CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011293
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger and BTB domain-containing protein 16 
Protein Synonyms/Alias
 Promyelocytic leukemia zinc finger protein; Zinc finger protein 145; Zinc finger protein PLZF 
Gene Name
 ZBTB16 
Gene Synonyms/Alias
 PLZF; ZNF145 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
154DRKARYLKNIFISKHubiquitination[1]
242HPGVAEVKTEMMQVDsumoylation[2, 3, 4]
387IQRELFSKLGELAVGsumoylation[3, 4]
396GELAVGMKSESRTIGsumoylation[3, 4]
562FRDESTLKSHKRIHTacetylation[5]
565ESTLKSHKRIHTGEKacetylation[5]
647PSLSSMQKHMKGHKPacetylation[5]
650SSMQKHMKGHKPEEIacetylation[5]
653QKHMKGHKPEEIPPDacetylation[5]
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] Modification of promyelocytic leukemia zinc finger protein (PLZF) by SUMO-1 conjugation regulates its transcriptional repressor activity.
 Kang SI, Chang WJ, Cho SG, Kim IY.
 J Biol Chem. 2003 Dec 19;278(51):51479-83. [PMID: 14527952]
 [3] SUMO modification modulates the transrepression activity of PLZF.
 Chao TT, Chang CC, Shih HM.
 Biochem Biophys Res Commun. 2007 Jun 29;358(2):475-82. [PMID: 17498654]
 [4] Redox-mediated modification of PLZF by SUMO-1 and ubiquitin.
 Kang SI, Choi HW, Kim IY.
 Biochem Biophys Res Commun. 2008 May 16;369(4):1209-14. [PMID: 18348865]
 [5] Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein.
 Guidez F, Howell L, Isalan M, Cebrat M, Alani RM, Ivins S, Hormaeche I, McConnell MJ, Pierce S, Cole PA, Licht J, Zelent A.
 Mol Cell Biol. 2005 Jul;25(13):5552-66. [PMID: 15964811] 
Functional Description
 Probable transcription factor. May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. 
Sequence Annotation
 DOMAIN 34 96 BTB.
 ZN_FING 404 426 C2H2-type 1.
 ZN_FING 432 454 C2H2-type 2.
 ZN_FING 461 483 C2H2-type 3.
 ZN_FING 490 512 C2H2-type 4.
 ZN_FING 518 540 C2H2-type 5.
 ZN_FING 546 568 C2H2-type 6.
 ZN_FING 574 596 C2H2-type 7.
 ZN_FING 602 624 C2H2-type 8.
 ZN_FING 630 652 C2H2-type 9.
 MOD_RES 76 76 Phosphoserine; by PDPK1 (Potential).
 MOD_RES 184 184 Phosphoserine; by PDPK1 (Potential).
 MOD_RES 197 197 Phosphoserine; by PDPK1 (Potential).
 MOD_RES 256 256 Phosphoserine; by PDPK1 (Potential).
 MOD_RES 282 282 Phosphothreonine; by PDPK1 (Potential).
 MOD_RES 628 628 Phosphoserine; by PDPK1 (Potential).  
Keyword
 3D-structure; Alternative splicing; Chromosomal rearrangement; Complete proteome; Disease mutation; DNA-binding; Mental retardation; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 673 AA 
Protein Sequence
MDLTKMGMIQ LQNPSHPTGL LCKANQMRLA GTLCDVVIMV DSQEFHAHRT VLACTSKMFE 60
ILFHRNSQHY TLDFLSPKTF QQILEYAYTA TLQAKAEDLD DLLYAAEILE IEYLEEQCLK 120
MLETIQASDD NDTEATMADG GAEEEEDRKA RYLKNIFISK HSSEESGYAS VAGQSLPGPM 180
VDQSPSVSTS FGLSAMSPTK AAVDSLMTIG QSLLQGTLQP PAGPEEPTLA GGGRHPGVAE 240
VKTEMMQVDE VPSQDSPGAA ESSISGGMGD KVEERGKEGP GTPTRSSVIT SARELHYGRE 300
ESAEQVPPPA EAGQAPTGRP EHPAPPPEKH LGIYSVLPNH KADAVLSMPS SVTSGLHVQP 360
ALAVSMDFST YGGLLPQGFI QRELFSKLGE LAVGMKSESR TIGEQCSVCG VELPDNEAVE 420
QHRKLHSGMK TYGCELCGKR FLDSLRLRMH LLAHSAGAKA FVCDQCGAQF SKEDALETHR 480
QTHTGTDMAV FCLLCGKRFQ AQSALQQHME VHAGVRSYIC SECNRTFPSH TALKRHLRSH 540
TGDHPYECEF CGSCFRDEST LKSHKRIHTG EKPYECNGCG KKFSLKHQLE THYRVHTGEK 600
PFECKLCHQR SRDYSAMIKH LRTHNGASPY QCTICTEYCP SLSSMQKHMK GHKPEEIPPD 660
WRIEKTYLYL CYV 673 
Gene Ontology
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0017053; C:transcriptional repressor complex; IDA:MGI.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009952; P:anterior/posterior pattern specification; IEA:Compara.
 GO:0006915; P:apoptotic process; NAS:UniProtKB.
 GO:0051216; P:cartilage development; IDA:UniProtKB.
 GO:0007417; P:central nervous system development; ISS:UniProtKB.
 GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
 GO:0009880; P:embryonic pattern specification; IEA:Compara.
 GO:0035136; P:forelimb morphogenesis; IEA:Compara.
 GO:0048133; P:male germ-line stem cell division; IEA:Compara.
 GO:0001823; P:mesonephros development; ISS:UniProtKB.
 GO:0030099; P:myeloid cell differentiation; TAS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0061036; P:positive regulation of cartilage development; IDA:UniProtKB.
 GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
 GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
 GO:0045778; P:positive regulation of ossification; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 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