| Tag | Content |
|---|
| CPLM ID | CPLM-000661 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | PHD finger protein 1 |
Protein Synonyms/Alias | Protein PHF1; hPHF1; Polycomb-like protein 1; hPCl1 |
Gene Name | PHF1 |
Gene Synonyms/Alias | PCL1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 172 | LSLPYGLKGLDWDAG | ubiquitination | [1, 2] |
|
Reference | [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] |
Functional Description | Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18285464 and PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. |
Sequence Annotation | DOMAIN 29 86 Tudor.
ZN_FING 87 142 PHD-type 1.
ZN_FING 186 240 PHD-type 2. |
Keyword | 3D-structure; Alternative splicing; Chromatin regulator; Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 567 AA |
Protein Sequence | MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV 60
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV 120
PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH 180
LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG 240
PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE 300
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG 360
VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS 420
PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG 480
FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD 540
PVRVLARRVR PDGSVQYLVE WGGGGIF 567 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0035861; C:site of double-strand break; IDA:UniProtKB. GO:0035064; F:methylated histone residue binding; IDA:UniProtKB. GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB. GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB. GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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