PHF14_MOUSE - dbPTM
PHF14_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF14_MOUSE
UniProt AC Q9D4H9
Protein Name PHD finger protein 14
Gene Name Phf14
Organism Mus musculus (Mouse).
Sequence Length 881
Subcellular Localization
Protein Description
Protein Sequence MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNVPAILRAPKERKPSKKEGGTQKTSALPTVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEAEMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECSTCKGTGDNENLVRNLT
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
23PhosphorylationSLLEALDYDSSDDSD
HHHHHHCCCCCCCCC		20.6918846507
25PhosphorylationLEALDYDSSDDSDFK
HHHHCCCCCCCCCCC		29.4521659605
26PhosphorylationEALDYDSSDDSDFKV
HHHCCCCCCCCCCCC		42.4121659605
29PhosphorylationDYDSSDDSDFKVGDA
CCCCCCCCCCCCCCC		50.3521743459
39PhosphorylationKVGDASDSEGSGNGS
CCCCCCCCCCCCCCC		41.1721183079
42PhosphorylationDASDSEGSGNGSEDP
CCCCCCCCCCCCCCC		25.6521183079
84PhosphorylationKEEQLKNSTEEIMPS
CHHHHHCCCCHHCCC		35.29-
132PhosphorylationEKDKEKATVSDSAAA
HHHHHHCCCCHHHHH		31.4528973931
148PhosphorylationAAGTTPATSPPAVTS
HCCCCCCCCCCCCCC		42.8630482847
149PhosphorylationAGTTPATSPPAVTSP
CCCCCCCCCCCCCCC		30.8730482847
189PhosphorylationRPLLDFVSMEELNAM
CCCCCCCCHHHHCCC		22.07-
199PhosphorylationELNAMDDYDSEDDND
HHCCCCCCCCCCCCC		19.6626745281
201PhosphorylationNAMDDYDSEDDNDWR
CCCCCCCCCCCCCCC		36.3726239621
210PhosphorylationDDNDWRPTVVKRKGR
CCCCCCCCEEEECCC		29.3823984901
225PhosphorylationSASQKEGSDGDNEDD
CCCCCCCCCCCCCCC		39.24-
237PhosphorylationEDDDDEGSGSEEDEN
CCCCCCCCCCCCCCC		36.78-
239PhosphorylationDDDEGSGSEEDENDE
CCCCCCCCCCCCCCC		39.24-
270PhosphorylationKKRSKVLSRNSADDE
HHHHHCCCCCCCCCH		32.1925619855
273PhosphorylationSKVLSRNSADDEELT
HHCCCCCCCCCHHHC		31.7827087446
280PhosphorylationSADDEELTNDSLTLS
CCCCHHHCCCCCEEC		40.0117525332
283PhosphorylationDEELTNDSLTLSQSK
CHHHCCCCCEECCCC		25.8917525332
285PhosphorylationELTNDSLTLSQSKSN
HHCCCCCEECCCCCC		28.4527087446
287PhosphorylationTNDSLTLSQSKSNED
CCCCCEECCCCCCCC		27.4617525332
289PhosphorylationDSLTLSQSKSNEDSL
CCCEECCCCCCCCCE		34.3725619855
291PhosphorylationLTLSQSKSNEDSLIL
CEECCCCCCCCCEEE		51.1825521595
295PhosphorylationQSKSNEDSLILEKSQ
CCCCCCCCEEEECCC		15.9026824392
301PhosphorylationDSLILEKSQNWSSQK
CCEEEECCCCCCCCC		21.2623375375
352PhosphorylationGVDGESDSIMSSASE
CCCCCCCCHHCCCCC		29.48-
523PhosphorylationQEREKQLSPEAQARI
HHHHHHCCHHHHHHH		20.4226745281
591PhosphorylationDIFPVDNSDTSSSVD
CEEECCCCCCCCCCC		37.4921183079
593PhosphorylationFPVDNSDTSSSVDGR
EECCCCCCCCCCCCC		30.2627600695
594PhosphorylationPVDNSDTSSSVDGRR
ECCCCCCCCCCCCCH		26.1329899451
595PhosphorylationVDNSDTSSSVDGRRK
CCCCCCCCCCCCCHH		36.1519060867
596PhosphorylationDNSDTSSSVDGRRKH
CCCCCCCCCCCCHHC		24.8021082442
774PhosphorylationSECDQAGSSDMEAEM
CCCCCCCCCCHHHHH		26.6119060867
775PhosphorylationECDQAGSSDMEAEMA
CCCCCCCCCHHHHHH		39.8119060867
785PhosphorylationEAEMAMETLPDGTKR
HHHHHHHHCCCCCHH		30.4221183079
790PhosphorylationMETLPDGTKRSRRQI
HHHCCCCCHHHHHHC		30.5721183079
828PhosphorylationRTRGRKRSFVPEEEK
CCCCCCCCCCCHHHH		33.3625521595
849PhosphorylationRERRQRQSVLQKKPK
HHHHHHHHHHHHCCC		27.3029514104
898 (in isoform 2)Phosphorylation--
902 (in isoform 2)Phosphorylation-23984901
904 (in isoform 2)Phosphorylation-23984901
913 (in isoform 2)Phosphorylation-25159016
914 (in isoform 2)Phosphorylation-25159016
915 (in isoform 2)Phosphorylation-25159016
916 (in isoform 2)Phosphorylation-25159016
929 (in isoform 2)Phosphorylation-26643407
938 (in isoform 2)Phosphorylation-29514104
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 PHF14_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF14_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 PHF14_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PHF14_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHF14_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-291 AND SER-295, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280; SER-283 ANDSER-287, AND MASS 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 THR-280 AND SER-283, ANDMASS SPECTROMETRY.

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