RN128_MOUSE - dbPTM
RN128_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN128_MOUSE
UniProt AC Q9D304
Protein Name E3 ubiquitin-protein ligase RNF128
Gene Name Rnf128
Organism Mus musculus (Mouse).
Sequence Length 428
Subcellular Localization Endomembrane system
Single-pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partiall
Protein Description E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals (By similarity)..
Protein Sequence MGPPPGIGVYCRGGCGAARLLAWCFLLALSPHAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVSGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLASERGASGAVIFNFPGTRNEVIPMSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGKLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNEASNTASPHEEDSRSETASSGYASVQGADEPPLEEHAQSANENLQLVNHEANSVAVDVVPHVDNPTFEEDETPDQEAAVREIKS
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
48N-linked_GlycosylationAVWTAYLNVSWRVPH
EEEEEEEEEEEECCC
17.07-
59N-linked_GlycosylationRVPHTGVNRTVWELS
ECCCCCCCCEEEEEC
34.94-
101N-linked_GlycosylationNACNPHTNFTVPTVW
HCCCCCCCCCCCCCC
27.79-
151PhosphorylationVIFNFPGTRNEVIPM
EEECCCCCCCCEECC
30.47-
159PhosphorylationRNEVIPMSHPGAGDI
CCCEECCCCCCCCCE
22.60-
257UbiquitinationDAKKAIGKLQLRTLK
HHHHHHHHHHHHHHH
27.26-
323UbiquitinationMCKCDILKALGIEVD
CCCCHHHHHHCCEEE
41.73-

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 RN128_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN128_MOUSE !!

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 RN128_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_MOUSETrp53physical
23370271
TBK1_MOUSETbk1physical
27776110

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN128_MOUSE

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Related Literatures of Post-Translational Modification

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