TRIM2_RAT - dbPTM
TRIM2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM2_RAT
UniProt AC D3ZQG6
Protein Name Tripartite motif-containing protein 2
Gene Name Trim2
Organism Rattus norvegicus (Rat).
Sequence Length 744
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase that mediates the ubiquitination of phosphorylated BCL2L11. Also mediates the UBE2D1-dependent ubiquitination of NEFL (By similarity). Plays a neuroprotective function (By similarity). May play a role in neuronal rapid ischemic tolerance..
Protein Sequence MASEGASIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNGEDPSILQTVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTSGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSNDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSSNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
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
10PhosphorylationSEGASIPSPVVRQID
CCCCCCCCHHHHHHC
28.7622673903
27PhosphorylationFLICSICLERYKNPK
HHEEHHHHHHHCCCC
3.91-
93PhosphorylationLMDVLQRTPGSNGED
HHHHHHHCCCCCCCC
21.0230240740
230UbiquitinationLMELEVNYGLKHKVL
EEEEEEHHHCCHHHH
29.07-
278PhosphorylationLLVKKQMSEKLNELA
EEEHHHHHHHHHHHH
29.1422276854
360PhosphorylationKDGELCKTGNAYLTA
CCCCEECCCCEEEEE
34.3728551015
364PhosphorylationLCKTGNAYLTAELST
EECCCCEEEEEEEEC
14.4828551015
366PhosphorylationKTGNAYLTAELSTPD
CCCCEEEEEEEECCC
12.8627097102
370PhosphorylationAYLTAELSTPDGSVA
EEEEEEEECCCCCCC
29.4227097102
371PhosphorylationYLTAELSTPDGSVAD
EEEEEEECCCCCCCC
37.7127097102
375PhosphorylationELSTPDGSVADGEIL
EEECCCCCCCCCEEE
22.8527097102
388PhosphorylationILDNKNGTYEFLYTV
EEECCCCEEEEEEEE
29.31-
392PhosphorylationKNGTYEFLYTVQKEG
CCCEEEEEEEEEECC
2.04-
424PhosphorylationFKLKVIRSADVSPTT
EEEEEEECCCCCCCC
20.0730411139
428PhosphorylationVIRSADVSPTTEGVK
EEECCCCCCCCHHHH
19.6530411139
430PhosphorylationRSADVSPTTEGVKRR
ECCCCCCCCHHHHHH
29.9425403869
431PhosphorylationSADVSPTTEGVKRRV
CCCCCCCCHHHHHHC
33.8425403869
440PhosphorylationGVKRRVKSPGSGHVK
HHHHHCCCCCCCCCC
31.4728432305
441PhosphorylationVKRRVKSPGSGHVKQ
HHHHCCCCCCCCCCH
34.94-
443PhosphorylationRRVKSPGSGHVKQKA
HHCCCCCCCCCCHHH
29.1628432305
445PhosphorylationVKSPGSGHVKQKAVK
CCCCCCCCCCHHHCC
25.87-
456PhosphorylationKAVKRPASMYSTGKR
HHCCCCHHHHCCCCC
22.4228432305
458PhosphorylationVKRPASMYSTGKRKE
CCCCHHHHCCCCCCC
10.6927097102
459PhosphorylationKRPASMYSTGKRKEN
CCCHHHHCCCCCCCC
23.2628432305
460PhosphorylationRPASMYSTGKRKENP
CCHHHHCCCCCCCCC
29.2728432305
483UbiquitinationVGTKGRNKGEFTNLQ
ECCCCCCCCCCCCCC
59.46-

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 TRIM2_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM2_RAT !!

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 TRIM2_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
B2L11_RATBcl2l11physical
21478148
B2L11_HUMANBCL2L11physical
21478148

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIM2_RAT

loading...

Related Literatures of Post-Translational Modification

TOP