TB10B_HUMAN - dbPTM
TB10B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TB10B_HUMAN
UniProt AC Q4KMP7
Protein Name TBC1 domain family member 10B
Gene Name TBC1D10B
Organism Homo sapiens (Human).
Sequence Length 808
Subcellular Localization Cytoplasm . In melanocytes, located at the periphery of cells.
Protein Description Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A, AND RAB35. Does not act on RAB2A and RAB6A..
Protein Sequence METGTAPLVAPPRRHGAPAAPSPPPRGSRAGPVVVVAPGPPVTTATSAPVTLVAPGEARPAWVPGSAETSAPAPAPAPAPAPAVTGSTVVVLTLEASPEAPKPQLPSGPESPEPAAVAGVETSRALAAGADSPKTEEARPSPAPGPGTPTGTPTRTPSRTAPGALTAKPPLAPKPGTTVASGVTARSASGQVTGGHGAAAATSASAGQAPEDPSGPGTGPSGTCEAPVAVVTVTPAPEPAENSQDLGSTSSLGPGISGPRGQAPDTLSYLDSVSLMSGTLESLADDVSSMGSDSEINGLALRKTDKYGFLGGSQYSGSLESSIPVDVARQRELKWLDMFSNWDKWLSRRFQKVKLRCRKGIPSSLRAKAWQYLSNSKELLEQNPGKFEELERAPGDPKWLDVIEKDLHRQFPFHEMFAARGGHGQQDLYRILKAYTIYRPDEGYCQAQAPVAAVLLMHMPAEQAFWCLVQICDKYLPGYYSAGLEAIQLDGEIFFALLRRASPLAHRHLRRQRIDPVLYMTEWFMCIFARTLPWASVLRVWDMFFCEGVKIIFRVALVLLRHTLGSVEKLRSCQGMYETMEQLRNLPQQCMQEDFLVHEVTNLPVTEALIERENAAQLKKWRETRGELQYRPSRRLHGSRAIHEERRRQQPPLGPSSSLLSLPGLKSRGSRAAGGAPSPPPPVRRASAGPAPGPVVTAEGLHPSLPSPTGNSTPLGSSKETRKQEKERQKQEKERQKQEKEREKERQKQEKEREKQEKEREKQEKERQKQEKKAQGRKLSLRRKADGPPGPHDGGDRPSAEARQDAYF
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
22PhosphorylationHGAPAAPSPPPRGSR
CCCCCCCCCCCCCCC		45.3629255136
28PhosphorylationPSPPPRGSRAGPVVV
CCCCCCCCCCCCEEE		21.9030576142
43O-linked_GlycosylationVAPGPPVTTATSAPV
ECCCCCCCCCCCCCE		19.2528657654
44O-linked_GlycosylationAPGPPVTTATSAPVT
CCCCCCCCCCCCCEE		28.3328657654
46O-linked_GlycosylationGPPVTTATSAPVTLV
CCCCCCCCCCCEEEE		24.2728657654
47O-linked_GlycosylationPPVTTATSAPVTLVA
CCCCCCCCCCEEEEC		28.2828657654
51O-linked_GlycosylationTATSAPVTLVAPGEA
CCCCCCEEEECCCCC		17.9228657654
93PhosphorylationGSTVVVLTLEASPEA
CCEEEEEEEEECCCC		15.7926074081
93 (in isoform 1)Ubiquitination-15.7921890473
97PhosphorylationVVLTLEASPEAPKPQ
EEEEEEECCCCCCCC		17.5626074081
107PhosphorylationAPKPQLPSGPESPEP
CCCCCCCCCCCCCCC		75.4726074081
111PhosphorylationQLPSGPESPEPAAVA
CCCCCCCCCCCCHHC		37.3825849741
123 (in isoform 1)Ubiquitination-11.3121890473
130 (in isoform 1)Ubiquitination-14.9121890473
132PhosphorylationALAAGADSPKTEEAR
HHHCCCCCCCCCCCC		27.9729255136
134UbiquitinationAAGADSPKTEEARPS
HCCCCCCCCCCCCCC		72.9524816145
135PhosphorylationAGADSPKTEEARPSP
CCCCCCCCCCCCCCC		42.3030278072
141PhosphorylationKTEEARPSPAPGPGT
CCCCCCCCCCCCCCC		28.3030266825
148PhosphorylationSPAPGPGTPTGTPTR
CCCCCCCCCCCCCCC		22.3229255136
150PhosphorylationAPGPGTPTGTPTRTP
CCCCCCCCCCCCCCC		54.2329255136
152PhosphorylationGPGTPTGTPTRTPSR
CCCCCCCCCCCCCCC		24.7829255136
154PhosphorylationGTPTGTPTRTPSRTA
CCCCCCCCCCCCCCC		47.1930266825
156PhosphorylationPTGTPTRTPSRTAPG
CCCCCCCCCCCCCCC		28.2623927012
158PhosphorylationGTPTRTPSRTAPGAL
CCCCCCCCCCCCCCC		41.4723927012
160PhosphorylationPTRTPSRTAPGALTA
CCCCCCCCCCCCCCC		41.3528464451
166PhosphorylationRTAPGALTAKPPLAP
CCCCCCCCCCCCCCC		31.9128464451
177PhosphorylationPLAPKPGTTVASGVT
CCCCCCCCEEECCCE		26.9928176443
178O-linked_GlycosylationLAPKPGTTVASGVTA
CCCCCCCEEECCCEE		21.7128657654
178PhosphorylationLAPKPGTTVASGVTA
CCCCCCCEEECCCEE		21.7128176443
181PhosphorylationKPGTTVASGVTARSA
CCCCEEECCCEEECC		29.4728176443
184PhosphorylationTTVASGVTARSASGQ
CEEECCCEEECCCCC		21.6328176443
186MethylationVASGVTARSASGQVT
EECCCEEECCCCCCC		24.32-
248PhosphorylationENSQDLGSTSSLGPG
CCCCCCCCCCCCCCC		32.2026074081
249PhosphorylationNSQDLGSTSSLGPGI
CCCCCCCCCCCCCCC		22.1226074081
250PhosphorylationSQDLGSTSSLGPGIS
CCCCCCCCCCCCCCC		25.8426074081
251PhosphorylationQDLGSTSSLGPGISG
CCCCCCCCCCCCCCC		37.1226074081
266PhosphorylationPRGQAPDTLSYLDSV
CCCCCCCHHHHHHHH		19.2826074081
268PhosphorylationGQAPDTLSYLDSVSL
CCCCCHHHHHHHHHH		26.2426074081
269PhosphorylationQAPDTLSYLDSVSLM
CCCCHHHHHHHHHHH		20.0326074081
304PhosphorylationNGLALRKTDKYGFLG
CCEEECCCCCCCCCC		31.15-
307PhosphorylationALRKTDKYGFLGGSQ
EECCCCCCCCCCCCC		18.8730576142
313PhosphorylationKYGFLGGSQYSGSLE
CCCCCCCCCCCCCCC		24.9324144214
315PhosphorylationGFLGGSQYSGSLESS
CCCCCCCCCCCCCCC		19.3930576142
316PhosphorylationFLGGSQYSGSLESSI
CCCCCCCCCCCCCCC		17.8024144214
318PhosphorylationGGSQYSGSLESSIPV
CCCCCCCCCCCCCCH		24.0324144214
321PhosphorylationQYSGSLESSIPVDVA
CCCCCCCCCCCHHHH		38.5730576142
322PhosphorylationYSGSLESSIPVDVAR
CCCCCCCCCCHHHHH		22.8724144214
364PhosphorylationCRKGIPSSLRAKAWQ
HCCCCCHHHHHHHHH		19.27-
368UbiquitinationIPSSLRAKAWQYLSN
CCHHHHHHHHHHHHC		43.6621890473
368 (in isoform 2)Ubiquitination-43.6621890473
368UbiquitinationIPSSLRAKAWQYLSN
CCHHHHHHHHHHHHC		43.6621890473
377UbiquitinationWQYLSNSKELLEQNP
HHHHHCCHHHHHHCC		57.5429967540
386UbiquitinationLLEQNPGKFEELERA
HHHHCCCCHHHHHCC		51.3532015554
398UbiquitinationERAPGDPKWLDVIEK
HCCCCCCHHHHHHHH		66.1922817900
398 (in isoform 2)Ubiquitination-66.1921890473
398UbiquitinationERAPGDPKWLDVIEK
HCCCCCCHHHHHHHH		66.1921890473
405 (in isoform 2)Ubiquitination-55.2421890473
405UbiquitinationKWLDVIEKDLHRQFP
HHHHHHHHHHHHHCC		55.2421890473
405UbiquitinationKWLDVIEKDLHRQFP
HHHHHHHHHHHHHCC		55.2421890473
433AcetylationQDLYRILKAYTIYRP
HHHHHHHHHHEEECC		36.6620167786
561UbiquitinationRVALVLLRHTLGSVE
HHHHHHHHHHHCCHH		19.3123000965
572PhosphorylationGSVEKLRSCQGMYET
CCHHHHHHCCCHHHH		22.64-
577PhosphorylationLRSCQGMYETMEQLR
