RN135_HUMAN - dbPTM
RN135_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN135_HUMAN
UniProt AC Q8IUD6
Protein Name E3 ubiquitin-protein ligase RNF135
Gene Name RNF135
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Cytoplasm .
Protein Description Acts as an E2-dependent E3 ubiquitin-protein ligase, involved in innate immune defense against viruses. Ubiquitinates DDX58 and is required for full activation of the DDX58 signaling resulting in interferon beta production..
Protein Sequence MAGLGLGSAVPVWLAEDDLGCIICQGLLDWPATLPCGHSFCRHCLEALWGARDARRWACPTCRQGAAQQPHLRKNTLLQDLADKYRRAAREIQAGSDPAHCPCPGSSSLSSAAARPRRRPELQRVAVEKSITEVAQELTELVEHLVDIVRSLQNQRPLSESGPDNELSILGKAFSSGVDLSMASPKLVTSDTAAGKIRDILHDLEEIQEKLQESVTWKEAPEAQMQGELLEAPSSSSCPLPDQSHPALRRASRFAQWAIHPTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLHPGNYLIIKQVKV
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
76PhosphorylationQPHLRKNTLLQDLAD
CCHHHHCHHHHHHHH
31.7028857561
84UbiquitinationLLQDLADKYRRAARE
HHHHHHHHHHHHHHH
34.74-
151PhosphorylationHLVDIVRSLQNQRPL
HHHHHHHHHHHCCCC
24.3428102081
159PhosphorylationLQNQRPLSESGPDNE
HHHCCCCCCCCCCCC
32.1928450419
161PhosphorylationNQRPLSESGPDNELS
HCCCCCCCCCCCCHH
52.8528450419
175PhosphorylationSILGKAFSSGVDLSM
HHHHHHHHCCCCHHH
30.9224719451
176PhosphorylationILGKAFSSGVDLSMA
HHHHHHHCCCCHHHC
36.0628348404
181PhosphorylationFSSGVDLSMASPKLV
HHCCCCHHHCCCCEE
14.0829255136
184PhosphorylationGVDLSMASPKLVTSD
CCCHHHCCCCEECCC
17.5829255136
186UbiquitinationDLSMASPKLVTSDTA
CHHHCCCCEECCCCH
53.76-
189PhosphorylationMASPKLVTSDTAAGK
HCCCCEECCCCHHHH
31.1824702127
190O-linked_GlycosylationASPKLVTSDTAAGKI
CCCCEECCCCHHHHH
26.0330059200
190PhosphorylationASPKLVTSDTAAGKI
CCCCEECCCCHHHHH
26.0324702127
192PhosphorylationPKLVTSDTAAGKIRD
CCEECCCCHHHHHHH
20.4124702127
196UbiquitinationTSDTAAGKIRDILHD
CCCCHHHHHHHHHHC
29.82-
228 (in isoform 3)Phosphorylation-33.03-
228PhosphorylationPEAQMQGELLEAPSS
CHHHHCCCEECCCCC
33.03-
275PhosphorylationLSCSLEVSKDSRTVT
EEEEEEECCCCCEEE
22.75-
282PhosphorylationSKDSRTVTVSHRPQP
CCCCCEEEEECCCCC
18.7128857561
400PhosphorylationDNQEKLLYECTISAS
CCHHEEEEEEEEECC
21.2825072903
403PhosphorylationEKLLYECTISASSPL
HEEEEEEEEECCCCC
13.1625072903
405PhosphorylationLLYECTISASSPLYP
EEEEEEEECCCCCCH
12.1625072903
407PhosphorylationYECTISASSPLYPAF
EEEEEECCCCCCHHH
26.2125072903
408PhosphorylationECTISASSPLYPAFW
EEEEECCCCCCHHHE
20.7425072903
411PhosphorylationISASSPLYPAFWLYG
EECCCCCCHHHEEEE
8.9025072903
417PhosphorylationLYPAFWLYGLHPGNY
CCHHHEEEECCCCCE
14.2925072903
424PhosphorylationYGLHPGNYLIIKQVK
EECCCCCEEEEEEEE
12.7525072903

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 RN135_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN135_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 RN135_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX58_HUMANDDX58physical
19484123
UB2D2_HUMANUBE2D2physical
19484123
RN135_HUMANRNF135physical
25416956
DDX58_HUMANDDX58physical
19017631
CTNL1_HUMANCTNNAL1physical
28514442
IQCB1_HUMANIQCB1physical
28514442
TF2H2_HUMANGTF2H2physical
28514442
XRCC4_HUMANXRCC4physical
28514442
TXLNA_HUMANTXLNAphysical
28514442
TES_HUMANTESphysical
28514442
E41L5_HUMANEPB41L5physical
28514442
KLH42_HUMANKLHL42physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN135_HUMAN

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Related Literatures of Post-Translational Modification

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