLYDQ IGMTYKESSS EDEGSSKPTE VIEIPDEDDD DVMSVGSGEA 

       130        140        150        160        170        180 
VSKIPKEKHL LREAMAAMKR SRQDVQSIVE AIQKKSDGPQ TRFSSHPSSP TSSVGGSNQA 

       190        200        210        220        230        240 
SASNDMSKDG DLVVGMRILG KKRTKTWHKG TLISIQCVGT GKKFKVKFDN KGKSLLSGNH 

       250        260        270        280        290        300 
IAYDYHPPPE NLTVGSRVVA KYKDGNQVWL YAGIVAEPPS SKNKMRYLIF FDDGYASYVT 

       310        320        330        340        350        360 
HAELYPVCRP WSKSWEDIED VSCRDFIQEY VNAYPNRPMV LLKSGQLIKT EWEGTWWKSK 

       370        380        390        400        410        420 
VEEVDGSLVK ILFLDDKRCE WIYRGSTRLE PMFSMKTSNA STQEKQQAGQ QRTRPNVGAI 

       430        440        450        460        470        480 
RSKGPVVQFT HDLTGNEPEH NPAAPPSPQS MPSPQLIDTD SDSQQAQSKK QVAKKSTSFR 

       490        500        510        520        530        540 
PGSAGSGQSS PIPTESVPQP PAAPRPFQSN QSVQPVQSIQ PIQPIHNIQT IQTIQGIQTI 

       550        560        570        580        590        600 
QAIQPIQSIQ TLQPIQTIQP LQTIQTLQGN RIVTSIQQFQ IIRTENIPAE STYKAPKEKL 

       610        620        630        640        650        660 
FYLPHVCNYT CLSRIRPLSH RGKNPLLVPL LYDFRRMTAR RRVNRKMGFH VIYKSPCGLS 

       670        680        690        700        710        720 
LRTMPEIERY LFETQCKMLF LEMFCLDPYV LVDRKFQPQK PFYYIPDITY GKEDVMLSCV 

       730        740        750        760        770        780 
NEIDRTPPPQ VAYSKERIPG KGVFINTGAD YLVGCDCTDG CRDKSKCACH QLTIQATACT 

       790        800        810        820        830        840 
PGAQSNPMAG YQHKRLEECL PTGVYECNKR CKCSANMCNN RLVQHGLQVR LQLFKTQNKG 

       850        860        870        880        890        900 
WGIRGLDDIA KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA 

       910        920        930        940        950        960 
KSSSDSSGVD LKEDHEENSG SEDQEESNDS SDDNFGKNED ITTSSVWRSY ATRRTTRGQK 

       970        980        990       1000       1010       1020 
ENGTSETASK DSRTRDETTD CKLPEETSKN KVASWLSSNT MADSVMDSDS RSSLKMGEAL 

      1030       1040       1050       1060       1070       1080 
ETDKPKESEE ASKYPRFAEG NRAYGYNPTP TKKDGVRRPV TKTALHQIKR QSSSAQPTEE 

      1090       1100       1110       1120       1130       1140 
VLTLSSSSDS EVGSGTNGSK KPAAQATAND SDDIQTISSG SDEEEEKKNV AASAGPVKRQ 

      1150       1160       1170       1180       1190       1200 
VAVKSTRGFA LKSTHGITVK SNMASGEGGP GRRNTRQFFD GEESCYIIDA KLEGNLGRYL 

      1210       1220       1230       1240       1250       1260 
NHSCSPNLFV QNVFVDTHDL RFPWVAFFAS KRIRAGTELT WDYNYEVGSV EGKKLLCCCG 


STECRGRLL 

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References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC072374 mRNA. Translation: AAH72374.1.
RefSeqNP_001085076.2. NM_001091607.1.
UniGeneXl.54988.

3D structure databases

ProteinModelPortalQ6INA9.
SMRQ6INA9. Positions 190-391.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID432147.
KEGGxla:432147.

Organism-specific databases

CTD9869.
XenbaseXB-GENE-866480. setdb1.

Phylogenomic databases

HOVERGENHBG061013.
KOK11421.

Family and domain databases

InterProIPR016177. DNA-bd_dom.
IPR025796. Hist-Lys_N-MeTrfase_SETDB1.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
IPR002999. Tudor.
[Graphical view]
PfamPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMSSF54171. SSF54171. 1 hit.
PROSITEPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51573. SAM_MT43_SUVAR39_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSETB1_XENLA
AccessionPrimary (citable) accession number: Q6INA9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families