STON2_HUMAN - dbPTM
STON2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STON2_HUMAN
UniProt AC Q8WXE9
Protein Name Stonin-2
Gene Name STON2
Organism Homo sapiens (Human).
Sequence Length 905
Subcellular Localization Cytoplasm . Membrane . Cell junction, synapse, synaptosome. Some fraction is membrane-associated.
Protein Description Adapter protein involved in endocytic machinery. Involved in the synaptic vesicle recycling. May facilitate clathrin-coated vesicle uncoating..
Protein Sequence MTTLDHVIATHQSEWVSFNEEPPFPAHSQGGTEEHLPGLSSSPDQSESSSGENHVVDGGSQDHSHSEQDDSSEKMGLISEAASPPGSPEQPPPDLASAISNWVQFEDDTPWASTSPPHQETAETALPLTMPCWTCPSFDSLGRCPLTSESSWTTHSEDTSSPSFGCSYTDLQLINAEEQTSGQASGADSTDNSSSLQEDEEVEMEAISWQASSPAMNGHPAPPVTSARFPSWVTFDDNEVSCPLPPVTSPLKPNTPPSASVIPDVPYNSMGSFKKRDRPKSTLMNFSKVQKLDISSLNRTPSVTEASPWRATNPFLNETLQDVQPSPINPFSAFFEEQERRSQNSSISSTTGKSQRDSLIVIYQDAISFDDSSKTQSHSDAVEKLKQLQIDDPDHFGSATLPDDDPVAWIELDAHPPGSARSQPRDGWPMMLRIPEKKNIMSSRHWGPIFVKLTDTGYLQLYYEQGLEKPFREFKLEICHEISEPRLQNYDENGRIHSLRIDRVTYKEKKKYQPKPAVAHTAEREQVIKLGTTNYDDFLSFIHAVQDRLMDLPVLSMDLSTVGLNYLEEEITVDVRDEFSGIVSKGDNQILQHHVLTRIHILSFLSGLAECRLGLNDILVKGNEIVLRQDIMPTTTTKWIKLHECRFHGCVDEDVFHNSRVILFNPLDACRFELMRFRTVFAEKTLPFTLRTATSVNGAEVEVQSWLRMSTGFSANRDPLTQVPCENVMIRYPVPSEWVKNFRRESVLGEKSLKAKVNRGASFGSTSVSGSEPVMRVTLGTAKYEHAFNSIVWRINRLPDKNSASGHPHCFFCHLELGSDREVPSRFANHVNVEFSMPTTSASKASVRSISVEDKTDVRKWVNYSAHYSYQVALGSIWLMLPTPFVHPTTLPLLFLLAMLTMFAW
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
168PhosphorylationSPSFGCSYTDLQLIN
CCCCCCCHHEEEEEC		14.3522817900
231PhosphorylationVTSARFPSWVTFDDN
CCCCCCCCCEEECCC		31.31-
234PhosphorylationARFPSWVTFDDNEVS
CCCCCCEEECCCEEC		18.32-
241PhosphorylationTFDDNEVSCPLPPVT
EECCCEECCCCCCCC		12.1127251275
248PhosphorylationSCPLPPVTSPLKPNT
CCCCCCCCCCCCCCC		30.3327251275
249PhosphorylationCPLPPVTSPLKPNTP
CCCCCCCCCCCCCCC		28.5924719451
255PhosphorylationTSPLKPNTPPSASVI
CCCCCCCCCCCCCCC		45.1427251275
267PhosphorylationSVIPDVPYNSMGSFK
CCCCCCCCCCCCCCC		21.5125627689
269PhosphorylationIPDVPYNSMGSFKKR
CCCCCCCCCCCCCCC		20.7625627689
272PhosphorylationVPYNSMGSFKKRDRP
CCCCCCCCCCCCCCC		25.8325159151
281PhosphorylationKKRDRPKSTLMNFSK
CCCCCCCCCCCCHHH		29.4730266825
282PhosphorylationKRDRPKSTLMNFSKV
CCCCCCCCCCCHHHC		35.8330266825
287PhosphorylationKSTLMNFSKVQKLDI
CCCCCCHHHCEECCH		27.2330266825
295PhosphorylationKVQKLDISSLNRTPS
HCEECCHHHCCCCCC		28.5630266825
296PhosphorylationVQKLDISSLNRTPSV
CEECCHHHCCCCCCC		29.9625849741
300PhosphorylationDISSLNRTPSVTEAS
CHHHCCCCCCCCCCC		20.8825159151
302PhosphorylationSSLNRTPSVTEASPW
HHCCCCCCCCCCCCC		40.8525159151
304PhosphorylationLNRTPSVTEASPWRA
CCCCCCCCCCCCCCC		30.1223186163
307PhosphorylationTPSVTEASPWRATNP
CCCCCCCCCCCCCCC		20.8225159151
319PhosphorylationTNPFLNETLQDVQPS
CCCCCCCCCCCCCCC		28.7527251275
326PhosphorylationTLQDVQPSPINPFSA
CCCCCCCCCCCCCHH		22.7125159151
342PhosphorylationFEEQERRSQNSSISS
HHHHHHHHCCCCCCC		39.6825627689
345PhosphorylationQERRSQNSSISSTTG
HHHHHCCCCCCCCCC		22.7825262027
346PhosphorylationERRSQNSSISSTTGK
HHHHCCCCCCCCCCC		33.7625262027
348PhosphorylationRSQNSSISSTTGKSQ
HHCCCCCCCCCCCCH		24.4725262027
349PhosphorylationSQNSSISSTTGKSQR
HCCCCCCCCCCCCHH		28.4625262027
350PhosphorylationQNSSISSTTGKSQRD
CCCCCCCCCCCCHHC		32.5525262027
351PhosphorylationNSSISSTTGKSQRDS
CCCCCCCCCCCHHCE		44.5625262027
353UbiquitinationSISSTTGKSQRDSLI
CCCCCCCCCHHCEEE		41.12-
354PhosphorylationISSTTGKSQRDSLIV
CCCCCCCCHHCEEEE		31.6228857561
358PhosphorylationTGKSQRDSLIVIYQD
CCCCHHCEEEEEEEE		23.3728857561
363PhosphorylationRDSLIVIYQDAISFD
HCEEEEEEEEECCCC		6.8828060719
368PhosphorylationVIYQDAISFDDSSKT
EEEEEECCCCCCCCC		25.0928060719
384UbiquitinationSHSDAVEKLKQLQID
CCHHHHHHHHHCCCC		55.152190698
384 (in isoform 1)Ubiquitination-55.1521906983
386UbiquitinationSDAVEKLKQLQIDDP
HHHHHHHHHCCCCCC		61.09-
437AcetylationMMLRIPEKKNIMSSR
EEEECCCCCCCCCCC		45.8518604539
498PhosphorylationDENGRIHSLRIDRVT
CCCCCEEEEEEEEEE		19.5724719451
512PhosphorylationTYKEKKKYQPKPAVA
EHHCCCCCCCCCCCC		38.6422210691
515UbiquitinationEKKKYQPKPAVAHTA
CCCCCCCCCCCCCHH		30.04-
580PhosphorylationVDVRDEFSGIVSKGD
EEEHHHHCCEEECCC		26.0922617229
621UbiquitinationGLNDILVKGNEIVLR
CCCCEEEECCEEEEC		53.20-
638UbiquitinationIMPTTTTKWIKLHEC
CCCCCCCCEEEEEEC		44.84-
684UbiquitinationFRTVFAEKTLPFTLR
HHHEECCCCCCEEEE		52.51-
684AcetylationFRTVFAEKTLPFTLR
HHHEECCCCCCEEEE		52.5126051181
689PhosphorylationAEKTLPFTLRTATSV
CCCCCCEEEEECCCC		17.2524719451
746PhosphorylationVKNFRRESVLGEKSL
HHHCHHHHHCCCHHH		22.3423312004
751UbiquitinationRESVLGEKSLKAKVN
HHHHCCCHHHHHHCC		60.33-
762PhosphorylationAKVNRGASFGSTSVS
HHCCCCCCCCCCCCC		32.7225159151
765PhosphorylationNRGASFGSTSVSGSE
CCCCCCCCCCCCCCC		18.5928857561
766PhosphorylationRGASFGSTSVSGSEP
CCCCCCCCCCCCCCC		33.2628857561
767PhosphorylationGASFGSTSVSGSEPV
CCCCCCCCCCCCCCE		18.9128857561
769PhosphorylationSFGSTSVSGSEPVMR
CCCCCCCCCCCCEEE		36.0526434776
771PhosphorylationGSTSVSGSEPVMRVT
CCCCCCCCCCEEEEE		31.0826434776
856PhosphorylationSISVEDKTDVRKWVN
EEECCCCCCHHHHHH		52.64-
914 (in isoform 3)Phosphorylation-27251275
915 (in isoform 3)Phosphorylation-27251275
918 (in isoform 3)Phosphorylation-27251275
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 STON2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STON2_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 STON2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP15R_HUMANEPS15L1physical
11381094
EPS15_HUMANEPS15physical
11381094
ITSN1_HUMANITSN1physical
11381094
SYT2_HUMANSYT2physical
11381094
SYT1_HUMANSYT1physical
11381094
SYT1_HUMANSYT1physical
11454741
AP2M1_HUMANAP2M1physical
11454741
CSN4_HUMANCOPS4physical
21102408
EPS15_HUMANEPS15physical
18200045
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 STON2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-300 AND SER-302, ANDMASS SPECTROMETRY.

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