PHF20_HUMAN - dbPTM
PHF20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF20_HUMAN
UniProt AC Q9BVI0
Protein Name PHD finger protein 20
Gene Name PHF20
Organism Homo sapiens (Human).
Sequence Length 1012
Subcellular Localization Nucleus .
Protein Description Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage..
Protein Sequence MTKHPPNRRGISFEVGAQLEARDRLKNWYPAHIEDIDYEEGKVLIHFKRWNHRYDEWFCWDSPYLRPLEKIQLRKEGLHEEDGSSEFQINEQVLACWSDCRFYPAKVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKDQNIVGNARPKETDHKSLSSSPDKREKFKEQRKATVNVKKDKEDKPLKTEKRPKQPDKEGKLICSEKGKVSEKSLPKNEKEDKENISENDREYSGDAQVDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDSNSQTLQPITLELRRRKISKGCEVPLKRPRLDKNSSQEKSKNYSENTDKDLSRRRSSRLSTNGTHEILDPDLVVSDLVDTDPLQDTLSSTKESEEGQLKSALEAGQVSSALTCHSFGDGSGAAGLELNCPSMGENTMKTEPTSPLVELQEISTVEVTNTFKKTDDFGSSNAPAVDLDHKFRCKVVDCLKFFRKAKLLHYHMKYFHGMEKSLEPEESPGKRHVQTRGPSASDKPSQETLTRKRVSASSPTTKDKEKNKEKKFKEFVRVKPKKKKKKKKKTKPECPCSEEISDTSQEPSPPKAFAVTRCGSSHKPGVHMSPQLHGPESGHHKGKVKALEEDNLSESSSESFLWSDDEYGQDVDVTTNPDEELDGDDRYDFEVVRCICEVQEENDFMIQCEECQCWQHGVCMGLLEENVPEKYTCYVCQDPPGQRPGFKYWYDKEWLSRGHMHGLAFLEENYSHQNAKKIVATHQLLGDVQRVIEVLHGLQLKMSILQSREHPDLPLWCQPWKQHSGEGRSHFRNIPVTDTRSKEEAPSYRTLNGAVEKPRPLALPLPRSVEESYITSEHCYQKPRAYYPAVEQKLVVETRGSALDDAVNPLHENGDDSLSPRLGWPLDQDRSKGDSDPKPGSPKVKEYVSKKALPEEAPARKLLDRGGEGLLSSQHQWQFNLLTHVESLQDEVTHRMDSIEKELDVLESWLDYTGELEPPEPLARLPQLKHCIKQLLMDLGKVQQIALCCST
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
103PhosphorylationCWSDCRFYPAKVTAV
HHCCCCEEEEEEEEE		5.28-
112UbiquitinationAKVTAVNKDGTYTVK
EEEEEECCCCCEEEE		51.4329967540
116PhosphorylationAVNKDGTYTVKFYDG
EECCCCCEEEEEECC		18.31-
155PhosphorylationPKETDHKSLSSSPDK
CCCCCCCCCCCCCCH		30.0230266825
157PhosphorylationETDHKSLSSSPDKRE
CCCCCCCCCCCCHHH		35.5430266825
158PhosphorylationTDHKSLSSSPDKREK
CCCCCCCCCCCHHHH		51.7030266825
159PhosphorylationDHKSLSSSPDKREKF
CCCCCCCCCCHHHHH		33.4730266825
177"N6,N6-dimethyllysine"RKATVNVKKDKEDKP
HHHHCCCCCCCCCCC		50.48-
177MethylationRKATVNVKKDKEDKP
HHHHCCCCCCCCCCC		50.48-
205AcetylationGKLICSEKGKVSEKS
CCEEECCCCCCCCCC		47.9725953088
209PhosphorylationCSEKGKVSEKSLPKN
ECCCCCCCCCCCCCC		42.6722817900
211AcetylationEKGKVSEKSLPKNEK
CCCCCCCCCCCCCCH		50.1925953088
225PhosphorylationKEDKENISENDREYS
HHHHCCCCCCHHHHC		41.7628985074
225 (in isoform 2)Phosphorylation-41.76-
231PhosphorylationISENDREYSGDAQVD
CCCCHHHHCCCCCCC		20.88-
232PhosphorylationSENDREYSGDAQVDK
CCCHHHHCCCCCCCC		25.99-
240SumoylationGDAQVDKKPENDIVK
CCCCCCCCCCCCCCC		53.77-
240SumoylationGDAQVDKKPENDIVK
CCCCCCCCCCCCCCC		53.77-
248PhosphorylationPENDIVKSPQENLRE
CCCCCCCCHHHHCCC		22.4128985074
254 (in isoform 2)Phosphorylation-70.5224260401
258 (in isoform 2)Phosphorylation-44.6224260401
263 (in isoform 2)Phosphorylation-29.7924260401
265PhosphorylationRKRGRPPSIAPTAVD
HHCCCCCCCCCCEEC		33.7827050516
269PhosphorylationRPPSIAPTAVDSNSQ
CCCCCCCCEECCCCC		30.2328122231
273PhosphorylationIAPTAVDSNSQTLQP
CCCCEECCCCCCCCE		31.6128122231
275PhosphorylationPTAVDSNSQTLQPIT
CCEECCCCCCCCEEE		28.6128122231
277PhosphorylationAVDSNSQTLQPITLE
EECCCCCCCCEEEHH		27.4726714015
291PhosphorylationELRRRKISKGCEVPL
HHHHHHHCCCCCCCC		26.4822334668
299AcetylationKGCEVPLKRPRLDKN
CCCCCCCCCCCCCCC		55.0425953088
321AcetylationNYSENTDKDLSRRRS
CCCCCCHHHHHHHHH		59.5425953088
328PhosphorylationKDLSRRRSSRLSTNG
HHHHHHHHHCCCCCC		20.2828450419
329PhosphorylationDLSRRRSSRLSTNGT
HHHHHHHHCCCCCCC		35.1128450419
332PhosphorylationRRRSSRLSTNGTHEI
HHHHHCCCCCCCCCC		20.7928387310
333PhosphorylationRRSSRLSTNGTHEIL
HHHHCCCCCCCCCCC		42.1128387310
336PhosphorylationSRLSTNGTHEILDPD
HCCCCCCCCCCCCCC		20.5728387310
347PhosphorylationLDPDLVVSDLVDTDP
CCCCCEEECCCCCCH		20.1128450419
360PhosphorylationDPLQDTLSSTKESEE
CHHHHHHHCCCCCCC		37.7522210691
361PhosphorylationPLQDTLSSTKESEEG
HHHHHHHCCCCCCCC		46.76-
365PhosphorylationTLSSTKESEEGQLKS
HHHCCCCCCCCHHHH		42.37-
408PhosphorylationCPSMGENTMKTEPTS
CCCCCCCCCCCCCCC		18.75-
411PhosphorylationMGENTMKTEPTSPLV
CCCCCCCCCCCCCCE		36.0530278072
414PhosphorylationNTMKTEPTSPLVELQ
CCCCCCCCCCCEEEE		36.4230278072
415PhosphorylationTMKTEPTSPLVELQE
CCCCCCCCCCEEEEE		27.2730278072
424PhosphorylationLVELQEISTVEVTNT
CEEEEECEEEEEECC		26.1622817900
425PhosphorylationVELQEISTVEVTNTF
EEEEECEEEEEECCE		26.7528122231
434UbiquitinationEVTNTFKKTDDFGSS
EEECCEEECCCCCCC		53.6629967540
440UbiquitinationKKTDDFGSSNAPAVD
EECCCCCCCCCCCCC		22.0321963094
451UbiquitinationPAVDLDHKFRCKVVD
CCCCCCHHHCCCHHH		33.8829967540
467AcetylationLKFFRKAKLLHYHMK
HHHHHHHHHHHHHHH		55.4025953088
488PhosphorylationKSLEPEESPGKRHVQ
CCCCCCCCCCCCCCC		36.9723401153
491AcetylationEPEESPGKRHVQTRG
CCCCCCCCCCCCCCC		42.5925953088
496PhosphorylationPGKRHVQTRGPSASD
CCCCCCCCCCCCCCC		36.1826552605
500PhosphorylationHVQTRGPSASDKPSQ
CCCCCCCCCCCCCCH		43.1428555341
502PhosphorylationQTRGPSASDKPSQET
CCCCCCCCCCCCHHH		50.9726552605
504AcetylationRGPSASDKPSQETLT
CCCCCCCCCCHHHHH		44.0425953088
504UbiquitinationRGPSASDKPSQETLT
CCCCCCCCCCHHHHH		44.0429967540
506PhosphorylationPSASDKPSQETLTRK
CCCCCCCCHHHHHCC		46.5228555341
509PhosphorylationSDKPSQETLTRKRVS
CCCCCHHHHHCCCCC		26.2826074081
511PhosphorylationKPSQETLTRKRVSAS
CCCHHHHHCCCCCCC		41.3826074081
516PhosphorylationTLTRKRVSASSPTTK
HHHCCCCCCCCCCCC		26.8528985074
518PhosphorylationTRKRVSASSPTTKDK
HCCCCCCCCCCCCCH		29.3730266825
519PhosphorylationRKRVSASSPTTKDKE
CCCCCCCCCCCCCHH		26.4430266825
521PhosphorylationRVSASSPTTKDKEKN
CCCCCCCCCCCHHHH		48.7230266825
522PhosphorylationVSASSPTTKDKEKNK
CCCCCCCCCCHHHHH		40.4030266825
552AcetylationKKKKKKTKPECPCSE
CCCCCCCCCCCCCCH		47.9326051181
558PhosphorylationTKPECPCSEEISDTS
CCCCCCCCHHCCCCC		24.3327732954
562PhosphorylationCPCSEEISDTSQEPS
CCCCHHCCCCCCCCC		37.8127732954
564PhosphorylationCSEEISDTSQEPSPP
CCHHCCCCCCCCCCC		26.0627732954
565PhosphorylationSEEISDTSQEPSPPK
CHHCCCCCCCCCCCC		37.2227732954
569PhosphorylationSDTSQEPSPPKAFAV
CCCCCCCCCCCEEEE		53.7527732954
590PhosphorylationHKPGVHMSPQLHGPE
CCCCCCCCCCCCCCC		8.4630576142
713UbiquitinationGFKYWYDKEWLSRGH
CCEEEECHHHHHHCC		34.78-
727UbiquitinationHMHGLAFLEENYSHQ
CHHHHHHHHHHCCCH		7.2121963094
737AcetylationNYSHQNAKKIVATHQ
HCCCHHHHHHHHHHH		51.0526051181
788UbiquitinationWKQHSGEGRSHFRNI
CCCCCCCCCHHCCCC		39.6621963094
802PhosphorylationIPVTDTRSKEEAPSY
CCCCCCCCHHHCCCC		46.65-
803AcetylationPVTDTRSKEEAPSYR
CCCCCCCHHHCCCCC		57.1726051181
803SumoylationPVTDTRSKEEAPSYR
CCCCCCCHHHCCCCC		57.17-
803SumoylationPVTDTRSKEEAPSYR
CCCCCCCHHHCCCCC		57.17-
818AcetylationTLNGAVEKPRPLALP
CCCCCCCCCCCCCCC		39.4623749302
829PhosphorylationLALPLPRSVEESYIT
CCCCCCCCHHHHHCC		31.7624719451
834PhosphorylationPRSVEESYITSEHCY
CCCHHHHHCCCHHHC		16.1124719451
843UbiquitinationTSEHCYQKPRAYYPA
CCHHHCCCCHHCCCC		15.2521963094
843AcetylationTSEHCYQKPRAYYPA
CCHHHCCCCHHCCCC		15.2519608861
854SumoylationYYPAVEQKLVVETRG
CCCCCCEEEEEEECC		29.73-
854SumoylationYYPAVEQKLVVETRG
CCCCCCEEEEEEECC		29.73-
862PhosphorylationLVVETRGSALDDAVN
EEEEECCCHHHHHCC		23.5128634120
878PhosphorylationLHENGDDSLSPRLGW
HHHCCCCCCCCCCCC		35.1730266825
880PhosphorylationENGDDSLSPRLGWPL
HCCCCCCCCCCCCCC		16.3630266825
892PhosphorylationWPLDQDRSKGDSDPK
CCCCCCCCCCCCCCC		49.6425159151
896PhosphorylationQDRSKGDSDPKPGSP
CCCCCCCCCCCCCCH		65.5630576142
902PhosphorylationDSDPKPGSPKVKEYV
CCCCCCCCHHHHHHH		30.0325159151
906UbiquitinationKPGSPKVKEYVSKKA
CCCCHHHHHHHCCCC		49.8329967540
911AcetylationKVKEYVSKKALPEEA
HHHHHHCCCCCCCCC		31.8325953088
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
265SPhosphorylationKinaseAKT1P31749
PSP
291SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF20_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 PHF20_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H31_HUMANHIST1H3Aphysical
22449972
P53_HUMANTP53physical
22864287
DPOE3_HUMANPOLE3physical
26344197
KANL3_HUMANKANSL3physical
28514442
KANL2_HUMANKANSL2physical
28514442
KAT8_HUMANKAT8physical
28514442
MCRS1_HUMANMCRS1physical
28514442
PTN14_HUMANPTPN14physical
28514442
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 PHF20_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-843, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASSSPECTROMETRY.

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