TBX3_HUMAN - dbPTM
TBX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBX3_HUMAN
UniProt AC O15119
Protein Name T-box transcription factor TBX3
Gene Name TBX3
Organism Homo sapiens (Human).
Sequence Length 743
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor involved in developmental processes. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence..
Protein Sequence MSLSMRDPVIPGTSMAYHPFLPHRAPDFAMSAVLGHQPPFFPALTLPPNGAAALSLPGALAKPIMDQLVGAAETGIPFSSLGPQAHLRPLKTMEPEEEVEDDPKVHLEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFTLAFPSDHATWQGNYSFGTQTILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLQSMRVFDERHKKENGTSDESSSEQAAFNCFAQASSPAASTVGTSNLKDLCPSEGESDAEAESKEEHGPEACDAAKISTTTSEEPCRDKGSPAVKAHLFAAERPRDSGRLDKASPDSRHSPATISSSTRGLGAEERRSPVREGTAPAKVEEARALPGKEAFAPLTVQTDAAAAHLAQGPLPGLGFAPGLAGQQFFNGHPLFLHPSQFAMGGAFSSMAAAGMGPLLATVSGASTGVSGLDSTAMASAAAAQGLSGASAATLPFHLQQHVLASQGLAMSPFGSLFPYPYTYMAAAAAASSAAASSSVHRHPFLNLNTMRPRLRYSPYSIPVPVPDGSSLLTTALPSMAAAAGPLDGKVAALAASPASVAVDSGSELNSRSSTLSSSSMSLSPKLCAEKEAATSELQSIQRLVSGLEAKPDRSRSASP
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
13PhosphorylationRDPVIPGTSMAYHPF
CCCCCCCCCHHCCCC		15.2424043423
14PhosphorylationDPVIPGTSMAYHPFL
CCCCCCCCHHCCCCC		13.8224043423
17PhosphorylationIPGTSMAYHPFLPHR
CCCCCHHCCCCCCCC		11.0324043423
104UbiquitinationEEVEDDPKVHLEAKE
HHCCCCCCCCHHHHH		49.64-
110UbiquitinationPKVHLEAKELWDQFH
CCCCHHHHHHHHHHH		43.92-
118UbiquitinationELWDQFHKRGTEMVI
HHHHHHHHHCCEEEE		54.53-
121PhosphorylationDQFHKRGTEMVITKS
HHHHHHCCEEEEECC		25.5822210691
127UbiquitinationGTEMVITKSGRRMFP
CCEEEEECCCCCCCC		39.53-
128PhosphorylationTEMVITKSGRRMFPP
CEEEEECCCCCCCCC		28.9622210691
163PhosphorylationIAADDCRYKFHNSRW
HHCCCCEEEECCCCE		25.08-
185PhosphorylationPEMPKRMYIHPDSPA
CCCCCCEEECCCCCC		10.50-
203PhosphorylationQWMSKVVTFHKLKLT
HHHHHEEEEEEEEEC		24.02-
206UbiquitinationSKVVTFHKLKLTNNI
HHEEEEEEEEECCCC		43.03-
208UbiquitinationVVTFHKLKLTNNISD
EEEEEEEEECCCCCC		59.05-
265PhosphorylationNDILKLPYSTFRTYL
HHCEECCCCCCCCCC		30.68-
293UbiquitinationNDKITQLKIDNNPFA
CCCCEEEEECCCCCC		37.89-
301UbiquitinationIDNNPFAKGFRDTGN
ECCCCCCCCCCCCCC		59.99-
313UbiquitinationTGNGRREKRKQLTLQ
CCCCHHHHHHHHHHH		64.18-
335PhosphorylationRHKKENGTSDESSSE
HHHHHCCCCCCCHHH		44.5828348404
336PhosphorylationHKKENGTSDESSSEQ
HHHHCCCCCCCHHHH		40.5628348404
353PhosphorylationFNCFAQASSPAASTV
HHHHHHCCCCCHHHC		25.4422210691
354PhosphorylationNCFAQASSPAASTVG
HHHHHCCCCCHHHCC		22.9026657352
371PhosphorylationNLKDLCPSEGESDAE
CHHHHCCCCCCCHHH		58.1825159151
375PhosphorylationLCPSEGESDAEAESK
HCCCCCCCHHHHHHH		53.6425159151
381PhosphorylationESDAEAESKEEHGPE
CCHHHHHHHHHHCHH		53.0322617229
396PhosphorylationACDAAKISTTTSEEP
HHHHCEECCCCCCCC		20.9923312004
397PhosphorylationCDAAKISTTTSEEPC
HHHCEECCCCCCCCC		37.2525002506
398PhosphorylationDAAKISTTTSEEPCR
HHCEECCCCCCCCCC		22.8725002506
399PhosphorylationAAKISTTTSEEPCRD
HCEECCCCCCCCCCC		33.9425002506
400PhosphorylationAKISTTTSEEPCRDK
CEECCCCCCCCCCCC		37.5621712546
407AcetylationSEEPCRDKGSPAVKA
CCCCCCCCCCHHHHH		41.7726051181
409PhosphorylationEPCRDKGSPAVKAHL
CCCCCCCCHHHHHHE		18.5430576142
413UbiquitinationDKGSPAVKAHLFAAE
CCCCHHHHHHEEEEC		31.99-
425PhosphorylationAAERPRDSGRLDKAS
EECCCCCCCCCCCCC		27.3923312004
432PhosphorylationSGRLDKASPDSRHSP
CCCCCCCCCCCCCCC		34.6725159151
435PhosphorylationLDKASPDSRHSPATI
CCCCCCCCCCCCCCC		34.9625159151
438PhosphorylationASPDSRHSPATISSS
CCCCCCCCCCCCCCC		18.3425159151
441PhosphorylationDSRHSPATISSSTRG
CCCCCCCCCCCCCCC		25.4425159151
443PhosphorylationRHSPATISSSTRGLG
CCCCCCCCCCCCCCC		17.5519276368
444PhosphorylationHSPATISSSTRGLGA
CCCCCCCCCCCCCCC		31.7020873877
445PhosphorylationSPATISSSTRGLGAE
CCCCCCCCCCCCCCC		18.4819276368
446PhosphorylationPATISSSTRGLGAEE
CCCCCCCCCCCCCCH		30.6119276368
456PhosphorylationLGAEERRSPVREGTA
CCCCHHCCCCCCCCC		33.6925159151
462PhosphorylationRSPVREGTAPAKVEE
CCCCCCCCCCHHHHH		25.3923312004
466AcetylationREGTAPAKVEEARAL
CCCCCCHHHHHHHCC		49.4726051181
466UbiquitinationREGTAPAKVEEARAL
CCCCCCHHHHHHHCC		49.47-
641PhosphorylationMRPRLRYSPYSIPVP
CCCCCCCCCCCCCEE		15.7828348404
680PhosphorylationKVAALAASPASVAVD
HHHHHHCCCCEEEEC		18.5228355574
683PhosphorylationALAASPASVAVDSGS
HHHCCCCEEEECCCC		17.6229978859
688PhosphorylationPASVAVDSGSELNSR
CCEEEECCCCHHHCC		37.3127732954
690PhosphorylationSVAVDSGSELNSRSS
EEEECCCCHHHCCCC		42.7527732954
694PhosphorylationDSGSELNSRSSTLSS
CCCCHHHCCCCCCCC		46.2827732954
696PhosphorylationGSELNSRSSTLSSSS
CCHHHCCCCCCCCCC		27.7430206219
697PhosphorylationSELNSRSSTLSSSSM
CHHHCCCCCCCCCCC		32.0523927012
698PhosphorylationELNSRSSTLSSSSMS
HHHCCCCCCCCCCCC		31.7230206219
700PhosphorylationNSRSSTLSSSSMSLS
HCCCCCCCCCCCCCC		28.4130206219
701PhosphorylationSRSSTLSSSSMSLSP
CCCCCCCCCCCCCCH		29.5530206219
702PhosphorylationRSSTLSSSSMSLSPK
CCCCCCCCCCCCCHH		27.0423927012
703PhosphorylationSSTLSSSSMSLSPKL
CCCCCCCCCCCCHHH		17.8423927012
705PhosphorylationTLSSSSMSLSPKLCA
CCCCCCCCCCHHHHH		27.8725159151
707PhosphorylationSSSSMSLSPKLCAEK
CCCCCCCCHHHHHCH		16.8119664994
714UbiquitinationSPKLCAEKEAATSEL
CHHHHHCHHHHHHHH		33.84-
714AcetylationSPKLCAEKEAATSEL
CHHHHHCHHHHHHHH		33.8426051181
718PhosphorylationCAEKEAATSELQSIQ
HHCHHHHHHHHHHHH		29.76-
719PhosphorylationAEKEAATSELQSIQR
HCHHHHHHHHHHHHH		31.42-
729PhosphorylationQSIQRLVSGLEAKPD
HHHHHHHHCHHCCCC		42.1028555341
734UbiquitinationLVSGLEAKPDRSRSA
HHHCHHCCCCCCCCC		37.77-
734AcetylationLVSGLEAKPDRSRSA
HHHCHHCCCCCCCCC		37.7726051181
738PhosphorylationLEAKPDRSRSASP--
HHCCCCCCCCCCC--		37.6620363803
740PhosphorylationAKPDRSRSASP----
CCCCCCCCCCC----		34.0520363803
742PhosphorylationPDRSRSASP------
CCCCCCCCC------		32.1820363803
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
719SPhosphorylationKinaseAKT3Q9Y243
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBX3_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 TBX3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBX3_HUMANTBX3physical
12005433
HDAC1_HUMANHDAC1physical
18245468
HDAC2_HUMANHDAC2physical
18245468
HDAC3_HUMANHDAC3physical
18245468
HDAC5_HUMANHDAC5physical
18245468
PKHF2_HUMANPLEKHF2physical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
181450Ulnar-mammary syndrome (UMS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBX3_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-371 AND SER-375, 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-371; SER-381; SER-707;SER-738; SER-740 AND SER-742, 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-432; SER-438 ANDTHR-441, AND MASS SPECTROMETRY.
"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-456, AND MASSSPECTROMETRY.

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