RNF25_MOUSE - dbPTM
RNF25_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF25_MOUSE
UniProt AC Q9QZR0
Protein Name E3 ubiquitin-protein ligase RNF25
Gene Name Rnf25
Organism Mus musculus (Mouse).
Sequence Length 456
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2. Stimulates transcription mediated by NF-kappa-B (By similarity)..
Protein Sequence MAASASTAAGEEDWVLPSEVEVLESIYLDELQVMKGNGRSPWEIFITLHPATAEVQDSQFVCFTLVLRIPVQYPHEVPQISIRNPRGLSDEQIHKISQALGHVAKEGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELTTQEQEQERQHVVTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEELKLLYQRQQEKGGIIDLEAERNRYFISLQQPPAALEPESAVDVSREPQPPNALSAEQSTSLADQSTLPTSLPMTTQYTYEKTSGAGPNQQRPGETQKSVLDPPRHGRGSWRQYDRRHPKGGECCTPKGTSEIHELPPPEKPLKETVDLKAEPRNKGLTGHPQEKGPGSWQGPSARRTRDCARWERSKNRTPGSCYPHLPRGQGAYRSGTRREPLGLESEEGS
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
119UbiquitinationMLYELIEKGKEILTD
HHHHHHHHCCHHCCC		69.1822790023
239PhosphorylationQEELKLLYQRQQEKG
HHHHHHHHHHHHHCC		16.46-
258PhosphorylationLEAERNRYFISLQQP
EEHHHCCEEEECCCC		14.6022871156
261PhosphorylationERNRYFISLQQPPAA
HHCCEEEECCCCCCC		15.3822871156
273PhosphorylationPAALEPESAVDVSRE
CCCCCCCCCCCCCCC		44.2922871156
316PhosphorylationTQYTYEKTSGAGPNQ
EEEEEEECCCCCCCC		22.0623970565
331UbiquitinationQRPGETQKSVLDPPR
CCCCCCCCCCCCCCC		50.3722790023
343PhosphorylationPPRHGRGSWRQYDRR
CCCCCCCCHHCCCCC		20.0923140645
353UbiquitinationQYDRRHPKGGECCTP
CCCCCCCCCCCCCCC		73.7122790023
361UbiquitinationGGECCTPKGTSEIHE
CCCCCCCCCCCCCCC		57.5822790023
374UbiquitinationHELPPPEKPLKETVD
CCCCCCCCCCCCCCC		62.5222790023
377UbiquitinationPPPEKPLKETVDLKA
CCCCCCCCCCCCCCC		60.9222790023
383AcetylationLKETVDLKAEPRNKG
CCCCCCCCCCCCCCC		46.366565983
398UbiquitinationLTGHPQEKGPGSWQG
CCCCCCCCCCCCCCC		66.2222790023
411PhosphorylationQGPSARRTRDCARWE
CCCCCCCHHHHHHHH		25.8828059163
429PhosphorylationNRTPGSCYPHLPRGQ
CCCCCCCCCCCCCCC		8.7229514104
434MethylationSCYPHLPRGQGAYRS
CCCCCCCCCCCCCCC		57.3318959377
440MethylationPRGQGAYRSGTRREP
CCCCCCCCCCCCCCC		28.2418958583
452PhosphorylationREPLGLESEEGS---
CCCCCCCCCCCC---		46.0926525534
456PhosphorylationGLESEEGS-------
CCCCCCCC-------		40.0929514104
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 RNF25_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF25_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 RNF25_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D2_MOUSEUbe2d2aphysical
10500182
UB2L3_MOUSEUbe2l3physical
10500182
UB2E3_MOUSEUbe2e3physical
10500182
UB2E1_MOUSEUbe2e1physical
10500182
UBC_HUMANUBCphysical
10500182
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF25_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory