TRIM2_HUMAN - dbPTM
TRIM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIM2_HUMAN
UniProt AC Q9C040
Protein Name Tripartite motif-containing protein 2
Gene Name TRIM2
Organism Homo sapiens (Human).
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 MASEGTNIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNAEESSILETVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
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
3Phosphorylation-----MASEGTNIPS
-----CCCCCCCCCC		34.9527251275
6Phosphorylation--MASEGTNIPSPVV
--CCCCCCCCCCHHH		26.3929255136
10PhosphorylationSEGTNIPSPVVRQID
CCCCCCCCHHHHHHC		26.9129255136
24PhosphorylationDKQFLICSICLERYK
CHHHHEEHHHHHHHC		14.8928464451
93PhosphorylationLMDVLQRTPGSNAEE
HHHHHHHCCCCCHHH		21.0226657352
96PhosphorylationVLQRTPGSNAEESSI
HHHHCCCCCHHHHCH		33.7927732954
101PhosphorylationPGSNAEESSILETVT
CCCCHHHHCHHHHHH		17.7427732954
102PhosphorylationGSNAEESSILETVTA
CCCHHHHCHHHHHHH		34.1827732954
181PhosphorylationKRLPEIDSALQFISE
HHCCHHHHHHHHHHH		36.2230619164
187PhosphorylationDSALQFISEIIHQLT
HHHHHHHHHHHHHHH		24.8320058876
194PhosphorylationSEIIHQLTNQKASIV
HHHHHHHHHCCHHHH		29.0930619164
213UbiquitinationSTFDELQKTLNVRKS
HHHHHHHHHHCCCHH		68.55-
220PhosphorylationKTLNVRKSVLLMELE
HHHCCCHHHHEEEEE		13.8722210691
230PhosphorylationLMELEVNYGLKHKVL
EEEEEEHHHCCHHHH		29.0722210691
253PhosphorylationQGQESIKSCSNFTAQ
HCHHHHHHCCHHHHH		22.5529083192
255PhosphorylationQESIKSCSNFTAQAL
HHHHHHCCHHHHHHH		41.9129083192
258PhosphorylationIKSCSNFTAQALNHG
HHHCCHHHHHHHHCC		23.3129083192
305PhosphorylationQLDFIVETEGLKKSI
CCCEEEECCCHHHHH		25.1825003641
311PhosphorylationETEGLKKSIHNLGTI
ECCCHHHHHHHHHHH		27.7422210691
317PhosphorylationKSIHNLGTILTTNAV
HHHHHHHHHHHCCCC		18.9124076635
338PhosphorylationTGEGLRQTIIGQPMS
CCCCHHHEECCCEEE		14.2324043423
345PhosphorylationTIIGQPMSVTITTKD
EECCCEEEEEEEECC		23.8525690035
347PhosphorylationIGQPMSVTITTKDKD
CCCEEEEEEEECCCC		12.8024667141
349PhosphorylationQPMSVTITTKDKDGE
CEEEEEEEECCCCCC		20.5925690035
350PhosphorylationPMSVTITTKDKDGEL
EEEEEEEECCCCCCE		33.1424043423
360PhosphorylationKDGELCKTGNAYLTA
CCCCEECCCCEEEEE		34.3727732954
364PhosphorylationLCKTGNAYLTAELST
EECCCCEEEEEEEEC		14.4827732954
366PhosphorylationKTGNAYLTAELSTPD
CCCCEEEEEEEECCC		12.8627732954
370PhosphorylationAYLTAELSTPDGSVA
EEEEEEEECCCCCCC		29.4226657352
371PhosphorylationYLTAELSTPDGSVAD
EEEEEEECCCCCCCC		37.7130175587
375PhosphorylationELSTPDGSVADGEIL
EEECCCCCCCCCEEE		22.8522777824
398PhosphorylationFLYTVQKEGDFTLSL
EEEEEEECCCEEEEE		47.0727251275
402PhosphorylationVQKEGDFTLSLRLYD
EEECCCEEEEEEEEC		21.8527251275
404PhosphorylationKEGDFTLSLRLYDQH
ECCCEEEEEEEECHH		14.3724719451
424PhosphorylationFKLKVIRSADVSPTT
EEEEEEECCCCCCCC		20.0729255136
428PhosphorylationVIRSADVSPTTEGVK
EEECCCCCCCCHHHH		19.6529255136
430PhosphorylationRSADVSPTTEGVKRR
ECCCCCCCCHHHHHH		29.9429255136
431PhosphorylationSADVSPTTEGVKRRV
CCCCCCCCHHHHHHC		33.8428102081
439AcetylationEGVKRRVKSPGSGHV
HHHHHHCCCCCCCCC		49.477707239
440PhosphorylationGVKRRVKSPGSGHVK
HHHHHCCCCCCCCCC		31.4721082442
443PhosphorylationRRVKSPGSGHVKQKA
HHCCCCCCCCCCHHH		29.1630576142
447AcetylationSPGSGHVKQKAVKRP
CCCCCCCCHHHCCCC		40.177707249
451PhosphorylationGHVKQKAVKRPASMY
CCCCHHHCCCCHHHH		7.5227251275
455PhosphorylationQKAVKRPASMYSTGK
HHHCCCCHHHHCCCC		15.8027251275
456PhosphorylationKAVKRPASMYSTGKR
HHCCCCHHHHCCCCC		22.4226657352
458PhosphorylationVKRPASMYSTGKRKE
CCCCHHHHCCCCCCC		10.6923090842
459PhosphorylationKRPASMYSTGKRKEN
CCCHHHHCCCCCCCC		23.2630576142
460PhosphorylationRPASMYSTGKRKENP
CCHHHHCCCCCCCCC		29.2729514088
467PhosphorylationTGKRKENPIEDDLIF
CCCCCCCCCCCCEEE		32.2227251275
470PhosphorylationRKENPIEDDLIFRVG
CCCCCCCCCEEEEEC		57.6527251275
486PhosphorylationKGRNKGEFTNLQGVA
CCCCCCCCCCCCEEE		8.1727251275
529PhosphorylationRFGIRGRSPGQLQRP
CCCCCCCCCCCCCCC		35.8828348404
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIM2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHPS1_HUMANSIRPAphysical
16189514
UB2D1_HUMANUBE2D1physical
21143188
CIB3_HUMANCIB3physical
25416956
SHPS1_HUMANSIRPAphysical
25416956
ODPA_HUMANPDHA1physical
26344197
LRC8E_HUMANLRRC8Ephysical
21516116
TRIM3_HUMANTRIM3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615490Charcot-Marie-Tooth disease 2R (CMT2R)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIM2_HUMAN

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Related Literatures of Post-Translational Modification

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