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Protein Page:
RNF25 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RNF25 E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2. Stimulates transcription mediated by NF-kappa-B. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; EC 6.3.2.19; EC 6.3.2.-; Ligase; Transcription, coactivator/corepressor; Ubiquitin ligase
Cellular Component: nucleus; cytosol
Molecular Function: NF-kappaB binding; protein binding; zinc ion binding; coenzyme F420-2 alpha-glutamyl ligase activity; metal ion binding; UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; ribosomal S6-glutamic acid ligase activity; ubiquitin-protein ligase activity; coenzyme F420-0 gamma-glutamyl ligase activity; ligase activity
Biological Process: protein ubiquitination; activation of NF-kappaB transcription factor
Reference #:  Q9QZR0 (UniProtKB)
Alt. Names/Synonyms: 0610009H16Rik; AO7; E3 ubiquitin-protein ligase RNF25; OTTMUSP00000024323; RING finger protein 25; RING finger protein AO7; Rnf25
Gene Symbols: Rnf25
Molecular weight: 51,227 Da
Basal Isoelectric point: 5.89  Predict pI for various phosphorylation states
Select Structure to View Below

RNF25

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 2 S89 IRNPRGLSDEQIHKI
0 4 K119-ub MLYELIEkGKEILTD
0 1 K210 VYDLASLKAAPEPQQ
0 1 Y239-p QEELKLLyQRQQEKG
0 1 S294 LSAEQSTSLADQSTL
0 5 K331-ub QRPGETQkSVLDPPR
0 3 R338 kSVLDPPRHGRGsWR
0 1 S343-p PPRHGRGsWRQYDRR
0 1 K353-ub QYDRRHPkGGECCTP
0 1 K361-ub GGECCTPkGTSEIHE
0 1 K383-ac LKETVDLkAEPRNKG
0 1 K383 LKETVDLKAEPRNKG
0 1 N388 DLkAEPRNKGLTGHP
0 1 K398-ub LTGHPQEkGPGSWQG
0 1 S402 PQEkGPGSWQGPSAR
0 2 Y429 NRTPGSCYPHLPrGQ
0 3 R434-m1 SCYPHLPrGQGAYrS
0 1 R440-m1 PrGQGAYrSGTRREP
0 11 P447 rSGTRREPLGLESEE
0 2 E453 EPLGLESEEGS____
0 1 S456 GLESEEGS_______
  human

 
S90-p IRNPRGLsDEQIHTI
K120-ub MLYELIEkGKEILTD
K213-ac VYDLASLkAAPEPQQ
Y242 QEERKRLYQRQQERG
S297-p LAAELSTsPAVQSTL
K334-ub QRLGETQkAMLDPPk
K341-ub kAMLDPPkPSRGPWR
P346 PPkPSRGPWRQPERR
K356 QPERRHPKGGECHAP
K364 GGECHAPKGTRDTQE
K386 LKEPMDLKPEPHsQG
K386-ub LKEPMDLkPEPHsQG
S391-p DLkPEPHsQGVEGPP
K401 VEGPPQEKGPGsWQG
S405-p PQEKGPGsWQGPPPR
Y432-p GRTPGSSyPRLPrGQ
R437-m1 SSyPRLPrGQGAYRP
R443 PrGQGAYRPGTRREs
S450-p RPGTRREsLGLESkD
K456-ub EsLGLESkDGs____
S459-p GLESkDGs_______
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