PHF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PHF1_MOUSE
• UniProt AC: Q9Z1B8
• Protein Name: PHD finger protein 1
• Gene Name: Phf1
• Organism: Mus musculus (Mouse).
• Sequence Length: 559
• Subcellular Localization: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Colocalizes with NEK6 in the centroso
• Protein 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: 18086877 According to other reports, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2. Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53.]
• Protein Sequence: MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGASWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSQLLSALNSHKDRFISGREIKKRKCLFGLHARTPPPVELLTGDGAPTSFPSGQGPGGGVSRPLGKRWRSEPEPLRRRQKGKVEELGPPTAAHSRHGSREQRALQASVSPPPPSPNQSYEGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSEPPDRSPLGLHIGFPTDTPKSSPHSVTASSSSVPALTPGFSRHSPPSPLCRSLSPGTGGGVRGGVSYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	PSLWDPASPAPTSGP CCCCCCCCCCCCCCC	27.30	29514104
50	Phosphorylation	DGLLYLGTIKKVDSA CCEEEEEEEEECCCC	27.33	-
145	Phosphorylation	QCVFAIATKRGGALK HHHHHHHHCCCCCCC	18.37	24759943
408	Phosphorylation	EQRALQASVSPPPPS HHHHHHCCCCCCCCC	15.35	25293948
410	Phosphorylation	RALQASVSPPPPSPN HHHHCCCCCCCCCCC	29.24	21183079
415	Phosphorylation	SVSPPPPSPNQSYEG CCCCCCCCCCCCCCC	42.11	17971449
423	Phosphorylation	PNQSYEGSSGYNFRP CCCCCCCCCCCCCCC	14.51	17971449
504	Phosphorylation	TPGFSRHSPPSPLCR CCCCCCCCCCCCCCC	37.08	22817900
507	Phosphorylation	FSRHSPPSPLCRSLS CCCCCCCCCCCCCCC	33.61	22817900
512	Phosphorylation	PPSPLCRSLSPGTGG CCCCCCCCCCCCCCC	32.00	28833060
514	Phosphorylation	SPLCRSLSPGTGGGV CCCCCCCCCCCCCCC	23.64	28833060
517	Phosphorylation	CRSLSPGTGGGVRGG CCCCCCCCCCCCCCC	35.72	28833060

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PHF1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PHF1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PHF1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PHF1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.