RBM39_MOUSE - dbPTM
RBM39_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM39_MOUSE
UniProt AC Q8VH51
Protein Name RNA-binding protein 39
Gene Name Rbm39
Organism Mus musculus (Mouse).
Sequence Length 530
Subcellular Localization Nucleus .
Protein Description Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1. May be involved in pre-mRNA splicing process..
Protein Sequence MADDIDIEAMLEAPYKKDENKLNSANGHEERSKKRKKSKSRSRSHERKRSKSKERKRSRDRERKKSKSRERKRSRSKERRRSRSRSRDRRFRGRYRSPYSGPKFNSAIRGKIGLPHSIKLSRRRSRSKSPFRKDKSPVREPIDNLTPEERDARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVEFVDVSSVPLAIGLTGQRVLGVPIIVQASQAEKNRAAAMANNLQKGSAGPMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDSETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDASSASSFLDSDELERTGIDLGTTGRLQLMARLAEGTGLQIPPAAQQALQMSGSLAFGAVAEFSFVIDLQTRLSQQTEASALAAAASVQPLATQCFQLSNMFNPQTEEEVGWDTEIKDDVIEECNKHGGVIHIYVDKNSAQGNVYVKCPSIAAAIAAVNALHGRWFAGKMITAAYVPLPTYHNLFPDSMTATQLLVPSRR
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
2Acetylation------MADDIDIEA
------CCCCCCHHH
24.15-
24PhosphorylationKDENKLNSANGHEER
CCCCCCCCCCCCHHH
33.2827841257
40PhosphorylationKKRKKSKSRSRSHER
HHHHHHHHHHHHHHH
42.4519367708
42PhosphorylationRKKSKSRSRSHERKR
HHHHHHHHHHHHHHH
45.2719367708
44PhosphorylationKSKSRSRSHERKRSK
HHHHHHHHHHHHHHH
30.8319367708
95PhosphorylationDRRFRGRYRSPYSGP
HHHHHCCCCCCCCCC
20.4727087446
97PhosphorylationRFRGRYRSPYSGPKF
HHHCCCCCCCCCCCH
21.1827087446
99PhosphorylationRGRYRSPYSGPKFNS
HCCCCCCCCCCCHHH
27.7523984901
100PhosphorylationGRYRSPYSGPKFNSA
CCCCCCCCCCCHHHH
52.5925521595
106PhosphorylationYSGPKFNSAIRGKIG
CCCCCHHHHHHCCCC
28.3629514104
109MethylationPKFNSAIRGKIGLPH
CCHHHHHHCCCCCCC
39.8212019205
117PhosphorylationGKIGLPHSIKLSRRR
CCCCCCCCHHHHCCC
21.3426824392
121PhosphorylationLPHSIKLSRRRSRSK
CCCCHHHHCCCCCCC
20.8126824392
125PhosphorylationIKLSRRRSRSKSPFR
HHHHCCCCCCCCCCC
38.8123684622
127PhosphorylationLSRRRSRSKSPFRKD
HHCCCCCCCCCCCCC
38.4423684622
129PhosphorylationRRRSRSKSPFRKDKS
CCCCCCCCCCCCCCC
30.4323684622
136PhosphorylationSPFRKDKSPVREPID
CCCCCCCCCCCCCCC
38.4724925903
146PhosphorylationREPIDNLTPEERDAR
CCCCCCCCHHHHHHH
34.6024925903
174PhosphorylationRDLEEFFSTVGKVRD
CCHHHHHHHCCCHHE
27.7529550500
175PhosphorylationDLEEFFSTVGKVRDV
CHHHHHHHCCCHHEE
28.2829550500
178UbiquitinationEFFSTVGKVRDVRMI
HHHHHCCCHHEEEEE
29.7522790023
232UbiquitinationVQASQAEKNRAAAMA
EECHHHHHHHHHHHH
55.5422790023
306UbiquitinationSDSECAKKALEQLNG
CCHHHHHHHHHHCCC
39.4122790023
330PhosphorylationVGHVTERTDASSASS
CCCCEECCCCCHHHH
29.6825619855
333PhosphorylationVTERTDASSASSFLD
CEECCCCCHHHHHCC
29.2825619855
334PhosphorylationTERTDASSASSFLDS
EECCCCCHHHHHCCH
33.6122942356
336PhosphorylationRTDASSASSFLDSDE
CCCCCHHHHHCCHHH
24.4625521595
337PhosphorylationTDASSASSFLDSDEL
CCCCHHHHHCCHHHH
29.5525521595
341PhosphorylationSASSFLDSDELERTG
HHHHHCCHHHHHHHC
34.8227149854
347PhosphorylationDSDELERTGIDLGTT
CHHHHHHHCCCCCHH
29.1619854140
353PhosphorylationRTGIDLGTTGRLQLM
HHCCCCCHHHHHHHH
33.1222942356
354PhosphorylationTGIDLGTTGRLQLMA
HCCCCCHHHHHHHHH
20.6422817900

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 RBM39_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM39_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 RBM39_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA6_HUMANNCOA6physical
11704680

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM39_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-136, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-136, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-337, ANDMASS SPECTROMETRY.

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