CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019103
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger and BTB domain-containing protein 9 
Protein Synonyms/Alias
  
Gene Name
 ZBTB9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76ASPYFHDKLLLGDAPubiquitination[1]
286PPKIFYIKQEPFEPKsumoylation[2]
307GTQPGGAKEETKVFSubiquitination[3]
382GTPPADGKRFGCLCGubiquitination[1, 3, 4]
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] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 DOMAIN 48 112 BTB.
 ZN_FING 411 433 C2H2-type 1.
 ZN_FING 438 460 C2H2-type 2; atypical.  
Keyword
 Complete proteome; DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 473 AA 
Protein Sequence
METPTPLPPV PASPTCNPAP RTIQIEFPQH SSSLLESLNR HRLEGKFCDV SLLVQGRELR 60
AHKAVLAAAS PYFHDKLLLG DAPRLTLPSV IEADAFEGLL QLIYSGRLRL PLDALPAHLL 120
VASGLQMWQV VDQCSEILRE LETSGGGISA RGGNSYHALL STTSSTGGWC IRSSPFQTPV 180
QSSASTESPA STESPVGGEG SELGEVLQIQ VEEEEEEEED DDDEDQGSAT LSQTPQPQRV 240
SGVFPRPHGP HPLPMTATPR KLPEGESAPL ELPAPPALPP KIFYIKQEPF EPKEEISGSG 300
TQPGGAKEET KVFSGGDTEG NGELGFLLPS GPGPTSGGGG PSWKPVDLHG NEILSGGGGP 360
GGAGQAVHGP VKLGGTPPAD GKRFGCLCGK RFAVKPKRDR HIMLTFSLRP FGCGICNKRF 420
KLKHHLTEHM KTHAGALHAC PHCGRRFRVH ACFLRHRDLC KGQGWATAHW TYK 473 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00651; BTB 
SMART
 SM00225; BTB
 SM00355; ZnF_C2H2 
PROSITE
 PS50097; BTB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS