CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023666
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger and BTB domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 ZBTB1 
Gene Synonyms/Alias
 KIAA0997 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MAKPSHSSYVubiquitination[1]
137ASSKQNSKMIFGVRMubiquitination[2]
194EPLFDVCKKSSVSKLubiquitination[2]
195PLFDVCKKSSVSKLSubiquitination[2]
229GFGFSCEKLLDEHVLubiquitination[2]
275FGEKDSSKTFSAQTDubiquitination[3]
303ASTTGSRKSSTVESEubiquitination[2, 4]
316SEIASEEKSRAAERKubiquitination[4]
328ERKRIIIKMEPEDIPsumoylation[5]
340DIPTDELKDFNIIKVubiquitination[2, 4]
459KCGQILVKGRQLQEHubiquitination[4]
577NERDHRRKHFCNLCGubiquitination[2]
585HFCNLCGKGFYQRCHubiquitination[4]
604YTVHTKEKQFVCQTCubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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]
 [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]
 [5] 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
Functional Description
 May be involved in transcriptional regulation. 
Sequence Annotation
 DOMAIN 24 91 BTB.
 ZN_FING 216 238 C2H2-type 1; atypical.
 ZN_FING 448 470 C2H2-type 2; atypical.
 ZN_FING 534 556 C2H2-type 3; atypical.
 ZN_FING 578 600 C2H2-type 4.
 ZN_FING 606 628 C2H2-type 5.
 ZN_FING 634 656 C2H2-type 6.
 ZN_FING 662 684 C2H2-type 7.
 ZN_FING 686 709 C2H2-type 8.
 MOD_RES 355 355 Phosphoserine.
 MOD_RES 356 356 Phosphothreonine.  
Keyword
 Alternative splicing; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 713 AA 
Protein Sequence
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR MFFMNHQHST 60
AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA MNYLQLYNVP DCLEDIQDAD 120
CSSSKCSSSA SSKQNSKMIF GVRMYEDTVA RNGNEANRWC AEPSSTVNTP HNREADEESL 180
QLGNFPEPLF DVCKKSSVSK LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN 240
RHLYQNTRSY HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG 300
SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK DCNESTDNDE 360
LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG GLENMRPPNN SSPVQEDAEN 420
ASCELCGLTI TEEDLSSHYL AKHIENICAC GKCGQILVKG RQLQEHAQRC GEPQDLTMNG 480
LGNTEEKMDL EENPDEQSEI RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG 540
QRFETENLVV EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH 600
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV RHMISHLSAG 660
ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD MRSHYNAKHL KRT 713 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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
 PF00096; zf-C2H2 
SMART
 SM00225; BTB
 SM00355; ZnF_C2H2 
PROSITE
 PS50097; BTB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS