SYBU_HUMAN - dbPTM
SYBU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYBU_HUMAN
UniProt AC Q9NX95
Protein Name Syntabulin
Gene Name SYBU
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Isoform 1: Cytoplasm, cytoskeleton. Cytoplasmic vesicle. Colocalizes with syntaxin vesicles along microtubules in neuronal processes.
Isoform 3: Golgi apparatus membrane
Single-pass membrane protein.
Isoform 4: Golgi apparatus membrane
Single-pas
Protein Description Part of a kinesin motor-adapter complex that is critical for the anterograde axonal transport of active zone components and contributes to activity-dependent presynaptic assembly during neuronal development..
Protein Sequence MGPLRESKKEHRVQHHDKEISRSRIPRLILRPHMPQQQHKVSPASESPFSEEESREFNPSSSGRSARTVSSNSFCSDDTGCPSSQSVSPVKTPSDAGNSPIGFCPGSDEGFTRKKCTIGMVGEGSIQSSRYKKESKSGLVKPGSEADFSSSSSTGSISAPEVHMSTAGSKRSSSSRNRGPHGRSNGASSHKPGSSPSSPREKDLLSMLCRNQLSPVNIHPSYAPSSPSSSNSGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLSLEEQVTGEGADRELLVGDSIANSTDLFDEIVTATTTESGDLELVHSTPGANVLELLPIVMGQEEGSVVVERAVQTDVVPYSPAISELIQSVLQKLQDPCPSSLASPDESEPDSMESFPESLSALVVDLTPRNPNSAILLSPVETPYANVDAEVHANRLMRELDFAACVEERLDGVIPLARGGVVRQYWSSSFLVDLLAVAAPVVPTVLWAFSTQRGGTDPVYNIGALLRGCCVVALHSLRRTAFRIKT
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
42PhosphorylationPQQQHKVSPASESPF
CCCCCCCCCCCCCCC		21.3925849741
45PhosphorylationQHKVSPASESPFSEE
CCCCCCCCCCCCCHH		41.8325849741
47PhosphorylationKVSPASESPFSEEES
CCCCCCCCCCCHHHH		28.8423663014
50PhosphorylationPASESPFSEEESREF
CCCCCCCCHHHHHCC		47.7025159151
54PhosphorylationSPFSEEESREFNPSS
CCCCHHHHHCCCCCC		40.1523312004
60PhosphorylationESREFNPSSSGRSAR
HHHCCCCCCCCCCCE		37.9423312004
61PhosphorylationSREFNPSSSGRSART
HHCCCCCCCCCCCEE		37.7623312004
62PhosphorylationREFNPSSSGRSARTV
HCCCCCCCCCCCEEE		42.4323312004
65PhosphorylationNPSSSGRSARTVSSN
CCCCCCCCCEEECCC		26.15-
68PhosphorylationSSGRSARTVSSNSFC
CCCCCCEEECCCCCC		25.1826471730
70PhosphorylationGRSARTVSSNSFCSD
CCCCEEECCCCCCCC		24.1625159151
71PhosphorylationRSARTVSSNSFCSDD
CCCEEECCCCCCCCC		31.9625159151
73PhosphorylationARTVSSNSFCSDDTG
CEEECCCCCCCCCCC		29.5826657352
76PhosphorylationVSSNSFCSDDTGCPS
ECCCCCCCCCCCCCC		36.1926471730
79PhosphorylationNSFCSDDTGCPSSQS
CCCCCCCCCCCCCCC		45.7528348404
88PhosphorylationCPSSQSVSPVKTPSD
CCCCCCCCCCCCCCC		29.2628985074
92PhosphorylationQSVSPVKTPSDAGNS
CCCCCCCCCCCCCCC		28.4125159151
94PhosphorylationVSPVKTPSDAGNSPI
