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A4IGY9

- SETB2_XENTR

UniProt

A4IGY9 - SETB2_XENTR

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Protein

Histone-lysine N-methyltransferase SETDB2

Gene

setdb2

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed - Annotation score: 3 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 represents a specific tag for epigenetic transcriptional repression by recruiting 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 bindingi306 – 3061Zinc 1By similarity
Metal bindingi306 – 3061Zinc 2By similarity
Metal bindingi308 – 3081Zinc 1By similarity
Metal bindingi312 – 3121Zinc 1By similarity
Metal bindingi312 – 3121Zinc 3By similarity
Metal bindingi318 – 3181Zinc 1By similarity
Metal bindingi320 – 3201Zinc 2By similarity
Metal bindingi359 – 3591Zinc 2By similarity
Metal bindingi359 – 3591Zinc 3By similarity
Metal bindingi363 – 3631Zinc 2By similarity
Metal bindingi365 – 3651Zinc 3By similarity
Metal bindingi370 – 3701Zinc 3By similarity
Binding sitei626 – 6261S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi632 – 6321Zinc 4By similarity
Metal bindingi685 – 6851Zinc 4By similarity
Metal bindingi687 – 6871Zinc 4By similarity
Metal bindingi692 – 6921Zinc 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):
SET domain bifurcated 2
Gene namesi
Name:setdb2
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
ProteomesiUP000008143: Unplaced

Organism-specific databases

XenbaseiXB-GENE-1219030. 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 – 697697Histone-lysine N-methyltransferase SETDB2PRO_0000398647Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi8364.ENSXETP00000034176.

Structurei

3D structure databases

ProteinModelPortaliA4IGY9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 24271MBDPROSITE-ProRule annotationAdd
BLAST
Domaini304 – 37875Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini381 – 672292SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni391 – 3933S-adenosyl-L-methionine bindingBy similarity
Regioni629 – 6302S-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 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
HOGENOMiHOG000060314.
HOVERGENiHBG106688.
InParanoidiA4IGY9.
KOiK18494.

Family and domain databases

InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
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.
PROSITEiPS50982. MBD. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4IGY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERSTNARHS TLSSWTRESN TLSVLSKDVS LEDAKEYWKD CQADGKVDWI
60 70 80 90 100
FEKLLNKLKI LWQKIKDGSA TNLEYVRAVI LVNEAEQLEE DTETLHTDIQ
110 120 130 140 150
KENKVQENTD CAPERKEDSC ADLNSDCETD VSGSECEHED HSTVSPPATG
160 170 180 190 200
AVCFGKHLCG PSCLSDINPS LLKKENPLNL PVSCDFQRWR VKTNGSEYPP
210 220 230 240 250
HILYKAPCGR SLRDSDEVHS YLTETGCHFL GVDNFSFSTQ VQLESHLSIK
260 270 280 290 300
QEIVQDCDIS NDVESVPVSL SNEIDDTRPT NFIYRKTSWP PGYSINNFTD
310 320 330 340 350
IFVKCCSCTD GCLDISTCSC LQLTAQAFEK FTDSSLGIGP LGYKHKRLQE
360 370 380 390 400
PVPTGLYECN LSCKCDRTLC QNRVVQHGLQ LRLQVFKTDT KGWGVRCLDD
410 420 430 440 450
VDNGTFVCIY AGRILIRTAD SSVKTTLEDS VACGNEAKED NGSTSTLMLS
460 470 480 490 500
KRKRKPSHSD SEVTVMHLTP YSMRSLGLSV HRQSNTLSLT HLRSGGREIS
510 520 530 540 550
LEPFRRPKTK TSMLQKRRRQ LIEEGACTVH NSSEEEGPTP PQSPKQKFNA
560 570 580 590 600
GRKIHRNENS DETASGYVSE ESSSSVISGG HPSEKPTCRT KSKLNKMTPH
610 620 630 640 650
LSTSPEQTCE EDLHFLDASK EGNVGRFLNH SCCPNLFVQH VFVDTHQKSF
660 670 680 690
PWVAFFTNSV VKAGTELTWD YNYVIGTAPD QEIQCLCGQQ TCKHKIV
Length:697
Mass (Da):78,015
Last modified:May 1, 2007 - v1
Checksum:i355475082EA9861D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC135302 mRNA. Translation: AAI35303.1.
RefSeqiNP_001096194.1. NM_001102724.2.
UniGeneiStr.16757.

Genome annotation databases

GeneIDi100124743.
KEGGixtr:100124743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC135302 mRNA. Translation: AAI35303.1 .
RefSeqi NP_001096194.1. NM_001102724.2.
UniGenei Str.16757.

3D structure databases

ProteinModelPortali A4IGY9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 8364.ENSXETP00000034176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100124743.
KEGGi xtr:100124743.

Organism-specific databases

CTDi 83852.
Xenbasei XB-GENE-1219030. setdb2.

Phylogenomic databases

eggNOGi COG2940.
HOGENOMi HOG000060314.
HOVERGENi HBG106688.
InParanoidi A4IGY9.
KOi K18494.

Family and domain databases

InterProi IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
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 PS50982. MBD. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiSETB2_XENTR
AccessioniPrimary (citable) accession number: A4IGY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3