TEAD1_HUMAN - dbPTM
TEAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEAD1_HUMAN
UniProt AC P28347
Protein Name Transcriptional enhancer factor TEF-1
Gene Name TEAD1
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Nucleus.
Protein Description Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif..
Protein Sequence MEPSSWSGSESPAENMERMSDSADKPIDNDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKSRDFHSKLKDQTAKDKALQHMAAMSSAQIVSATAIHNKLGLPGIPRPTFPGAPGFWPGMIQTGQPGSSQDVKPFVQQAYPIQPAVTAPIPGFEPASAPAPSVPAWQGRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFFLVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFIHKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
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
1Acetylation-------MEPSSWSG
-------CCCCCCCC		18.0321406692
4Phosphorylation----MEPSSWSGSES
----CCCCCCCCCCC		31.0023663014
5Phosphorylation---MEPSSWSGSESP
---CCCCCCCCCCCH		35.6623663014
7Phosphorylation-MEPSSWSGSESPAE
-CCCCCCCCCCCHHH		34.1025159151
9PhosphorylationEPSSWSGSESPAENM
CCCCCCCCCCHHHHH		29.4117081983
11PhosphorylationSSWSGSESPAENMER
CCCCCCCCHHHHHHH		30.9828355574
20PhosphorylationAENMERMSDSADKPI
HHHHHHHCCCCCCCC		34.3326657352
22PhosphorylationNMERMSDSADKPIDN
HHHHHCCCCCCCCCC		30.9328387310
36PhosphorylationNDAEGVWSPDIEQSF
CCCCCCCCCCHHHHH		15.4125159151
42PhosphorylationWSPDIEQSFQEALAI
CCCCHHHHHHHHHHH		18.9925106551
50UbiquitinationFQEALAIYPPCGRRK
HHHHHHHCCCCCCCE		8.7721890473
53S-palmitoylationALAIYPPCGRRKIIL
HHHHCCCCCCCEEEE		5.9826900866
57UbiquitinationYPPCGRRKIILSDEG
CCCCCCCEEEECCCC		32.51-
57AcetylationYPPCGRRKIILSDEG
CCCCCCCEEEECCCC		32.5126051181
61PhosphorylationGRRKIILSDEGKMYG
CCCEEEECCCCCEEC		24.1730266825
65UbiquitinationIILSDEGKMYGRNEL
EEECCCCCEECHHHH		27.222189047
76PhosphorylationRNELIARYIKLRTGK
HHHHHHHHHHHHCCC		8.0621403953
83MethylationYIKLRTGKTRTRKQV
HHHHHCCCCCCHHHH		33.93-
86MethylationLRTGKTRTRKQVSSH
HHCCCCCCHHHHHHH		47.66-
88UbiquitinationTGKTRTRKQVSSHIQ
CCCCCCHHHHHHHHH		55.21-
101MethylationIQVLARRKSRDFHSK
HHHHHHHHCHHHHHH		44.2723644510
101"N6,N6-dimethyllysine"IQVLARRKSRDFHSK
HHHHHHHHCHHHHHH		44.27-
102PhosphorylationQVLARRKSRDFHSKL
HHHHHHHCHHHHHHH		34.9620068231
108UbiquitinationKSRDFHSKLKDQTAK
HCHHHHHHHCCCHHH		51.49-
117UbiquitinationKDQTAKDKALQHMAA
CCCHHHHHHHHHHHH		50.74-
126O-linked_GlycosylationLQHMAAMSSAQIVSA
HHHHHHHCHHHHHHH		20.1430059200
126PhosphorylationLQHMAAMSSAQIVSA
HHHHHHHCHHHHHHH		20.1429978859
127O-linked_GlycosylationQHMAAMSSAQIVSAT
HHHHHHCHHHHHHHH		15.8830059200
127PhosphorylationQHMAAMSSAQIVSAT
HHHHHHCHHHHHHHH		15.8829978859
132PhosphorylationMSSAQIVSATAIHNK
HCHHHHHHHHHHHHH		22.8729978859
132O-linked_GlycosylationMSSAQIVSATAIHNK
HCHHHHHHHHHHHHH		22.8730059200
134PhosphorylationSAQIVSATAIHNKLG
HHHHHHHHHHHHHCC		20.7329978859
173SumoylationPGSSQDVKPFVQQAY
CCCCCCCHHHHHHHC		40.82-
2152-HydroxyisobutyrylationGRSIGTTKLRLVEFS
CCCCCCCEEEEEEHH		31.29-
263PhosphorylationSVDIRQIYDKFPEKK
CCCHHHHHHHCCHHC		12.54-
265UbiquitinationDIRQIYDKFPEKKGG
CHHHHHHHCCHHCCC		45.94-
270AcetylationYDKFPEKKGGLKELF
HHHCCHHCCCHHHHH		57.4518528473
274AcetylationPEKKGGLKELFGKGP
CHHCCCHHHHHCCCC		56.5018528481
327S-palmitoylationVTCSTKVCSFGKQVV
EEEEEEECCCCHHHH		2.7326900866
331UbiquitinationTKVCSFGKQVVEKVE
EEECCCCHHHHHHHH		37.60-
331AcetylationTKVCSFGKQVVEKVE
EEECCCCHHHHHHHH		37.6026051181
336AcetylationFGKQVVEKVETEYAR
CCHHHHHHHHHHEEE		33.4926051181
339PhosphorylationQVVEKVETEYARFEN
HHHHHHHHHEEEEEC		36.9628152594
341PhosphorylationVEKVETEYARFENGR
HHHHHHHEEEEECCE		15.5328152594
351PhosphorylationFENGRFVYRINRSPM
EECCEEEEEECCCHH		11.7630622161
359S-palmitoylationRINRSPMCEYMINFI
EECCCHHHHHHHHHH		3.7326900866
368AcetylationYMINFIHKLKHLPEK
HHHHHHHHHCCCCHH		55.1826051181
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 TEAD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEAD1_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 TEAD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEF2C_HUMANMEF2Cphysical
12061776
MAX_HUMANMAXphysical
9199327
SRF_HUMANSRFphysical
11136726
RAD51_HUMANRAD51physical
26186194
RAD51_HUMANRAD51physical
28514442
YAP1_HUMANYAP1physical
25796446
PFKAM_HUMANPFKMphysical
25796446
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
108985Sveinsson chorioretinal atrophy (SCRA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEAD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-7; SER-9 AND SER-11, ANDMASS SPECTROMETRY.

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