TRIP6_MOUSE - dbPTM
TRIP6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIP6_MOUSE
UniProt AC Q9Z1Y4
Protein Name Thyroid receptor-interacting protein 6
Gene Name Trip6
Organism Mus musculus (Mouse).
Sequence Length 480
Subcellular Localization Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Nucleus . Cytoplasm . Shuttles between nucleus and cytoplasm. Colocalizes with actin.
Protein Description Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor (By similarity)..
Protein Sequence MSGPTWLPPKQPEPSRLPQGRSLPRGALGPPTAHGATLQPHPRVNFCPLPPEHCYQPPGVPEDRGPTWVGSHGTPQRLQGLPPDRGIIRPGSLDAEIDSLTSMLADLDGGRSHAPRRPDRQAFEAPPPHAYRGGSLKPSGGAVPTPMLPASHYGGPTPASYATASTPAGPAFPVQVKVAQPVRGCGLPRRGASQASGPLPGPHFPLTGRGEVWGAGYRSHREPGPGVPEGPSGVHIPAGGGRGGGHEPQGPLGQPPEEELERLTKKLVHDMSHPPSGEYFGRCGGCGEDVVGDGAGVVALDRVFHIGCFVCSTCRAQLRGQHFYAVERRAYCESCYVATLEKCSTCSEPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC
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
22PhosphorylationSRLPQGRSLPRGALG
CCCCCCCCCCCCCCC
49.9329514104
25MethylationPQGRSLPRGALGPPT
CCCCCCCCCCCCCCC
48.5924129315
25Asymmetric dimethylargininePQGRSLPRGALGPPT
CCCCCCCCCCCCCCC
48.59-
55PhosphorylationPLPPEHCYQPPGVPE
CCCHHHCCCCCCCCC
26.4322817900
92PhosphorylationRGIIRPGSLDAEIDS
CCCCCCCCCHHHHHH
26.2626239621
99PhosphorylationSLDAEIDSLTSMLAD
CCHHHHHHHHHHHHH
38.9323984901
101PhosphorylationDAEIDSLTSMLADLD
HHHHHHHHHHHHHCC
18.9523984901
102PhosphorylationAEIDSLTSMLADLDG
HHHHHHHHHHHHCCC
19.6623984901
111MethylationLADLDGGRSHAPRRP
HHHCCCCCCCCCCCC
30.69-
183MethylationVKVAQPVRGCGLPRR
EEEECCCCCCCCCCC
41.1712019297
190MethylationRGCGLPRRGASQASG
CCCCCCCCCCCCCCC
42.9924129315
193PhosphorylationGLPRRGASQASGPLP
CCCCCCCCCCCCCCC
29.1522817900
196PhosphorylationRRGASQASGPLPGPH
CCCCCCCCCCCCCCC
33.0518846507
207PhosphorylationPGPHFPLTGRGEVWG
CCCCCCCCCCCCCCC
25.6818846507
209MethylationPHFPLTGRGEVWGAG
CCCCCCCCCCCCCCC
32.6324129315
218MethylationEVWGAGYRSHREPGP
CCCCCCCCCCCCCCC
25.6812019327
242MethylationHIPAGGGRGGGHEPQ
CCCCCCCCCCCCCCC
43.8124129315
279PhosphorylationSHPPSGEYFGRCGGC
CCCCCCCCCCCCCCC
18.1729514104
344PhosphorylationVATLEKCSTCSEPIL
EEEHHHHCCCCHHHH
43.4421454597
345PhosphorylationATLEKCSTCSEPILD
EEHHHHCCCCHHHHH
29.5321454597
347PhosphorylationLEKCSTCSEPILDRI
HHHHCCCCHHHHHHH
46.6321454597
419PhosphorylationPEPGQEETVRIVALD
CCCCCCCCEEEEEEE
17.84-
428PhosphorylationRIVALDRSFHIGCYK
EEEEEECCEEEECEE
22.35-

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
55YPhosphorylationKinaseSRCP12931
PSP
55YPhosphorylationKinaseSRCP05480
Uniprot
55YPhosphorylationKinaseSRC64-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIP6_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 TRIP6_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TRIP6_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIP6_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.

TOP