TRI50_HUMAN - dbPTM
TRI50_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI50_HUMAN
UniProt AC Q86XT4
Protein Name E3 ubiquitin-protein ligase TRIM50
Gene Name TRIM50
Organism Homo sapiens (Human).
Sequence Length 487
Subcellular Localization Cytoplasm . Localizes mainly into discrete cytoplasmic punctuate structures heterogeneous in size and shape containing polyubiquitinated proteins.
Protein Description E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction..
Protein Sequence MAWQVSLLELEDWLQCPICLEVFKEPLMLQCGHSYCKGCLVSLSCHLDAELRCPVCRQAVDGSSSLPNVSLARVIEALRLPGDPEPKVCVHHRNPLSLFCEKDQELICGLCGLLGSHQHHPVTPVSTVYSRMKEELAALISELKQEQKKVDELIAKLVNNRTRIVNESDVFSWVIRREFQELHHLVDEEKARCLEGIGGHTRGLVASLDMQLEQAQGTRERLAQAECVLEQFGNEDHHKFIRKFHSMASRAEMPQARPLEGAFSPISFKPGLHQADIKLTVWKRLFRKVLPAPEPLKLDPATAHPLLELSKGNTVVQCGLLAQRRASQPERFDYSTCVLASRGFSCGRHYWEVVVGSKSDWRLGVIKGTASRKGKLNRSPEHGVWLIGLKEGRVYEAFACPRVPLPVAGHPHRIGLYLHYEQGELTFFDADRPDDLRPLYTFQADFQGKLYPILDTCWHERGSNSLPMVLPPPSGPGPLSPEQPTKL
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
267PhosphorylationEGAFSPISFKPGLHQ
CCCCCCCCCCCCCCH
30.5124719451
327PhosphorylationLLAQRRASQPERFDY
HHHHHCCCCCCCCCH
44.44-
373AcetylationIKGTASRKGKLNRSP
EEECCCCCCCCCCCC
58.8863828007
463PhosphorylationTCWHERGSNSLPMVL
CCCCCCCCCCCCEEC
29.4828634298
465PhosphorylationWHERGSNSLPMVLPP
CCCCCCCCCCEECCC
35.2328634298
474PhosphorylationPMVLPPPSGPGPLSP
CEECCCCCCCCCCCC
64.4928634298
480PhosphorylationPSGPGPLSPEQPTKL
CCCCCCCCCCCCCCC
29.5328634298

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 TRI50_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI50_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 TRI50_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D1_HUMANUBE2D1physical
21143188
UB2D2_HUMANUBE2D2physical
21143188
UB2D3_HUMANUBE2D3physical
21143188
UB2E1_HUMANUBE2E1physical
21143188
UB2E2_HUMANUBE2E2physical
21143188
UB2E3_HUMANUBE2E3physical
21143188
UBE2N_HUMANUBE2Nphysical
21143188
UB2D4_HUMANUBE2D4physical
21143188
HDAC6_HUMANHDAC6physical
22792322
SQSTM_HUMANSQSTM1physical
22792322
ACK1_HUMANTNK2physical
24308962

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI50_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP