SHAN2_RAT - dbPTM
SHAN2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHAN2_RAT
UniProt AC Q9QX74
Protein Name SH3 and multiple ankyrin repeat domains protein 2
Gene Name Shank2
Organism Rattus norvegicus (Rat).
Sequence Length 1474
Subcellular Localization Apical cell membrane . Cytoplasm . Cell junction, synapse . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell projection, growth cone . Cell projection, dendritic spine. Colocalizes with cortactin in growth cones in diff
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..
Protein Sequence MKSLLNAFTKKEVPFREAPAYSNRRRRPPNTLAAPRVLLRSNSDNNLNAGAPEWAVCSAATSHRSLSPQLLQQTPSKPDGATKSLGSYAPGPRSRSPSLNRLGGAGEDGKRPQPPHWHVGSPFTPGANKDSLSTFEYPGPRRKLYSAVPGRLFVAIKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQCKPRDSQAETRADRSKKLFRHYTVGSYDSFDAASDCIIEDKTVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLVLKVVTVTRNLDPDDTARKKAPPPPKRAPTTALTLRSKSMTAELEELGLSLVDKASVRKKKDKPEEIVPASKPSRTAENVAIESRVATIKQRPTSRCFPAASDVNSVYERQGIAVMTPTVPGSPKGPFLGLPRGTMRRQKSIDSRIFLSGITEEERQFLAPPMLKFTRSLSMPDTSEDIPPPPQSVPPSPPPPSPTTYNCPRSPTPRVYGTIKPAFNQNPVAKVPPATRSDTVATMMREKGMFYRRELDRFSLDSEDVYSRSPAPQAAFRTKRGQMPENPYSEVGKIASKAVYVPAKPARRKGMLVKQSNVEDSPEKTCSIPIPTIIVKEPSTSSSGKSSQGSSMEIDPQATEPGQLRPDDSLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRMQPSKFPEEGGFGDEDETEQPLLPTPGAAPRELENHFLGGGEAGAQGEAGGPLSSTSKAKGPESGPAAALKSSSPASPENYVHPLTGRLLDPSSPLALALSARDRAMQESQQGHKGEAPKADLNKPLYIDTKMRPSVESGFPPVTRQNTRGPLRRQETENKYETDLSKDRRADDKKNMLINIVDTAQQKSAGLLMVHTVDIPVAGPPLEEEEDREDGDTKPDHSPSTVPEGVPKTEGALQISAAPEPAAAPGRTIVAAGSVEEAVILPFRIPPPPLASVDLDEDFLFTEPLPPPLEFANSFDIPDDRAASVPALADLVKQKKSDTPQPPSLNSSQPANSTDSKKPAGISNCLPSSFLPPPESFDAVTDSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGESMDTCTVYADGQAFVVDKPPVPPKPKMKPIVHKSNALYQDTLPEEDTDGFVIPPPAPPPPPGSAQAGVAKVIQPRTSKLWGDVTEVKSPILSGPKANVISELNSILQQMNRGKSVKPGEGLELPVGAKSANLAPRSPEVMSTVSGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGPRRAPSPVVSPTELSKEILPTPPSAAAASPSPTLSDVFSLPSQSPAGDLFGLNPAGRSRSPSPSILQQPISNKPFTTKPVHLWTKPDVADWLESLNLGEHKETFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR
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
26 (in isoform 4)Phosphorylation-52.8228432305
26 (in isoform 5)Phosphorylation-52.8228432305
26 (in isoform 6)Phosphorylation-52.8228432305
28PhosphorylationYSNRRRRPPNTLAAP
CCCCCCCCCCCCCCC		25.36-
28 (in isoform 4)Phosphorylation-25.36-
28 (in isoform 5)Phosphorylation-25.36-
28 (in isoform 6)Phosphorylation-25.36-
36 (in isoform 7)Phosphorylation-27.3030181290
41PhosphorylationAPRVLLRSNSDNNLN
CCEEEECCCCCCCCC		40.4327097102
43PhosphorylationRVLLRSNSDNNLNAG
EEEECCCCCCCCCCC		42.8527097102
61PhosphorylationWAVCSAATSHRSLSP
HHHHHHHCCCCCCCH		25.4528689409
65PhosphorylationSAATSHRSLSPQLLQ
HHHCCCCCCCHHHHH		27.9823984901
67PhosphorylationATSHRSLSPQLLQQT
HCCCCCCCHHHHHCC		16.3123984901
88PhosphorylationATKSLGSYAPGPRSR
CCCCCCCCCCCCCCC		18.28-
96PhosphorylationAPGPRSRSPSLNRLG
CCCCCCCCCCHHCCC		21.7829779826
98PhosphorylationGPRSRSPSLNRLGGA
CCCCCCCCHHCCCCC		39.25-
145PhosphorylationPGPRRKLYSAVPGRL
CCCCHHHEEECCCCE		9.53-
160 (in isoform 4)Phosphorylation-30.4028432305
160 (in isoform 5)Phosphorylation-30.4028432305
160 (in isoform 6)Phosphorylation-30.4028432305
162PhosphorylationAIKPYQPQVDGEIPL
EECCCCCCCCCCCCC		30.34-
162 (in isoform 4)Phosphorylation-30.3428432305
162 (in isoform 5)Phosphorylation-30.3428432305
162 (in isoform 6)Phosphorylation-30.3428432305
164 (in isoform 4)Phosphorylation-43.7028432305
164 (in isoform 5)Phosphorylation-43.7028432305
164 (in isoform 6)Phosphorylation-43.7028432305
227PhosphorylationRSKKLFRHYTVGSYD
HHHHHHHHCCCCCCC		18.45-
332UbiquitinationNMIRQGGNHLVLKVV
HHHEECCCEEEEEEE		31.95-
342UbiquitinationVLKVVTVTRNLDPDD
EEEEEEEECCCCCCC		12.41-
371PhosphorylationTTALTLRSKSMTAEL
CCEEHHCCCCCCHHH		31.9928432305
371 (in isoform 2)Phosphorylation-31.9928432305
371 (in isoform 3)Phosphorylation-31.9928432305
373PhosphorylationALTLRSKSMTAELEE
EEHHCCCCCCHHHHH		23.7028432305
373 (in isoform 2)Phosphorylation-23.7028432305
373 (in isoform 3)Phosphorylation-23.7028432305
375 (in isoform 2)Phosphorylation-24.8728432305
375 (in isoform 3)Phosphorylation-24.8728432305
378PhosphorylationSKSMTAELEELGLSL
CCCCCHHHHHHCCCH		6.01-
400PhosphorylationKKKDKPEEIVPASKP
CCCCCCHHHCCCCCC		58.79-
409UbiquitinationVPASKPSRTAENVAI
CCCCCCCCCHHHHEE		46.62-
442PhosphorylationASDVNSVYERQGIAV
HHHCCCHHHHCCEEE		12.76-
451PhosphorylationRQGIAVMTPTVPGSP
HCCEEEECCCCCCCC		14.8122108457
453PhosphorylationGIAVMTPTVPGSPKG
CEEEECCCCCCCCCC		30.1128432305
457PhosphorylationMTPTVPGSPKGPFLG
ECCCCCCCCCCCCCC		19.8522108457
475PhosphorylationGTMRRQKSIDSRIFL
CCCCCCCCCCHHHHH		24.2425403869
477 (in isoform 7)Phosphorylation-38.67-
483PhosphorylationIDSRIFLSGITEEER
CCHHHHHCCCCHHHH		19.8728432305
486PhosphorylationRIFLSGITEEERQFL
HHHHCCCCHHHHHHH		40.6528432305
543PhosphorylationRSPTPRVYGTIKPAF
CCCCCCCEEECCCCC		15.1622276854
547UbiquitinationPRVYGTIKPAFNQNP
CCCEEECCCCCCCCC		30.08-
557UbiquitinationFNQNPVAKVPPATRS
CCCCCCCCCCCCCCC		56.35-
566PhosphorylationPPATRSDTVATMMRE
CCCCCCHHHHHHHHH		17.1828432305
586PhosphorylationRRELDRFSLDSEDVY
EHHCCCCCCCCHHCC		31.9622108457
589PhosphorylationLDRFSLDSEDVYSRS
CCCCCCCCHHCCCCC		40.7828432305
593PhosphorylationSLDSEDVYSRSPAPQ
CCCCHHCCCCCCCCH		15.64-
615PhosphorylationGQMPENPYSEVGKIA
CCCCCCCHHHHHHHH		29.1028432305
616PhosphorylationQMPENPYSEVGKIAS
CCCCCCHHHHHHHHC		27.3628432305
624UbiquitinationEVGKIASKAVYVPAK
HHHHHHCEEEEECCC		32.61-
627PhosphorylationKIASKAVYVPAKPAR
HHHCEEEEECCCCCH		12.94-
648PhosphorylationKQSNVEDSPEKTCSI
ECCCCCCCCCCCCCC		22.8125403869
666PhosphorylationTIIVKEPSTSSSGKS
EEEEECCCCCCCCCC		41.8525403869
673PhosphorylationSTSSSGKSSQGSSME
CCCCCCCCCCCCCCE		31.2728432305
674PhosphorylationTSSSGKSSQGSSMEI
CCCCCCCCCCCCCEE		41.8928432305
677PhosphorylationSGKSSQGSSMEIDPQ
CCCCCCCCCCEECCC		20.9028432305
678PhosphorylationGKSSQGSSMEIDPQA
CCCCCCCCCEECCCC		27.5328432305
724PhosphorylationRLEARRNSPAFLSTD
HHHHHHCCCCCCCCC		18.7827097102
729PhosphorylationRNSPAFLSTDLGDED
HCCCCCCCCCCCCCC		17.2727097102
730PhosphorylationNSPAFLSTDLGDEDV
CCCCCCCCCCCCCCC		37.0727097102
750 (in isoform 7)Phosphorylation-72.1728432305
752 (in isoform 7)Phosphorylation-42.3328432305
