SIPA1_HUMAN - dbPTM
SIPA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIPA1_HUMAN
UniProt AC Q96FS4
Protein Name Signal-induced proliferation-associated protein 1
Gene Name SIPA1
Organism Homo sapiens (Human).
Sequence Length 1042
Subcellular Localization Nucleus . Cytoplasm, perinuclear region . Endomembrane system
Peripheral membrane protein . Mostly localized in the perinuclear membraneous region.
Protein Description GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting them to the putatively inactive GDP-bound state. [PubMed: 9346962 Affects cell cycle progression (By similarity]
Protein Sequence MPMWAGGVGSPRRGMAPASTDDLFARKLRQPARPPLTPHTFEPRPVRGPLLRSGSDAGEARPPTPASPRARAHSHEEASRPAATSTRLFTDPLALLGLPAEEPEPAFPPVLEPRWFAHYDVQSLLFDWAPRSQGMGSHSEASSGTLASAEDQAASSDLLHGAPGFVCELGGEGELGLGGPASPPVPPALPNAAVSILEEPQNRTSAYSLEHADLGAGYYRKYFYGKEHQNFFGMDESLGPVAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPQLSPSCLRLGSASPKVPRTLLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGPAFMQFLTLLGDVVRLKGFESYRAQLDTKTDSTGTHSLYTTYQDHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHTPCTPHTTYRVAVSRTQDTPAFGPALPAGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSLGGRRRAAPRGPGAELQAAGSLVWGVRAAPGARVAAGAQASGPEGIEVPCLLGISAEALVLVAPRDGRVVFNCACRDVLAWTFSEQQLDLYHGRGEAITLRFDGSPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFVTHVERFTFAETAGLRPGARLLRVCGQTLPSLRPEAAAQLLRSAPKVCVTVLPPDESGRPRRSFSELYTLSLQEPSRRGAPDPVQDEVQGVTLLPTTKQLLHLCLQDGGSPPGPGDLAEERTEFLHSQNSLSPRSSLSDEAPVLPNTTPDLLLATTAKPSVPSADSETPLTQDRPGSPSGSEDKGNPAPELRASFLPRTLSLRNSISRIMSEAGSGTLEDEWQAISEIASTCNTILESLSREGQPIPESGDPKGTPKSDAEPEPGNLSEKVSHLESMLRKLQEDLQKEKADRAALEEEVRSLRHNNRRLQAESESAATRLLLASKQLGSPTADLA
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
12MethylationAGGVGSPRRGMAPAS
CCCCCCCCCCCCCCC
49.86115391815
13MethylationGGVGSPRRGMAPAST
CCCCCCCCCCCCCCH
42.4954559297
19PhosphorylationRRGMAPASTDDLFAR
CCCCCCCCHHHHHHH
31.1723401153
20PhosphorylationRGMAPASTDDLFARK
CCCCCCCHHHHHHHH
35.3223401153
27AcetylationTDDLFARKLRQPARP
HHHHHHHHHCCCCCC
44.5912650523
47DimethylationTFEPRPVRGPLLRSG
CCCCCCCCCCCCCCC
43.63-
47MethylationTFEPRPVRGPLLRSG
CCCCCCCCCCCCCCC
43.6354539415
53PhosphorylationVRGPLLRSGSDAGEA
CCCCCCCCCCCCCCC
42.4929255136
55PhosphorylationGPLLRSGSDAGEARP
CCCCCCCCCCCCCCC
26.0729255136
61MethylationGSDAGEARPPTPASP
CCCCCCCCCCCCCCH
33.17115916989
64PhosphorylationAGEARPPTPASPRAR
CCCCCCCCCCCHHHH
33.8823401153
67PhosphorylationARPPTPASPRARAHS
CCCCCCCCHHHHCCC
19.0029255136
74PhosphorylationSPRARAHSHEEASRP
CHHHHCCCCHHHCCC
31.4423401153
79PhosphorylationAHSHEEASRPAATST
CCCCHHHCCCCCCCH
41.9229978859
84PhosphorylationEASRPAATSTRLFTD
HHCCCCCCCHHHCCC
32.5129978859
85PhosphorylationASRPAATSTRLFTDP
HCCCCCCCHHHCCCH
13.5529978859
86PhosphorylationSRPAATSTRLFTDPL
CCCCCCCHHHCCCHH
27.3423312004
148PhosphorylationASSGTLASAEDQAAS
CCCCCCCCHHHHHHH
34.99-
182PhosphorylationLGLGGPASPPVPPAL
CCCCCCCCCCCCCCC
32.6324275569
226UbiquitinationYRKYFYGKEHQNFFG
HHHHHCCCCCCCCCC
40.4129967540
260PhosphorylationSGGGTLHSYRVIVRT
CCCCCCEEEEEEEEE
20.1128857561
267PhosphorylationSYRVIVRTTQLRTLR
EEEEEEEECCCEECC
14.1729496963
268PhosphorylationYRVIVRTTQLRTLRG
EEEEEEECCCEECCC
18.2929496963
294UbiquitinationPRGLSPRKLLEHVAP
CCCCCHHHHHHHHHH
61.89-
304PhosphorylationEHVAPQLSPSCLRLG
HHHHHHCCHHHHHCC
14.9824732914
306PhosphorylationVAPQLSPSCLRLGSA
HHHHCCHHHHHCCCC
23.5424732914
312PhosphorylationPSCLRLGSASPKVPR
HHHHHCCCCCCCCCC
30.1123186163
314PhosphorylationCLRLGSASPKVPRTL
HHHCCCCCCCCCCEE
27.2723403867
316UbiquitinationRLGSASPKVPRTLLT
HCCCCCCCCCCEEEE
63.4829967540
323PhosphorylationKVPRTLLTLDEQVLS
CCCCEEEEHHHHHHH
34.9618452278
330PhosphorylationTLDEQVLSFQRKVGI
EHHHHHHHHHHHHEE
22.0724719451
334UbiquitinationQVLSFQRKVGILYCR
HHHHHHHHHEEEEEE
33.75-
389PhosphorylationQLDTKTDSTGTHSLY
EEECCCCCCCCCCEE
33.69-
510UbiquitinationFRAFLLAKALNGEQA
HHHHHHHHHHCCCCH
54.07-
559PhosphorylationASRFGLPSLGGRRRA
HHHHCCCCCCCCCCC
44.6930576142
580PhosphorylationAELQAAGSLVWGVRA
HHHHCCCCEEEEEEE
18.2824732914
664PhosphorylationITLRFDGSPGQAVGE
EEEEECCCCCCHHHH
27.9220068231
680PhosphorylationVARLQLVSRGCETRE
HHHHHHHHCCCCEEE
31.3920068231
685PhosphorylationLVSRGCETRELALPR
HHHCCCCEEEEECCC
33.2620068231
738PhosphorylationVCGQTLPSLRPEAAA
HCCCCCCCCCHHHHH
39.8724719451
770PhosphorylationESGRPRRSFSELYTL
CCCCCCCCHHHHEEE
34.1129888752
772PhosphorylationGRPRRSFSELYTLSL
CCCCCCHHHHEEEEC
28.1229888752
775PhosphorylationRRSFSELYTLSLQEP
CCCHHHHEEEECCCC
11.1129888752
776PhosphorylationRSFSELYTLSLQEPS
CCHHHHEEEECCCCC
23.6129888752
778PhosphorylationFSELYTLSLQEPSRR
HHHHEEEECCCCCCC
21.8729888752
805UbiquitinationVTLLPTTKQLLHLCL
EEEECCHHHHHHHHH
41.2329967540
817PhosphorylationLCLQDGGSPPGPGDL
HHHHCCCCCCCCCCH
33.1923401153
829PhosphorylationGDLAEERTEFLHSQN
CCHHHHHHHHHHHCC
34.0823927012
834PhosphorylationERTEFLHSQNSLSPR
HHHHHHHHCCCCCCC
32.9530266825
837PhosphorylationEFLHSQNSLSPRSSL
HHHHHCCCCCCCCCC
23.6923927012
839PhosphorylationLHSQNSLSPRSSLSD
HHHCCCCCCCCCCCC
20.3525159151
842PhosphorylationQNSLSPRSSLSDEAP
CCCCCCCCCCCCCCC
38.7326657352
843PhosphorylationNSLSPRSSLSDEAPV
CCCCCCCCCCCCCCC
32.9226657352
845PhosphorylationLSPRSSLSDEAPVLP
CCCCCCCCCCCCCCC
35.0430108239
854PhosphorylationEAPVLPNTTPDLLLA
CCCCCCCCCCCEEEE
37.4526074081
862PhosphorylationTPDLLLATTAKPSVP
CCCEEEECCCCCCCC
27.5326074081
863PhosphorylationPDLLLATTAKPSVPS
CCEEEECCCCCCCCC
27.3826074081
867PhosphorylationLATTAKPSVPSADSE
EECCCCCCCCCCCCC
46.0520873877
870PhosphorylationTAKPSVPSADSETPL
CCCCCCCCCCCCCCC
42.4223898821
873PhosphorylationPSVPSADSETPLTQD
CCCCCCCCCCCCCCC
42.9823401153
875PhosphorylationVPSADSETPLTQDRP
CCCCCCCCCCCCCCC
27.7930266825
878PhosphorylationADSETPLTQDRPGSP
CCCCCCCCCCCCCCC
29.6323401153
884PhosphorylationLTQDRPGSPSGSEDK
CCCCCCCCCCCCCCC
20.6929255136
886PhosphorylationQDRPGSPSGSEDKGN
CCCCCCCCCCCCCCC
57.5630266825
888PhosphorylationRPGSPSGSEDKGNPA
CCCCCCCCCCCCCCC
47.1330266825
901PhosphorylationPAPELRASFLPRTLS
CCHHHHHHHCHHHHH
22.3823312004
906PhosphorylationRASFLPRTLSLRNSI
HHHHCHHHHHHHHHH
20.8223403867
908PhosphorylationSFLPRTLSLRNSISR
HHCHHHHHHHHHHHH
25.3522617229
912PhosphorylationRTLSLRNSISRIMSE
HHHHHHHHHHHHHHH
18.5923401153
914PhosphorylationLSLRNSISRIMSEAG
HHHHHHHHHHHHHHC
18.6423403867
956PhosphorylationEGQPIPESGDPKGTP
CCCCCCCCCCCCCCC
43.0430108239
962PhosphorylationESGDPKGTPKSDAEP
CCCCCCCCCCCCCCC
33.4021712546
965PhosphorylationDPKGTPKSDAEPEPG
CCCCCCCCCCCCCCC
43.1721712546
1008PhosphorylationALEEEVRSLRHNNRR
HHHHHHHHHHHHCHH
34.6227251275
1022PhosphorylationRLQAESESAATRLLL
HHHHHCHHHHHHHHH
32.2726074081
1025PhosphorylationAESESAATRLLLASK
HHCHHHHHHHHHHHH
22.9026074081
1031PhosphorylationATRLLLASKQLGSPT
HHHHHHHHHHHCCCC
22.3926074081
1032UbiquitinationTRLLLASKQLGSPTA
HHHHHHHHHHCCCCC
43.8929967540
1036PhosphorylationLASKQLGSPTADLA-
HHHHHHCCCCCCCC-
27.8930266825
1038PhosphorylationSKQLGSPTADLA---
HHHHCCCCCCCC---
34.2030266825

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
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:21502543

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIPA1_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 SIPA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRD4_HUMANBRD4physical
15456879

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 SIPA1_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 SER-67, AND MASSSPECTROMETRY.
"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-53; SER-55; THR-64;SER-67 AND SER-839, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839, AND MASSSPECTROMETRY.
"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-74, AND MASSSPECTROMETRY.

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