TBD2B_HUMAN - dbPTM
TBD2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBD2B_HUMAN
UniProt AC Q9UPU7
Protein Name TBC1 domain family member 2B
Gene Name TBC1D2B
Organism Homo sapiens (Human).
Sequence Length 963
Subcellular Localization
Protein Description May act as a GTPase-activating protein..
Protein Sequence MPGAGARAEEGGGGGEGAAQGAAAEPGAGPAREPARLCGYLQKLSGKGPLRGYRSRWFVFDARRCYLYYFKSPQDALPLGHLDIADACFSYQGPDEAAEPGTEPPAHFQVHSAGAVTVLKAPNRQLMTYWLQELQQKRWEYCNSLDMVKWDSRTSPTPGDFPKGLVARDNTDLIYPHPNASAEKARNVLAVETVPGELVGEQAANQPAPGHPNSINFYSLKQWGNELKNSMSSFRPGRGHNDSRRTVFYTNEEWELLDPTPKDLEESIVQEEKKKLTPEGNKGVTGSGFPFDFGRNPYKGKRPLKDIIGSYKNRHSSGDPSSEGTSGSGSVSIRKPASEMQLQVQSQQEELEQLKKDLSSQKELVRLLQQTVRSSQYDKYFTSSRLCEGVPKDTLELLHQKDDQILGLTSQLERFSLEKESLQQEVRTLKSKVGELNEQLGMLMETIQAKDEVIIKLSEGEGNGPPPTVAPSSPSVVPVARDQLELDRLKDNLQGYKTQNKFLNKEILELSALRRNAERRERDLMAKYSSLEAKLCQIESKYLILLQEMKTPVCSEDQGPTREVIAQLLEDALQVESQEQPEQAFVKPHLVSEYDIYGFRTVPEDDEEEKLVAKVRALDLKTLYLTENQEVSTGVKWENYFASTVNREMMCSPELKNLIRAGIPHEHRSKVWKWCVDRHTRKFKDNTEPGHFQTLLQKALEKQNPASKQIELDLLRTLPNNKHYSCPTSEGIQKLRNVLLAFSWRNPDIGYCQGLNRLVAVALLYLEQEDAFWCLVTIVEVFMPRDYYTKTLLGSQVDQRVFRDLMSEKLPRLHGHFEQYKVDYTLITFNWFLVVFVDSVVSDILFKIWDSFLYEGPKVIFRFALALFKYKEEEILKLQDSMSIFKYLRYFTRTILDARKLISISFGDLNPFPLRQIRNRRAYHLEKVRLELTELEAIREDFLRERDTSPDKGELVSDEEEDT
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
40PhosphorylationEPARLCGYLQKLSGK
CHHHHHHHHHHHCCC		12.6429496907
43AcetylationRLCGYLQKLSGKGPL
HHHHHHHHHCCCCCC		41.8625953088
43UbiquitinationRLCGYLQKLSGKGPL
HHHHHHHHHCCCCCC		41.86-
45PhosphorylationCGYLQKLSGKGPLRG
HHHHHHHCCCCCCCC		45.5629978859
47MalonylationYLQKLSGKGPLRGYR
HHHHHCCCCCCCCCC		54.7126320211
47UbiquitinationYLQKLSGKGPLRGYR
HHHHHCCCCCCCCCC		54.71-
54DimethylationKGPLRGYRSRWFVFD
CCCCCCCCEEEEEEE		23.67-
54MethylationKGPLRGYRSRWFVFD
CCCCCCCCEEEEEEE		23.6724390517
56DimethylationPLRGYRSRWFVFDAR
CCCCCCEEEEEEECC		23.12-
56MethylationPLRGYRSRWFVFDAR
CCCCCCEEEEEEECC		23.1224390527
120AcetylationAGAVTVLKAPNRQLM
CCCEEEEECCCHHHH		58.4230592849
128PhosphorylationAPNRQLMTYWLQELQ
CCCHHHHHHHHHHHH		21.8224043423
129PhosphorylationPNRQLMTYWLQELQQ
CCHHHHHHHHHHHHH		7.0824043423
137UbiquitinationWLQELQQKRWEYCNS
HHHHHHHHHHHHHCC		46.66-
141PhosphorylationLQQKRWEYCNSLDMV
HHHHHHHHHCCCCCC		7.0327642862
149UbiquitinationCNSLDMVKWDSRTSP
HCCCCCCCCCCCCCC		38.35-
152PhosphorylationLDMVKWDSRTSPTPG
CCCCCCCCCCCCCCC		36.0223403867
154PhosphorylationMVKWDSRTSPTPGDF
CCCCCCCCCCCCCCC		42.9023401153
155PhosphorylationVKWDSRTSPTPGDFP
CCCCCCCCCCCCCCC		26.1823401153
157PhosphorylationWDSRTSPTPGDFPKG
CCCCCCCCCCCCCCC		39.4030266825
163UbiquitinationPTPGDFPKGLVARDN
CCCCCCCCCEECCCC		65.94-
175PhosphorylationRDNTDLIYPHPNASA
CCCCCCCCCCCCCCH		11.64-
181PhosphorylationIYPHPNASAEKARNV
CCCCCCCCHHHHHCE		43.5322199227
184UbiquitinationHPNASAEKARNVLAV