754 (in isoform 7)Phosphorylation-65.9328432305
817PhosphorylationGPAAALKSSSPASPE
CCCHHHHCCCCCCHH		36.5828432305
818PhosphorylationPAAALKSSSPASPEN
CCHHHHCCCCCCHHH		38.4628432305
819PhosphorylationAAALKSSSPASPENY
CHHHHCCCCCCHHHC		31.4128432305
822PhosphorylationLKSSSPASPENYVHP
HHCCCCCCHHHCCCC		35.8128432305
826PhosphorylationSPASPENYVHPLTGR
CCCCHHHCCCCCCCC		9.8528432305
838PhosphorylationTGRLLDPSSPLALAL
CCCCCCCCCHHHHHH		44.2328432305
839PhosphorylationGRLLDPSSPLALALS
CCCCCCCCHHHHHHH		29.3528432305
873PhosphorylationADLNKPLYIDTKMRP
HCCCCCEEEECCCCC		12.79-
881PhosphorylationIDTKMRPSVESGFPP
EECCCCCCHHHCCCC		28.3128432305
884PhosphorylationKMRPSVESGFPPVTR
CCCCCHHHCCCCCCC		43.5128432305
890PhosphorylationESGFPPVTRQNTRGP
HHCCCCCCCCCCCCC		32.1028432305
903PhosphorylationGPLRRQETENKYETD
CCCCHHHHCCCCCCC		36.2028432305
907PhosphorylationRQETENKYETDLSKD
HHHHCCCCCCCCCCC		35.3328432305
909PhosphorylationETENKYETDLSKDRR
HHCCCCCCCCCCCCC		38.8728432305
912PhosphorylationNKYETDLSKDRRADD
CCCCCCCCCCCCCHH		35.0128432305
964PhosphorylationEDREDGDTKPDHSPS
CCCCCCCCCCCCCCC		50.4330181290
969PhosphorylationGDTKPDHSPSTVPEG
CCCCCCCCCCCCCCC		28.1130181290
971PhosphorylationTKPDHSPSTVPEGVP
CCCCCCCCCCCCCCC		45.0830181290
972PhosphorylationKPDHSPSTVPEGVPK
CCCCCCCCCCCCCCC		43.3930181290
999PhosphorylationPAAAPGRTIVAAGSV
CCCCCCCEEEECCCC		26.2228432305
1005PhosphorylationRTIVAAGSVEEAVIL
CEEEECCCCEEEEEE		22.9428432305
1055PhosphorylationIPDDRAASVPALADL
CCCCHHHHHHHHHHH		27.8728432305
1107PhosphorylationSFLPPPESFDAVTDS
HHCCCCHHHCCCCCC		33.9128432305
1234PhosphorylationSKLWGDVTEVKSPIL
CCCCCCCCCCCCCHH		39.5428432305
1238PhosphorylationGDVTEVKSPILSGPK
CCCCCCCCCHHCCCC		23.5028432305
1264PhosphorylationQQMNRGKSVKPGEGL
HHHHCCCCCCCCCCC		37.8928432305
1286PhosphorylationSANLAPRSPEVMSTV
CCCCCCCCHHHHHEE		25.0928432305
1292O-linked_GlycosylationRSPEVMSTVSGTRST
CCHHHHHEECCCCEE		10.70-
1334PhosphorylationSGPRRAPSPVVSPTE
CCCCCCCCCCCCHHH		29.3728689409
1338PhosphorylationRAPSPVVSPTELSKE
CCCCCCCCHHHHCHH		26.7428689409
1340PhosphorylationPSPVVSPTELSKEIL
CCCCCCHHHHCHHHC		41.8927097102
1343PhosphorylationVVSPTELSKEILPTP
CCCHHHHCHHHCCCC		23.2427097102
1386PhosphorylationGLNPAGRSRSPSPSI
CCCCCCCCCCCCCCH		35.8728432305
1388PhosphorylationNPAGRSRSPSPSILQ
CCCCCCCCCCCCHHC		30.8628432305
1390PhosphorylationAGRSRSPSPSILQQP
CCCCCCCCCCHHCCC		32.3128432305
1392PhosphorylationRSRSPSPSILQQPIS
CCCCCCCCHHCCCCC		40.0228432305
1399PhosphorylationSILQQPISNKPFTTK
CHHCCCCCCCCCCCC		45.5528432305
1404PhosphorylationPISNKPFTTKPVHLW
CCCCCCCCCCCEEEE		42.3028432305
1405PhosphorylationISNKPFTTKPVHLWT
CCCCCCCCCCEEEEC		33.4628432305
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
477SPhosphorylationKinaseSGK1O00141
PSP
477SPhosphorylationKinaseSGK1Q9WVC6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHAN2_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SHAN2_RAT !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHAN2_RAT

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Related Literatures of Post-Translational Modification

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