TFE3_HUMAN - dbPTM
TFE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFE3_HUMAN
UniProt AC P19532
Protein Name Transcription factor E3
Gene Name TFE3
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Nucleus.
Protein Description Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF. In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer. It also binds very well to a USF/MLTF site..
Protein Sequence MSHAAEPARDGVEASAEGPRAVFVLLEERRPADSAQLLSLNSLLPESGIVADIELENVLDPDSFYELKSQPLPLRSSLPISLQATPATPATLSASSSAGGSRTPAMSSSSSSRVLLRQQLMRAQAQEQERRERREQAAAAPFPSPAPASPAISVVGVSAGGHTLSRPPPAQVPREVLKVQTHLENPTRYHLQQARRQQVKQYLSTTLGPKLASQALTPPPGPASAQPLPAPEAAHTTGPTGSAPNSPMALLTIGSSSEKEIDDVIDEIISLESSYNDEMLSYLPGGTTGLQLPSTLPVSGNLLDVYSSQGVATPAITVSNSCPAELPNIKREISETEAKALLKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSSDPEMRWNKGTILKASVDYIRKLQKEQQRSKDLESRQRSLEQANRSLQLRIQELELQAQIHGLPVPPTPGLLSLATTSASDSLKPEQLDIEEEGRPGAATFHVGGGPAQNAPHQQPPAPPSDALLDLHFPSDHLGDLGDPFHLGLEDILMEEEEGVVGGLSGGALSPLRAASDPLLSSVSPAVSKASSRRSSFSMEEES
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------MSHAAEPAR
------CCCCCCCCC		23.10-
68SumoylationPDSFYELKSQPLPLR
HHHHCCCCCCCCCCC		34.80-
76PhosphorylationSQPLPLRSSLPISLQ
CCCCCCCCCCCEEEE		43.8628348404
77PhosphorylationQPLPLRSSLPISLQA
CCCCCCCCCCEEEEE		31.5628348404
85PhosphorylationLPISLQATPATPATL
CCEEEEECCCCCCEE		10.65-
101PhosphorylationASSSAGGSRTPAMSS
CCCCCCCCCCCCCCC		31.87-
103PhosphorylationSSAGGSRTPAMSSSS
CCCCCCCCCCCCCCH		19.6620860994
108PhosphorylationSRTPAMSSSSSSRVL
CCCCCCCCCHHHHHH		22.5820860994
109PhosphorylationRTPAMSSSSSSRVLL
CCCCCCCCHHHHHHH		27.25-
110PhosphorylationTPAMSSSSSSRVLLR
CCCCCCCHHHHHHHH		33.9920860994
112PhosphorylationAMSSSSSSRVLLRQQ
CCCCCHHHHHHHHHH		28.49-
122MethylationLLRQQLMRAQAQEQE
HHHHHHHHHHHHHHH		31.94115918389
144PhosphorylationAAAAPFPSPAPASPA
HHHCCCCCCCCCCCC		33.7922199227
149PhosphorylationFPSPAPASPAISVVG
CCCCCCCCCCEEEEE		17.5022199227
153PhosphorylationAPASPAISVVGVSAG
CCCCCCEEEEEECCC		16.9222199227
158PhosphorylationAISVVGVSAGGHTLS
CEEEEEECCCCCCCC		18.4423312004
163PhosphorylationGVSAGGHTLSRPPPA
EECCCCCCCCCCCCC		29.6923312004
165PhosphorylationSAGGHTLSRPPPAQV
CCCCCCCCCCCCCCC		43.8523312004
178MethylationQVPREVLKVQTHLEN
CCCHHHHHHHHHCCC		37.16115979993
188Asymmetric dimethylarginineTHLENPTRYHLQQAR
HHCCCCCHHHHHHHH		20.38-
188MethylationTHLENPTRYHLQQAR
HHCCCCCHHHHHHHH		20.38-
200UbiquitinationQARRQQVKQYLSTTL
HHHHHHHHHHHHHCC		28.96-
202PhosphorylationRRQQVKQYLSTTLGP
HHHHHHHHHHHCCCH		9.2625159151
213PhosphorylationTLGPKLASQALTPPP
CCCHHHHHCCCCCCC		26.8220068231
217PhosphorylationKLASQALTPPPGPAS
HHHHCCCCCCCCCCC		36.4420068231
224PhosphorylationTPPPGPASAQPLPAP
CCCCCCCCCCCCCCC		30.4827080861
236PhosphorylationPAPEAAHTTGPTGSA
CCCCCCCCCCCCCCC		28.8120068231
237PhosphorylationAPEAAHTTGPTGSAP
CCCCCCCCCCCCCCC		31.1520068231
240PhosphorylationAAHTTGPTGSAPNSP
CCCCCCCCCCCCCCC		45.1520068231
242PhosphorylationHTTGPTGSAPNSPMA
CCCCCCCCCCCCCEE		42.9330278072
246PhosphorylationPTGSAPNSPMALLTI
CCCCCCCCCEEEEEC		18.2630278072
252PhosphorylationNSPMALLTIGSSSEK
CCCEEEEECCCCCHH		24.9220068231
255PhosphorylationMALLTIGSSSEKEID
EEEEECCCCCHHHHH		27.1730278072
256PhosphorylationALLTIGSSSEKEIDD
EEEECCCCCHHHHHH		36.9930278072
257PhosphorylationLLTIGSSSEKEIDDV
EEECCCCCHHHHHHH		55.1530278072
321PhosphorylationPAITVSNSCPAELPN
CEEEECCCCCCCCCC		17.61-
330SumoylationPAELPNIKREISETE
CCCCCCHHHHCCHHH		51.09-
334PhosphorylationPNIKREISETEAKAL
CCHHHHCCHHHHHHH		33.4429691806
336PhosphorylationIKREISETEAKALLK
HHHHCCHHHHHHHHH		34.1626699800
339UbiquitinationEISETEAKALLKERQ
HCCHHHHHHHHHHHH		33.08-
339SumoylationEISETEAKALLKERQ
HCCHHHHHHHHHHHH		33.0828112733
365MethylationRRFNINDRIKELGTL
HHCCHHHHHHHHHHC		37.07-
385UbiquitinationDPEMRWNKGTILKAS
CCCCCCCCHHHHHHH		50.93-
392PhosphorylationKGTILKASVDYIRKL
CHHHHHHHHHHHHHH		17.59-
401AcetylationDYIRKLQKEQQRSKD
HHHHHHHHHHHHHHH		68.857683013
537PhosphorylationEGVVGGLSGGALSPL
CCCCCCCCCCCCHHH		38.1624275569
542PhosphorylationGLSGGALSPLRAASD
CCCCCCCHHHHHHCC		22.7320058876
548PhosphorylationLSPLRAASDPLLSSV
CHHHHHHCCCCHHCC		38.4829255136
553PhosphorylationAASDPLLSSVSPAVS
HHCCCCHHCCCHHHH		36.0530266825
554PhosphorylationASDPLLSSVSPAVSK
HCCCCHHCCCHHHHH		26.9522167270
556PhosphorylationDPLLSSVSPAVSKAS
CCCHHCCCHHHHHHH		14.7529255136
560PhosphorylationSSVSPAVSKASSRRS
HCCCHHHHHHHHCCC		25.3029255136
560O-linked_GlycosylationSSVSPAVSKASSRRS
HCCCHHHHHHHHCCC		25.3028657654
563PhosphorylationSPAVSKASSRRSSFS
CHHHHHHHHCCCCCC		28.2825850435
564PhosphorylationPAVSKASSRRSSFSM
HHHHHHHHCCCCCCC		36.2525850435
567PhosphorylationSKASSRRSSFSMEEE
HHHHHCCCCCCCCCC		34.3323401153
568PhosphorylationKASSRRSSFSMEEES
HHHHCCCCCCCCCCC		21.3829255136
570PhosphorylationSSRRSSFSMEEES--
HHCCCCCCCCCCC--		27.5129255136
575PhosphorylationSFSMEEES-------
CCCCCCCC-------		49.1223927012
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
321SPhosphorylationKinaseMTORP42345
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFE3_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 TFE3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALDR_HUMANAKR1B1physical
17353931
CLH1_HUMANCLTCphysical
17353931
PHB2_HUMANPHB2physical
17353931
ACLY_HUMANACLYphysical
17353931
CUL2_HUMANCUL2physical
17353931
SYEP_HUMANEPRSphysical
17353931
PUR4_HUMANPFASphysical
17353931
SYVC_HUMANVARSphysical
17353931
NEDD8_HUMANNEDD8physical
17353931
RL38_HUMANRPL38physical
17353931
TIF1B_HUMANTRIM28physical
17353931
EIF3A_HUMANEIF3Aphysical
17353931
RFA3_HUMANRPA3physical
17353931
SMCE1_HUMANSMARCE1physical
11018012
MITF_HUMANMITFgenetic
11930005
TFE3_HUMANTFE3physical
2044953
SMAD3_HUMANSMAD3physical
10557285
SMAD4_HUMANSMAD4physical
10557285
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 TFE3_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-556, AND MASSSPECTROMETRY.

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