TFPT_HUMAN - dbPTM
TFPT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFPT_HUMAN
UniProt AC P0C1Z6
Protein Name TCF3 fusion partner
Gene Name TFPT
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Nucleus .
Protein Description Appears to promote apoptosis in a p53/TP53-independent manner.; Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair..
Protein Sequence MELEQREGTMAAVGFEEFSAPPGSELALPPLFGGHILESELETEVEFVSGGLGGSGLRERDEEEEAARGRRRRQRELNRRKYQALGRRCREIEQVNERVLNRLHQVQRITRRLQQERRFLMRVLDSYGDDYRASQFTIVLEDEGSQGTDAPTPGNAENEPPEKETLSPPRRTPAPPEPGSPAPGEGPSGRKRRRVPRDGRRAGNALTPELAPVQIKVEEDFGFEADEALDSSWVSRGPDKLLPYPTLASPASD
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
55PhosphorylationVSGGLGGSGLRERDE
CCCCCCCCCCCHHHH		32.6224275569
68DimethylationDEEEEAARGRRRRQR
HHHHHHHHHHHHHHH		46.31-
68MethylationDEEEEAARGRRRRQR
HHHHHHHHHHHHHHH		46.3116287839
131PhosphorylationLDSYGDDYRASQFTI
HHHHCCCCCEEEEEE		16.90-
145PhosphorylationIVLEDEGSQGTDAPT
EEEECCCCCCCCCCC		24.3230576142
148PhosphorylationEDEGSQGTDAPTPGN
ECCCCCCCCCCCCCC		22.7330576142
152PhosphorylationSQGTDAPTPGNAENE
CCCCCCCCCCCCCCC		45.6130576142
165PhosphorylationNEPPEKETLSPPRRT
CCCCCCCCCCCCCCC		43.5323403867
167PhosphorylationPPEKETLSPPRRTPA
CCCCCCCCCCCCCCC		40.0330266825
172PhosphorylationTLSPPRRTPAPPEPG
CCCCCCCCCCCCCCC		25.6930278072
180PhosphorylationPAPPEPGSPAPGEGP
CCCCCCCCCCCCCCC		28.7119664994
188PhosphorylationPAPGEGPSGRKRRRV
CCCCCCCCCCCCCCC		63.1923927012
207PhosphorylationRRAGNALTPELAPVQ
CCCCCCCCCCCCCCE		16.5930266825
216SumoylationELAPVQIKVEEDFGF
CCCCCEEEEEECCCC		26.8828112733
231PhosphorylationEADEALDSSWVSRGP
CHHHHHCCCCHHCCC		27.2726074081
232PhosphorylationADEALDSSWVSRGPD
HHHHHCCCCHHCCCC		31.0326074081
235PhosphorylationALDSSWVSRGPDKLL
HHCCCCHHCCCCCCC		25.8426074081
240UbiquitinationWVSRGPDKLLPYPTL
CHHCCCCCCCCCCCC		55.87-
244PhosphorylationGPDKLLPYPTLASPA
CCCCCCCCCCCCCCC		14.6023927012
246PhosphorylationDKLLPYPTLASPASD
CCCCCCCCCCCCCCC		29.1623927012
249PhosphorylationLPYPTLASPASD---
CCCCCCCCCCCC---		24.9023927012
252PhosphorylationPTLASPASD------
CCCCCCCCC------		47.4323927012
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
180SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFPT_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 TFPT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IN80E_HUMANINO80Ephysical
17721549
RUVB1_HUMANRUVBL1physical
17721549
RUVB2_HUMANRUVBL2physical
17721549
ACL6A_HUMANACTL6Aphysical
17721549
IN80C_HUMANINO80Cphysical
17721549
TYY1_HUMANYY1physical
17721549
INO80_HUMANINO80physical
17721549
NFRKB_HUMANNFRKBphysical
17721549
TFPT_HUMANTFPTphysical
17721549
ARP5_HUMANACTR5physical
17721549
ARP8_HUMANACTR8physical
17721549
IN80B_HUMANINO80Bphysical
17721549
UCHL5_HUMANUCHL5physical
17721549
IN80D_HUMANINO80Dphysical
17721549
MCRS1_HUMANMCRS1physical
17721549
EAF2_HUMANEAF2physical
17395368
EAF1_HUMANEAF1physical
17395368
ELL_HUMANELLphysical
17395368
A4_HUMANAPPphysical
21832049
TFPT_HUMANTFPTphysical
25416956
CDA7L_HUMANCDCA7Lphysical
25416956
RPGR1_HUMANRPGRIP1physical
25416956
HAUS1_HUMANHAUS1physical
25416956
DYDC1_HUMANDYDC1physical
25416956
DEUP1_HUMANCCDC67physical
25416956
CD046_HUMANC4orf46physical
25416956
PKN3_HUMANPKN3physical
27173435
YETS4_HUMANYEATS4physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS50_HUMANCCDC132physical
27173435
CAVN1_HUMANPTRFphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
STRN_HUMANSTRNphysical
27173435
CC122_HUMANCCDC122physical
27173435
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 TFPT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-180 AND SER-252, 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-180; SER-188; SER-249AND SER-252, AND MASS 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-180, AND MASSSPECTROMETRY.
"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-180; SER-249 ANDSER-252, AND MASS SPECTROMETRY.

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