| Tag | Content |
|---|
| CPLM ID | CPLM-018982 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lethal(3)malignant brain tumor-like protein 2 |
Protein Synonyms/Alias | H-l(3)mbt-like protein 2; L(3)mbt-like protein 2 |
Gene Name | L3MBTL2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 294 | HAKFTDWKGYLMKRL | ubiquitination | [1] | | 405 | AHHPTFRKIYCDAVP | ubiquitination | [1] | | 541 | HGFKVGMKLEAVDLM | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. |
Sequence Annotation | REPEAT 179 283 MBT 1.
REPEAT 291 391 MBT 2.
REPEAT 397 500 MBT 3.
REPEAT 508 604 MBT 4.
ZN_FING 81 116 FCS-type.
MOD_RES 13 13 Phosphoserine.
MOD_RES 338 338 Phosphoserine.
MOD_RES 683 683 Phosphoserine.
MOD_RES 688 688 Phosphoserine.
MOD_RES 689 689 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 705 AA |
Protein Sequence | MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE SSEAENEDRE 60
AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS 120
NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHSQG TGQLADGTPT GQDALVLGFD 180
WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG 240
YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR 300
LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG GRLRLLYEDG 360
DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH PTFRKIYCDA VPYLFKKVRA 420
VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS 480
SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM 540
KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ 600
LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL EDDPQGARKI 660
SSEPVPGEII AVRVKEEHLD VASPDKASSP ELPVSVENIK QETDD 705 |
Gene Ontology | GO:0005634; C:nucleus; NAS:UniProtKB. GO:0035064; F:methylated histone residue binding; IDA:UniProtKB. GO:0003714; F:transcription corepressor activity; NAS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0016568; P:chromatin modification; NAS:UniProtKB. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |