TGFI1_MOUSE - dbPTM
TGFI1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGFI1_MOUSE
UniProt AC Q62219
Protein Name Transforming growth factor beta-1-induced transcript 1 protein
Gene Name Tgfb1i1
Organism Mus musculus (Mouse).
Sequence Length 461
Subcellular Localization Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Associated with the actin cytoskeleton, colocalizes with stress fibers.
Protein Description Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity..
Protein Sequence MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGTTGDKDHLYSTVCKPRSPKPVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEEKEDQSEDKSSPTVPPSPFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAASPTREGCPSPPGQTSKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCSGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGEEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECLAPFSGGSFFEHEGRPLCENHFHAQRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERASKPYCQPCFLKLFG
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-------MEDLDALL
-------CHHHHHHH
9.02-
2 (in isoform 2)Phosphorylation-68.2525266776
2 (in isoform 7)Phosphorylation-68.2525266776
2 (in isoform 8)Phosphorylation-68.2525266776
3 (in isoform 5)Phosphorylation-48.8530635358
4 (in isoform 5)Phosphorylation-2.3630635358
7 (in isoform 7)Phosphorylation-4.7325266776
9PhosphorylationEDLDALLSDLETTTS
HHHHHHHHHHHHHHH
40.7923649490
18 (in isoform 5)Phosphorylation-2.2130635358
19PhosphorylationETTTSHMSRLGAPKE
HHHHHHHHHCCCCCC
20.9425266776
31PhosphorylationPKERPPETLTPPPPY
CCCCCCCCCCCCCCC
41.5326824392
33PhosphorylationERPPETLTPPPPYGH
CCCCCCCCCCCCCCC
40.9630352176
38PhosphorylationTLTPPPPYGHQPQTG
CCCCCCCCCCCCCCC
32.7716183059
44PhosphorylationPYGHQPQTGSGESSG
CCCCCCCCCCCCCCC
39.74-
52PhosphorylationGSGESSGTTGDKDHL
CCCCCCCCCCCCCCE
29.5622871156
60PhosphorylationTGDKDHLYSTVCKPR
CCCCCCEEEEECCCC
10.0126824392
61PhosphorylationGDKDHLYSTVCKPRS
CCCCCEEEEECCCCC
22.2618515860
68PhosphorylationSTVCKPRSPKPVAPV
EEECCCCCCCCCCCC
45.8926824392
80PhosphorylationAPVAPPFSSSSGVLG
CCCCCCCCCCCCCCC
34.7825777480
81PhosphorylationPVAPPFSSSSGVLGN
CCCCCCCCCCCCCCC
28.9829550500
82PhosphorylationVAPPFSSSSGVLGNG
CCCCCCCCCCCCCCH
29.8829550500
83PhosphorylationAPPFSSSSGVLGNGL
CCCCCCCCCCCCCHH
34.5626824392
113PhosphorylationNITDEIMSQFPSSKM
CCCHHHHHHCCCHHC
34.0425266776
118PhosphorylationIMSQFPSSKMAEGEE
HHHHCCCHHCCCCCC
27.0425266776
130PhosphorylationGEEKEDQSEDKSSPT
CCCCCCCCCCCCCCC
61.1526824392
134PhosphorylationEDQSEDKSSPTVPPS
CCCCCCCCCCCCCCC
54.6029472430
135PhosphorylationDQSEDKSSPTVPPSP
CCCCCCCCCCCCCCC
30.2629472430
137PhosphorylationSEDKSSPTVPPSPFP
CCCCCCCCCCCCCCC
47.8225777480
141PhosphorylationSSPTVPPSPFPAPSK
CCCCCCCCCCCCCCC
32.8627180971
147PhosphorylationPSPFPAPSKPSATSA
CCCCCCCCCCCCCCH
60.3425777480
150PhosphorylationFPAPSKPSATSATQE
CCCCCCCCCCCHHHH
48.1725777480
152PhosphorylationAPSKPSATSATQELD
CCCCCCCCCHHHHHH
24.1925777480
153PhosphorylationPSKPSATSATQELDR
CCCCCCCCHHHHHHH
29.0925777480
155PhosphorylationKPSATSATQELDRLM
CCCCCCHHHHHHHHH
23.4925777480
164PhosphorylationELDRLMASLSDFRVQ
HHHHHHHHHHHCCHH
17.9127180971
166PhosphorylationDRLMASLSDFRVQNH
HHHHHHHHHCCHHHC
32.0121082442
177PhosphorylationVQNHLPASGPPQPPA
HHHCCCCCCCCCCCC
50.3125619855
186PhosphorylationPPQPPAASPTREGCP
CCCCCCCCCCCCCCC
28.9825521595
188PhosphorylationQPPAASPTREGCPSP
CCCCCCCCCCCCCCC
38.5726824392
194PhosphorylationPTREGCPSPPGQTSK
CCCCCCCCCCCCCCC
48.0425521595
199PhosphorylationCPSPPGQTSKGSLDT
CCCCCCCCCCCCHHH
38.0221659605
200PhosphorylationPSPPGQTSKGSLDTM
CCCCCCCCCCCHHHH
27.4221659605
203PhosphorylationPGQTSKGSLDTMLGL
CCCCCCCCHHHHHHH
27.1527180971
206PhosphorylationTSKGSLDTMLGLLQS
CCCCCHHHHHHHHHH
21.4229472430
403PhosphorylationHFHAQRGSLCATCGL
CCCCCCCCCHHHCCC
23.5925521595
407PhosphorylationQRGSLCATCGLPVTG
CCCCCHHHCCCCCCC
13.2027742792
418PhosphorylationPVTGRCVSALGRRFH
CCCCCHHHHHCCCCC
22.7722817900
439PhosphorylationTFCLRPLTKGSFQER
EEECCCCCCCCHHHH
35.7226824392
448PhosphorylationGSFQERASKPYCQPC
CCHHHHCCCCCCCCH
40.1426824392

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
141SPhosphorylationKinaseMAPK1P63085
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGFI1_MOUSE !!

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 TGFI1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAK1_HUMANPTK2physical
9756887
GIT1_MOUSEGit1physical
12153727
TLX3_MOUSETlx3physical
20211142
SMAD3_MOUSESmad3physical
14755691

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGFI1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation.";
Hetey S.E., Lalonde D.P., Turner C.E.;
Exp. Cell Res. 311:147-156(2005).
Cited for: FUNCTION, MUTAGENESIS OF TYR-38; TYR-60; CYS-369 AND CYS-372,SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-38 AND TYR-60.

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