TRIM2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRIM2_MOUSE
• UniProt AC: Q9ESN6
• Protein Name: Tripartite motif-containing protein 2
• Gene Name: Trim2
• Organism: Mus musculus (Mouse).
• Sequence Length: 744
• Subcellular Localization: Cytoplasm .
• Protein Description: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance..
• Protein Sequence: MASEGASIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNGEDSSILETVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTSGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSNDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ

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
3	Phosphorylation	-----MASEGASIPS -----CCCCCCCCCC	34.95	25619855
7	Phosphorylation	-MASEGASIPSPVVR -CCCCCCCCCCHHHH	45.98	25619855
10	Phosphorylation	SEGASIPSPVVRQID CCCCCCCCHHHHHHC	28.76	25619855
93	Phosphorylation	LMDVLQRTPGSNGED HHHHHHHCCCCCCCC	21.02	21082442
96	Phosphorylation	VLQRTPGSNGEDSSI HHHHCCCCCCCCCCH	42.75	21082442
213	Ubiquitination	STFDELQKTLNVRKS HHHHHHHHHHCCCHH	68.55	-
235	Ubiquitination	VNYGLKHKVLQSQLD EHHHCCHHHHHHHHH	42.95	-
311	Phosphorylation	ETEGLKKSIHNLGTI ECCCHHHHHHHHHHH	27.74	29899451
338	Phosphorylation	TGEGLRQTIIGQPMS CCCCHHHEECCCEEE	14.23	28059163
360	Phosphorylation	KDGELCKTGNAYLTA CCCCEECCCCEEEEE	34.37	25619855
364	Phosphorylation	LCKTGNAYLTAELST EECCCCEEEEEEEEC	14.48	25619855
366	Phosphorylation	KTGNAYLTAELSTPD CCCCEEEEEEEECCC	12.86	25619855
370	Phosphorylation	AYLTAELSTPDGSVA EEEEEEEECCCCCCC	29.42	25619855
371	Phosphorylation	YLTAELSTPDGSVAD EEEEEEECCCCCCCC	37.71	25521595
375	Phosphorylation	ELSTPDGSVADGEIL EEECCCCCCCCCEEE	22.85	21082442
424	Phosphorylation	FKLKVIRSADVSPTT EEEEEEECCCCCCCC	20.07	25521595
428	Phosphorylation	VIRSADVSPTTEGVK EEECCCCCCCCHHHH	19.65	25521595
430	Phosphorylation	RSADVSPTTEGVKRR ECCCCCCCCHHHHHH	29.94	25521595
431	Phosphorylation	SADVSPTTEGVKRRV CCCCCCCCHHHHHHC	33.84	25521595
440	Phosphorylation	GVKRRVKSPGSGHVK HHHHHCCCCCCCCCC	31.47	26824392
443	Phosphorylation	RRVKSPGSGHVKQKA HHCCCCCCCCCCHHH	29.16	22324799
456	Phosphorylation	KAVKRPASMYSTGKR HHCCCCHHHHCCCCC	22.42	22324799
458	Phosphorylation	VKRPASMYSTGKRKE CCCCHHHHCCCCCCC	10.69	29550500
459	Phosphorylation	KRPASMYSTGKRKEN CCCHHHHCCCCCCCC	23.26	22324799
460	Phosphorylation	RPASMYSTGKRKENP CCHHHHCCCCCCCCC	29.27	22324799
483	Ubiquitination	VGTKGRNKGEFTNLQ ECCCCCCCCCCCCCC	59.46	-
497	Phosphorylation	QGVAASTSGKILIAD CCEEECCCCCEEEEC	35.28	25521595
529	Phosphorylation	RFGIRGRSPGQLQRP CCCCCCCCCCCCCCC	35.88	28418008
565	Ubiquitination	SIFSNDGKFKTKIGS EEEECCCCEEEEECC	46.69	-
572	Phosphorylation	KFKTKIGSGKLMGPK CEEEEECCCCCCCCC	35.91	25619855
598	S-palmitoylation	VVDNKACCVFIFQPN EECCCEEEEEEECCC	3.15	28680068

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TRIM2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRIM2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRIM2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM2_MOUSE	Trim2	physical	18687884
MYO5A_RAT	Myo5a	physical	11432975

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-440, AND MASSSPECTROMETRY.
PubMed: 19367708