CCCCCHHHHHCEEEE		52.98-
193PhosphorylationRNVLAVETVPGELVG
HCEEEEEECCCHHHC		25.9629978859
214PhosphorylationPAPGHPNSINFYSLK
CCCCCCCCCCEECHH		24.3028857561
218PhosphorylationHPNSINFYSLKQWGN
CCCCCCEECHHHHHH		14.4929978859
219PhosphorylationPNSINFYSLKQWGNE
CCCCCEECHHHHHHH		25.5924719451
221UbiquitinationSINFYSLKQWGNELK
CCCEECHHHHHHHHH		37.76-
230PhosphorylationWGNELKNSMSSFRPG
HHHHHHHHHHHCCCC		20.6023403867
232PhosphorylationNELKNSMSSFRPGRG
HHHHHHHHHCCCCCC		26.5823403867
233PhosphorylationELKNSMSSFRPGRGH
HHHHHHHHCCCCCCC		19.3427251275
246PhosphorylationGHNDSRRTVFYTNEE
CCCCCCCEEEEECCC		17.5428122231
249PhosphorylationDSRRTVFYTNEEWEL
CCCCEEEEECCCEEE		12.3427642862
267PhosphorylationTPKDLEESIVQEEKK
CCCCHHHHHHHHHHH		20.7729214152
275UbiquitinationIVQEEKKKLTPEGNK
HHHHHHHCCCCCCCC		69.53-
277PhosphorylationQEEKKKLTPEGNKGV
HHHHHCCCCCCCCCC		28.3326657352
310PhosphorylationPLKDIIGSYKNRHSS
CHHHHHHHHCCCCCC		23.6423401153
311PhosphorylationLKDIIGSYKNRHSSG
HHHHHHHHCCCCCCC		13.6823312004
312UbiquitinationKDIIGSYKNRHSSGD
HHHHHHHCCCCCCCC		49.56-
316PhosphorylationGSYKNRHSSGDPSSE
HHHCCCCCCCCCCCC		32.5529255136
317PhosphorylationSYKNRHSSGDPSSEG
HHCCCCCCCCCCCCC		40.8823401153
321PhosphorylationRHSSGDPSSEGTSGS
CCCCCCCCCCCCCCC		45.8428450419
322PhosphorylationHSSGDPSSEGTSGSG
CCCCCCCCCCCCCCC		45.4922496350
325PhosphorylationGDPSSEGTSGSGSVS
CCCCCCCCCCCCCEE		26.3423927012
326PhosphorylationDPSSEGTSGSGSVSI
CCCCCCCCCCCCEEE		41.6423927012
328PhosphorylationSSEGTSGSGSVSIRK
CCCCCCCCCCEEEEC		27.8823927012
330PhosphorylationEGTSGSGSVSIRKPA
CCCCCCCCEEEECCC		17.8723927012
332PhosphorylationTSGSGSVSIRKPASE
CCCCCCEEEECCCHH		20.5523927012
335UbiquitinationSGSVSIRKPASEMQL
CCCEEEECCCHHHHH		43.18-
338PhosphorylationVSIRKPASEMQLQVQ
EEEECCCHHHHHHHH		41.9728857561
355UbiquitinationQEELEQLKKDLSSQK
HHHHHHHHHHHHHHH		43.89-
362UbiquitinationKKDLSSQKELVRLLQ
HHHHHHHHHHHHHHH		55.77-
379UbiquitinationVRSSQYDKYFTSSRL
HHHHHHHHHHCCCCC		37.01-
380PhosphorylationRSSQYDKYFTSSRLC
HHHHHHHHHCCCCCC		14.8027642862
392UbiquitinationRLCEGVPKDTLELLH
CCCCCCCHHHHHHHH		62.02-
401UbiquitinationTLELLHQKDDQILGL
HHHHHHHCCHHHHHH		53.15-
409PhosphorylationDDQILGLTSQLERFS
CHHHHHHHHHHHHHH		16.7822798277
419UbiquitinationLERFSLEKESLQQEV
HHHHHCCHHHHHHHH		58.87-
431PhosphorylationQEVRTLKSKVGELNE
HHHHHHHHHHHHHHH		35.37-
458PhosphorylationDEVIIKLSEGEGNGP
CEEEEECCCCCCCCC		38.2626074081
468PhosphorylationEGNGPPPTVAPSSPS
CCCCCCCCCCCCCCC		34.7625850435
472PhosphorylationPPPTVAPSSPSVVPV
CCCCCCCCCCCCCCE		45.1825159151
473PhosphorylationPPTVAPSSPSVVPVA
CCCCCCCCCCCCCEE		21.8225159151
475PhosphorylationTVAPSSPSVVPVARD
CCCCCCCCCCCEEHH		37.3822199227
490UbiquitinationQLELDRLKDNLQGYK
HHHHHHHHHHHCHHH		45.52-
497UbiquitinationKDNLQGYKTQNKFLN
HHHHCHHHHHCHHHC		50.92-
501UbiquitinationQGYKTQNKFLNKEIL
