SDK2_HUMAN - dbPTM
SDK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDK2_HUMAN
UniProt AC Q58EX2
Protein Name Protein sidekick-2 {ECO:0000250|UniProtKB:Q6V4S5}
Gene Name SDK2 {ECO:0000250|UniProtKB:Q6V4S5, ECO:0000312|HGNC:HGNC:19308}
Organism Homo sapiens (Human).
Sequence Length 2172
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell junction, synapse .
Protein Description Adhesion molecule that promotes lamina-specific synaptic connections in the retina and is specifically required for the formation of neuronal circuits that detect motion. Acts by promoting formation of synapses between two specific retinal cell types: the retinal ganglion cells W3B-RGCs and the excitatory amacrine cells VG3-ACs. Formation of synapses between these two cells plays a key role in detection of motion. Promotes synaptic connectivity via homophilic interactions..
Protein Sequence MWGLLIWTLLALHQIRAARAQDDVSPYFKTEPVRTQVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTKFSLEYRYMITSLDRTHAGFYRCIVRNRMGALLQRQTEVQVAYMGSFEEGEKHQSVSHGEAAVIRAPRIASFPQPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQPITLTVENVGGPADPIAPTIIIPPKNTSVVAGTSEVTLECVANARPLIKLHIIWKKDGVLLSGGISDHNRRLTIPNPTGSDAGYYECEAVLRSSSVPSVVRGAYLSVLEPPQFVKEPERHITAEMEKVVDIPCQAKGVPPPSITWYKDAAVVEVEKLTRFRQRNDGGLQISGLVPDDTGMFQCFARNAAGEVQTSTYLAVTSIAPNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTPLESGSLLISPTHISDAGTYTCLATNSRGVDEASADLVVWARTRITKPPQDQSVIKGTQASMVCGVTHDPRVTIRYIWEKDGATLGTESHPRIRLDRNGSLHISQTWSGDIGTYTCRVISAGGNDSRSAHLRVRQLPHAPEHPVATLSTVERRAINLTWTKPFDGNSPLIRYILEMSENNAPWTVLLASVDPKATSVTVKGLVPARSYQFRLCAVNDVGKGQFSKDTERVSLPEEPPTAPPQNVIASGRTNQSIMIQWQPPPESHQNGILKGYIIRYCLAGLPVGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNSAGLGVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTWNAPSPQFINGINQGYKLIAWEPEQEEEVTMVTARPNFQDSIHVGFVSGLKKFTEYFTSVLCFTTPGDGPRSTPQLVRTHEDVPGPVGHLSFSEILDTSLKVSWQEPGEKNGILTGYRISWEEYNRTNTRVTHYLPNVTLEYRVTGLTALTTYTIEVAAMTSKGQGQVSASTISSGVPPELPGPPTNLGISNIGPRSVTLQFRPGYDGKTSISRWLVEAQVGVVGEGEEWLLIHQLSNEPDARSMEVPDLNPFTCYSFRMRQVNIVGTSPPSQPSRKIQTLQAPPDMAPANVSLRTASETSLWLRWMPLPEMEYNGNPESVGYKIKYSRSDGHGKTLSHVVQDRVERDYTIEDLEEWTEYRVQVQAFNAIGSGPWSQTVVGRTRESVPSSGPTNVSALATTSSSMLVRWSEVPEADRNGLVLGYKVMYKEKDSDTQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFTRIGDGSPSHPPILERTLDDVPGPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRLNTTTANTATVEVLAPSARQYTATGLKPESVYLFRITAQTRKGWGEAAEALVVTTEKRDRPQPPSRPMVQQEDVRARSVLLSWEPGSDGLSPVRYYTIQTRELPSGRWALHSASVSHNASSFIVDRLKPFTSYKFRVKATNDIGDSEFSEESESLTTLQAAPDEAPTILSVTPHTTTSVLIRWQPPAEDKINGILLGFRIRYRELLYEGLRGFTLRGINNPGATWAELTSMYSMRNLSRPSLTQYELDNLNKHRRYEIRMSVYNAVGEGPSSPPQEVFVGEAVPTAAPRNVVVHGATATQLDVTWEPPPLDSQNGDIQGYKIYFWEAQRGNLTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNAAGDGPRSTPTQGQTQQAAPSAPSSVKFSELTTTSVNVSWEAPQFPNGILEGYRLVYEPCSPVDGVSKIVTVDVKGNSPLWLKVKDLAEGVTYRFRIRAKTFTYGPEIEANVTTGPGEGAPGPPGVPIIVRYSSAIAIHWSSGDPGKGPITRYVIEARPSDEGLWDILIKDIPKEVSSYTFSMDILKPGVSYDFRVIAVNDYGFGTPSSPSQSVPAQKANPFYEEWWFLVVIALVGLIFILLLVFVLIIRGQSKKYAKKTDSGNSAKSGALGHSEMMSLDESSFPALELNNRRLSVKNSFCRKNGLYTRSPPRPSPGSLHYSDEDVTKYNDLIPAESSSLTEKPSEISDSQGSDSEYEVDSNHQKAHSFVNHYISDPTYYNSWRRQQKGISRAQAYSYTESDSGEPDHTTVTNSTSTQQGSLFRPKASRTPTPQNPPNPPSQQSTLYRPPSSLAPGSRAPIAGFSSFV
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
25PhosphorylationARAQDDVSPYFKTEP
HHCCCCCCCCCCCCC		22.3721815630
27PhosphorylationAQDDVSPYFKTEPVR
CCCCCCCCCCCCCCE		15.3623186163
193N-linked_GlycosylationVNDKNGDNKTSQPIT
EECCCCCCCCCCCEE		51.40UniProtKB CARBOHYD
259PhosphorylationKKDGVLLSGGISDHN
ECCCEEECCCCCCCC		30.7123403867
263PhosphorylationVLLSGGISDHNRRLT
EEECCCCCCCCCCEE		35.7723403867
290PhosphorylationECEAVLRSSSVPSVV
EEEEEHHCCCCCHHC		23.8622210691
295PhosphorylationLRSSSVPSVVRGAYL
HHCCCCCHHCCCEEE		30.9622210691
319PhosphorylationKEPERHITAEMEKVV
CCCCCCCEEEEEEEE		15.50-
537PhosphorylationIWEKDGATLGTESHP
EEECCCCCCCCCCCC		31.1124719451
542PhosphorylationGATLGTESHPRIRLD
CCCCCCCCCCEEEEC		38.3324719451
557PhosphorylationRNGSLHISQTWSGDI
CCCCEEEEEECCCCC		15.71-
609N-linked_GlycosylationTVERRAINLTWTKPF
HHEEECCCCEECCCC		30.36UniProtKB CARBOHYD
620PhosphorylationTKPFDGNSPLIRYIL
CCCCCCCCHHHHHHH		26.9824719451
743N-linked_GlycosylationPVGYQFKNITDADVN
CCCCCCCCCCHHHHH		43.62UniProtKB CARBOHYD
936N-linked_GlycosylationRISWEEYNRTNTRVT
EEEHHHHCCCCCEEE		47.80UniProtKB CARBOHYD
948N-linked_GlycosylationRVTHYLPNVTLEYRV
EEEEECCCCEEEEEE		36.49UniProtKB CARBOHYD
1024PhosphorylationYDGKTSISRWLVEAQ
CCCCCCHHHHEEEEE		19.71-
1079PhosphorylationRQVNIVGTSPPSQPS
EEEEEECCCCCCCCC		27.4523312004
1080PhosphorylationQVNIVGTSPPSQPSR
EEEEECCCCCCCCCC		28.9619845377
1083PhosphorylationIVGTSPPSQPSRKIQ
EECCCCCCCCCCCEE		59.0919845377
1086PhosphorylationTSPPSQPSRKIQTLQ
CCCCCCCCCCEEECC		38.2719845377
1091PhosphorylationQPSRKIQTLQAPPDM
CCCCCEEECCCCCCC		25.0623403867
1102N-linked_GlycosylationPPDMAPANVSLRTAS
CCCCCCCCCCCCCCC		23.89UniProtKB CARBOHYD
