CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010587
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Zinc finger BED domain-containing protein 6 
Protein Synonyms/Alias
  
Gene Name
 ZBED6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
289RAVCNICKRSVSRGRubiquitination[1]
467LYDCVREKIFLTLENmethylation[2]
479LENVQSQKIHLTVDImethylation[2]
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]
 [2] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3' and represses transcription of IGF2. May also regulate expression of other target genes containing this consensus binding site (By similarity). 
Sequence Annotation
 ZN_FING 130 187 BED-type 1.
 ZN_FING 264 321 BED-type 2.
 REGION 866 948 HATC (Hobo-Ac-Tam3) domain.  
Keyword
 Complete proteome; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 979 AA 
Protein Sequence
MSVCTLSVPV SSLSPGRRCN TFSDSGILGC VPINSNTDEE DVVEEKMVAE GVNKEAKQPA 60
KKKRKKGLRI KGKRRRKKLI LAKKFSKDLG SGRPVADAPA LLASNDPEQD EESLFESNIE 120
KQIYLPSTRA KTSIVWHFFH VDPQYTWRAI CNLCEKSVSR GKPGSHLGTS TLQRHLQARH 180
SPHWTRANKF GVASGEEDFT LDVSLSPSSG SNGSFEYIPT DPLDDNRMGK KHDKSASDAL 240
RAERGRFLIK SNIVKHALIP GTRAKTSAVW NFFYTDPQHI SRAVCNICKR SVSRGRPGSH 300
LGTSTLQRHL QATHPIHWAV ANKDSGAVAN GLDEAETERS DLLSDTLHGE KSTGSQDLTA 360
EDLSDSDSDE PMLEVENRSE SPIPVAEQGT LMRAQERETT CCGNPVSSHI SQAIIQMIVE 420
DMHPYNYFST PAFQRFMQIV APDYRLPSET YFFTKAVPQL YDCVREKIFL TLENVQSQKI 480
HLTVDIWTHD PSTDYFIVTV HWVSLETASF LNNGRIPDFR KWAVLCVTGL AKDCLITNIL 540
QELNDQIGLW LSPNFLIPSF IVSDNSSNVV HAIKDGGFTH VPCFLHCLNM VIQDFFCEHK 600
SIENMLVAAR KTCHHFSHSV KARQILQEFQ NDHQLPWKNL KQDETGHWIS TFYMLKWLLE 660
HCYSVHHSLG RASGVVLTSL QWTLMTYVCD ILKPFEEATQ KVSVKTAGLN QVLPLIHHLL 720
LSLQKLREDF QVRGITQALN LVDSLSLKLE TDTLLSAMLK SKPCILATLL DPCFKNSLED 780
FFPQGADLET YKQFLAEEVC NYMESSPEIC QIPTSEASCP SVTVGADSFT SSLKEGTSSS 840
GSVDSSAVDN VALGSKSFMF PSAVAVVDEY FKEKYSEFSG GDDPLIYWQR KISIWPALTQ 900
VAIQYLSCPM CSWQSECIFT KNSHFHPKQI MSLDFDNIEQ LMFLKMNLKN VNYDYSTLVL 960
SWDPEQNEVV QSSEKEILP 979 
Gene Ontology
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR008906; HATC.
 IPR012337; RNaseH-like_dom.
 IPR003656; Znf_BED_prd. 
Pfam
 PF05699; Dimer_Tnp_hAT
 PF02892; zf-BED 
SMART
 SM00614; ZnF_BED 
PROSITE
 PS50808; ZF_BED 
PRINTS