CHHHHHCHHHCHHHH		41.22-
505UbiquitinationTQNKFLNKEILELSA
HHCHHHCHHHHHHHH		48.56-
511PhosphorylationNKEILELSALRRNAE
CHHHHHHHHHHHHHH		18.8421082442
527UbiquitinationRERDLMAKYSSLEAK
HHHHHHHHHHHHHHH		31.53-
529PhosphorylationRDLMAKYSSLEAKLC
HHHHHHHHHHHHHHH		27.9527251275
530PhosphorylationDLMAKYSSLEAKLCQ
HHHHHHHHHHHHHHH		27.4330631047
534UbiquitinationKYSSLEAKLCQIESK
HHHHHHHHHHHHHHH		40.18-
540PhosphorylationAKLCQIESKYLILLQ
HHHHHHHHHHHHHHH		28.38-
542PhosphorylationLCQIESKYLILLQEM
HHHHHHHHHHHHHHH		14.3020068231
551PhosphorylationILLQEMKTPVCSEDQ
HHHHHHCCCCCCCCC		21.4623312004
561PhosphorylationCSEDQGPTREVIAQL
CCCCCCCHHHHHHHH		46.41-
577PhosphorylationEDALQVESQEQPEQA
HHHHHHCCCCCHHHH		39.9125159151
594PhosphorylationKPHLVSEYDIYGFRT
CHHHCCCCEEECEEE		10.51-
597PhosphorylationLVSEYDIYGFRTVPE
HCCCCEEECEEECCC		13.81-
610UbiquitinationPEDDEEEKLVAKVRA
CCCCHHHHHHHHHHH		52.09-
614UbiquitinationEEEKLVAKVRALDLK
HHHHHHHHHHHCCCE		25.44-
621UbiquitinationKVRALDLKTLYLTEN
HHHHCCCEEEEEECC		35.83-
652PhosphorylationVNREMMCSPELKNLI
CCHHHHCCHHHHHHH		11.9624719451
698UbiquitinationHFQTLLQKALEKQNP
HHHHHHHHHHHHCCC		55.71-
702UbiquitinationLLQKALEKQNPASKQ
HHHHHHHHCCCCCCH		57.11-
707PhosphorylationLEKQNPASKQIELDL
HHHCCCCCCHHHHHH		26.7525262027
708UbiquitinationEKQNPASKQIELDLL
HHCCCCCCHHHHHHH		58.35-
722UbiquitinationLRTLPNNKHYSCPTS
HHCCCCCCCCCCCCH		51.03-
787PhosphorylationEVFMPRDYYTKTLLG
HHHCCCCHHHHHHHC		17.83-
788PhosphorylationVFMPRDYYTKTLLGS
HHCCCCHHHHHHHCC		13.17-
789PhosphorylationFMPRDYYTKTLLGSQ
HCCCCHHHHHHHCCH		16.01-
791PhosphorylationPRDYYTKTLLGSQVD
CCCHHHHHHHCCHHC		21.29-
809UbiquitinationFRDLMSEKLPRLHGH
HHHHHHHCCHHHCCC		57.39-
881PhosphorylationEILKLQDSMSIFKYL
HHHHHHHHHHHHHHH		11.0627499020
883PhosphorylationLKLQDSMSIFKYLRY
HHHHHHHHHHHHHHH		28.9124719451
886UbiquitinationQDSMSIFKYLRYFTR
HHHHHHHHHHHHHHH		41.53-
933PhosphorylationEKVRLELTELEAIRE
HHHHHHHHHHHHHHH		29.2028258704
948PhosphorylationDFLRERDTSPDKGEL
HHHHHCCCCCCCCCC		48.6723927012
949PhosphorylationFLRERDTSPDKGELV
HHHHCCCCCCCCCCC		35.0823927012
957PhosphorylationPDKGELVSDEEEDT-
CCCCCCCCCCCCCC-		52.5129255136
963PhosphorylationVSDEEEDT-------
CCCCCCCC-------		43.7323927012
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 TBD2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBD2B_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 TBD2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRDMT_HUMANTRDMT1physical
21988832
S10A6_HUMANS100A6physical
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 TBD2B_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-957, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, 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-949 AND SER-957, ANDMASS SPECTROMETRY.

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