TFEC_HUMAN - dbPTM
TFEC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFEC_HUMAN
UniProt AC O14948
Protein Name Transcription factor EC
Gene Name TFEC
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Nucleus .
Protein Description Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence). Binds to element F in an E-box sequence-specific manner. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter (By similarity). Collaborates with MITF in target gene activation (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form..
Protein Sequence MTLDHQIINPTLKWSQPAVPSGGPLVQHAHTTLDSDAGLTENPLTKLLAIGKEDDNAQWHMEDVIEDIIGMESSFKEEGADSPLLMQRTLSGSILDVYSGEQGISPINMGLTSASCPSSLPMKREITETDTRALAKERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVEYIKWLQKEQQRARELEHRQKKLEQANRRLLLRIQELEIQARTHGLPTLASLGTVDLGAHVTKQQSHPEQNSVDYCQQLTVSQGPSPELCDQAIAFSDPLSYFTDLSFSAALKEEQRLDGMLLDDTISPFGTDPLLSATSPAVSKESSRRSSFSSDDGDEL
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------MTLDHQIIN
------CCCCCCCCC
40.67-
15PhosphorylationINPTLKWSQPAVPSG
CCCCCCCCCCCCCCC
25.3824719451
24 (in isoform 4)Phosphorylation-32.6522210691
35PhosphorylationHAHTTLDSDAGLTEN
ECCCCCCCCCCCCCC
32.2624719451
40PhosphorylationLDSDAGLTENPLTKL
CCCCCCCCCCCHHHH
32.5724719451
51 (in isoform 4)Phosphorylation-22.9922210691
52 (in isoform 4)Phosphorylation-52.4322210691
89PhosphorylationSPLLMQRTLSGSILD
CCCEEEHHHCCCEEE
14.3727251275
91PhosphorylationLLMQRTLSGSILDVY
CEEEHHHCCCEEEEC
29.8627251275
93PhosphorylationMQRTLSGSILDVYSG
EEHHHCCCEEEECCC
19.3227251275
111UbiquitinationISPINMGLTSASCPS
CCCCCCCCCCCCCCC
2.0830230243
119PhosphorylationTSASCPSSLPMKREI
CCCCCCCCCCCCCCC
22.95-
149UbiquitinationDNHNLIERRRRYNIN
HCCCHHHHHHHHCCC
30.3430230243
178UbiquitinationDPDMRWNKGTILKAS
CCCCCCCHHHHHHHH
50.9330230243
318PhosphorylationDTISPFGTDPLLSAT
CCCCCCCCCCCCCCC
34.5222115753
323PhosphorylationFGTDPLLSATSPAVS
CCCCCCCCCCCCCCC
36.8622115753
325PhosphorylationTDPLLSATSPAVSKE
CCCCCCCCCCCCCCH
31.6922115753
326PhosphorylationDPLLSATSPAVSKES
CCCCCCCCCCCCCHH
15.5822115753
330PhosphorylationSATSPAVSKESSRRS
CCCCCCCCCHHHCCC
32.5822115753
333PhosphorylationSPAVSKESSRRSSFS
CCCCCCHHHCCCCCC
32.6420068231
334PhosphorylationPAVSKESSRRSSFSS
CCCCCHHHCCCCCCC
32.5720068231

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 TFEC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFEC_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 TFEC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFEC_HUMANTFECphysical
11467950
TFE3_HUMANTFE3physical
11467950
ZMAT2_HUMANZMAT2physical
21988832
SNAB_HUMANNAPBphysical
25416956
DB127_HUMANDEFB127physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TFEC_HUMAN

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Related Literatures of Post-Translational Modification

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