TRI58_HUMAN - dbPTM
TRI58_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI58_HUMAN
UniProt AC Q8NG06
Protein Name E3 ubiquitin-protein ligase TRIM58
Gene Name TRIM58
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization
Protein Description E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nuclear polarization..
Protein Sequence MAWAPPGERLREDARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDGAQGGVYACPQCRGPFRPSGFRPNRQLAGLVESVRRLGLGAGPGARRCARHGEDLSRFCEEDEAALCWVCDAGPEHRTHRTAPLQEAAGSYQVKLQMALELMRKELEDALTQEANVGKKTVIWKEKVEMQRQRFRLEFEKHRGFLAQEEQRQLRRLEAEERATLQRLRESKSRLVQQSKALKELADELQERCQRPALGLLEGVRGVLSRSKAVTRLEAENIPMELKTACCIPGRRELLRKFQVDVKLDPATAHPSLLLTADLRSVQDGEPWRDVPNNPERFDTWPCILGLQSFSSGRHYWEVLVGEGAEWGLGVCQDTLPRKGETTPSPENGVWALWLLKGNEYMVLASPSVPLLQLESPRCIGIFLDYEAGEISFYNVTDGSYIYTFNQLFSGLLRPYFFICDATPLILPPTTIAGSGNWASRDHLDPASDVRDDHL
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
47PhosphorylationISEFCEKSDGAQGGV
HHHHHHHCCCCCCCE
20.9828258704
55PhosphorylationDGAQGGVYACPQCRG
CCCCCCEEECCCCCC
13.0328258704
159PhosphorylationKELEDALTQEANVGK
HHHHHHHHHHCCCCC
26.53-
256PhosphorylationEGVRGVLSRSKAVTR
HHHHHHHHCCCHHHH
31.9124719451
392PhosphorylationWLLKGNEYMVLASPS
EEEECCEEEEEECCC
9.12-
397PhosphorylationNEYMVLASPSVPLLQ
CEEEEEECCCCCEEE
17.34-

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 TRI58_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI58_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 TRI58_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYHC1_HUMANDYNC1H1physical
25241935
DC1I1_HUMANDYNC1I1physical
25241935
DC2L1_HUMANDYNC2LI1physical
25241935
DC1L2_HUMANDYNC1LI2physical
25241935
TRI58_HUMANTRIM58physical
25241935
UB2D3_HUMANUBE2D3physical
25241935

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI58_HUMAN

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Related Literatures of Post-Translational Modification

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