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Protein

Histone-lysine N-methyltransferase SETDB1

Gene

setdb1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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. Plays a role in promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi755Zinc 1By similarity1
Metal bindingi755Zinc 2By similarity1
Metal bindingi757Zinc 1By similarity1
Metal bindingi761Zinc 1By similarity1
Metal bindingi761Zinc 3By similarity1
Metal bindingi767Zinc 1By similarity1
Metal bindingi769Zinc 2By similarity1
Metal bindingi807Zinc 2By similarity1
Metal bindingi807Zinc 3By similarity1
Metal bindingi811Zinc 2By similarity1
Metal bindingi813Zinc 3By similarity1
Metal bindingi818Zinc 3By similarity1
Binding sitei877S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei879S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei1198S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi1204Zinc 4By similarity1
Metal bindingi1257Zinc 4By similarity1
Metal bindingi1259Zinc 4By similarity1
Metal bindingi1264Zinc 4By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002818211 – 1269Histone-lysine N-methyltransferase SETDB1Add BLAST1269

Proteomic databases

PRIDEiQ6INA9

Structurei

3D structure databases

ProteinModelPortaliQ6INA9
SMRiQ6INA9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini250 – 312Tudor 1Add BLAST63
Domaini340 – 395Tudor 2Add BLAST56
Domaini620 – 691MBDPROSITE-ProRule annotationAdd BLAST72
Domaini753 – 826Pre-SETPROSITE-ProRule annotationAdd BLAST74
Domaini829 – 1244SETPROSITE-ProRule annotationAdd BLAST416
Domaini1253 – 1269Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni839 – 841S-adenosyl-L-methionine bindingBy similarity3
Regioni1201 – 1202S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili9 – 63Sequence analysisAdd BLAST55

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi508 – 580Gln-richAdd BLAST73

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

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG061013
KOiK11421

Family and domain databases

InterProiView protein in InterPro
IPR016177 DNA-bd_dom_sf
IPR025796 Hist-Lys_N-MeTrfase_SETDB1
IPR001739 Methyl_CpG_DNA-bd
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR002999 Tudor
PfamiView protein in Pfam
PF01429 MBD, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit
SMARTiView protein in SMART
SM00391 MBD, 1 hit
SM00468 PreSET, 1 hit
SM00317 SET, 1 hit
SM00333 TUDOR, 2 hits
SUPFAMiSSF54171 SSF54171, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

Q6INA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELEQMVVKE LGISMDDLRE LIDRELEKIE FVKQRKAQLL EMEQLVKQKE
60 70 80 90 100
AEVDHVDKLF DNATRAVDDC ETLVKSLYDQ IGMTYKESSS EDEGSSKPTE
110 120 130 140 150
VIEIPDEDDD DVMSVGSGEA VSKIPKEKHL LREAMAAMKR SRQDVQSIVE
160 170 180 190 200
AIQKKSDGPQ TRFSSHPSSP TSSVGGSNQA SASNDMSKDG DLVVGMRILG
210 220 230 240 250
KKRTKTWHKG TLISIQCVGT GKKFKVKFDN KGKSLLSGNH IAYDYHPPPE
260 270 280 290 300
NLTVGSRVVA KYKDGNQVWL YAGIVAEPPS SKNKMRYLIF FDDGYASYVT
310 320 330 340 350
HAELYPVCRP WSKSWEDIED VSCRDFIQEY VNAYPNRPMV LLKSGQLIKT
360 370 380 390 400
EWEGTWWKSK VEEVDGSLVK ILFLDDKRCE WIYRGSTRLE PMFSMKTSNA
410 420 430 440 450
STQEKQQAGQ QRTRPNVGAI RSKGPVVQFT HDLTGNEPEH NPAAPPSPQS
460 470 480 490 500
MPSPQLIDTD SDSQQAQSKK QVAKKSTSFR PGSAGSGQSS PIPTESVPQP
510 520 530 540 550
PAAPRPFQSN QSVQPVQSIQ PIQPIHNIQT IQTIQGIQTI QAIQPIQSIQ
560 570 580 590 600
TLQPIQTIQP LQTIQTLQGN RIVTSIQQFQ IIRTENIPAE STYKAPKEKL
610 620 630 640 650
FYLPHVCNYT CLSRIRPLSH RGKNPLLVPL LYDFRRMTAR RRVNRKMGFH
660 670 680 690 700
VIYKSPCGLS LRTMPEIERY LFETQCKMLF LEMFCLDPYV LVDRKFQPQK
710 720 730 740 750
PFYYIPDITY GKEDVMLSCV NEIDRTPPPQ VAYSKERIPG KGVFINTGAD
760 770 780 790 800
YLVGCDCTDG CRDKSKCACH QLTIQATACT PGAQSNPMAG YQHKRLEECL
810 820 830 840 850
PTGVYECNKR CKCSANMCNN RLVQHGLQVR LQLFKTQNKG WGIRGLDDIA
860 870 880 890 900
KGSFVCIYAG KILTDDFADK EGLEMGDEYF ANLDHIESVE NFKEGYESDA
910 920 930 940 950
KSSSDSSGVD LKEDHEENSG SEDQEESNDS SDDNFGKNED ITTSSVWRSY
960 970 980 990 1000
ATRRTTRGQK ENGTSETASK DSRTRDETTD CKLPEETSKN KVASWLSSNT
1010 1020 1030 1040 1050
MADSVMDSDS RSSLKMGEAL ETDKPKESEE ASKYPRFAEG NRAYGYNPTP
1060 1070 1080 1090 1100
TKKDGVRRPV TKTALHQIKR QSSSAQPTEE VLTLSSSSDS EVGSGTNGSK
1110 1120 1130 1140 1150
KPAAQATAND SDDIQTISSG SDEEEEKKNV AASAGPVKRQ VAVKSTRGFA
1160 1170 1180 1190 1200
LKSTHGITVK SNMASGEGGP GRRNTRQFFD GEESCYIIDA KLEGNLGRYL
1210 1220 1230 1240 1250
NHSCSPNLFV QNVFVDTHDL RFPWVAFFAS KRIRAGTELT WDYNYEVGSV
1260
EGKKLLCCCG STECRGRLL
Length:1,269
Mass (Da):141,777
Last modified:July 5, 2004 - v1
Checksum:i6241910CB4266FAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC072374 mRNA Translation: AAH72374.1
RefSeqiNP_001085076.2, NM_001091607.1
UniGeneiXl.54988

Genome annotation databases

GeneIDi432147
KEGGixla:432147

Similar proteinsi

Entry informationi

Entry nameiSETB1_XENLA
AccessioniPrimary (citable) accession number: Q6INA9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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