TRIM3_MOUSE - dbPTM
TRIM3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM3_MOUSE
UniProt AC Q9R1R2
Protein Name Tripartite motif-containing protein 3
Gene Name Trim3
Organism Mus musculus (Mouse).
Sequence Length 744
Subcellular Localization Cytoplasm. Early endosome . Golgi apparatus, trans-Golgi network . Cell projection, dendrite .
Protein Description Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Positively regulates motility of microtubule-dependent motor protein KIF21B. [PubMed: 24086586]
Protein Sequence MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPEGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSATAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIEDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
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
2Acetylation------MAKREDSPG
------CCCCCCCCC
21.44-
7Phosphorylation-MAKREDSPGPEVQP
-CCCCCCCCCCCCCC
27.3124925903
344PhosphorylationVGQPASLTVTTKDKD
CCCCCEEEEEEECCC
17.2025338131
346PhosphorylationQPASLTVTTKDKDGR
CCCEEEEEEECCCCC
23.9325338131
357PhosphorylationKDGRLVRTGSAELCA
CCCCEEECCCCEEEE
28.1923527152
359PhosphorylationGRLVRTGSAELCAEI
CCEEECCCCEEEEEE
20.2523527152
427PhosphorylationRPGDLPPSPDDVKRR
CCCCCCCCHHHHHHH
38.7325521595
437PhosphorylationDVKRRVKSPGGPGSH
HHHHHCCCCCCCCHH
26.3925521595
443PhosphorylationKSPGGPGSHVRQKAV
CCCCCCCHHHHHHHH
23.1825367039
454PhosphorylationQKAVRRPSSMYSTGG
HHHHCCCHHHCCCCC
26.4025521595
455PhosphorylationKAVRRPSSMYSTGGK
HHHCCCHHHCCCCCC
25.1527087446
457PhosphorylationVRRPSSMYSTGGKRK
HCCCHHHCCCCCCCC
12.6722817900
458PhosphorylationRRPSSMYSTGGKRKD
CCCHHHCCCCCCCCC
16.3727087446
459PhosphorylationRPSSMYSTGGKRKDN
CCHHHCCCCCCCCCC
32.2529472430
487PhosphorylationGREKGEFTNLQGVSA
CCCCCCCCCCCCCCC
30.6226643407
493PhosphorylationFTNLQGVSAASSGRI
CCCCCCCCCCCCCCE
25.5826643407
496PhosphorylationLQGVSAASSGRIVVA
CCCCCCCCCCCEEEE
32.8026643407
529PhosphorylationRFGVRGRSPGQLQRP
EEECCCCCCCCCCCC
35.8828418008
565UbiquitinationSIFSPEGKFKTKIGA
EEECCCCCCCCEECC
41.8622790023
568PhosphorylationSPEGKFKTKIGAGRL
CCCCCCCCEECCCCC
30.9028059163

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 TRIM3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM3_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 TRIM3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LST2_HUMANZFYVE28physical
19460345
CDN1A_MOUSECdkn1aphysical
23318451

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIM3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.

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