PHF1_HUMAN - dbPTM
PHF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF1_HUMAN
UniProt AC O43189
Protein Name PHD finger protein 1
Gene Name PHF1
Organism Homo sapiens (Human).
Sequence Length 567
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. Co-localizes 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: 18285464 and 23273982). According to another report]
Protein Sequence MAQPPRLSRSGASSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGTSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSRLLSALNSHKDRFISGREIKKRKCLFGLHARMPPPVEPPTGDGALTSFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPPSAVRNQPEPQEQRERAHLQRALQASVSPPSPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSGPPDRSPLELHIGFPTDIPKSAPHSMTASSSSVSSPSPGLPRRSAPPSPLCRSLSPGTGGGVRGGVGYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF
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 Orthologous
Protein Cluster
8PhosphorylationMAQPPRLSRSGASSL
CCCCCCCCCCCCCCC		26.1927251275
10PhosphorylationQPPRLSRSGASSLWD
CCCCCCCCCCCCCCC		35.0223403867
13PhosphorylationRLSRSGASSLWDPAS
CCCCCCCCCCCCCCC		29.5023403867
14PhosphorylationLSRSGASSLWDPASP
CCCCCCCCCCCCCCC		32.7123403867
20PhosphorylationSSLWDPASPAPTSGP
CCCCCCCCCCCCCCC		27.3023401153
24PhosphorylationDPASPAPTSGPRPRL
CCCCCCCCCCCCCCC		48.7123403867
25PhosphorylationPASPAPTSGPRPRLW
CCCCCCCCCCCCCCC		45.8223403867
145PhosphorylationQCVFAIATKRGGALK
HHHHHHHHCCCCCCC		18.3720860994
156PhosphorylationGALKKGPYARAMLGM
CCCCCCHHHHHHHCC		19.86-
169PhosphorylationGMKLSLPYGLKGLDW
CCEECCCCCCCCCCC		40.14-
172UbiquitinationLSLPYGLKGLDWDAG
ECCCCCCCCCCCCCH		53.7321890473
172UbiquitinationLSLPYGLKGLDWDAG
ECCCCCCCCCCCCCH		53.7321890473
172 (in isoform 2)Ubiquitination-53.7321890473
172 (in isoform 1)Ubiquitination-53.7321890473
182PhosphorylationDWDAGHLSNRQQSYC
CCCCHHCCCCCCCEE		25.0527251275
187PhosphorylationHLSNRQQSYCYCGGP
HCCCCCCCEEECCCC		14.6130576142
188PhosphorylationLSNRQQSYCYCGGPG
CCCCCCCEEECCCCC		5.3230576142
190PhosphorylationNRQQSYCYCGGPGEW
CCCCCEEECCCCCHH		5.9630576142
220PhosphorylationEACTQCLSKPLLYGD
HHHHHHHHCCCCCCC		39.5924719451
260PhosphorylationDVAHLVLYHLSVCCK
HHHHHHHHHHHHHCC		8.01-
307PhosphorylationERSSRLLSALNSHKD
HHHHHHHHHHHHCCC		34.9925003641
311PhosphorylationRLLSALNSHKDRFIS
HHHHHHHHCCCCCCC		32.5325003641
313UbiquitinationLSALNSHKDRFISGR
HHHHHHCCCCCCCHH		50.88-
318PhosphorylationSHKDRFISGREIKKR
HCCCCCCCHHHHHHC		29.1424719451
343PhosphorylationPPPVEPPTGDGALTS
CCCCCCCCCCCCCCC		59.63-
353PhosphorylationGALTSFPSGQGPGGG
CCCCCCCCCCCCCCC		41.5626714015
359 (in isoform 2)Phosphorylation-36.1430266825
359PhosphorylationPSGQGPGGGVSRPLG
CCCCCCCCCCCCCCC		36.1427251275
360PhosphorylationSGQGPGGGVSRPLGK
CCCCCCCCCCCCCCC		21.8324719451
360 (in isoform 2)Phosphorylation-21.8330266825
391PhosphorylationVEELGPPSAVRNQPE
HHHCCCCHHHHCCCC		42.3921815630
415PhosphorylationLQRALQASVSPPSPS
HHHHHHHHCCCCCCC		15.3527251275
417PhosphorylationRALQASVSPPSPSPN
HHHHHHCCCCCCCCC		28.7030108239
420PhosphorylationQASVSPPSPSPNQSY
HHHCCCCCCCCCCCC		41.2023142980
422PhosphorylationSVSPPSPSPNQSYQG
HCCCCCCCCCCCCCC		40.6029496963
426PhosphorylationPSPSPNQSYQGSSGY
CCCCCCCCCCCCCCC		26.5127251275
427PhosphorylationSPSPNQSYQGSSGYN
CCCCCCCCCCCCCCC		13.7130108239
430PhosphorylationPNQSYQGSSGYNFRP
CCCCCCCCCCCCCCC		12.6927251275
431PhosphorylationNQSYQGSSGYNFRPT
CCCCCCCCCCCCCCC		52.7127251275
433PhosphorylationSYQGSSGYNFRPTDA
CCCCCCCCCCCCCCC		17.0527251275
438PhosphorylationSGYNFRPTDARCLPS
CCCCCCCCCCCCCCC		37.7330108239
445PhosphorylationTDARCLPSSPIRMFA
CCCCCCCCCCCEEEE		35.4827251275
446PhosphorylationDARCLPSSPIRMFAS
CCCCCCCCCCEEEEE		23.5428985074
453PhosphorylationSPIRMFASFHPSAST
CCCEEEEEECCCCCC		16.9024114839
457PhosphorylationMFASFHPSASTAGTS
EEEEECCCCCCCCCC		26.7024114839
460PhosphorylationSFHPSASTAGTSGDS
EECCCCCCCCCCCCC		28.9024114839
467PhosphorylationTAGTSGDSGPPDRSP
CCCCCCCCCCCCCCC		57.6426714015
473PhosphorylationDSGPPDRSPLELHIG
CCCCCCCCCCEEEEE		41.0126714015
483PhosphorylationELHIGFPTDIPKSAP
EEEEECCCCCCCCCC		44.2820873877
488O-linked_GlycosylationFPTDIPKSAPHSMTA
CCCCCCCCCCCCCCC		41.5029351928
496PhosphorylationAPHSMTASSSSVSSP
CCCCCCCCCCCCCCC		22.9127251275
497PhosphorylationPHSMTASSSSVSSPS
CCCCCCCCCCCCCCC		24.9427251275
498PhosphorylationHSMTASSSSVSSPSP
CCCCCCCCCCCCCCC		32.0627251275
499PhosphorylationSMTASSSSVSSPSPG
CCCCCCCCCCCCCCC		28.1527251275
501PhosphorylationTASSSSVSSPSPGLP
CCCCCCCCCCCCCCC		38.1827251275
502PhosphorylationASSSSVSSPSPGLPR
CCCCCCCCCCCCCCC		27.5226714015
504PhosphorylationSSSVSSPSPGLPRRS
CCCCCCCCCCCCCCC		33.2827251275
511PhosphorylationSPGLPRRSAPPSPLC
CCCCCCCCCCCCCCC		46.5427251275
515PhosphorylationPRRSAPPSPLCRSLS
CCCCCCCCCCCCCCC		29.4630266825
520PhosphorylationPPSPLCRSLSPGTGG
CCCCCCCCCCCCCCC		32.0026055452
522PhosphorylationSPLCRSLSPGTGGGV
CCCCCCCCCCCCCCC		23.6426055452
530MethylationPGTGGGVRGGVGYLS
CCCCCCCCCCCCCCC		39.15115383519
535PhosphorylationGVRGGVGYLSRGDPV
CCCCCCCCCCCCCCE		10.0917929957
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PHF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF1_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PHF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBPMS_HUMANRBPMSphysical
16189514
THAP1_HUMANTHAP1physical
16189514
EZH2_HUMANEZH2physical
11571280
H31_HUMANHIST1H3Aphysical
21167174
XRCC5_HUMANXRCC5physical
18385154
XRCC6_HUMANXRCC6physical
18385154
SMC1A_HUMANSMC1Aphysical
18385154
P53_HUMANTP53physical
18385154
NCTR1_HUMANNCR1physical
18385154
RAD50_HUMANRAD50physical
18385154
DHX9_HUMANDHX9physical
18385154
EZH2_HUMANEZH2physical
18385154
RBBP7_HUMANRBBP7physical
18385154
SUZ12_HUMANSUZ12physical
18385154
EZH2_HUMANEZH2physical
18285464
SUZ12_HUMANSUZ12physical
18285464
EED_HUMANEEDphysical
18285464
RBBP7_HUMANRBBP7physical
18285464
HIC1_HUMANHIC1physical
22315224
P53_HUMANTP53physical
23150668
TFCP2_HUMANTFCP2physical
25416956
PDLI7_HUMANPDLIM7physical
25416956
CACO2_HUMANCALCOCO2physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
DHB14_HUMANHSD17B14physical
25416956
VAC14_HUMANVAC14physical
25416956
BIRC7_HUMANBIRC7physical
25416956
AT7L1_HUMANATXN7L1physical
25416956
H31T_HUMANHIST3H3physical
23273982
SUZ12_HUMANSUZ12physical
23273982
EED_HUMANEEDphysical
23273982
HDAC1_HUMANHDAC1physical
23273982
RBBP4_HUMANRBBP4physical
23273982
EZH1_HUMANEZH1physical
23273982
EZH2_HUMANEZH2physical
23273982
RPB7_HUMANPOLR2Gphysical
23273982
TFCP2_HUMANTFCP2physical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND MASSSPECTROMETRY.

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