RN125_HUMAN - dbPTM
RN125_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN125_HUMAN
UniProt AC Q96EQ8
Protein Name E3 ubiquitin-protein ligase RNF125 {ECO:0000305}
Gene Name RNF125 {ECO:0000312|HGNC:HGNC:21150}
Organism Homo sapiens (Human).
Sequence Length 232
Subcellular Localization Golgi apparatus membrane
Lipid-anchor . Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane.
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins, such as DDX58/RIG-I, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53. [PubMed: 15843525]
Protein Sequence MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDENPSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT
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
2Myristoylation------MGSVLSTDS
------CCCCCCCCC
26.8517990982
3Phosphorylation-----MGSVLSTDSG
-----CCCCCCCCCC
20.7024719451
7Phosphorylation-MGSVLSTDSGKSAP
-CCCCCCCCCCCCCC
29.9829759185
9PhosphorylationGSVLSTDSGKSAPAS
CCCCCCCCCCCCCCH
48.4829759185
66UbiquitinationSCIATSLKNNKWTCP
HHHHHHHHCCCEECC
59.2421963094
69UbiquitinationATSLKNNKWTCPYCR
HHHHHCCCEECCCHH
53.9622817900
91UbiquitinationVPATDVAKRMKSEYK
CCHHHHHHHHHHHHC
53.5321906983
94UbiquitinationTDVAKRMKSEYKNCA
HHHHHHHHHHHCCHH
44.1422817900
95PhosphorylationDVAKRMKSEYKNCAE
HHHHHHHHHHCCHHH
36.4927251275
97PhosphorylationAKRMKSEYKNCAECD
HHHHHHHHCCHHHCC
18.0027251275
98UbiquitinationKRMKSEYKNCAECDT
HHHHHHHCCHHHCCH
41.31-
110PhosphorylationCDTLVCLSEMRAHIR
CCHHHHHHHHHHHHH
24.9927251275
118PhosphorylationEMRAHIRTCQKYIDK
HHHHHHHHHHHHHHH
20.7729083192
121UbiquitinationAHIRTCQKYIDKYGP
HHHHHHHHHHHHHCC
46.4422817900
122PhosphorylationHIRTCQKYIDKYGPL
HHHHHHHHHHHHCCH
6.6229083192
125UbiquitinationTCQKYIDKYGPLQEL
HHHHHHHHHCCHHHH
42.4222817900
126PhosphorylationCQKYIDKYGPLQELE
HHHHHHHHCCHHHHH
21.8929083192
135PhosphorylationPLQELEETAARCVCP
CHHHHHHHHHHHHCH
19.0829083192

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 RN125_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN125_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 RN125_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
17990982
PML_HUMANPMLphysical
22493164
CHFR_HUMANCHFRphysical
22493164
RN125_HUMANRNF125physical
21571784
JAK1_HUMANJAK1physical
26027934
P53_HUMANTP53physical
25591766
TRI14_HUMANTRIM14physical
28476934
RN125_HUMANRNF125physical
27411375
UB2D1_HUMANUBE2D1physical
27411375
ILRL2_HUMANIL1RL2physical
29176319

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616260Tenorio syndrome (TNORS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN125_HUMAN

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Related Literatures of Post-Translational Modification

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