CCCCCCCCCCCCCCC		45.3725159151
99PhosphorylationTPSDAGNSPIGFCPG
CCCCCCCCCCCCCCC		19.5826657352
107PhosphorylationPIGFCPGSDEGFTRK
CCCCCCCCCCCCCCC		20.0328985074
117PhosphorylationGFTRKKCTIGMVGEG
CCCCCCCEEEEECCC		29.4627732954
125PhosphorylationIGMVGEGSIQSSRYK
EEEECCCCCCCCCCC		17.1027732954
128PhosphorylationVGEGSIQSSRYKKES
ECCCCCCCCCCCCCC		18.3427732954
129PhosphorylationGEGSIQSSRYKKESK
CCCCCCCCCCCCCCC		24.2127050516
131PhosphorylationGSIQSSRYKKESKSG
CCCCCCCCCCCCCCC		28.4929449344
149PhosphorylationPGSEADFSSSSSTGS
CCCCCCCCCCCCCCC		29.8317081983
150PhosphorylationGSEADFSSSSSTGSI
CCCCCCCCCCCCCCC		33.9430576142
151PhosphorylationSEADFSSSSSTGSIS
CCCCCCCCCCCCCCC		27.4030576142
152PhosphorylationEADFSSSSSTGSISA
CCCCCCCCCCCCCCC		33.5917081983
153PhosphorylationADFSSSSSTGSISAP
CCCCCCCCCCCCCCC		38.4417081983
156PhosphorylationSSSSSTGSISAPEVH
CCCCCCCCCCCCEEE		17.2917081983
165PhosphorylationSAPEVHMSTAGSKRS
CCCEEEECCCCCCCC		10.5417081983
166PhosphorylationAPEVHMSTAGSKRSS
CCEEEECCCCCCCCC		27.7117081983
169PhosphorylationVHMSTAGSKRSSSSR
EEECCCCCCCCCCCC		23.5617081983
184PhosphorylationNRGPHGRSNGASSHK
CCCCCCCCCCCCCCC		44.1827251275
188PhosphorylationHGRSNGASSHKPGSS
CCCCCCCCCCCCCCC		34.0827251275
189PhosphorylationGRSNGASSHKPGSSP
CCCCCCCCCCCCCCC		34.6927251275
194O-linked_GlycosylationASSHKPGSSPSSPRE
CCCCCCCCCCCCHHH		47.8330379171
194PhosphorylationASSHKPGSSPSSPRE
CCCCCCCCCCCCHHH		47.8325002506
195PhosphorylationSSHKPGSSPSSPREK
CCCCCCCCCCCHHHH		34.4128985074
197PhosphorylationHKPGSSPSSPREKDL
CCCCCCCCCHHHHHH		55.7225849741
198PhosphorylationKPGSSPSSPREKDLL
CCCCCCCCHHHHHHH		31.2128985074
202UbiquitinationSPSSPREKDLLSMLC
CCCCHHHHHHHHHHH		55.76-
214PhosphorylationMLCRNQLSPVNIHPS
HHHHCCCCCCCCCCC		19.6223927012
221PhosphorylationSPVNIHPSYAPSSPS
CCCCCCCCCCCCCCC		21.5523927012
222PhosphorylationPVNIHPSYAPSSPSS
CCCCCCCCCCCCCCC		27.2923927012
225PhosphorylationIHPSYAPSSPSSSNS
CCCCCCCCCCCCCCC		46.8623927012
226PhosphorylationHPSYAPSSPSSSNSG
CCCCCCCCCCCCCCC		27.9520873877
228PhosphorylationSYAPSSPSSSNSGSY
CCCCCCCCCCCCCCC		48.6323927012
229PhosphorylationYAPSSPSSSNSGSYK
CCCCCCCCCCCCCCC		36.6023927012
230PhosphorylationAPSSPSSSNSGSYKG
CCCCCCCCCCCCCCC		39.0823927012
232PhosphorylationSSPSSSNSGSYKGSD
CCCCCCCCCCCCCCC		30.9423927012
234PhosphorylationPSSSNSGSYKGSDCS
CCCCCCCCCCCCCCH		24.4023927012
235PhosphorylationSSSNSGSYKGSDCSP
CCCCCCCCCCCCCHH		23.9320873877
238PhosphorylationNSGSYKGSDCSPIMR
