RNF12_MOUSE - dbPTM
RNF12_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF12_MOUSE
UniProt AC Q9WTV7
Protein Name E3 ubiquitin-protein ligase RLIM
Gene Name Rlim
Organism Mus musculus (Mouse).
Sequence Length 600
Subcellular Localization Nucleus .
Protein Description E3 ubiquitin-protein ligase that acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals..
Protein Sequence MENSDSNDKGSDQSAAQRRSQMDRLDREEAFYQFVNNLSEEDYRLMRDNNLLGTPGESTEEELLRRLQQIKEGPPPQSPDENRAGESSDDVTNSDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRNNGSQTSENESEPSTRRLSVENMESSSQRQMENSASESASARPSRAERNSAEAVTEVPTTRAQRRARSRSPEHRRTRARAERSRSPLQPTSEIPRRAPTLEQSSENEPEGSSRTRHHVTLRQQISGPELLGRGLFAASGSRNPSQGTSSSDTGSNSESSGSGQRPPTIVLDLQVRRVRPGEYRQRDSIASRTRSRSQAPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYSDSDSEPSASVSSRNVERVESRNGRGSSGGGNSSGSSSSSSPSPSSSGESSESSSEMFEGSSEGGSSGPSRRDGRHRAPVTFDESGSLPFLSLAQFFLLNEDDEDQPRGLTKEQIDNLAMRSFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLSSGNRESVV
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
1Acetylation-------MENSDSND
-------CCCCCCCC
11.25-
78PhosphorylationKEGPPPQSPDENRAG
HCCCCCCCCCCCCCC
39.8425521595
87PhosphorylationDENRAGESSDDVTNS
CCCCCCCCCCCCCCC
37.8426745281
88PhosphorylationENRAGESSDDVTNSD
CCCCCCCCCCCCCCH
33.2626745281
148PhosphorylationNVNRNNGSQTSENES
EECCCCCCCCCCCCC
32.2018779572
150PhosphorylationNRNNGSQTSENESEP
CCCCCCCCCCCCCCC
39.4418779572
163PhosphorylationEPSTRRLSVENMESS
CCCHHCCCHHHHHHH
26.1027087446
169PhosphorylationLSVENMESSSQRQME
CCHHHHHHHHHHHHH
25.2328833060
170PhosphorylationSVENMESSSQRQMEN
CHHHHHHHHHHHHHH
19.7228833060
171PhosphorylationVENMESSSQRQMENS
HHHHHHHHHHHHHHH
38.3728833060
194PhosphorylationPSRAERNSAEAVTEV
CCHHHHHCCHHHHCC
33.4428833060
203PhosphorylationEAVTEVPTTRAQRRA
HHHHCCCCHHHHHHH
33.8025195567
204PhosphorylationAVTEVPTTRAQRRAR
HHHCCCCHHHHHHHH
20.2425195567
212PhosphorylationRAQRRARSRSPEHRR
HHHHHHHHCCHHHHH
35.8027717184
214PhosphorylationQRRARSRSPEHRRTR
HHHHHHCCHHHHHHH
35.5725266776
227PhosphorylationTRARAERSRSPLQPT
HHHHHHHHCCCCCCC
28.7227087446
229PhosphorylationARAERSRSPLQPTSE
HHHHHHCCCCCCCCC
31.0727087446
234PhosphorylationSRSPLQPTSEIPRRA
HCCCCCCCCCCCCCC
26.4825619855
235PhosphorylationRSPLQPTSEIPRRAP
CCCCCCCCCCCCCCC
39.9625619855
243PhosphorylationEIPRRAPTLEQSSEN
CCCCCCCCCCCCCCC
41.7829899451
269PhosphorylationVTLRQQISGPELLGR
EEEEHCCCCHHHHHC
43.9125266776
284PhosphorylationGLFAASGSRNPSQGT
CEEECCCCCCCCCCC
26.7918779572
311PhosphorylationGSGQRPPTIVLDLQV
CCCCCCCEEEEEEEE
26.8022817900
340PhosphorylationASRTRSRSQAPNNTV
HHCCCCCCCCCCCEE
31.76-
346PhosphorylationRSQAPNNTVTYESER
CCCCCCCEEEEEECC
22.3618779572
357MethylationESERGGFRRTFSRSE
EECCCCCEECCCHHH
39.7530989223
526UbiquitinationDQPRGLTKEQIDNLA
CCCCCCCHHHHHHHH
53.30-
553PhosphorylationCSVCITEYTEGNKLR
CCEEEEECCCCCCEE
11.05-
558UbiquitinationTEYTEGNKLRKLPCS
EECCCCCCEEECCCC
61.60-

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 RNF12_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF12_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 RNF12_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZFP42_MOUSEZfp42physical
22596162

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF12_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-229, ANDMASS SPECTROMETRY.

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