RBM14_MOUSE - dbPTM
RBM14_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM14_MOUSE
UniProt AC Q8C2Q3
Protein Name RNA-binding protein 14
Gene Name Rbm14
Organism Mus musculus (Mouse).
Sequence Length 669
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm . In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Cytoplasmic localization is crucial for its function in suppressing the formation of aberrant centriolar pr
Protein Description May function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1 (By similarity). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. [PubMed: 25385835 Prevents the formation of the STIL-CENPJ complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CENPJ (By similarity Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.]
Protein Sequence MKIFVGNVDGADTTPEELAALFAPYGTVMSCAVMKQFAFVHMRENAGAVRAIEALHGHELRPGRALVVEMSRPRPLNTWKIFVGNVSAACTSQELRSLFERRGRVIECDVVKDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPALAIQSGDKTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPPRASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMAAQAASYRAQPSVSLGAPYRGQLASPSSQSAAASSLGPYGGVQPSASALSTYGGQAAAASSLNSYGAQGSSLASYGNQPSSYGAQAASSYGVRAAASSYNTQGAASSLGSYGAQAASYGAQSAASSLAYGAQAASYSAQPSASYSAQSAPYAAQQAASYSSQPAAYVAQPATAAAYASQPAAYAAQATTPMAGSYGAQPVVQTQLNSYGAQASIGLSGSYGAQSAAAATGSYGAAAAYGAQPSATLAAPYRTQSSASLAASYAAQQHPQAAASYRGQPGSAYDGTGQPSAAYLSMSQGAVANANSTPPPYERTRLSPPRASYDDPYKKAVAMSKRYGSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYNDYLRAAQMHSGYQRRM
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
112AcetylationVIECDVVKDYAFVHM
EEECEEECCEEEEEE		44.8922826441
114PhosphorylationECDVVKDYAFVHMEK
ECEEECCEEEEEECC		9.0229514104
135AcetylationAIAQLNGKEVKGKRI
HHHHHCCCEECCEEE		59.2669473
135MalonylationAIAQLNGKEVKGKRI
HHHHHCCCEECCEEE		59.2626320211
135UbiquitinationAIAQLNGKEVKGKRI
HHHHHCCCEECCEEE		59.26-
147PhosphorylationKRINVELSTKGQKKG
EEEEEEECCCCCCCC		17.9929176673
148PhosphorylationRINVELSTKGQKKGP
EEEEEECCCCCCCCC		52.3929176673
149AcetylationINVELSTKGQKKGPA
EEEEECCCCCCCCCE		56.8423806337
149UbiquitinationINVELSTKGQKKGPA
EEEEECCCCCCCCCE		56.8422790023
153MalonylationLSTKGQKKGPALAIQ
ECCCCCCCCCEEEEE		63.3426320211
161PhosphorylationGPALAIQSGDKTKKP
CCEEEEECCCCCCCC		42.7326824392
164AcetylationLAIQSGDKTKKPGAG
EEEECCCCCCCCCCC		66.8123806337
206PhosphorylationDGQARQPTPPFFGRD
CCCCCCCCCCCCCCC		34.9424925903
215PhosphorylationPFFGRDRSPLRRSPP
CCCCCCCCCCCCCCC		32.3526824392
220PhosphorylationDRSPLRRSPPRASYV
CCCCCCCCCCCCCCC		32.5923527152
225PhosphorylationRRSPPRASYVAPLTA
CCCCCCCCCCCCCCC		22.7821082442
226PhosphorylationRSPPRASYVAPLTAQ
CCCCCCCCCCCCCCC		10.3121082442
231O-linked_GlycosylationASYVAPLTAQPATYR
CCCCCCCCCCCCEEC		23.3755413531
231PhosphorylationASYVAPLTAQPATYR
CCCCCCCCCCCCEEC		23.3729472430
242O-linked_GlycosylationATYRAQPSVSLGAAY
CEECCCCCCCCCCEE		16.5630059200
242PhosphorylationATYRAQPSVSLGAAY
CEECCCCCCCCCCEE		16.56-
244O-linked_GlycosylationYRAQPSVSLGAAYRA
ECCCCCCCCCCEEEC		25.9830059200
244PhosphorylationYRAQPSVSLGAAYRA
ECCCCCCCCCCEEEC		25.9828725479
254PhosphorylationAAYRAQPSASLGVGY
CEEECCCCCCCCCCC		20.5728833060
256PhosphorylationYRAQPSASLGVGYRT
EECCCCCCCCCCCCC		29.9628725479
256O-linked_GlycosylationYRAQPSASLGVGYRT
EECCCCCCCCCCCCC		29.9630059200
272PhosphorylationPMAAQAASYRAQPSV
CCHHHHHHHHCCCCC		20.4029176673
273PhosphorylationMAAQAASYRAQPSVS
CHHHHHHHHCCCCCC		12.7722802335
278PhosphorylationASYRAQPSVSLGAPY
HHHHCCCCCCCCCCC		16.5628833060
280PhosphorylationYRAQPSVSLGAPYRG
HHCCCCCCCCCCCCC		25.9828725479
280O-linked_GlycosylationYRAQPSVSLGAPYRG
HHCCCCCCCCCCCCC		25.9830059200
291PhosphorylationPYRGQLASPSSQSAA
CCCCCCCCCCCHHHH		33.6322006019
518PhosphorylationTLAAPYRTQSSASLA
EEECCCCCCCHHHHH		27.2826643407
520PhosphorylationAAPYRTQSSASLAAS
ECCCCCCCHHHHHHH		27.5325521595
521PhosphorylationAPYRTQSSASLAASY
CCCCCCCHHHHHHHH		16.4425266776
523PhosphorylationYRTQSSASLAASYAA
CCCCCHHHHHHHHHH		22.0821659605
527O-linked_GlycosylationSSASLAASYAAQQHP
CHHHHHHHHHHHHCC		15.0830059200
527PhosphorylationSSASLAASYAAQQHP
CHHHHHHHHHHHHCC		15.0825293948
528PhosphorylationSASLAASYAAQQHPQ
HHHHHHHHHHHHCCH		10.9625293948
546PhosphorylationSYRGQPGSAYDGTGQ
HHCCCCCCCCCCCCC		30.2725159016
548PhosphorylationRGQPGSAYDGTGQPS
CCCCCCCCCCCCCCC		19.3225159016
551PhosphorylationPGSAYDGTGQPSAAY
CCCCCCCCCCCCCEE		29.7325159016
555PhosphorylationYDGTGQPSAAYLSMS
CCCCCCCCCEEEECC		20.0425159016
558PhosphorylationTGQPSAAYLSMSQGA
CCCCCCEEEECCCCC		10.0625159016
560PhosphorylationQPSAAYLSMSQGAVA
CCCCEEEECCCCCHH		12.0525159016
562PhosphorylationSAAYLSMSQGAVANA
CCEEEECCCCCHHCC		23.3025159016
571PhosphorylationGAVANANSTPPPYER
CCHHCCCCCCCCCCC		39.6224925903
572PhosphorylationAVANANSTPPPYERT
CHHCCCCCCCCCCCC		39.3525521595
576PhosphorylationANSTPPPYERTRLSP
CCCCCCCCCCCCCCC		24.6624925903
579PhosphorylationTPPPYERTRLSPPRA
CCCCCCCCCCCCCCC		24.8327149854
582PhosphorylationPYERTRLSPPRASYD
CCCCCCCCCCCCCCC		29.5726824392
587PhosphorylationRLSPPRASYDDPYKK
CCCCCCCCCCCHHHH		30.3025266776
588PhosphorylationLSPPRASYDDPYKKA
CCCCCCCCCCHHHHH		24.3129472430
592PhosphorylationRASYDDPYKKAVAMS
CCCCCCHHHHHHHHH		31.9228576409
599PhosphorylationYKKAVAMSKRYGSDR
HHHHHHHHHHHCCCH		12.3018779572
600MalonylationKKAVAMSKRYGSDRR
HHHHHHHHHHCCCHH		36.2326320211
612PhosphorylationDRRLAELSDYRRLSE
CHHHHHHHHHHHHCH		24.89-
618PhosphorylationLSDYRRLSESQLSFR
HHHHHHHCHHHHCCC		33.1326824392
620PhosphorylationDYRRLSESQLSFRRS
HHHHHCHHHHCCCCC		32.8027566939
623PhosphorylationRLSESQLSFRRSPTK
HHCHHHHCCCCCCCC		14.7427149854
627PhosphorylationSQLSFRRSPTKSSLD
HHHCCCCCCCCCCCC		32.4426824392
629PhosphorylationLSFRRSPTKSSLDYR
HCCCCCCCCCCCCHH		44.8222802335
631PhosphorylationFRRSPTKSSLDYRRL
CCCCCCCCCCCHHCC		38.3129176673
632PhosphorylationRRSPTKSSLDYRRLP
CCCCCCCCCCHHCCC		27.1514729942
643PhosphorylationRRLPDAHSDYARYSG
HCCCCCCHHHHHHCC		33.7529514104
645PhosphorylationLPDAHSDYARYSGSY
CCCCCHHHHHHCCCH		8.9422817900
648PhosphorylationAHSDYARYSGSYNDY
CCHHHHHHCCCHHHH		14.8221082442
649PhosphorylationHSDYARYSGSYNDYL
CHHHHHHCCCHHHHH		18.7321082442
651PhosphorylationDYARYSGSYNDYLRA
HHHHHCCCHHHHHHH		18.1530635358
663PhosphorylationLRAAQMHSGYQRRM-
HHHHHHHHCCCCCC-		33.5827149854
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 RBM14_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM14_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 RBM14_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RBM14_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM14_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206 AND SER-582, ANDMASS SPECTROMETRY.
"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-582 AND SER-618, ANDMASS SPECTROMETRY.
"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-256 AND SER-520, ANDMASS SPECTROMETRY.
"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 THR-629 AND SER-632, ANDMASS SPECTROMETRY.
"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 THR-206, AND MASSSPECTROMETRY.

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