TRIM9_MOUSE - dbPTM
TRIM9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM9_MOUSE
UniProt AC Q8C7M3
Protein Name E3 ubiquitin-protein ligase TRIM9
Gene Name Trim9
Organism Mus musculus (Mouse).
Sequence Length 817
Subcellular Localization Cytoplasm . Cell projection, dendrite . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle . Cell junction, synapse . Cytoplasm, cytoskeleton . Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle-associated f
Protein Description E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation..
Protein Sequence MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSRRASGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPPTHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRTMVQQIQENSVEFEACLVAQCDALIDALNRRKAQLLARVNKEHEHKLKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQWGKGTLTPRMTTDFDLSLDNSPLLQSIHQLDFVQVKASSPVPATPILQLEECCTHNNSATLSWKQPPLSTVAADGYILELDDGSGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVLQTSEAAGAHETKPMKDTDSEEQTLPFPVPSERLPLRRMSPFSSTLNLQPSFPGRSYFDFRSSPHQLSLHSSLQSLNAPGCNFETQSASYSQLVDIKKLLAVAWFAFDPGSAHSDIIFSNDNLTVTCSSYDDRVVLGKTGFSKGVHYWELTIDRYDNHPDPAFGVARIDVMKDMMLGKDDKAWAMYVDNNRSWFMHNNSHTNRTEGGITKGATIGVLLDLNRKTLTFFVNNEQQGPIAFENVEGLFFPAVSLNRNVQVSLWAPGLRACSGCYFKVCPGAVKSPQAPAP
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
41PhosphorylationARNILVQTPESESPQ
HHHCCCCCCCCCCCC
22.8825521595
44PhosphorylationILVQTPESESPQSRR
CCCCCCCCCCCCCCC
44.5725521595
46PhosphorylationVQTPESESPQSRRAS
CCCCCCCCCCCCCCC
37.2025521595
49PhosphorylationPESESPQSRRASGSG
CCCCCCCCCCCCCCC
27.4129899451
53PhosphorylationSPQSRRASGSGVSDY
CCCCCCCCCCCCCCC
31.5125521595
55PhosphorylationQSRRASGSGVSDYDY
CCCCCCCCCCCCCCC
33.2625521595
58PhosphorylationRASGSGVSDYDYLDL
CCCCCCCCCCCCCCH
33.7028066266
437PhosphorylationDFVQVKASSPVPATP
CEEEEEECCCCCCCC
29.4729899451
443PhosphorylationASSPVPATPILQLEE
ECCCCCCCCEEEHHH
12.5621082442
569PhosphorylationRLPLRRMSPFSSTLN
CCCCCCCCCCCCCCC
22.4519060867
580PhosphorylationSTLNLQPSFPGRSYF
CCCCCCCCCCCCCCC
30.9829899451

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 TRIM9_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM9_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 TRIM9_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLU2B_MOUSEPrkcshphysical
22337885

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIM9_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP