IASPP_MOUSE - dbPTM
IASPP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IASPP_MOUSE
UniProt AC Q5I1X5
Protein Name RelA-associated inhibitor
Gene Name Ppp1r13l {ECO:0000312|MGI:MGI:3525053}
Organism Mus musculus (Mouse).
Sequence Length 824
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic but also nuclear.
Protein Description Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis (By similarity)..
Protein Sequence MDSEAFQHARDLLDLNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGAQAGVPSRMARYSTSPVPEHFGSRGSPQKIATDGIEARFGRSESAPSLHPYSPLSPKGRPSSPRTPIYLQPDTYSSLDRAPSPRPRAFDGAGSPHGRAPSPRPGIGPVRQPGPSTPFDYLGRAGSPRGSPLAEGPQAFFPERGPSPRPPAAAYDTAGTFGSPLLGAGGSAFTPPLRAQDDSTLRRRPPKAWNESDLDVAYEKKSSQTASYERLDVFTRPASPGLQLLPWRESSLDGLGASGKDHLTSATLPRNYKVSPLASDRRSDVGSYRRSLGSAGPSGTLPRSWQPVSRIPMPPSSPQPRSTPRQRPIPLSMIFKLQNAFWEHGAGRAVLPGSPIFSRAPPPKLPPQPPPQPQMQPQPQPQPQMQPQSQAQPQTPAPQQTWSPMNEGLLKSPAELEPEPELEVLLAPVEEAGDADEGTVTRPLSPTRLQPALPPEAQTVPELEEVARVLAEIPRPLKRRGSMEQSPAVALPPTHKKQYQQIINRLFHRHGGPGPGGPEPELSTITEGSEARAGPPAPAPPAPIPPPAPPQSSPPEQPQSMEMRSVLRKVGSPRKARRARLNPLVLLLDAALTGELDVVQQAVKEMNDPSQPNEEGITALHNAICGANYPIVDFLIAAGANVNSPDSHGWTPLHCAASCNDTAICTALVQHGAAIFATTLSDGATAIEKCDPYREGYADCATYLADVEQSMGLMHNGVVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWASLHGQEGYVPRNYFGLFPRVKSQRSKI
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-------MDSEAFQH
-------CCHHHHHH		13.28-
70PhosphorylationVPSRMARYSTSPVPE
CCCHHHCCCCCCCCC		13.5327742792
71PhosphorylationPSRMARYSTSPVPEH
CCHHHCCCCCCCCCC		19.4926745281
72PhosphorylationSRMARYSTSPVPEHF
CHHHCCCCCCCCCCC		28.2826239621
73PhosphorylationRMARYSTSPVPEHFG
HHHCCCCCCCCCCCC		20.2626824392
81PhosphorylationPVPEHFGSRGSPQKI
CCCCCCCCCCCCCCC		32.3126239621
84PhosphorylationEHFGSRGSPQKIATD
CCCCCCCCCCCCCCC		24.0524453211
100PhosphorylationIEARFGRSESAPSLH
HHHHCCCCCCCCCCC		35.9627087446
102PhosphorylationARFGRSESAPSLHPY
HHCCCCCCCCCCCCC		46.8827087446
105PhosphorylationGRSESAPSLHPYSPL
CCCCCCCCCCCCCCC		38.7425619855
109PhosphorylationSAPSLHPYSPLSPKG
CCCCCCCCCCCCCCC		16.5125619855
110PhosphorylationAPSLHPYSPLSPKGR
CCCCCCCCCCCCCCC		24.6627087446
113PhosphorylationLHPYSPLSPKGRPSS
CCCCCCCCCCCCCCC		28.1327087446
119PhosphorylationLSPKGRPSSPRTPIY
CCCCCCCCCCCCCCE		52.1725293948
120PhosphorylationSPKGRPSSPRTPIYL
CCCCCCCCCCCCCEE		22.5323737553
123PhosphorylationGRPSSPRTPIYLQPD
CCCCCCCCCCEECCC		19.8822817900
126PhosphorylationSSPRTPIYLQPDTYS
CCCCCCCEECCCCCC		10.6525293948
131PhosphorylationPIYLQPDTYSSLDRA
CCEECCCCCCCCCCC		31.8025777480
132PhosphorylationIYLQPDTYSSLDRAP
CEECCCCCCCCCCCC		12.0225777480
133PhosphorylationYLQPDTYSSLDRAPS
EECCCCCCCCCCCCC		26.9025777480
134PhosphorylationLQPDTYSSLDRAPSP
ECCCCCCCCCCCCCC		24.7125777480
137MethylationDTYSSLDRAPSPRPR
CCCCCCCCCCCCCCC		54.4124129315
140PhosphorylationSSLDRAPSPRPRAFD
CCCCCCCCCCCCCCC		32.3426643407
142MethylationLDRAPSPRPRAFDGA
CCCCCCCCCCCCCCC		37.3624129315
144MethylationRAPSPRPRAFDGAGS
CCCCCCCCCCCCCCC		49.5224129315
151PhosphorylationRAFDGAGSPHGRAPS
CCCCCCCCCCCCCCC		17.1224899341
158PhosphorylationSPHGRAPSPRPGIGP
CCCCCCCCCCCCCCC		32.3426824392
160MethylationHGRAPSPRPGIGPVR
CCCCCCCCCCCCCCC		46.5524129315
167MethylationRPGIGPVRQPGPSTP
CCCCCCCCCCCCCCC		39.8624129315
180MethylationTPFDYLGRAGSPRGS
CCCCCCCCCCCCCCC		32.93-
183PhosphorylationDYLGRAGSPRGSPLA
CCCCCCCCCCCCCCC		15.5024899341
187PhosphorylationRAGSPRGSPLAEGPQ
CCCCCCCCCCCCCCC		20.3026824392
203PhosphorylationFFPERGPSPRPPAAA
CCCCCCCCCCCCCHH		36.0425293948
205MethylationPERGPSPRPPAAAYD
CCCCCCCCCCCHHHC		54.9224129315
211PhosphorylationPRPPAAAYDTAGTFG
CCCCCHHHCCCCCCC		14.7525293948
213PhosphorylationPPAAAYDTAGTFGSP
CCCHHHCCCCCCCCC		17.8225293948
216PhosphorylationAAYDTAGTFGSPLLG
HHHCCCCCCCCCCCC		23.5125293948
219PhosphorylationDTAGTFGSPLLGAGG
CCCCCCCCCCCCCCC		14.2625293948
227PhosphorylationPLLGAGGSAFTPPLR
CCCCCCCCCCCCCCC		21.2025293948
230PhosphorylationGAGGSAFTPPLRAQD
CCCCCCCCCCCCCCC		24.5826643407
234MethylationSAFTPPLRAQDDSTL
CCCCCCCCCCCCCCH		35.6658859113
242MethylationAQDDSTLRRRPPKAW
CCCCCCHHCCCCCCC		32.4258859121
262PhosphorylationDVAYEKKSSQTASYE
HHHHCCCCCCCCCEE		38.4526643407
263PhosphorylationVAYEKKSSQTASYER
HHHCCCCCCCCCEEE		40.1926643407
265PhosphorylationYEKKSSQTASYERLD
HCCCCCCCCCEEEEE		21.3726643407
267PhosphorylationKKSSQTASYERLDVF
CCCCCCCCEEEEECC		30.8024899341
268PhosphorylationKSSQTASYERLDVFT
CCCCCCCEEEEECCC		11.5626643407
275PhosphorylationYERLDVFTRPASPGL
EEEEECCCCCCCCCC		35.2726239621
279PhosphorylationDVFTRPASPGLQLLP
ECCCCCCCCCCCCCC		23.3727180971
290PhosphorylationQLLPWRESSLDGLGA
CCCCCCHHCCCCCCC		27.8523984901
291PhosphorylationLLPWRESSLDGLGAS
CCCCCHHCCCCCCCC		26.2323984901
298PhosphorylationSLDGLGASGKDHLTS
CCCCCCCCCCCCCCC		44.5723984901
304PhosphorylationASGKDHLTSATLPRN
CCCCCCCCCCCCCCC		16.9428066266
305PhosphorylationSGKDHLTSATLPRNY
CCCCCCCCCCCCCCC		26.1426824392
307PhosphorylationKDHLTSATLPRNYKV
CCCCCCCCCCCCCCC		36.7426824392
315PhosphorylationLPRNYKVSPLASDRR
CCCCCCCCCCCCCCC		15.2828066266
319PhosphorylationYKVSPLASDRRSDVG
CCCCCCCCCCCCCCC		39.0628066266
331PhosphorylationDVGSYRRSLGSAGPS
CCCHHHHHCCCCCCC		28.2526239621
334PhosphorylationSYRRSLGSAGPSGTL
HHHHHCCCCCCCCCC		35.0329514104
338PhosphorylationSLGSAGPSGTLPRSW
HCCCCCCCCCCCCCC		43.4226643407
340PhosphorylationGSAGPSGTLPRSWQP
CCCCCCCCCCCCCCC		37.6226745281
356PhosphorylationSRIPMPPSSPQPRST
CCCCCCCCCCCCCCC		49.1026239621
357PhosphorylationRIPMPPSSPQPRSTP
CCCCCCCCCCCCCCC		33.0726239621
362PhosphorylationPSSPQPRSTPRQRPI
CCCCCCCCCCCCCCC		49.8229550500
363PhosphorylationSSPQPRSTPRQRPIP
CCCCCCCCCCCCCCC		24.6229550500
394PhosphorylationGRAVLPGSPIFSRAP
CCEECCCCCCCCCCC		16.9426824392
398PhosphorylationLPGSPIFSRAPPPKL
CCCCCCCCCCCCCCC		28.4028066266
452PhosphorylationMNEGLLKSPAELEPE
CCCCCCCCCCCCCCC		29.3418846507
479PhosphorylationAGDADEGTVTRPLSP
HCCCCCCCCCCCCCC		19.3626239621
481PhosphorylationDADEGTVTRPLSPTR
CCCCCCCCCCCCCCC		26.8026239621
485PhosphorylationGTVTRPLSPTRLQPA
CCCCCCCCCCCCCCC		27.2326824392
487PhosphorylationVTRPLSPTRLQPALP
CCCCCCCCCCCCCCC		40.4122942356
522PhosphorylationRPLKRRGSMEQSPAV
CCHHHCCCCCCCCCC		19.8226824392
526PhosphorylationRRGSMEQSPAVALPP
HCCCCCCCCCCCCCC		11.0827742792
563PhosphorylationGGPEPELSTITEGSE
CCCCCCCCCCCCCCC		18.99-
592PhosphorylationPPPAPPQSSPPEQPQ
CCCCCCCCCCCCCCC		51.0622006019
593PhosphorylationPPAPPQSSPPEQPQS
CCCCCCCCCCCCCCC		38.9528507225
782PhosphorylationFREGESVTVLRRDGP
ECCCCEEEEEECCCC		24.0928973931
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 IASPP_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of IASPP_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IASPP_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-102, 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 THR-307, AND MASSSPECTROMETRY.

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