HHHCCCHHHHHHHHH		18.3121945579
579PhosphorylationSCQGMYETMEQLRNL
HCCCHHHHHHHHHCC		14.4421945579
620AcetylationENAAQLKKWRETRGE
HCHHHHHHHHHHHCC		61.1419825037
630PhosphorylationETRGELQYRPSRRLH
HHHCCCCCCCCCCCC		36.8028060719
633PhosphorylationGELQYRPSRRLHGSR
CCCCCCCCCCCCCCC		22.4930108239
650UbiquitinationHEERRRQQPPLGPSS
HHHHHHHCCCCCCCH		39.5024816145
656PhosphorylationQQPPLGPSSSLLSLP
HCCCCCCCHHHHCCC		30.6629255136
657PhosphorylationQPPLGPSSSLLSLPG
CCCCCCCHHHHCCCC		28.3029255136
658PhosphorylationPPLGPSSSLLSLPGL
CCCCCCHHHHCCCCC		37.3529255136
661PhosphorylationGPSSSLLSLPGLKSR
CCCHHHHCCCCCCCC		37.5029255136
664UbiquitinationSSLLSLPGLKSRGSR
HHHHCCCCCCCCCCC		51.5424816145
666UbiquitinationLLSLPGLKSRGSRAA
HHCCCCCCCCCCCCC		43.9823000965
667PhosphorylationLSLPGLKSRGSRAAG
HCCCCCCCCCCCCCC		47.0928111955
678PhosphorylationRAAGGAPSPPPPVRR
CCCCCCCCCCCCCCC		49.8929255136
679UbiquitinationAAGGAPSPPPPVRRA
CCCCCCCCCCCCCCC		44.3424816145
687PhosphorylationPPPVRRASAGPAPGP
CCCCCCCCCCCCCCC		31.7629255136
697PhosphorylationPAPGPVVTAEGLHPS
CCCCCEEEECCCCCC		21.1623927012
704PhosphorylationTAEGLHPSLPSPTGN
EECCCCCCCCCCCCC		42.0123927012
707PhosphorylationGLHPSLPSPTGNSTP
CCCCCCCCCCCCCCC		40.1525159151
709PhosphorylationHPSLPSPTGNSTPLG
CCCCCCCCCCCCCCC		54.0223927012
712PhosphorylationLPSPTGNSTPLGSSK
CCCCCCCCCCCCCCH		32.5230278072
713PhosphorylationPSPTGNSTPLGSSKE
CCCCCCCCCCCCCHH		26.9130278072
717PhosphorylationGNSTPLGSSKETRKQ
CCCCCCCCCHHHHHH		46.0123927012
718PhosphorylationNSTPLGSSKETRKQE
CCCCCCCCHHHHHHH		32.4823927012
721PhosphorylationPLGSSKETRKQEKER
CCCCCHHHHHHHHHH		47.0727174698
755UbiquitinationKQEKEREKQEKEREK
HHHHHHHHHHHHHHH		70.7224816145
769UbiquitinationKQEKERQKQEKKAQG
HHHHHHHHHHHHHHH		67.6524816145
780PhosphorylationKAQGRKLSLRRKADG
HHHHCHHCHHHCCCC		23.9026437602
784UbiquitinationRKLSLRRKADGPPGP
CHHCHHHCCCCCCCC		44.3824816145
799PhosphorylationHDGGDRPSAEARQDA
CCCCCCCCHHHHHHH		39.3728985074
807PhosphorylationAEARQDAYF------
HHHHHHHCC------		20.3623312004
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 TB10B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TB10B_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 TB10B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TB10B_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 TB10B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661; SER-678AND SER-687, AND MASS SPECTROMETRY.
"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-678, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-661; SER-678;SER-687; SER-707 AND THR-709, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASSSPECTROMETRY.

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