1107PhosphorylationPANVSLRTASETSLW
CCCCCCCCCCCCEEE		39.57-
1213PhosphorylationVSALATTSSSMLVRW
HHHEEECCCCCEEEH		18.9628787133
1214PhosphorylationSALATTSSSMLVRWS
HHEEECCCCCEEEHH		20.0628787133
1215PhosphorylationALATTSSSMLVRWSE
HEEECCCCCEEEHHH		18.8628787133
1221PhosphorylationSSMLVRWSEVPEADR
CCCEEEHHHCCHHHC		20.39-
1235PhosphorylationRNGLVLGYKVMYKEK
CCCEEEEEEEEEEEC		9.03-
1240AcetylationLGYKVMYKEKDSDTQ
EEEEEEEEECCCCCC		39.947680119
1244PhosphorylationVMYKEKDSDTQPRFW
EEEEECCCCCCCCEE		54.33-
1246PhosphorylationYKEKDSDTQPRFWLV
EEECCCCCCCCEEEE		44.41-
1269PhosphorylationQLTGLGKYVLYEVQV
ECCCCCCEEEEEEEE		8.22-
1272PhosphorylationGLGKYVLYEVQVLAF
CCCCEEEEEEEEEEE		12.19-
1314PhosphorylationILFPEVRTTSVRLIW
EECCCCEECEEEEEE		28.71-
1337PhosphorylationIILAYQITHRLNTTT
EEEEEEEEECCCCCC		5.85-
1417PhosphorylationQEDVRARSVLLSWEP
HHHHHHHEEEEECCC		19.01-
1435PhosphorylationGLSPVRYYTIQTREL
CCCCEEEEEEEEEEC		6.1825690035
1436PhosphorylationLSPVRYYTIQTRELP
CCCEEEEEEEEEECC		9.5525690035
1553PhosphorylationYEGLRGFTLRGINNP
HHHCCCCEECCCCCC		20.5424719451
1670N-linked_GlycosylationFWEAQRGNLTERVKT
EEECCCCCCHHHHHH		46.08UniProtKB CARBOHYD
1676UbiquitinationGNLTERVKTLFLAEN
CCCHHHHHHHHHCCC		45.8129967540
1771PhosphorylationCSPVDGVSKIVTVDV
CCCCCCCCEEEEEEC		23.3819690332
1775PhosphorylationDGVSKIVTVDVKGNS
CCCCEEEEEECCCCC		17.9219690332
1845PhosphorylationSAIAIHWSSGDPGKG
CEEEEEECCCCCCCC		15.41-
1881PhosphorylationKDIPKEVSSYTFSMD
ECCCHHHHCEEEEEE		20.7925002506
1882PhosphorylationDIPKEVSSYTFSMDI
CCCHHHHCEEEEEEE		33.1125002506
1883PhosphorylationIPKEVSSYTFSMDIL
CCHHHHCEEEEEEEE		12.3325002506
1884PhosphorylationPKEVSSYTFSMDILK
CHHHHCEEEEEEEEC		15.9225002506
1886PhosphorylationEVSSYTFSMDILKPG
HHHCEEEEEEEECCC		14.0325002506
1972PhosphorylationDSGNSAKSGALGHSE
CCCCCCCCCCCCCHH		29.0822496350
1978PhosphorylationKSGALGHSEMMSLDE
CCCCCCCHHCCCCCC		25.9522496350
1999PhosphorylationELNNRRLSVKNSFCR
HCCCCCEEECCCHHH		29.2722496350
2003PhosphorylationRRLSVKNSFCRKNGL
CCEEECCCHHHCCCC		21.7222496350
2007AcetylationVKNSFCRKNGLYTRS
ECCCHHHCCCCCCCC		57.4511794007
2011PhosphorylationFCRKNGLYTRSPPRP
HHHCCCCCCCCCCCC		11.0829449344
2012PhosphorylationCRKNGLYTRSPPRPS
HHCCCCCCCCCCCCC		29.7029449344
2014PhosphorylationKNGLYTRSPPRPSPG
CCCCCCCCCCCCCCC		31.3022496350
2019PhosphorylationTRSPPRPSPGSLHYS
CCCCCCCCCCCCCCC		43.0823312004
2022PhosphorylationPPRPSPGSLHYSDED
CCCCCCCCCCCCCCC		18.5029978859
2025PhosphorylationPSPGSLHYSDEDVTK
CCCCCCCCCCCCCHH		24.1026657352
