TCF25_HUMAN - dbPTM
TCF25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCF25_HUMAN
UniProt AC Q9BQ70
Protein Name Transcription factor 25
Gene Name TCF25
Organism Homo sapiens (Human).
Sequence Length 676
Subcellular Localization Nucleus . Some staining in the cytosol.
Protein Description May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development..
Protein Sequence MSRRALRRLRGEQRGQEPLGPGALHFDLRDDDDAEEEGPKRELGVRRPGGAGKEGVRVNNRFELINIDDLEDDPVVNGERSGCALTDAVAPGNKGRGQRGNTESKTDGDDTETVPSEQSHASGKLRKKKKKQKNKKSSTGEASENGLEDIDRILERIEDSTGLNRPGPAPLSSRKHVLYVEHRHLNPDTELKRYFGARAILGEQRPRQRQRVYPKCTWLTTPKSTWPRYSKPGLSMRLLESKKGLSFFAFEHSEEYQQAQHKFLVAVESMEPNNIVVLLQTSPYHVDSLLQLSDACRFQEDQEMARDLVERALYSMECAFHPLFSLTSGACRLDYRRPENRSFYLALYKQMSFLEKRGCPRTALEYCKLILSLEPDEDPLCMLLLIDHLALRARNYEYLIRLFQEWEAHRNLSQLPNFAFSVPLAYFLLSQQTDLPECEQSSARQKASLLIQQALTMFPGVLLPLLESCSVRPDASVSSHRFFGPNAEISQPPALSQLVNLYLGRSHFLWKEPATMSWLEENVHEVLQAVDAGDPAVEACENRRKVLYQRAPRNIHRHVILSEIKEAVAALPPDVTTQSVMGFDPLPPSDTIYSYVRPERLSPISHGNTIALFFRSLLPNYTMEGERPEEGVAGGLNRNQGLNRLMLAVRDMMANFHLNDLEAPHEDDAEGEGEWD
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
2Phosphorylation------MSRRALRRL
------CCHHHHHHH		30.3920068231
7Ubiquitination-MSRRALRRLRGEQR
-CCHHHHHHHHHCCC		34.3027667366
29MethylationGALHFDLRDDDDAEE
CCEEEECCCCCCCHH		47.35115918333
53UbiquitinationRRPGGAGKEGVRVNN
CCCCCCCCCCCEECC		51.2529967540
81PhosphorylationPVVNGERSGCALTDA
CCCCCCCCCEEECCC		33.6420068231
86PhosphorylationERSGCALTDAVAPGN
CCCCEEECCCCCCCC		11.9120068231
94UbiquitinationDAVAPGNKGRGQRGN
CCCCCCCCCCCCCCC		56.7724816145
102PhosphorylationGRGQRGNTESKTDGD
CCCCCCCCCCCCCCC		44.4529255136
104PhosphorylationGQRGNTESKTDGDDT
CCCCCCCCCCCCCCC		38.5229255136
105UbiquitinationQRGNTESKTDGDDTE
CCCCCCCCCCCCCCC		44.3922817900
106UbiquitinationRGNTESKTDGDDTET
CCCCCCCCCCCCCCC		55.2722817900
106PhosphorylationRGNTESKTDGDDTET
CCCCCCCCCCCCCCC		55.2729255136
111PhosphorylationSKTDGDDTETVPSEQ
CCCCCCCCCCCCHHH		37.9929255136
113PhosphorylationTDGDDTETVPSEQSH
CCCCCCCCCCHHHHH		39.5523403867
116PhosphorylationDDTETVPSEQSHASG
CCCCCCCHHHHHHHH		43.8823403867
119PhosphorylationETVPSEQSHASGKLR
CCCCHHHHHHHHHHH		19.5730576142
121UbiquitinationVPSEQSHASGKLRKK
CCHHHHHHHHHHHHH		25.8122817900
122PhosphorylationPSEQSHASGKLRKKK
CHHHHHHHHHHHHHH		30.9122199227
124UbiquitinationEQSHASGKLRKKKKK
HHHHHHHHHHHHHHH		42.4921906983
124AcetylationEQSHASGKLRKKKKK
HHHHHHHHHHHHHHH		42.4925953088
127UbiquitinationHASGKLRKKKKKQKN
HHHHHHHHHHHHHCC		78.4022817900
128UbiquitinationASGKLRKKKKKQKNK
HHHHHHHHHHHHCCC		64.4922817900
129UbiquitinationSGKLRKKKKKQKNKK
HHHHHHHHHHHCCCC		69.1422817900
131UbiquitinationKLRKKKKKQKNKKSS
HHHHHHHHHCCCCCC		75.3222817900
133UbiquitinationRKKKKKQKNKKSSTG
HHHHHHHCCCCCCCC		78.5722817900
135UbiquitinationKKKKQKNKKSSTGEA
HHHHHCCCCCCCCCH		62.1522817900
136AcetylationKKKQKNKKSSTGEAS
HHHHCCCCCCCCCHH		60.0630592883
136UbiquitinationKKKQKNKKSSTGEAS
HHHHCCCCCCCCCHH		60.0621906983
137PhosphorylationKKQKNKKSSTGEASE
HHHCCCCCCCCCHHH		34.4423927012
138PhosphorylationKQKNKKSSTGEASEN
HHCCCCCCCCCHHHH		49.6825159151
139PhosphorylationQKNKKSSTGEASENG
HCCCCCCCCCHHHHH		46.2423927012
143PhosphorylationKSSTGEASENGLEDI
CCCCCCHHHHHHHHH		27.5623927012
160PhosphorylationILERIEDSTGLNRPG
HHHHHHHCCCCCCCC		16.1628555341
161PhosphorylationLERIEDSTGLNRPGP
HHHHHHCCCCCCCCC		58.9928555341
172PhosphorylationRPGPAPLSSRKHVLY
CCCCCCCCCCCEEEE		27.3425159151
173PhosphorylationPGPAPLSSRKHVLYV
CCCCCCCCCCEEEEE		53.7022468782
175UbiquitinationPAPLSSRKHVLYVEH
CCCCCCCCEEEEEEC		39.7627667366
179PhosphorylationSSRKHVLYVEHRHLN
CCCCEEEEEECCCCC		11.6028152594
192MethylationLNPDTELKRYFGARA
CCCCHHHHHHHCHHH		38.5342372549
192UbiquitinationLNPDTELKRYFGARA
CCCCHHHHHHHCHHH		38.5321906983
193UbiquitinationNPDTELKRYFGARAI
CCCHHHHHHHCHHHH		44.6421890473
198MethylationLKRYFGARAILGEQR
HHHHHCHHHHHCCCC		23.6554561879
198DimethylationLKRYFGARAILGEQR
HHHHHCHHHHHCCCC		23.65-
205DimethylationRAILGEQRPRQRQRV
HHHHCCCCCCCCCCC		24.86-
205MethylationRAILGEQRPRQRQRV
HHHHCCCCCCCCCCC		24.8654561885
209UbiquitinationGEQRPRQRQRVYPKC
CCCCCCCCCCCCCCC		27.7921890473
215UbiquitinationQRQRVYPKCTWLTTP
CCCCCCCCCCEECCC		26.9823000965
220UbiquitinationYPKCTWLTTPKSTWP
CCCCCEECCCCCCCC		32.3927667366
221PhosphorylationPKCTWLTTPKSTWPR
CCCCEECCCCCCCCC		26.92-
223UbiquitinationCTWLTTPKSTWPRYS
CCEECCCCCCCCCCC		59.43-
225PhosphorylationWLTTPKSTWPRYSKP
EECCCCCCCCCCCCC		45.69-
229PhosphorylationPKSTWPRYSKPGLSM
CCCCCCCCCCCCCCH		19.5721214269
231UbiquitinationSTWPRYSKPGLSMRL
CCCCCCCCCCCCHHH		33.8823000965
235PhosphorylationRYSKPGLSMRLLESK
CCCCCCCCHHHHHHC		14.0521214269
242UbiquitinationSMRLLESKKGLSFFA
CHHHHHHCCCCCEEE		41.2927667366
243UbiquitinationMRLLESKKGLSFFAF
HHHHHHCCCCCEEEE		74.49-
295UbiquitinationSLLQLSDACRFQEDQ
HHHHHHHHHCCHHCH		5.3027667366
304SulfoxidationRFQEDQEMARDLVER
CCHHCHHHHHHHHHH		2.8530846556
310UbiquitinationEMARDLVERALYSME
HHHHHHHHHHHHHHH		39.2627667366
315UbiquitinationLVERALYSMECAFHP
HHHHHHHHHHHHHHH		14.6822817900
319UbiquitinationALYSMECAFHPLFSL
HHHHHHHHHHHHHHC		7.7722817900
330UbiquitinationLFSLTSGACRLDYRR
HHHCCCCCCCCCCCC		3.8121963094
334UbiquitinationTSGACRLDYRRPENR
CCCCCCCCCCCCCCH		18.6222817900
335UbiquitinationSGACRLDYRRPENRS
CCCCCCCCCCCCCHH		17.0822817900
341UbiquitinationDYRRPENRSFYLALY
CCCCCCCHHHHHHHH		26.8722817900
356UbiquitinationKQMSFLEKRGCPRTA
HHHHHHHHCCCCHHH		57.1227667366
508UbiquitinationLYLGRSHFLWKEPAT
HHHCCCCCCCCCCCC		10.3127667366
523UbiquitinationMSWLEENVHEVLQAV
CHHHHHCHHHHHHHH		4.6327667366
528UbiquitinationENVHEVLQAVDAGDP
HCHHHHHHHHHCCCH		44.5121963094
530UbiquitinationVHEVLQAVDAGDPAV
HHHHHHHHHCCCHHH		3.1427667366
535UbiquitinationQAVDAGDPAVEACEN
HHHHCCCHHHHHHHH		36.9727667366
543UbiquitinationAVEACENRRKVLYQR
HHHHHHHHHHHHHHH		19.9421963094
545UbiquitinationEACENRRKVLYQRAP
HHHHHHHHHHHHHCC		33.1027667366
548UbiquitinationENRRKVLYQRAPRNI
HHHHHHHHHHCCCCC		10.0322817900
550UbiquitinationRRKVLYQRAPRNIHR
HHHHHHHHCCCCCHH		32.7621963094
555UbiquitinationYQRAPRNIHRHVILS
HHHCCCCCHHHHHHH		2.9721963094
565UbiquitinationHVILSEIKEAVAALP
HHHHHHHHHHHHCCC		35.2521963094
570UbiquitinationEIKEAVAALPPDVTT
HHHHHHHCCCCCCCC		17.6321963094
576PhosphorylationAALPPDVTTQSVMGF
HCCCCCCCCCCCCCC		26.8824043423
577PhosphorylationALPPDVTTQSVMGFD
CCCCCCCCCCCCCCC		20.7824043423
579PhosphorylationPPDVTTQSVMGFDPL
CCCCCCCCCCCCCCC		16.3924043423
589PhosphorylationGFDPLPPSDTIYSYV
CCCCCCCCCCCHHCC		45.5024043423
591PhosphorylationDPLPPSDTIYSYVRP
CCCCCCCCCHHCCCH		26.5924043423
593PhosphorylationLPPSDTIYSYVRPER
CCCCCCCHHCCCHHH		8.9524043423
594PhosphorylationPPSDTIYSYVRPERL
CCCCCCHHCCCHHHC		17.1924043423
595PhosphorylationPSDTIYSYVRPERLS
CCCCCHHCCCHHHCC		5.4124043423
602PhosphorylationYVRPERLSPISHGNT
CCCHHHCCCCCCCCH		26.8030266825
605PhosphorylationPERLSPISHGNTIAL
HHHCCCCCCCCHHHH		28.8230266825
609PhosphorylationSPISHGNTIALFFRS
CCCCCCCHHHHHHHH		16.5430266825
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 TCF25_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCF25_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 TCF25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_HUMANXIAPphysical
18068114
SAT1_HUMANSAT1physical
19060904
GASP2_HUMANGPRASP2physical
24778252
DERL1_HUMANDERL1physical
25416956
GASP2_HUMANGPRASP2physical
25416956
KASH5_HUMANCCDC155physical
25416956
SAT1_HUMANSAT1physical
21516116
GASP2_HUMANGPRASP2physical
28514442
ODBB_HUMANBCKDHBphysical
28514442
DCAF5_HUMANDCAF5physical
28514442
SHPK_HUMANSHPKphysical
28514442
UBP7_HUMANUSP7physical
28514442
DCAM_HUMANAMD1physical
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 TCF25_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-602, AND MASSSPECTROMETRY.

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