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Protein

DNA (cytosine-5)-methyltransferase 3-like

Gene

Dnmt3l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytically inactive regulatory factor of DNA methyltransferases. It is essential for the function of DNMT3A and DNMT3B. Activates DNMT3A and DNMT3B by binding to their catalytic domain. Accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri87 – 11731GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri128 – 18457PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • DNA methylation Source: InterPro
  • response to ethanol Source: RGD
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 3-like
Gene namesi
Name:Dnmt3l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303239. Dnmt3l.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422DNA (cytosine-5)-methyltransferase 3-likePRO_0000281744Add
BLAST

Proteomic databases

PaxDbiQ1LZ50.
PRIDEiQ1LZ50.

Interactioni

Subunit structurei

Homodimer. Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with histone H3 (via N-terminus) (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001610.

Structurei

3D structure databases

ProteinModelPortaliQ1LZ50.
SMRiQ1LZ50. Positions 69-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 208133ADDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ADD domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri87 – 11731GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri128 – 18457PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IIXK. Eukaryota.
ENOG4111C55. LUCA.
HOGENOMiHOG000246422.
HOVERGENiHBG051382.
InParanoidiQ1LZ50.
KOiK17400.
PhylomeDBiQ1LZ50.

Family and domain databases

InterProiIPR025766. ADD.
IPR030486. DNMT3L.
[Graphical view]
PANTHERiPTHR23068:SF13. PTHR23068:SF13. 1 hit.
PROSITEiPS51533. ADD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1LZ50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRETPSSC SKTHETLNLE TPESSSTDPD SPLEEQWPKS APDLKEEDSM
60 70 80 90 100
DMVLEDSKEP LTPSSPPTGR EVIRYEVNVN QRNIEDICLC CGSLQVYAQH
110 120 130 140 150
PLFEGGICAP CKDKFLETLF LYDEDGHQSY CTICCSGHTL FICESPDCTR
160 170 180 190 200
CYCFECVDIL VGPGTSERIN AMACWVCFLC LPFSRSGLLQ RRKKWRHQLK
210 220 230 240 250
AFHDREGASP VEIYKTVSAW KRQPVRVLSL FGNIDKELKS LGFLESSSGS
260 270 280 290 300
EGGTLKYVED VTNVVRREVE KWGPFDLVYG STQPLGYSCD RCPGWYMFQF
310 320 330 340 350
HRILQYARPR QDSQQPFFWI FVDNLLLTED DQETTVRFLQ TEAVTLQDVR
360 370 380 390 400
GRVLQNAMRV WSNIPGLKSK HADLTPKEEQ SLQTQVRTRS KLAAQKVDSL
410 420
VKYCLLPLRE YFKYFSQNSL PL
Length:422
Mass (Da):48,279
Last modified:May 30, 2006 - v1
Checksum:iBFA7A78D1E7CBD90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03116801 Genomic DNA. No translation available.
AABR03116733 Genomic DNA. No translation available.
BN000398 mRNA. Translation: CAE52320.1.
RefSeqiNP_001003964.1. NM_001003964.1.
UniGeneiRn.129905.

Genome annotation databases

GeneIDi309680.
KEGGirno:309680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03116801 Genomic DNA. No translation available.
AABR03116733 Genomic DNA. No translation available.
BN000398 mRNA. Translation: CAE52320.1.
RefSeqiNP_001003964.1. NM_001003964.1.
UniGeneiRn.129905.

3D structure databases

ProteinModelPortaliQ1LZ50.
SMRiQ1LZ50. Positions 69-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001610.

Proteomic databases

PaxDbiQ1LZ50.
PRIDEiQ1LZ50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi309680.
KEGGirno:309680.

Organism-specific databases

CTDi29947.
RGDi1303239. Dnmt3l.

Phylogenomic databases

eggNOGiENOG410IIXK. Eukaryota.
ENOG4111C55. LUCA.
HOGENOMiHOG000246422.
HOVERGENiHBG051382.
InParanoidiQ1LZ50.
KOiK17400.
PhylomeDBiQ1LZ50.

Miscellaneous databases

NextBioi661203.
PROiQ1LZ50.

Family and domain databases

InterProiIPR025766. ADD.
IPR030486. DNMT3L.
[Graphical view]
PANTHERiPTHR23068:SF13. PTHR23068:SF13. 1 hit.
PROSITEiPS51533. ADD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Identification of 11 pseudogenes in the DNA methyltransferase gene family in rodents and humans and implications for the functional loci."
    Lees-Murdock D.J., McLoughlin G.A., McDaid J.R., Quinn L.M., O'Doherty A., Hiripi L., Hack C.J., Walsh C.P.
    Genomics 84:193-204(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiDNM3L_RAT
AccessioniPrimary (citable) accession number: Q1LZ50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 30, 2006
Last modified: January 20, 2016
This is version 60 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.