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Q6INA9

- SETB1_XENLA

UniProt

Q6INA9 - SETB1_XENLA

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Protein

Histone-lysine N-methyltransferase SETDB1

Gene
setdb1
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi755 – 7551Zinc 1 By similarity
Metal bindingi755 – 7551Zinc 2 By similarity
Metal bindingi757 – 7571Zinc 1 By similarity
Metal bindingi761 – 7611Zinc 1 By similarity
Metal bindingi761 – 7611Zinc 3 By similarity
Metal bindingi767 – 7671Zinc 1 By similarity
Metal bindingi769 – 7691Zinc 2 By similarity
Metal bindingi807 – 8071Zinc 2 By similarity
Metal bindingi807 – 8071Zinc 3 By similarity
Metal bindingi811 – 8111Zinc 2 By similarity
Metal bindingi813 – 8131Zinc 3 By similarity
Metal bindingi818 – 8181Zinc 3 By similarity
Binding sitei877 – 8771S-adenosyl-L-methionine By similarity
Binding sitei879 – 8791S-adenosyl-L-methionine By similarity
Binding sitei1198 – 11981S-adenosyl-L-methionine By similarity
Metal bindingi1204 – 12041Zinc 4 By similarity
Metal bindingi1257 – 12571Zinc 4 By similarity
Metal bindingi1259 – 12591Zinc 4 By similarity
Metal bindingi1264 – 12641Zinc 4 By similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETDB1 (EC:2.1.1.43)
Alternative name(s):
SET domain bifurcated 1
Gene namesi
Name:setdb1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-866480. setdb1.

Subcellular locationi

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

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12691269Histone-lysine N-methyltransferase SETDB1PRO_0000281821Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6INA9.
SMRiQ6INA9. Positions 190-391.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 31263Tudor 1Add
BLAST
Domaini340 – 39556Tudor 2Add
BLAST
Domaini620 – 69172MBDAdd
BLAST
Domaini753 – 82674Pre-SETAdd
BLAST
Domaini829 – 1244416SETAdd
BLAST
Domaini1253 – 126917Post-SETAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni839 – 8413S-adenosyl-L-methionine binding By similarity
Regioni1201 – 12022S-adenosyl-L-methionine binding By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili9 – 6355 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi508 – 58073Gln-richAdd
BLAST

Domaini

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 similaritiesi

Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.
Contains 2 Tudor domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG061013.
KOiK11421.

Family and domain databases

InterProiIPR016177. 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]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. 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]

Sequencei

Sequence statusi: Complete.

Q6INA9-1 [UniParc]FASTAAdd to Basket

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MELEQMVVKE LGISMDDLRE LIDRELEKIE FVKQRKAQLL EMEQLVKQKE     50
AEVDHVDKLF DNATRAVDDC ETLVKSLYDQ IGMTYKESSS EDEGSSKPTE 100
VIEIPDEDDD DVMSVGSGEA VSKIPKEKHL LREAMAAMKR SRQDVQSIVE 150
AIQKKSDGPQ TRFSSHPSSP TSSVGGSNQA SASNDMSKDG DLVVGMRILG 200
KKRTKTWHKG TLISIQCVGT GKKFKVKFDN KGKSLLSGNH IAYDYHPPPE 250
NLTVGSRVVA KYKDGNQVWL YAGIVAEPPS SKNKMRYLIF FDDGYASYVT 300
HAELYPVCRP WSKSWEDIED VSCRDFIQEY VNAYPNRPMV LLKSGQLIKT 350
EWEGTWWKSK VEEVDGSLVK ILFLDDKRCE WIYRGSTRLE PMFSMKTSNA 400
STQEKQQAGQ QRTRPNVGAI RSKGPVVQFT HDLTGNEPEH NPAAPPSPQS 450
MPSPQLIDTD SDSQQAQSKK QVAKKSTSFR PGSAGSGQSS PIPTESVPQP 500
PAAPRPFQSN QSVQPVQSIQ PIQPIHNIQT IQTIQGIQTI QAIQPIQSIQ 550
TLQPIQTIQP LQTIQTLQGN RIVTSIQQFQ IIRTENIPAE STYKAPKEKL 600
FYLPHVCNYT CLSRIRPLSH RGKNPLLVPL LYDFRRMTAR RRVNRKMGFH 650
VIYKSPCGLS LRTMPEIERY LFETQCKMLF LEMFCLDPYV LVDRKFQPQK 700
PFYYIPDITY GKEDVMLSCV NEIDRTPPPQ VAYSKERIPG KGVFINTGAD 750
YLVGCDCTDG CRDKSKCACH QLTIQATACT PGAQSNPMAG YQHKRLEECL 800
PTGVYECNKR CKCSANMCNN RLVQHGLQVR LQLFKTQNKG WGIRGLDDIA 850
KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA 900
KSSSDSSGVD LKEDHEENSG SEDQEESNDS SDDNFGKNED ITTSSVWRSY 950
ATRRTTRGQK ENGTSETASK DSRTRDETTD CKLPEETSKN KVASWLSSNT 1000
MADSVMDSDS RSSLKMGEAL ETDKPKESEE ASKYPRFAEG NRAYGYNPTP 1050
TKKDGVRRPV TKTALHQIKR QSSSAQPTEE VLTLSSSSDS EVGSGTNGSK 1100
KPAAQATAND SDDIQTISSG SDEEEEKKNV AASAGPVKRQ VAVKSTRGFA 1150
LKSTHGITVK SNMASGEGGP GRRNTRQFFD GEESCYIIDA KLEGNLGRYL 1200
NHSCSPNLFV QNVFVDTHDL RFPWVAFFAS KRIRAGTELT WDYNYEVGSV 1250
EGKKLLCCCG STECRGRLL 1269
Length:1,269
Mass (Da):141,777
Last modified:July 5, 2004 - v1
Checksum:i6241910CB4266FAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC072374 mRNA. Translation: AAH72374.1.
RefSeqiNP_001085076.2. NM_001091607.1.
UniGeneiXl.54988.

Genome annotation databases

GeneIDi432147.
KEGGixla:432147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC072374 mRNA. Translation: AAH72374.1 .
RefSeqi NP_001085076.2. NM_001091607.1.
UniGenei Xl.54988.

3D structure databases

ProteinModelPortali Q6INA9.
SMRi Q6INA9. Positions 190-391.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 432147.
KEGGi xla:432147.

Organism-specific databases

CTDi 9869.
Xenbasei XB-GENE-866480. setdb1.

Phylogenomic databases

HOVERGENi HBG061013.
KOi K11421.

Family and domain databases

InterProi IPR016177. 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 ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50982. 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSETB1_XENLA
AccessioniPrimary (citable) accession number: Q6INA9
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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