PHF2_MOUSE - dbPTM
PHF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF2_MOUSE
UniProt AC Q9WTU0
Protein Name Lysine-specific demethylase PHF2
Gene Name Phf2
Organism Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGPTPDVKPVQNGSQLFIKELRSRTFPSAEDVVSRVPGSQLTVGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKIFYLIRPASANISLYERWRSASNHSEMFFADQVDRCYKCTVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFRPSQLIKDLAKEIRLSENASKTVRPEVNAAASSDEVCDGDREKEEPPSPVETTPPRSLLEKVSKKKTSKTVKMPKPSKIPKPPKSPKPPKTLKLKDGSKKKGKKCKESASPTIPNLDLLEAHTKEALTKMEPPKKGKTPKSVLSVPNKDTVHTQNDMERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQRLEKSPLAGNKDKFSFSFSNRKLLGSKALRPPSSPGVFGALQSFKEDKAKPVRDEYEYVSDDGELKIDEFPIRRKKSAPKRDLSFLLDKKEALLMPTSKPKLDSAVYKSDDSSDEGSLHIDTDTKPGRNAKVKKESGSSAAGILDLLQASEEVGALEYNPNSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGTGQAKGGSLAAHGARKIGGGNKGTGKRLLKRTAKNSVDLEDYEEQDHLDACFKDSDYVYPSLESDEDNPVFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKNRKKKNTKRKPAPNTASPSISTSASASTGTTSASTTPASTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFSGSQAGRASQPMAPGVFLTQRRPSASSPNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL
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		9.32-
48PhosphorylationEAPDIDIYHCPNCEK
CCCCCEEEECCCCHH		8.13-
56PhosphorylationHCPNCEKTHGKSTLK
ECCCCHHHCCCCCCH		17.36-
412UbiquitinationAFRSWTKKQALAEHE
HHHHHCHHHHHHHCH		33.1722790023
448PhosphorylationLSENASKTVRPEVNA
CCCCCCCCCCHHHHH		21.1725619855
458PhosphorylationPEVNAAASSDEVCDG
HHHHHHCCCCCCCCC		33.3323684622
459PhosphorylationEVNAAASSDEVCDGD
HHHHHCCCCCCCCCC		32.8225619855
474PhosphorylationREKEEPPSPVETTPP
CCCCCCCCCCCCCCC		52.9025521595
478PhosphorylationEPPSPVETTPPRSLL
CCCCCCCCCCCHHHH		44.8525619855
479PhosphorylationPPSPVETTPPRSLLE
CCCCCCCCCCHHHHH		20.1425521595
483PhosphorylationVETTPPRSLLEKVSK
CCCCCCHHHHHHHHC		42.9824719451
511PhosphorylationKIPKPPKSPKPPKTL
CCCCCCCCCCCCCCC		43.8822817900
534PhosphorylationKGKKCKESASPTIPN
CCCCCHHCCCCCCCC		21.3824925903
536PhosphorylationKKCKESASPTIPNLD
CCCHHCCCCCCCCHH		31.6825521595
538PhosphorylationCKESASPTIPNLDLL
CHHCCCCCCCCHHHH		46.7124925903
549PhosphorylationLDLLEAHTKEALTKM
HHHHHHHHHHHHHCC		37.3125619855
567PhosphorylationKKGKTPKSVLSVPNK
CCCCCCCCCCCCCCC		29.5122817900
570PhosphorylationKTPKSVLSVPNKDTV
CCCCCCCCCCCCCCC		33.1122817900
622PhosphorylationEEQRLEKSPLAGNKD
HHHHHHHCCCCCCCC		18.7726824392
632PhosphorylationAGNKDKFSFSFSNRK
CCCCCCEEEEECCCC		26.2222871156
634PhosphorylationNKDKFSFSFSNRKLL
CCCCEEEEECCCCEE		26.9422871156
636PhosphorylationDKFSFSFSNRKLLGS
CCEEEEECCCCEECC		34.2322871156
650PhosphorylationSKALRPPSSPGVFGA
CCCCCCCCCCCHHHH		52.4222942356
651PhosphorylationKALRPPSSPGVFGAL
CCCCCCCCCCHHHHH		31.2926824392
660PhosphorylationGVFGALQSFKEDKAK
CHHHHHHHHCCCCCC		38.8525367039
673PhosphorylationAKPVRDEYEYVSDDG
CCCCCCCCEEECCCC		19.4927149854
675PhosphorylationPVRDEYEYVSDDGEL
CCCCCCEEECCCCCE		12.3527742792
677PhosphorylationRDEYEYVSDDGELKI
CCCCEEECCCCCEEE		29.1427087446
701PhosphorylationSAPKRDLSFLLDKKE
CCCCCCHHHHHCHHH		20.3825521595
716AcetylationALLMPTSKPKLDSAV
HHHCCCCCCCCCCCE		48.9623806337
721PhosphorylationTSKPKLDSAVYKSDD
CCCCCCCCCEECCCC		30.0320415495
724PhosphorylationPKLDSAVYKSDDSSD
CCCCCCEECCCCCCC		12.4222817900
726PhosphorylationLDSAVYKSDDSSDEG
CCCCEECCCCCCCCC		29.0326824392
729PhosphorylationAVYKSDDSSDEGSLH
CEECCCCCCCCCCEE		44.6826824392
730PhosphorylationVYKSDDSSDEGSLHI
EECCCCCCCCCCEEE		46.8326824392
734PhosphorylationDDSSDEGSLHIDTDT
CCCCCCCCEEEECCC		18.0921082442
739PhosphorylationEGSLHIDTDTKPGRN
CCCEEEECCCCCCCC		44.9921743459
741PhosphorylationSLHIDTDTKPGRNAK
CEEEECCCCCCCCCE		41.0321743459
844PhosphorylationGKRLLKRTAKNSVDL
HHHHHHHHHCCCCCH		40.1625619855
848PhosphorylationLKRTAKNSVDLEDYE
HHHHHCCCCCHHHHH		19.1225521595
854PhosphorylationNSVDLEDYEEQDHLD
CCCCHHHHHHHHCHH		16.4025619855
867PhosphorylationLDACFKDSDYVYPSL
HHHHCCCCCCCCCCC		31.2825619855
869PhosphorylationACFKDSDYVYPSLES
HHCCCCCCCCCCCCC		13.0625619855
871PhosphorylationFKDSDYVYPSLESDE
CCCCCCCCCCCCCCC		4.8525619855
873PhosphorylationDSDYVYPSLESDEDN
CCCCCCCCCCCCCCC		27.3827087446
876PhosphorylationYVYPSLESDEDNPVF
CCCCCCCCCCCCCCC		52.1427087446
893PhosphorylationRSKKRKGSDDAPYSP
CCCCCCCCCCCCCCC		35.0426824392
898PhosphorylationKGSDDAPYSPTARVG
CCCCCCCCCCCCCCC		29.0625619855
899PhosphorylationGSDDAPYSPTARVGP
CCCCCCCCCCCCCCC		18.0823527152
901PhosphorylationDDAPYSPTARVGPSV
CCCCCCCCCCCCCCC		22.5827566939
907PhosphorylationPTARVGPSVPRQDRP
CCCCCCCCCCCCCCC		38.5322817900
923PhosphorylationREGTRVASIETGLAA
CCCCEEEEHHHHHHH		20.3528833060
926PhosphorylationTRVASIETGLAAAAA
CEEEEHHHHHHHHHH		35.5129899451
1042PhosphorylationGSQAGRASQPMAPGV
CCCCCCCCCCCCCCE		33.1922802335
1052PhosphorylationMAPGVFLTQRRPSAS
CCCCEEEEECCCCCC		14.4722802335
1057PhosphorylationFLTQRRPSASSPNNT
EEEECCCCCCCCCCC		38.6825521595
1059PhosphorylationTQRRPSASSPNNTAA
EECCCCCCCCCCCCC		51.1427087446
1060PhosphorylationQRRPSASSPNNTAAK
ECCCCCCCCCCCCCC		31.2225521595
1064PhosphorylationSASSPNNTAAKGKRT
CCCCCCCCCCCCCCC		34.3322802335
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
651SPhosphorylationKinaseMAPK1P63085
GPS
1057SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFE2_MOUSETcf3physical
20211142
MAML1_MOUSEMaml1physical
20211142
FOXP1_MOUSEFoxp1physical
20211142
TOX3_MOUSETox3physical
20211142
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHF2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-459, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASSSPECTROMETRY.

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