PHF2_HUMAN - dbPTM
PHF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF2_HUMAN
UniProt AC O75151
Protein Name Lysine-specific demethylase PHF2
Gene Name PHF2 {ECO:0000312|HGNC:HGNC:8920}
Organism Homo sapiens (Human).
Sequence Length 1096
Subcellular Localization Nucleus, nucleolus . Chromosome, centromere, kinetochore .
Protein Description Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA..
Protein Sequence MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGQAPDVKPVQNGSQLFIKELRSRTFPSAEDVVARVPGSQLTLGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKTFYLIRPASANISLYERWRSASNHSEMFFADQVDKCYKCIVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFKPSQLIKDLAKEIRLSENASKAVRPEVNTVASSDEVCDGDREKEEPPSPIEATPPQSLLEKVSKKKTPKTVKMPKPSKIPKPPKPPKPPRPPKTLKLKDGGKKKGKKSRESASPTIPNLDLLEAHTKEALTKMEPPKKGKATKSVLSVPNKDVVHMQNDVERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQKLEKSPLAGNKDNKFSFSFSNKKLLGSKALRPPTSPGVFGALQNFKEDKPKPVRDEYEYVSDDGELKIDEFPIRRKKNAPKRDLSFLLDKKAVLPTPVTKPKLDSAAYKSDDSSDEGSLHIDTDTKPGRNARVKKESGSSAAGILDLLQASEEVGALEYNPSSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGAGQAKGSSLAAHGARKNGGGSGKSAGKRLLKRAAKNSVDLDDYEEEQDHLDACFKDSDYVYPSLESDEDNPIFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKSKKKKSAKRKLTPNTTSPSTSTSISAGTTSTSTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFTGAQAGRTSQPMAPGVFLTQRRPSASSPNNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL
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
33PhosphorylationCKDWFHGSCVGVEEE
CCHHHCCCCCCCCCC		9.3222817900
80SumoylationPGQAPDVKPVQNGSQ
CCCCCCCCCCCCCCE		47.02-
80SumoylationPGQAPDVKPVQNGSQ
CCCCCCCCCCCCCCE		47.02-
86PhosphorylationVKPVQNGSQLFIKEL
CCCCCCCCEEHHHHH		31.12-
158PhosphorylationNYVGPERSVDVTDVT
HCCCCCCCCCCCCCC		22.4720068231
162PhosphorylationPERSVDVTDVTKQKD
CCCCCCCCCCCCCCC		21.9320068231
165PhosphorylationSVDVTDVTKQKDCKM
CCCCCCCCCCCCCCC		30.4820068231
166AcetylationVDVTDVTKQKDCKMK
CCCCCCCCCCCCCCH		56.0225953088
171UbiquitinationVTKQKDCKMKLKEFV
CCCCCCCCCHHHHHH		49.5622817900
173UbiquitinationKQKDCKMKLKEFVDY
CCCCCCCHHHHHHHH		41.7322817900
175AcetylationKDCKMKLKEFVDYYY
CCCCCHHHHHHHHHH		43.5226051181
175UbiquitinationKDCKMKLKEFVDYYY
CCCCCHHHHHHHHHH		43.5221890473
180PhosphorylationKLKEFVDYYYSTNRK
HHHHHHHHHHHCCCC		10.0524043423
181PhosphorylationLKEFVDYYYSTNRKR
HHHHHHHHHHCCCCE		6.1024043423
182PhosphorylationKEFVDYYYSTNRKRV
HHHHHHHHHCCCCEE		11.6424043423
183PhosphorylationEFVDYYYSTNRKRVL
HHHHHHHHCCCCEEE		11.7724043423
184PhosphorylationFVDYYYSTNRKRVLN
HHHHHHHCCCCEEEE		23.9524043423
200PhosphorylationTNLEFSDTRMSSFVE
ECCEECCCCHHHCCC		27.3730576142
214UbiquitinationEPPDIVKKLSWVENY
CCHHHHHHHHCHHHH		36.5429967540
259PhosphorylationSGGASAWYHVLKGEK
CCCCCEEEEEECCCE		5.0329396449
382UbiquitinationKHLLEAFKGSHKSGK
HHHHHHHCCCCCCCC		67.5629967540
389UbiquitinationKGSHKSGKQLPPHLV
CCCCCCCCCCCCHHH		56.6129967540
392UbiquitinationHKSGKQLPPHLVQGA
CCCCCCCCCHHHHHH		16.2721890473
412UbiquitinationAFRSWTKKQALAEHE
HHHHHCHHHHHHHCH		33.1733845483
427UbiquitinationDELPEHFKPSQLIKD
HHCCHHCCHHHHHHH		45.7422817900
455PhosphorylationAVRPEVNTVASSDEV
HCCCCCCCCCCCCCC		23.7123663014
458PhosphorylationPEVNTVASSDEVCDG
CCCCCCCCCCCCCCC		33.7029255136
459PhosphorylationEVNTVASSDEVCDGD
CCCCCCCCCCCCCCC		28.2229255136
474PhosphorylationREKEEPPSPIEATPP
CCCCCCCCCCCCCCC		49.5829255136
479PhosphorylationPPSPIEATPPQSLLE
CCCCCCCCCCHHHHH		23.7830266825
483PhosphorylationIEATPPQSLLEKVSK
CCCCCCHHHHHHHHC		40.4730266825
493PhosphorylationEKVSKKKTPKTVKMP
HHHHCCCCCCCCCCC		38.6126074081
496PhosphorylationSKKKTPKTVKMPKPS
HCCCCCCCCCCCCCC		26.9426074081
532UbiquitinationDGGKKKGKKSRESAS
CCCCCCCCCCCCCCC		57.3630230243
534PhosphorylationGKKKGKKSRESASPT
CCCCCCCCCCCCCCC		44.7830266825
537PhosphorylationKGKKSRESASPTIPN
CCCCCCCCCCCCCCC		32.7029255136
539PhosphorylationKKSRESASPTIPNLD
CCCCCCCCCCCCCHH		31.6829255136
541PhosphorylationSRESASPTIPNLDLL
CCCCCCCCCCCHHHH		46.7122167270
552PhosphorylationLDLLEAHTKEALTKM
HHHHHHHHHHHHHCC		37.3123927012
570PhosphorylationKKGKATKSVLSVPNK
CCCCCCCEEECCCCC		24.7624247654
612PhosphorylationYKNSKPDSLLKMEEE
HCCCCCCHHHHHHHH		44.0925159151
625PhosphorylationEEQKLEKSPLAGNKD
HHHHHHHCCCCCCCC		18.7723401153
631"N6,N6-dimethyllysine"KSPLAGNKDNKFSFS
HCCCCCCCCCCCEEE		62.86-
631MethylationKSPLAGNKDNKFSFS
HCCCCCCCCCCCEEE		62.86-
636PhosphorylationGNKDNKFSFSFSNKK
CCCCCCCEEEECCCE		22.9124719451
638PhosphorylationKDNKFSFSFSNKKLL
CCCCCEEEECCCEEC		26.9425159151
640PhosphorylationNKFSFSFSNKKLLGS
CCCEEEECCCEECCC		46.6825159151
642"N6,N6-dimethyllysine"FSFSFSNKKLLGSKA
CEEEECCCEECCCCC		43.53-
642AcetylationFSFSFSNKKLLGSKA
CEEEECCCEECCCCC		43.5325953088
642MethylationFSFSFSNKKLLGSKA
CEEEECCCEECCCCC		43.53-
647PhosphorylationSNKKLLGSKALRPPT
CCCEECCCCCCCCCC		18.0929496963
648UbiquitinationNKKLLGSKALRPPTS
CCEECCCCCCCCCCC		50.0329967540
654PhosphorylationSKALRPPTSPGVFGA
CCCCCCCCCCCHHHH		50.6829255136
655PhosphorylationKALRPPTSPGVFGAL
CCCCCCCCCCHHHHH		25.9829255136
677PhosphorylationPKPVRDEYEYVSDDG
CCCCCCCCEEECCCC		19.4930576142
679PhosphorylationPVRDEYEYVSDDGEL
CCCCCCEEECCCCCE		12.3526657352
681PhosphorylationRDEYEYVSDDGELKI
CCCCEEECCCCCEEE		29.1425159151
705PhosphorylationNAPKRDLSFLLDKKA
CCCCCCHHHHHCCCC		20.3823401153
711SumoylationLSFLLDKKAVLPTPV
HHHHHCCCCCCCCCC		43.3128112733
716PhosphorylationDKKAVLPTPVTKPKL
CCCCCCCCCCCCCCC		26.6528122231
719PhosphorylationAVLPTPVTKPKLDSA
CCCCCCCCCCCCCCC		42.7228122231
720AcetylationVLPTPVTKPKLDSAA
CCCCCCCCCCCCCCC		40.1523954790
725PhosphorylationVTKPKLDSAAYKSDD
CCCCCCCCCCCCCCC		25.8228634120
728PhosphorylationPKLDSAAYKSDDSSD
CCCCCCCCCCCCCCC		15.6728634120
730PhosphorylationLDSAAYKSDDSSDEG
CCCCCCCCCCCCCCC		33.6920363803
733PhosphorylationAAYKSDDSSDEGSLH
CCCCCCCCCCCCCEE		44.6820363803
734PhosphorylationAYKSDDSSDEGSLHI
CCCCCCCCCCCCEEE		46.8320363803
738PhosphorylationDDSSDEGSLHIDTDT
CCCCCCCCEEECCCC		18.0920363803
743PhosphorylationEGSLHIDTDTKPGRN
CCCEEECCCCCCCCC		44.9923312004
745PhosphorylationSLHIDTDTKPGRNAR
CEEECCCCCCCCCCE		41.0323312004
757PhosphorylationNARVKKESGSSAAGI
CCEEEECCCCCHHHH		53.5121532585
771PhosphorylationILDLLQASEEVGALE
HHHHHHHHHHHCCCC		22.71-
788PhosphorylationPSSQPPASPSTQEAI
CCCCCCCCHHHHHHH		25.7526074081
790PhosphorylationSQPPASPSTQEAIQG
CCCCCCHHHHHHHHH		39.9826074081
791PhosphorylationQPPASPSTQEAIQGM
CCCCCHHHHHHHHHH		33.5426074081
853PhosphorylationLKRAAKNSVDLDDYE
HHHHHHCCCCCCHHH		19.1230266825
859PhosphorylationNSVDLDDYEEEQDHL
CCCCCCHHHHHHHHH		25.5527642862
873PhosphorylationLDACFKDSDYVYPSL
HHHHCCCCCCCCCCC		31.2828796482
875PhosphorylationACFKDSDYVYPSLES
HHCCCCCCCCCCCCC		13.0630266825
877PhosphorylationFKDSDYVYPSLESDE
CCCCCCCCCCCCCCC		4.8530266825
879PhosphorylationDSDYVYPSLESDEDN
CCCCCCCCCCCCCCC		27.3830266825
882PhosphorylationYVYPSLESDEDNPIF
CCCCCCCCCCCCCCC		52.1423927012
891PhosphorylationEDNPIFKSRSKKRKG
CCCCCCCCCCCCCCC		30.9128111955
899PhosphorylationRSKKRKGSDDAPYSP
CCCCCCCCCCCCCCC		35.0429255136
904PhosphorylationKGSDDAPYSPTARVG
CCCCCCCCCCCCCCC		29.0630266825
905PhosphorylationGSDDAPYSPTARVGP
CCCCCCCCCCCCCCC		18.0829255136
907PhosphorylationDDAPYSPTARVGPSV
CCCCCCCCCCCCCCC		22.5829255136
913PhosphorylationPTARVGPSVPRQDRP
CCCCCCCCCCCCCCC		38.5325954137
925PhosphorylationDRPVREGTRVASIET
CCCCCCCCEEEEHHH		19.74-
929PhosphorylationREGTRVASIETGLAA
CCCCEEEEHHHHHHH		20.3525159151
932PhosphorylationTRVASIETGLAAAAA
CEEEEHHHHHHHHHH		35.5129978859
940AcetylationGLAAAAAKLSQQEEQ
HHHHHHHHHHHHHHH		43.9025953088
942PhosphorylationAAAAAKLSQQEEQKS
HHHHHHHHHHHHHHH		29.1625849741
954PhosphorylationQKSKKKKSAKRKLTP
HHHHHHHHHHCCCCC		48.1521532585
1008PhosphorylationSQASQEGSSPEPPPE
HHHCCCCCCCCCCCC		41.8022468782
1040PhosphorylationTGAQAGRTSQPMAPG
CCCCCCCCCCCCCCC		30.6920860994
1041PhosphorylationGAQAGRTSQPMAPGV
CCCCCCCCCCCCCCE		30.8123090842
1051PhosphorylationMAPGVFLTQRRPSAS
CCCCEEEEECCCCCC		14.4723090842
1056PhosphorylationFLTQRRPSASSPNNN
EEEECCCCCCCCCCC		38.6823401153
1058PhosphorylationTQRRPSASSPNNNTA
EECCCCCCCCCCCCC		51.1423401153
1059PhosphorylationQRRPSASSPNNNTAA
ECCCCCCCCCCCCCC		31.2222167270
1064PhosphorylationASSPNNNTAAKGKRT
CCCCCCCCCCCCCCC		30.0722167270
1067AcetylationPNNNTAAKGKRTKKG
CCCCCCCCCCCCHHH		63.6025953088
1072AcetylationAAKGKRTKKGMATAK
CCCCCCCHHHHHHHH		51.9022362403
1079AcetylationKKGMATAKQRLGKIL
HHHHHHHHHHHHHHH		31.4325953088
1087SumoylationQRLGKILKIHRNGKL
HHHHHHHHCCCCCEE		39.68-
1087SumoylationQRLGKILKIHRNGKL
HHHHHHHHCCCCCEE		39.68-
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
929SPhosphorylationKinaseCHEK1O14757
GPS
1056SPhosphorylationKinasePKA-FAMILY-GPS
1056SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF2_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 PHF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PHF2_HUMAN !!
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 PHF2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"PKA-dependent regulation of the histone lysine demethylase complexPHF2-ARID5B.";
Baba A., Ohtake F., Okuno Y., Yokota K., Okada M., Imai Y., Ni M.,Meyer C.A., Igarashi K., Kanno J., Brown M., Kato S.;
Nat. Cell Biol. 13:668-675(2011).
Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION BY PKA, PHOSPHORYLATIONAT SER-1056, INTERACTION WITH ARID5B; HNF4A AND NR1H4, IDENTIFICATIONBY MASS SPECTROMETRY, TISSUE SPECIFICITY, IDENTIFICATION IN THEPHF2-ARID5B COMPLEX, AND MUTAGENESIS OF HIS-249; SER-757; SER-899;SER-954 AND SER-1056.
"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-882, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, AND MASSSPECTROMETRY.
"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-539 AND SER-882, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899, AND MASSSPECTROMETRY.

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