CCCCCCCCCCHHHHH		31.1528102081
241PhosphorylationSYKGSDCSPIMRRSG
CCCCCCCHHHHHHCC		23.5825849741
252PhosphorylationRRSGRYMSCGENHGV
HHCCCCCCCCCCCCC		15.2728348404
269PhosphorylationPNPEQYLTPLQQKEV
CCHHHCCCHHHHCCH		19.6127251275
277PhosphorylationPLQQKEVTVRHLKTK
HHHHCCHHHHHHHHH		16.9524719451
303UbiquitinationESEIVELKSQLARMR
HHHHHHHHHHHHHHH		23.73-
328UbiquitinationVEAQLALKEARKEIK
HHHHHHHHHHHHHHH		43.66-
343PhosphorylationQLKQVIETMRSSLAD
HHHHHHHHHHHHHCC		13.5317322306
344OxidationLKQVIETMRSSLADK
HHHHHHHHHHHHCCC		2.2517322306
346PhosphorylationQVIETMRSSLADKDK
HHHHHHHHHHCCCCC		20.9125278378
347PhosphorylationVIETMRSSLADKDKG
HHHHHHHHHCCCCCC		19.7425278378
358PhosphorylationKDKGIQKYFVDINIQ
CCCCCHHEEEEEECC		7.77-
396PhosphorylationCLDFPCDSPEKSLTL
EECCCCCCCCCCCCC		41.4927732954
400PhosphorylationPCDSPEKSLTLNPPL
CCCCCCCCCCCCCCC		25.5627251275
402PhosphorylationDSPEKSLTLNPPLDT
CCCCCCCCCCCCCCC		31.4227251275
409PhosphorylationTLNPPLDTMADGLSL
CCCCCCCCCCCCCCH		23.1827251275
415PhosphorylationDTMADGLSLEEQVTG
CCCCCCCCHHHHHHC		38.9827251275
496PhosphorylationQTDVVPYSPAISELI
ECCCCCCCHHHHHHH		11.2029496963
520PhosphorylationPCPSSLASPDESEPD
CCCHHCCCCCCCCCC		37.8727251275
524PhosphorylationSLASPDESEPDSMES
HCCCCCCCCCCHHHH		62.9128348404
528PhosphorylationPDESEPDSMESFPES
CCCCCCCHHHHCCHH		34.8528348404
531PhosphorylationSEPDSMESFPESLSA
CCCCHHHHCCHHHHH		37.1428348404
550PhosphorylationLTPRNPNSAILLSPV
CCCCCCCCEEEECCC		20.2426425664
555PhosphorylationPNSAILLSPVETPYA
CCCEEEECCCCCCCC		24.3725159151
559PhosphorylationILLSPVETPYANVDA
EEECCCCCCCCCCCH		23.1030624053
561PhosphorylationLSPVETPYANVDAEV
ECCCCCCCCCCCHHH		20.4427732954
653PhosphorylationCCVVALHSLRRTAFR
HHHHHHHHHHHHHHC		25.1528787133
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 SYBU_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYBU_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 SYBU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BICD1_HUMANBICD1physical
28514442
CE162_HUMANCEP162physical
28514442
SNPH_HUMANSNPHphysical
28514442
CLAP1_HUMANCLASP1physical
28514442
MARC2_HUMANMARC2physical
28514442
BL1S2_HUMANBLOC1S2physical
28514442
TRAF7_HUMANTRAF7physical
28514442
SNAPN_HUMANSNAPINphysical
28514442
TPH2_HUMANTPH2physical
28514442
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 SYBU_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-197, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory