CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013993
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PHD finger protein 19 
Protein Synonyms/Alias
 Polycomb-like protein 3; hPCL3 
Gene Name
 PHF19 
Gene Synonyms/Alias
 PCL3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105KCNICLGKTSGPLNEubiquitination[1]
355PGKLLPDKGLLPNENubiquitination[1]
375LRKRGKSKPGLLPHEubiquitination[1]
554GRLACGEKYQVLARRubiquitination[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
 Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys- 36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. 
Sequence Annotation
 DOMAIN 40 93 Tudor.
 ZN_FING 96 151 PHD-type 1.
 ZN_FING 195 249 PHD-type 2.
 REGION 74 80 Histone H3K36me3 binding.
 BINDING 47 47 Histone H3K36me3.
 BINDING 55 55 Histone H3K36me3.  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 580 AA 
Protein Sequence
MENRALDPGT RDSYGATSHL PNKGALAKVK NNFKDLMSKL TEGQYVLCRW TDGLYYLGKI 60
KRVSSSKQSC LVTFEDNSKY WVLWKDIQHA GVPGEEPKCN ICLGKTSGPL NEILICGKCG 120
LGYHQQCHIP IAGSADQPLL TPWFCRRCIF ALAVRKGGAL KKGAIARTLQ AVKMVLSYQP 180
EELEWDSPHR TNQQQCYCYC GGPGEWYLRM LQCYRCRQWF HEACTQCLNE PMMFGDRFYL 240
FFCSVCNQGP EYIERLPLRW VDVVHLALYN LGVQSKKKYF DFEEILAFVN HHWELLQLGK 300
LTSTPVTDRG PHLLNALNSY KSRFLCGKEI KKKKCIFRLR IRVPPNPPGK LLPDKGLLPN 360
ENSASSELRK RGKSKPGLLP HEFQQQKRRV YRRKRSKFLL EDAIPSSDFT SAWSTNHHLA 420
SIFDFTLDEI QSLKSASSGQ TFFSDVDSTD AASTSGSAST SLSYDSRWTV GSRKRKLAAK 480
AYMPLRAKRW AAELDGRCPS DSSAEGASVP ERPDEGIDSH TFESISEDDS SLSHLKSSIT 540
NYFGAAGRLA CGEKYQVLAR RVTPEGKVQY LVEWEGTTPY 580 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR025894; Mtf2_C_dom.
 IPR002999; Tudor.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF14061; Mtf2_C
 PF00628; PHD 
SMART
 SM00249; PHD
 SM00333; TUDOR 
PROSITE
 PS50304; TUDOR
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS