SHAN2_MOUSE - dbPTM
SHAN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHAN2_MOUSE
UniProt AC Q80Z38
Protein Name SH3 and multiple ankyrin repeat domains protein 2
Gene Name Shank2
Organism Mus musculus (Mouse).
Sequence Length 1476
Subcellular Localization Apical cell membrane. Cytoplasm . Cell junction, synapse . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell projection, dendritic spine . Cell projection, growth cone. Colocalizes with cortactin in growth cones in diffe
Protein Description Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction (By similarity)..
Protein Sequence MKSLLNAFTKKEVPFREAPAYSNRRRRPPNTLAAPRVLLRSNSDNNLNAGAPEWAVCSAATSHRSLSPQLLQQTPSKPDGATKSLGSYTPGPRSRSPSLNRLGGTAEDGKRTQPHWHVGSPFTPGANKDSLSTFEYPGPRRKLYSAVPGRLFVAVKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQCKPRDSQAETRADRSKKLFRHYTVGSYDSFDAASDCIIEDKTVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLILKVVTVTRNLDPDDTARKKAPPPPKRAPTTALTLRSKSMTAELEELGLSLVDKASVRKKKDKPEEIVPASKPSRTAENVAIESRVATIKQRPTSRCFPAASDVNSVYERQGIAVMTPTVPGSPKGPFLGLPRGTMRRQKSIDSRIFLSGITEEERQFLAPPMLKFTRSLSMPDTSEDIPPPPQSVPPSPPPPSPTTYNCPRSPTPRVYGTIKPAFNQNPVVAKVPPATRSDTVATMMREKGMFYRRELDRFSLDSEDVYSRSPAPQAAFRTKRGQMPENPYSEVGKIASKAVYVPAKPARRKGVLVKQSNVEDSPEKTCSIPIPTIIVKEPSTSSSGKSSQGSSMEIDPQATEPGQLRPDDSLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRMQASKFPEEGGFGDEDETEQPLLPTPGAAPRELENHFLGGGEAGAQGEAGGPLSSTSKAKGPESGPAAPLKSSSPAGPENYVHPLTGRLLDPSSPLALALSARDRAMQESQQGHKGEAPKADLNKPLYIDTKMRPSVESGFPPVTRQNTRGPLRRQETENKYETDLGKDRRADDKKNMLINIVDTAQQKSAGLLMVHTVDVPMAGPPLEEEEDREDGDTKPDHSPSTVPEGVPKTEGALQISAAPEPAVAPGRTIVAAGSVEEAVILPFRIPPPPLASVDLDEDFLFTEPLPPPLEFANSFDIPDDRAASVPALADLVKQKKNDTSQPPTLNSSQPANSTDSKKPAGISNCLPSSFLPPPESFDAVTDSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGESMDTCTVYADGQAFVVDKPPVPPKPKMKPIVHKSNALYQDTLPEEDTDGFVIPPPAPPPPPGSAQAGVAKVIQPRTSKLWGDVPEVKSPILSGPKANVISELNSILQQMNRGKSVKPGEGLELPVGAKSANLAPRSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGPRRAPSPVVSPTELSKEILPTPPPPSATAASPSPTLSDVFSLPSQSPAGDLFGLNPAGRSRSPSPSILQQPISNKPFTTKPVHLWTKPDVADWLESLNLGEHKETFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR
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
15PhosphorylationFTKKEVPFREAPAYS
HHCCCCCCCCCCCCC
15.47-
15 (in isoform 3)Phosphorylation-15.4722807455
17 (in isoform 3)Phosphorylation-60.4221183079
26 (in isoform 3)Phosphorylation-52.8227841257
41PhosphorylationAPRVLLRSNSDNNLN
CCEEEECCCCCCCCC
40.4325521595
43PhosphorylationRVLLRSNSDNNLNAG
EEEECCCCCCCCCCC
42.8526643407
65PhosphorylationSAATSHRSLSPQLLQ
HHHCCCCCCCHHHHH
27.9826643407
67PhosphorylationATSHRSLSPQLLQQT
HCCCCCCCHHHHHCC
16.3126239621
88PhosphorylationATKSLGSYTPGPRSR
CCCCCCCCCCCCCCC
18.3723984901
89PhosphorylationTKSLGSYTPGPRSRS
CCCCCCCCCCCCCCC
24.3823984901
94PhosphorylationSYTPGPRSRSPSLNR
CCCCCCCCCCCCCCC
40.0029514104
96PhosphorylationTPGPRSRSPSLNRLG
CCCCCCCCCCCCCCC
21.7829899451
144PhosphorylationPGPRRKLYSAVPGRL
CCCCHHHEEECCCCE
9.53-
160PhosphorylationVAVKPYQPQVDGEIP
EEECCCCCCCCCCCC
30.25-
160 (in isoform 3)Phosphorylation-30.2522807455
162PhosphorylationVKPYQPQVDGEIPLH
ECCCCCCCCCCCCCC
15.07-
162 (in isoform 3)Phosphorylation-15.0725521595
164 (in isoform 3)Phosphorylation-35.5622324799
175 (in isoform 3)Phosphorylation-38.0529899451
227PhosphorylationSKKLFRHYTVGSYDS
HHHHHHHCCCCCCCC
10.0029899451
228PhosphorylationKKLFRHYTVGSYDSF
HHHHHHCCCCCCCCC
16.5629899451
231PhosphorylationFRHYTVGSYDSFDAA
HHHCCCCCCCCCCCH
22.7929899451
232PhosphorylationRHYTVGSYDSFDAAS
HHCCCCCCCCCCCHH
15.0729899451
234PhosphorylationYTVGSYDSFDAASDC
CCCCCCCCCCCHHCE
19.4519060867
363PhosphorylationPPPKRAPTTALTLRS
CCCCCCCCCEEHHCC
24.5820415495
367PhosphorylationRAPTTALTLRSKSMT
CCCCCEEHHCCCCCC
20.0520415495
370PhosphorylationTTALTLRSKSMTAEL
CCEEHHCCCCCCHHH
31.9919060867
370 (in isoform 2)Phosphorylation-31.9922807455
372PhosphorylationALTLRSKSMTAELEE
EEHHCCCCCCHHHHH
23.7019060867
372 (in isoform 2)Phosphorylation-23.7025521595
374PhosphorylationTLRSKSMTAELEELG
HHCCCCCCHHHHHHC
24.8719060867
374 (in isoform 2)Phosphorylation-24.8722324799
385 (in isoform 2)Phosphorylation-6.7929899451
404O-linked_GlycosylationPEEIVPASKPSRTAE
CHHHCCCCCCCCCHH
38.7430059200
427O-linked_GlycosylationATIKQRPTSRCFPAA
EECCCCCCCCCCCCH
30.8730059200
450PhosphorylationRQGIAVMTPTVPGSP
HCCEEEECCCCCCCC
14.8128066266
452PhosphorylationGIAVMTPTVPGSPKG
CEEEECCCCCCCCCC
30.1126643407
456PhosphorylationMTPTVPGSPKGPFLG
ECCCCCCCCCCCCCC
19.8525521595
474PhosphorylationGTMRRQKSIDSRIFL
CCCCCCCCCCHHHHH
24.2422324799
477PhosphorylationRRQKSIDSRIFLSGI
CCCCCCCHHHHHCCC
26.1322324799
482PhosphorylationIDSRIFLSGITEEER
CCHHHHHCCCCHHHH
19.8722324799
485O-linked_GlycosylationRIFLSGITEEERQFL
HHHHCCCCHHHHHHH
40.65145269
485PhosphorylationRIFLSGITEEERQFL
HHHHCCCCHHHHHHH
40.6522324799
502PhosphorylationPMLKFTRSLSMPDTS
CCHHHHCCCCCCCCC
23.0319060867
509PhosphorylationSLSMPDTSEDIPPPP
CCCCCCCCCCCCCCC
40.4224759943
518PhosphorylationDIPPPPQSVPPSPPP
CCCCCCCCCCCCCCC
42.2221183079
522PhosphorylationPPQSVPPSPPPPSPT
CCCCCCCCCCCCCCC
43.9222807455
529PhosphorylationSPPPPSPTTYNCPRS
CCCCCCCCCCCCCCC
46.3728576409
542PhosphorylationRSPTPRVYGTIKPAF
CCCCCCCCCEECCHH
15.1629899451
562O-linked_GlycosylationVAKVPPATRSDTVAT
EEECCCCCCCHHHHH
36.1630059200
566PhosphorylationPPATRSDTVATMMRE
CCCCCCHHHHHHHHH
17.1825521595
586PhosphorylationRRELDRFSLDSEDVY
EHHCCCCCCCCHHCC
31.9625521595
589PhosphorylationLDRFSLDSEDVYSRS
CCCCCCCCHHCCCCC
40.7826239621
593PhosphorylationSLDSEDVYSRSPAPQ
CCCCHHCCCCCCCCH
15.6424925903
594PhosphorylationLDSEDVYSRSPAPQA
CCCHHCCCCCCCCHH
26.5724925903
615PhosphorylationGQMPENPYSEVGKIA
CCCCCCCHHHHHHHC
29.1029899451
616PhosphorylationQMPENPYSEVGKIAS
CCCCCCHHHHHHHCC
27.3626643407
643PhosphorylationKGVLVKQSNVEDSPE
CCEEEECCCCCCCCC
36.8120415495
648PhosphorylationKQSNVEDSPEKTCSI
ECCCCCCCCCCCCCC
22.8125521595
652PhosphorylationVEDSPEKTCSIPIPT
CCCCCCCCCCCCCCE
15.1520415495
654PhosphorylationDSPEKTCSIPIPTII
CCCCCCCCCCCCEEE
36.3120415495
659PhosphorylationTCSIPIPTIIVKEPS
CCCCCCCEEEEECCC
24.8520415495
668PhosphorylationIVKEPSTSSSGKSSQ
EEECCCCCCCCCCCC
27.1829899451
673PhosphorylationSTSSSGKSSQGSSME
CCCCCCCCCCCCCCE
31.2729899451
674PhosphorylationTSSSGKSSQGSSMEI
CCCCCCCCCCCCCEE
41.8929899451
678PhosphorylationGKSSQGSSMEIDPQA
CCCCCCCCCEECCCC
27.5329899451
724PhosphorylationRLEARRNSPAFLSTD
HHHHHHCCCCCCCCC
18.7824925903
729PhosphorylationRNSPAFLSTDLGDED
HCCCCCCCCCCCCCC
17.2725521595
730PhosphorylationNSPAFLSTDLGDEDV
CCCCCCCCCCCCCCC
37.0725521595
817PhosphorylationGPAAPLKSSSPAGPE
CCCCCCCCCCCCCCC
43.6726643407
818PhosphorylationPAAPLKSSSPAGPEN
CCCCCCCCCCCCCCC
38.4626643407
819PhosphorylationAAPLKSSSPAGPENY
CCCCCCCCCCCCCCC
26.3426643407
838PhosphorylationTGRLLDPSSPLALAL
CCCCCCCCCHHHHHH
44.23-
839PhosphorylationGRLLDPSSPLALALS
CCCCCCCCHHHHHHH
29.35-
881PhosphorylationIDTKMRPSVESGFPP
EECCCCCCHHHCCCC
28.3121189417
884PhosphorylationKMRPSVESGFPPVTR
CCCCCHHHCCCCCCC
43.5124759943
890O-linked_GlycosylationESGFPPVTRQNTRGP
HHCCCCCCCCCCCCC
32.1055413759
890PhosphorylationESGFPPVTRQNTRGP
HHCCCCCCCCCCCCC
32.10-
894PhosphorylationPPVTRQNTRGPLRRQ
CCCCCCCCCCCCCHH
28.76-
903PhosphorylationGPLRRQETENKYETD
CCCCHHHHCCHHCCC
36.2025521595
907PhosphorylationRQETENKYETDLGKD
HHHHCCHHCCCCCCC
35.3325521595
980O-linked_GlycosylationVPEGVPKTEGALQIS
CCCCCCCCCCCEEEE
33.3130059200
999PhosphorylationPAVAPGRTIVAAGSV
CCCCCCCEEEECCCC
26.22-
1005PhosphorylationRTIVAAGSVEEAVIL
CEEEECCCCEEEEEE
22.9418056256
1055PhosphorylationIPDDRAASVPALADL
CCCCHHHHHHHHHHH
27.8729899451
1107PhosphorylationSFLPPPESFDAVTDS
HHCCCCHHHCCCCCC
33.9129899451
1112PhosphorylationPESFDAVTDSGIEEV
CHHHCCCCCCCCCCC
26.6029899451
1191PhosphorylationSNALYQDTLPEEDTD
CCCCCCCCCCCCCCC
28.7824759943
1226PhosphorylationAKVIQPRTSKLWGDV
EEHHCCCCHHHCCCC
36.5821082442
1227PhosphorylationKVIQPRTSKLWGDVP
EHHCCCCHHHCCCCC
27.3422807455
1238PhosphorylationGDVPEVKSPILSGPK
CCCCCCCCCHHCCCC
23.5029899451
1242PhosphorylationEVKSPILSGPKANVI
CCCCCHHCCCCHHHH
54.4923984901
1264PhosphorylationQQMNRGKSVKPGEGL
HHHHCCCCCCCCCCC
37.8925521595
1286PhosphorylationSANLAPRSPEVMSTV
CCCCCCCCHHHHHEE
25.0928066266
1291O-linked_GlycosylationPRSPEVMSTVSGTRS
CCCHHHHHEECCCCE
30.728522215
1291PhosphorylationPRSPEVMSTVSGTRS
CCCHHHHHEECCCCE
30.72-
1292O-linked_GlycosylationRSPEVMSTVSGTRST
CCHHHHHEECCCCEE
10.7030059200
1292PhosphorylationRSPEVMSTVSGTRST
CCHHHHHEECCCCEE
10.70-
1294O-linked_GlycosylationPEVMSTVSGTRSTTV
HHHHHEECCCCEEEE
34.248522223
1294PhosphorylationPEVMSTVSGTRSTTV
HHHHHEECCCCEEEE
34.24-
1296O-linked_GlycosylationVMSTVSGTRSTTVTF
HHHEECCCCEEEEEE
17.598522207
1296PhosphorylationVMSTVSGTRSTTVTF
HHHEECCCCEEEEEE
17.59-
1302O-linked_GlycosylationGTRSTTVTFTVRPGT
CCCEEEEEEEECCCC
16.1130059200
1334PhosphorylationSGPRRAPSPVVSPTE
CCCCCCCCCCCCHHH
29.3725521595
1338PhosphorylationRAPSPVVSPTELSKE
CCCCCCCCHHHHHHC
26.7425521595
1340PhosphorylationPSPVVSPTELSKEIL
CCCCCCHHHHHHCCC
41.8925521595
1343PhosphorylationVVSPTELSKEILPTP
CCCHHHHHHCCCCCC
23.2424925903
1359PhosphorylationPPSATAASPSPTLSD
CCCCCCCCCCCCHHH
24.3629899451
1361PhosphorylationSATAASPSPTLSDVF
CCCCCCCCCCHHHHH
28.2029899451
1365PhosphorylationASPSPTLSDVFSLPS
CCCCCCHHHHHCCCC
33.9229899451
1388PhosphorylationGLNPAGRSRSPSPSI
CCCCCCCCCCCCCCH
35.8721743459
1390PhosphorylationNPAGRSRSPSPSILQ
CCCCCCCCCCCCHHC
30.8621743459
1392PhosphorylationAGRSRSPSPSILQQP
CCCCCCCCCCHHCCC
32.3121743459
1394PhosphorylationRSRSPSPSILQQPIS
CCCCCCCCHHCCCCC
40.0221743459
1401PhosphorylationSILQQPISNKPFTTK
CHHCCCCCCCCCCCC
45.5520469934
1468MethylationGHRMNIERALKQLLD
HHHHCHHHHHHHHHC
41.2318959257

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 SHAN2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHAN2_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 SHAN2_MOUSE !!

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

Oops, there are no PPI records of SHAN2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHAN2_MOUSE

loading...

Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"O-linked N-acetylglucosamine proteomics of postsynaptic densitypreparations using lectin weak affinity chromatography and massspectrometry.";
Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,Maltby D.A., Schoepfer R., Burlingame A.L.;
Mol. Cell. Proteomics 5:923-934(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1292, AND MASSSPECTROMETRY.
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-1334 AND SER-1338, 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 SER-586; THR-730; THR-903AND SER-1338, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1340, AND MASSSPECTROMETRY.

TOP