IASPP_HUMAN - dbPTM
IASPP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IASPP_HUMAN
UniProt AC Q8WUF5
Protein Name RelA-associated inhibitor
Gene Name PPP1R13L
Organism Homo sapiens (Human).
Sequence Length 828
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. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis..
Protein Sequence MDSEAFQSARDFLDMNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGPQAGPPSRPPRYSSSSIPEPFGSRGSPRKAATDGADTPFGRSESAPTLHPYSPLSPKGRPSSPRTPLYLQPDAYGSLDRATSPRPRAFDGAGSSLGRAPSPRPGPGPLRQQGPPTPFDFLGRAGSPRGSPLAEGPQAFFPERGPSPRPPATAYDAPASAFGSSLLGSGGSAFAPPLRAQDDLTLRRRPPKAWNESDLDVAYEKKPSQTASYERLDVFARPASPSLQLLPWRESSLDGLGGTGKDNLTSATLPRNYKVSPLASDRRSDAGSYRRSLGSAGPSGTLPRSWQPVSRIPMPPSSPQPRGAPRQRPIPLSMIFKLQNAFWEHGASRAMLPGSPLFTRAPPPKLQPQPQPQPQPQSQPQPQLPPQPQTQPQTPTPAPQHPQQTWPPVNEGPPKPPTELEPEPEIEGLLTPVLEAGDVDEGPVARPLSPTRLQPALPPEAQSVPELEEVARVLAEIPRPLKRRGSMEQAPAVALPPTHKKQYQQIISRLFHRHGGPGPGGPEPELSPITEGSEARAGPPAPAPPAPIPPPAPSQSSPPEQPQSMEMRSVLRKAGSPRKARRARLNPLVLLLDAALTGELEVVQQAVKEMNDPSQPNEEGITALHNAICGANYSIVDFLITAGANVNSPDSHGWTPLHCAASCNDTVICMALVQHGAAIFATTLSDGATAFEKCDPYREGYADCATYLADVEQSMGLMNSGAVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWAALHGQEGYVPRNYFGLFPRVKPQRSKV
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-------MDSEAFQS
-------CCHHHHHH
13.2822814378
19PhosphorylationFLDMNFQSLAMKHMD
HHHHHHHHHHHHHCC
17.6028555341
28UbiquitinationAMKHMDLKQMELDTA
HHHHCCHHHHHHHHH
43.25-
43PhosphorylationAAKVDELTKQLESLW
HHHHHHHHHHHHHHH
18.0724719451
48PhosphorylationELTKQLESLWSDSPA
HHHHHHHHHHCCCCC
43.6724719451
51PhosphorylationKQLESLWSDSPAPPG
HHHHHHHCCCCCCCC
33.2422199227
53PhosphorylationLESLWSDSPAPPGPQ
HHHHHCCCCCCCCCC
19.9022199227
65PhosphorylationGPQAGPPSRPPRYSS
CCCCCCCCCCCCCCC
61.6324719451
70PhosphorylationPPSRPPRYSSSSIPE
CCCCCCCCCCCCCCC
20.7628985074
71PhosphorylationPSRPPRYSSSSIPEP
CCCCCCCCCCCCCCC
25.6425159151
72PhosphorylationSRPPRYSSSSIPEPF
CCCCCCCCCCCCCCC
21.1230278072
73PhosphorylationRPPRYSSSSIPEPFG
CCCCCCCCCCCCCCC
26.7530278072
74PhosphorylationPPRYSSSSIPEPFGS
CCCCCCCCCCCCCCC
44.0730278072
81PhosphorylationSIPEPFGSRGSPRKA
CCCCCCCCCCCCCCC
33.5722167270
82MethylationIPEPFGSRGSPRKAA
CCCCCCCCCCCCCCC
50.4154558243
84PhosphorylationEPFGSRGSPRKAATD
CCCCCCCCCCCCCCC
22.0322167270
87MethylationGSRGSPRKAATDGAD
CCCCCCCCCCCCCCC
45.84116253281
87UbiquitinationGSRGSPRKAATDGAD
CCCCCCCCCCCCCCC
45.84-
90PhosphorylationGSPRKAATDGADTPF
CCCCCCCCCCCCCCC
39.5622199227
95PhosphorylationAATDGADTPFGRSES
CCCCCCCCCCCCCCC
21.7121815630
100PhosphorylationADTPFGRSESAPTLH
CCCCCCCCCCCCCCC
35.9621945579
102PhosphorylationTPFGRSESAPTLHPY
CCCCCCCCCCCCCCC
40.5725159151
105PhosphorylationGRSESAPTLHPYSPL
CCCCCCCCCCCCCCC
37.1021945579
109PhosphorylationSAPTLHPYSPLSPKG
CCCCCCCCCCCCCCC
16.5121945579
110PhosphorylationAPTLHPYSPLSPKGR
CCCCCCCCCCCCCCC
24.6622167270
113PhosphorylationLHPYSPLSPKGRPSS
CCCCCCCCCCCCCCC
28.1325159151
117MethylationSPLSPKGRPSSPRTP
CCCCCCCCCCCCCCC
33.77115488459
119PhosphorylationLSPKGRPSSPRTPLY
CCCCCCCCCCCCCCC
52.1723927012
120PhosphorylationSPKGRPSSPRTPLYL
CCCCCCCCCCCCCCC
22.5325159151
122DimethylationKGRPSSPRTPLYLQP
CCCCCCCCCCCCCCC
51.42-
122MethylationKGRPSSPRTPLYLQP
CCCCCCCCCCCCCCC
51.4254558235
123PhosphorylationGRPSSPRTPLYLQPD
CCCCCCCCCCCCCCC
22.4921945579
126PhosphorylationSSPRTPLYLQPDAYG
CCCCCCCCCCCCCCC
12.4221945579
132PhosphorylationLYLQPDAYGSLDRAT
CCCCCCCCCCCCCCC
18.0321945579
134PhosphorylationLQPDAYGSLDRATSP
CCCCCCCCCCCCCCC
17.8922167270
137MethylationDAYGSLDRATSPRPR
CCCCCCCCCCCCCCC
45.0958859091
139PhosphorylationYGSLDRATSPRPRAF
CCCCCCCCCCCCCCC
39.9130576142
140PhosphorylationGSLDRATSPRPRAFD
CCCCCCCCCCCCCCC
20.2330576142
142MethylationLDRATSPRPRAFDGA
CCCCCCCCCCCCCCC
32.8658859107
144MethylationRATSPRPRAFDGAGS
CCCCCCCCCCCCCCC
49.5258859131
151PhosphorylationRAFDGAGSSLGRAPS
CCCCCCCCCCCCCCC
23.1220873877
152PhosphorylationAFDGAGSSLGRAPSP
CCCCCCCCCCCCCCC
33.6521712546
155DimethylationGAGSSLGRAPSPRPG
CCCCCCCCCCCCCCC
48.93-
155MethylationGAGSSLGRAPSPRPG
CCCCCCCCCCCCCCC
48.9354558251
158PhosphorylationSSLGRAPSPRPGPGP
CCCCCCCCCCCCCCC
32.3425159151
160MethylationLGRAPSPRPGPGPLR
CCCCCCCCCCCCCCH
53.8254558267
167DimethylationRPGPGPLRQQGPPTP
CCCCCCCHHCCCCCC
29.88-
167MethylationRPGPGPLRQQGPPTP
CCCCCCCHHCCCCCC
29.8824129315
173PhosphorylationLRQQGPPTPFDFLGR
CHHCCCCCCCCCCCC
39.4628188228
180MethylationTPFDFLGRAGSPRGS
CCCCCCCCCCCCCCC
37.6124129315
183PhosphorylationDFLGRAGSPRGSPLA
CCCCCCCCCCCCCCC
15.5022167270
185MethylationLGRAGSPRGSPLAEG
CCCCCCCCCCCCCCC
60.9854558259
187PhosphorylationRAGSPRGSPLAEGPQ
CCCCCCCCCCCCCCC
20.3022167270
200MethylationPQAFFPERGPSPRPP
CCCCCCCCCCCCCCC
63.6658854889
203PhosphorylationFFPERGPSPRPPATA
CCCCCCCCCCCCCCC
36.0425159151
205MethylationPERGPSPRPPATAYD
CCCCCCCCCCCCCCC
54.9258859099
209O-linked_GlycosylationPSPRPPATAYDAPAS
CCCCCCCCCCCCCHH
31.3731492838
209PhosphorylationPSPRPPATAYDAPAS
CCCCCCCCCCCCCHH
31.3725394399
211PhosphorylationPRPPATAYDAPASAF
CCCCCCCCCCCHHHH
14.3221712546
216PhosphorylationTAYDAPASAFGSSLL
CCCCCCHHHHCHHHH
24.0725106551
220PhosphorylationAPASAFGSSLLGSGG
CCHHHHCHHHHCCCC
16.0326356563
221PhosphorylationPASAFGSSLLGSGGS
CHHHHCHHHHCCCCC
28.1726356563
225PhosphorylationFGSSLLGSGGSAFAP
HCHHHHCCCCCCCCC
39.6926356563
228PhosphorylationSLLGSGGSAFAPPLR
HHHCCCCCCCCCCCC
24.6026356563
235MethylationSAFAPPLRAQDDLTL
CCCCCCCCCCCCCCC
35.6658859115
241PhosphorylationLRAQDDLTLRRRPPK
CCCCCCCCCCCCCCC
25.8018212344
243MethylationAQDDLTLRRRPPKAW
CCCCCCCCCCCCCCC
27.5958859123
253PhosphorylationPPKAWNESDLDVAYE
CCCCCCHHHCCCCCC
40.0228555341
259PhosphorylationESDLDVAYEKKPSQT
HHHCCCCCCCCCCCC
28.2925394399
264PhosphorylationVAYEKKPSQTASYER
CCCCCCCCCCCCEEE
49.3930576142
266PhosphorylationYEKKPSQTASYERLD
CCCCCCCCCCEEEEE
23.1626356563
268PhosphorylationKKPSQTASYERLDVF
CCCCCCCCEEEEEEE
30.8030576142
269PhosphorylationKPSQTASYERLDVFA
CCCCCCCEEEEEEEC
11.5627259358
280PhosphorylationDVFARPASPSLQLLP
EEECCCCCCCCCCCC
20.0825159151
282PhosphorylationFARPASPSLQLLPWR
ECCCCCCCCCCCCCC
26.6725159151
291PhosphorylationQLLPWRESSLDGLGG
CCCCCCHHCCCCCCC
27.8523403867
292PhosphorylationLLPWRESSLDGLGGT
CCCCCHHCCCCCCCC
26.2327794612
299PhosphorylationSLDGLGGTGKDNLTS
CCCCCCCCCCCCCCC
38.9823403867
301UbiquitinationDGLGGTGKDNLTSAT
CCCCCCCCCCCCCCC
43.19-
305PhosphorylationGTGKDNLTSATLPRN
CCCCCCCCCCCCCCC
23.6729255136
306PhosphorylationTGKDNLTSATLPRNY
CCCCCCCCCCCCCCC
23.5629255136
308PhosphorylationKDNLTSATLPRNYKV
CCCCCCCCCCCCCCC
36.7429255136
313PhosphorylationSATLPRNYKVSPLAS
CCCCCCCCCCCCCCC
17.6623403867
314MethylationATLPRNYKVSPLASD
CCCCCCCCCCCCCCC
39.52115975571
314UbiquitinationATLPRNYKVSPLASD
CCCCCCCCCCCCCCC
39.52-
316PhosphorylationLPRNYKVSPLASDRR
CCCCCCCCCCCCCCC
15.2825159151
320PhosphorylationYKVSPLASDRRSDAG
CCCCCCCCCCCCCCC
39.0629255136
324PhosphorylationPLASDRRSDAGSYRR
CCCCCCCCCCCCHHH
32.4828555341
328PhosphorylationDRRSDAGSYRRSLGS
CCCCCCCCHHHHCCC
19.7228555341
332PhosphorylationDAGSYRRSLGSAGPS
CCCCHHHHCCCCCCC
28.2522167270
335PhosphorylationSYRRSLGSAGPSGTL
CHHHHCCCCCCCCCC
35.0322167270
339PhosphorylationSLGSAGPSGTLPRSW
HCCCCCCCCCCCCCC
43.4222617229
341PhosphorylationGSAGPSGTLPRSWQP
CCCCCCCCCCCCCCC
37.6225159151
344MethylationGPSGTLPRSWQPVSR
CCCCCCCCCCCCCCC
54.3582797337
345PhosphorylationPSGTLPRSWQPVSRI
CCCCCCCCCCCCCCC
28.2929759185
350PhosphorylationPRSWQPVSRIPMPPS
CCCCCCCCCCCCCCC
31.0429759185
357PhosphorylationSRIPMPPSSPQPRGA
CCCCCCCCCCCCCCC
49.1030266825
358PhosphorylationRIPMPPSSPQPRGAP