2026PhosphorylationSPGSLHYSDEDVTKY
CCCCCCCCCCCCHHH		24.6325849741
2031PhosphorylationHYSDEDVTKYNDLIP
CCCCCCCHHHHCCCC		39.8829978859
2033PhosphorylationSDEDVTKYNDLIPAE
CCCCCHHHHCCCCCC		12.4429449344
2041PhosphorylationNDLIPAESSSLTEKP
HCCCCCCCCCCCCCC		27.6029449344
2042PhosphorylationDLIPAESSSLTEKPS
CCCCCCCCCCCCCCC		22.3729449344
2043PhosphorylationLIPAESSSLTEKPSE
CCCCCCCCCCCCCCC		48.9019413330
2045PhosphorylationPAESSSLTEKPSEIS
CCCCCCCCCCCCCCC		43.8619413330
2049PhosphorylationSSLTEKPSEISDSQG
CCCCCCCCCCCCCCC		59.6429449344
2052PhosphorylationTEKPSEISDSQGSDS
CCCCCCCCCCCCCCC		27.4529449344
2054PhosphorylationKPSEISDSQGSDSEY
CCCCCCCCCCCCCCE		29.6526471730
2057PhosphorylationEISDSQGSDSEYEVD
CCCCCCCCCCCEEEC		30.2626471730
2059PhosphorylationSDSQGSDSEYEVDSN
CCCCCCCCCEEECCC		43.7229449344
2061PhosphorylationSQGSDSEYEVDSNHQ
CCCCCCCEEECCCCH		25.7926471730
2082PhosphorylationNHYISDPTYYNSWRR
HHHHCCHHHHHHHHH		43.5628348404
2083PhosphorylationHYISDPTYYNSWRRQ
HHHCCHHHHHHHHHH		13.16-
2086PhosphorylationSDPTYYNSWRRQQKG
CCHHHHHHHHHHHCC		13.0728348404
2100PhosphorylationGISRAQAYSYTESDS
CCCHHHEEEEECCCC		7.0729449344
2101PhosphorylationISRAQAYSYTESDSG
CCHHHEEEEECCCCC		28.7029449344
2102PhosphorylationSRAQAYSYTESDSGE
CHHHEEEEECCCCCC		11.2329449344
2103PhosphorylationRAQAYSYTESDSGEP
HHHEEEEECCCCCCC		24.0729449344
2105PhosphorylationQAYSYTESDSGEPDH
HEEEEECCCCCCCCC		29.3129449344
2107PhosphorylationYSYTESDSGEPDHTT
EEEECCCCCCCCCCE		55.1029449344
2113PhosphorylationDSGEPDHTTVTNSTS
CCCCCCCCEEECCCC		30.2729449344
2114PhosphorylationSGEPDHTTVTNSTST
CCCCCCCEEECCCCC		23.1629449344
2116PhosphorylationEPDHTTVTNSTSTQQ
CCCCCEEECCCCCCC		22.7429449344
2118PhosphorylationDHTTVTNSTSTQQGS
CCCEEECCCCCCCCC		17.8629449344
2132 (in isoform 4)Phosphorylation-42.7022210691
2134 (in isoform 4)Phosphorylation-29.0822210691
2155PhosphorylationSTLYRPPSSLAPGSR
CCCCCCCHHCCCCCC		40.44-
2156PhosphorylationTLYRPPSSLAPGSRA
CCCCCCHHCCCCCCC		34.03-
2170PhosphorylationAPIAGFSSFV-----
CCCCCCCCCC-----		27.97-
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 SDK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDK2_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 SDK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SDK2_HUMAN !!
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 SDK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2043 AND THR-2045, ANDMASS SPECTROMETRY.

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