PAIRB_MOUSE - dbPTM
PAIRB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAIRB_MOUSE
UniProt AC Q9CY58
Protein Name Plasminogen activator inhibitor 1 RNA-binding protein
Gene Name Serbp1
Organism Mus musculus (Mouse).
Sequence Length 407
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, perinuclear region . Also found in perinuclear regions.
Protein Description May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay..
Protein Sequence MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVADKKEETQPPVALKKEGIRRVGRRPDQQLQGDGKLIDRRAERRPPRERRFEKPLEEKGEGGEFSVDRPIIERPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA
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
11S-nitrosocysteineHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.76-
11S-nitrosylationHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.7620925432
11S-palmitoylationHLQEGFGCVVTNRFD
CCCCCCCEEEECCHH		1.7626165157
14PhosphorylationEGFGCVVTNRFDQLF
CCCCEEEECCHHHHC		10.5723984901
25PhosphorylationDQLFDDESDPFEVLK
HHHCCCCCCHHHHHH		58.5424925903
32UbiquitinationSDPFEVLKAAENKKK
CCHHHHHHHHHHHCC		51.2122790023
52AcetylationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.6823806337
52UbiquitinationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.68-
52MalonylationGVGGPGAKSAAQAAA
CCCCHHHHHHHHHHH		46.6826320211
53PhosphorylationVGGPGAKSAAQAAAQ
CCCHHHHHHHHHHHH		28.4428066266
61PhosphorylationAAQAAAQTNSNAAGK
HHHHHHHCCCCHHHH		35.5729233185
63PhosphorylationQAAAQTNSNAAGKQL
HHHHHCCCCHHHHHH		31.1025266776
68AcetylationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.24-
68SuccinylationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.24-
68UbiquitinationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.24-
68MalonylationTNSNAAGKQLRKESQ
CCCCHHHHHHHHHHH		41.2426320211
74PhosphorylationGKQLRKESQKDRKNP
HHHHHHHHHHHCCCC		45.6322324799
122AcetylationQQLQGDGKLIDRRAE
HHCCCCCCCCCHHHH		47.1923806337
122UbiquitinationQQLQGDGKLIDRRAE
HHCCCCCCCCCHHHH		47.19-
122MalonylationQQLQGDGKLIDRRAE
HHCCCCCCCCCHHHH		47.1926320211
140UbiquitinationPRERRFEKPLEEKGE
CCHHHCCCCCHHCCC		52.79-
140AcetylationPRERRFEKPLEEKGE
CCHHHCCCCCHHCCC		52.79-
152PhosphorylationKGEGGEFSVDRPIIE
CCCCCCCCCCCCCCC		20.8526824392
155MethylationGGEFSVDRPIIERPI
CCCCCCCCCCCCCCC		23.3558858761
160DimethylationVDRPIIERPIRGRGG
CCCCCCCCCCCCCCC		22.87-
160MethylationVDRPIIERPIRGRGG
CCCCCCCCCCCCCCC		22.8724384579
163DimethylationPIIERPIRGRGGLGR
CCCCCCCCCCCCCCC		31.29-
163MethylationPIIERPIRGRGGLGR
CCCCCCCCCCCCCCC		31.2912019671
165MethylationIERPIRGRGGLGRGR
CCCCCCCCCCCCCCC		26.5924129315
181MethylationGRGRGMGRGDGFDSR
CCCCCCCCCCCCCCC		31.0112019707
181DimethylationGRGRGMGRGDGFDSR
CCCCCCCCCCCCCCC		31.01-
187PhosphorylationGRGDGFDSRGKREFD
CCCCCCCCCCCCCCC		40.44-
188MethylationRGDGFDSRGKREFDR
CCCCCCCCCCCCCCC		57.4024129315
197 (in isoform 3)Phosphorylation-40.6725266776
197PhosphorylationKREFDRHSGSDRSSF
CCCCCCCCCCCCHHH		40.6726824392
199 (in isoform 3)Phosphorylation-32.6326824392
199PhosphorylationEFDRHSGSDRSSFSH
CCCCCCCCCCHHHCC		32.6325266776
202PhosphorylationRHSGSDRSSFSHYSG
CCCCCCCHHHCCCCC		40.5027742792
203PhosphorylationHSGSDRSSFSHYSGL
CCCCCCHHHCCCCCC		31.4926824392
205PhosphorylationGSDRSSFSHYSGLKH
CCCCHHHCCCCCCCC		24.3827742792
207PhosphorylationDRSSFSHYSGLKHED
CCHHHCCCCCCCCCC		11.8428833060
208PhosphorylationRSSFSHYSGLKHEDK
CHHHCCCCCCCCCCC		32.0225266776
211AcetylationFSHYSGLKHEDKRGG
HCCCCCCCCCCCCCC		48.77-
211UbiquitinationFSHYSGLKHEDKRGG
HCCCCCCCCCCCCCC		48.77-
216MethylationGLKHEDKRGGSGSHN
CCCCCCCCCCCCCCC		68.0124129315
219PhosphorylationHEDKRGGSGSHNWGT
CCCCCCCCCCCCCCC		39.6923684622
221PhosphorylationDKRGGSGSHNWGTVK
CCCCCCCCCCCCCCC		18.4920469934
226PhosphorylationSGSHNWGTVKDELTE
CCCCCCCCCCCHHHC		18.9225619855
226 (in isoform 3)Phosphorylation-18.9226239621
228UbiquitinationSHNWGTVKDELTESP
CCCCCCCCCHHHCCH		45.37-
231 (in isoform 3)Phosphorylation-10.3826824392
232PhosphorylationGTVKDELTESPKYIQ
CCCCCHHHCCHHHHH		32.1625521595
232 (in isoform 2)Phosphorylation-32.1626239621
234 (in isoform 3)Phosphorylation-22.8125521595
234PhosphorylationVKDELTESPKYIQKQ
CCCHHHCCHHHHHHH		22.8125521595
236AcetylationDELTESPKYIQKQIS
CHHHCCHHHHHHHHH		65.3544497845
236UbiquitinationDELTESPKYIQKQIS
CHHHCCHHHHHHHHH		65.3522790023
237PhosphorylationELTESPKYIQKQISY
HHHCCHHHHHHHHHC		16.3925777480
237 (in isoform 2)Phosphorylation-16.3926824392
237 (in isoform 3)Phosphorylation-16.3930352176
240 (in isoform 2)Phosphorylation-39.7925521595
243 (in isoform 2)Phosphorylation-14.0630352176
243PhosphorylationKYIQKQISYNCSDLD
HHHHHHHHCCCHHCC		14.0625521595
244PhosphorylationYIQKQISYNCSDLDQ
HHHHHHHCCCHHCCC		23.0922802335
247PhosphorylationKQISYNCSDLDQSNV
HHHHCCCHHCCCCCC		37.2525521595
252PhosphorylationNCSDLDQSNVTEETP
CCHHCCCCCCCCCCC		32.6925159016
255PhosphorylationDLDQSNVTEETPEGE
HCCCCCCCCCCCCCC		32.1425159016
258PhosphorylationQSNVTEETPEGEEHP
CCCCCCCCCCCCCCC		22.0225159016
269PhosphorylationEEHPVADTENKENEV
CCCCCCCCCCCCCCH		31.5523984901
293AcetylationEMTLDEWKAIQNKDR
CCCHHHHHHHHCCCC		33.30-
293UbiquitinationEMTLDEWKAIQNKDR
CCCHHHHHHHHCCCC		33.3022790023
319MalonylationEGADGQWKKGFVLHK
CCCCCCEEEEEEEEC		34.8226320211
319UbiquitinationEGADGQWKKGFVLHK
CCCCCCEEEEEEEEC		34.82-
320AcetylationGADGQWKKGFVLHKS
CCCCCEEEEEEEECC		55.4072663183
320MalonylationGADGQWKKGFVLHKS
CCCCCEEEEEEEECC		55.4026320211
327PhosphorylationKGFVLHKSKSEEAHA
EEEEEECCCCCHHHH		30.5725521595
328AcetylationGFVLHKSKSEEAHAE
EEEEECCCCCHHHHH		67.6923806337
329PhosphorylationFVLHKSKSEEAHAED
EEEECCCCCHHHHHH		48.0025521595
337PhosphorylationEEAHAEDSVMDHHFR
CHHHHHHHHHHHHCC		15.7327742792
352PhosphorylationKPANDITSQLEINFG
CCHHHHCCCCEEECC		32.85-
363MethylationINFGDLGRPGRGGRG
EECCCCCCCCCCCCC		37.4824129315
366MethylationGDLGRPGRGGRGGRG
CCCCCCCCCCCCCCC		47.2624129315
369MethylationGRPGRGGRGGRGGRG
CCCCCCCCCCCCCCC		47.4124129315
387PhosphorylationRPNRGSRTDKSSASA
CCCCCCCCCCCCCCC		49.8527087446
390PhosphorylationRGSRTDKSSASAPDV
CCCCCCCCCCCCCCC		33.6722942356
391PhosphorylationGSRTDKSSASAPDVD
CCCCCCCCCCCCCCC		31.8027087446
393PhosphorylationRTDKSSASAPDVDDP
CCCCCCCCCCCCCCH		42.1322942356
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 PAIRB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of PAIRB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAIRB_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-329, AND MASSSPECTROMETRY.
"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 SER-25, AND MASSSPECTROMETRY.
"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-234; SER-252 ANDTYR-244, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-390, AND MASSSPECTROMETRY.

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