Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6YI93

- SETB2_XENLA

UniProt

Q6YI93 - SETB2_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone-lysine N-methyltransferase SETDB2

Gene

setdb2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis (By similarity).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 bindingi312 – 3121Zinc 1By similarity
Metal bindingi312 – 3121Zinc 2By similarity
Metal bindingi314 – 3141Zinc 1By similarity
Metal bindingi318 – 3181Zinc 1By similarity
Metal bindingi318 – 3181Zinc 3By similarity
Metal bindingi324 – 3241Zinc 1By similarity
Metal bindingi326 – 3261Zinc 2By similarity
Metal bindingi365 – 3651Zinc 2By similarity
Metal bindingi365 – 3651Zinc 3By similarity
Metal bindingi369 – 3691Zinc 2By similarity
Metal bindingi371 – 3711Zinc 3By similarity
Metal bindingi376 – 3761Zinc 3By similarity
Binding sitei632 – 6321S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi638 – 6381Zinc 4By similarity
Metal bindingi691 – 6911Zinc 4By similarity
Metal bindingi693 – 6931Zinc 4By similarity
Metal bindingi698 – 6981Zinc 4By similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. heart looping Source: UniProtKB
  3. histone H3-K9 methylation Source: UniProtKB
  4. left/right axis specification Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETDB2 (EC:2.1.1.43)
Alternative name(s):
Chronic lymphocytic leukemia deletion region gene 8 protein homolog
SET domain bifurcated 2
Gene namesi
Name:setdb2
Synonyms:clld8
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1219036. setdb2.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 703703Histone-lysine N-methyltransferase SETDB2PRO_0000281825Add
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 24871MBDAdd
BLAST
Domaini310 – 38475Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini387 – 678292SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni397 – 3993S-adenosyl-L-methionine bindingBy similarity
Regioni635 – 6362S-adenosyl-L-methionine bindingBy similarity

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.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG106688.
KOiK18494.

Family and domain databases

InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6YI93-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQSANARQS TLRSRTQELN TLSVLSKDVS LEDAKKYWKD RQADGKVDWI
60 70 80 90 100
FEKVLNKLKI LWQKIKDGSA TNLEYVRAVI LVNEAGNLEE DLEEDLKEDT
110 120 130 140 150
DTIHIDIHKE NEVQENTDCS PERKEDTCLN LNTDCGTDVS GSEPECNSTV
160 170 180 190 200
SPPAAERVYF GNHSCGPSCL SGINSFLFTK GNPLQLPISC DFQRCHLKIN
210 220 230 240 250
SPDDLSHILY KAPCGRSLRD YDEVHSYLTE TGCHFLAVDN FSFNNHVRLD
260 270 280 290 300
SNSSFNQGIV QDCDISNDVE SVPVAFSNEI DNTRPSNFIY RKTSWPPGYS
310 320 330 340 350
LNNFTDIFVK CCNCTDGCLD ILTCSCLQLT AQAFTKCMES SLGIGPLGYK
360 370 380 390 400
HKRLQEPIPT GLYECNVSCK CDRMLCQNRV VQHGLKLRLQ VFKTNTKGWG
410 420 430 440 450
VRCLDDVDKG TFVCIYAGRI LIRTADCTVK STPDDSVACG NEDHEDSTST
460 470 480 490 500
CALILSKRKR KTSHSDSEVT VMHTNPYSMR SHGLSVHRLS NTFSPRQARS
510 520 530 540 550
GEREFSLQPL RRPKTKTSML QKRRRQLIEE GACTVQNSSE EEGPTPPQSP
560 570 580 590 600
EQKSSAGTKI QRNENSDETA SGYVSEESSS SVISGGHPLE KPISKFKSKL
610 620 630 640 650
NKTTVYLSTS PEQTCEENLH FLDASKEGNV GRFLNHSCCP NLFVQQVFVD
660 670 680 690 700
THQKCFPWVA FFTNSVVKAG TELTWDYSYD IGTAADQEIQ CLCGQKTCKN

KVV
Length:703
Mass (Da):78,698
Last modified:October 5, 2010 - v2
Checksum:i12D86C32892B5325
GO

Sequence cautioni

The sequence AAN61106.1 differs from that shown. Reason: Frameshift at position 695.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971K → Q in AAN61106. 1 PublicationCurated
Sequence conflicti175 – 1751S → P in AAN61106. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145835 mRNA. Translation: AAN61106.1. Frameshift.
BC170303 mRNA. Translation: AAI70303.1.
RefSeqiNP_001082765.1. NM_001089296.1.
UniGeneiXl.29790.

Genome annotation databases

GeneIDi398711.
KEGGixla:398711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145835 mRNA. Translation: AAN61106.1 . Frameshift.
BC170303 mRNA. Translation: AAI70303.1 .
RefSeqi NP_001082765.1. NM_001089296.1.
UniGenei Xl.29790.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398711.
KEGGi xla:398711.

Organism-specific databases

CTDi 83852.
Xenbasei XB-GENE-1219036. setdb2.

Phylogenomic databases

HOVERGENi HBG106688.
KOi K18494.

Family and domain databases

InterProi IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and analysis of the expression of SET-domain putative histone methyltransferase CLLD8 in Xenopus laevis."
    Ruzov A., Meehan R.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Oocyte.

Entry informationi

Entry nameiSETB2_XENLA
AccessioniPrimary (citable) accession number: Q6YI93
Secondary accession number(s): B7ZRV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 66 of the entry and version 2 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