CCCCCCCCCCCCCCC
33.0730266825
362MethylationPPSSPQPRGAPRQRP
CCCCCCCCCCCCCCC
48.9782796411
373PhosphorylationRQRPIPLSMIFKLQN
CCCCCCHHHHHHHHH
12.4128555341
395PhosphorylationSRAMLPGSPLFTRAP
CCCCCCCCCCCCCCC
19.2522167270
399PhosphorylationLPGSPLFTRAPPPKL
CCCCCCCCCCCCCCC
33.3423403867
400MethylationPGSPLFTRAPPPKLQ
CCCCCCCCCCCCCCC
37.4554558227
489PhosphorylationGPVARPLSPTRLQPA
CCCCCCCCCCCCCCC
27.2324505115
491PhosphorylationVARPLSPTRLQPALP
CCCCCCCCCCCCCCC
40.4123312004
522MethylationAEIPRPLKRRGSMEQ
HHCCCCHHHCCCHHH
42.61115975579
522UbiquitinationAEIPRPLKRRGSMEQ
HHCCCCHHHCCCHHH
42.61-
526PhosphorylationRPLKRRGSMEQAPAV
CCHHHCCCHHHCCCC
19.8230266825
538PhosphorylationPAVALPPTHKKQYQQ
CCCCCCCCCHHHHHH
44.3720068231
541UbiquitinationALPPTHKKQYQQIIS
CCCCCCHHHHHHHHH
46.782189047
541 (in isoform 1)Ubiquitination-46.7821890473
543PhosphorylationPPTHKKQYQQIISRL
CCCCHHHHHHHHHHH
15.9727642862
567PhosphorylationGGPEPELSPITEGSE
CCCCCCCCCCCCCCC
16.7625159151
570PhosphorylationEPELSPITEGSEARA
CCCCCCCCCCCCCCC
37.3623927012
573PhosphorylationLSPITEGSEARAGPP
CCCCCCCCCCCCCCC
23.1120873877
594PhosphorylationPIPPPAPSQSSPPEQ
CCCCCCCCCCCCCCC
44.8121712546
596PhosphorylationPPPAPSQSSPPEQPQ
CCCCCCCCCCCCCCC
49.5023663014
597PhosphorylationPPAPSQSSPPEQPQS
CCCCCCCCCCCCCCC
36.5221712546
604PhosphorylationSPPEQPQSMEMRSVL
CCCCCCCCHHHHHHH
24.3222199227
616PhosphorylationSVLRKAGSPRKARRA
HHHHHCCCHHHHHHH
26.7926853621

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
84SPhosphorylationKinaseCDK1P06493
PSP
113SPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IASPP_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
12134007
SP1_HUMANSP1physical
12134007
TF65_HUMANRELAphysical
10336463
P53_HUMANTP53physical
20840860
EP300_HUMANEP300physical
21513714
P53_HUMANTP53physical
21513714
P53_HUMANTP53physical
17906639
CBP_HUMANCREBBPphysical
25675294
EP300_HUMANEP300physical
25675294
NF2L2_HUMANNFE2L2physical
29033244
KEAP1_HUMANKEAP1physical
29033244

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70; SER-183 AND SER-187,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-110; SER-113;SER-119; SER-120; THR-123; SER-134; SER-158; SER-183; SER-187;SER-203; SER-225; SER-316; SER-332; SER-526; SER-567 AND SER-597, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-113; SER-183AND SER-187, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, AND MASSSPECTROMETRY.

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