TB10A_HUMAN - dbPTM
TB10A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TB10A_HUMAN
UniProt AC Q9BXI6
Protein Name TBC1 domain family member 10A
Gene Name TBC1D10A
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Cell projection, microvillus . Localizes to the microvilli-rich region of the syncytiotrophoblast. In melanocytes, located at the periphery of cells.
Protein Description Acts as GTPase-activating protein for RAB27A, but not for RAB2A, RAB3A, nor RAB4A..
Protein Sequence MAKSNGENGPRAPAAGESLSGTRESLAQGPDAATTDELSSLGSDSEANGFAERRIDKFGFIVGSQGAEGALEEVPLEVLRQRESKWLDMLNNWDKWMAKKHKKIRLRCQKGIPPSLRGRAWQYLSGGKVKLQQNPGKFDELDMSPGDPKWLDVIERDLHRQFPFHEMFVSRGGHGQQDLFRVLKAYTLYRPEEGYCQAQAPIAAVLLMHMPAEQAFWCLVQICEKYLPGYYSEKLEAIQLDGEILFSLLQKVSPVAHKHLSRQKIDPLLYMTEWFMCAFSRTLPWSSVLRVWDMFFCEGVKIIFRVGLVLLKHALGSPEKVKACQGQYETIERLRSLSPKIMQEAFLVQEVVELPVTERQIEREHLIQLRRWQETRGELQCRSPPRLHGAKAILDAEPGPRPALQPSPSIRLPLDAPLPGSKAKPKPPKQAQKEQRKQMKGRGQLEKPPAPNQAMVVAAAGDACPPQHVPPKDSAPKDSAPQDLAPQVSAHHRSQESLTSQESEDTYL
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
4Phosphorylation----MAKSNGENGPR
----CCCCCCCCCCC		40.2922468782
18PhosphorylationRAPAAGESLSGTRES
CCCCCCCCCCCHHHH		27.2423401153
20PhosphorylationPAAGESLSGTRESLA
CCCCCCCCCHHHHHH		47.6125849741
22PhosphorylationAGESLSGTRESLAQG
CCCCCCCHHHHHHCC		28.0825849741
25PhosphorylationSLSGTRESLAQGPDA
CCCCHHHHHHCCCCC		26.2225849741
34PhosphorylationAQGPDAATTDELSSL
HCCCCCCCHHHHHHC		36.1828450419
35PhosphorylationQGPDAATTDELSSLG
CCCCCCCHHHHHHCC		23.8120363803
39PhosphorylationAATTDELSSLGSDSE
CCCHHHHHHCCCCHH		22.8225159151
40PhosphorylationATTDELSSLGSDSEA
CCHHHHHHCCCCHHH		49.7430278072
43PhosphorylationDELSSLGSDSEANGF
HHHHHCCCCHHHCCC		43.1730278072
45PhosphorylationLSSLGSDSEANGFAE
HHHCCCCHHHCCCHH		40.0630278072
64PhosphorylationKFGFIVGSQGAEGAL
HCCEEECCCCCCCCH		17.9724719451
95UbiquitinationDMLNNWDKWMAKKHK
HHHHCHHHHHHHHHH		30.40-
99UbiquitinationNWDKWMAKKHKKIRL
CHHHHHHHHHHHHHH		39.03-
100UbiquitinationWDKWMAKKHKKIRLR
HHHHHHHHHHHHHHH		51.63-
106 (in isoform 2)Ubiquitination-7.96-
107 (in isoform 2)Ubiquitination-15.80-
125PhosphorylationGRAWQYLSGGKVKLQ
CCHHHHHHCCEEEEC		40.3327251275
132PhosphorylationSGGKVKLQQNPGKFD
HCCEEEECCCCCCCC		34.9727251275
137UbiquitinationKLQQNPGKFDELDMS
EECCCCCCCCCCCCC		51.3921890473
137UbiquitinationKLQQNPGKFDELDMS
EECCCCCCCCCCCCC		51.3921890473
144UbiquitinationKFDELDMSPGDPKWL
CCCCCCCCCCCCHHH		25.9521890473
144 (in isoform 2)Ubiquitination-25.95-
226PhosphorylationLVQICEKYLPGYYSE
HHHHHHHHCCCCCHH		8.88-
230PhosphorylationCEKYLPGYYSEKLEA
HHHHCCCCCHHHHHE		11.24-
231PhosphorylationEKYLPGYYSEKLEAI
HHHCCCCCHHHHHEE		19.10-
232PhosphorylationKYLPGYYSEKLEAIQ
HHCCCCCHHHHHEEE		21.55-
258UbiquitinationKVSPVAHKHLSRQKI
HHCHHHHHHHCCCCC		36.18-
265 (in isoform 2)Ubiquitination-5.09-
317PhosphorylationLLKHALGSPEKVKAC
HHHHHHCCHHHHHHC		30.6428985074
322UbiquitinationLGSPEKVKACQGQYE
HCCHHHHHHCCCHHH		55.29-
328PhosphorylationVKACQGQYETIERLR
HHHCCCHHHHHHHHH		23.1228796482
329 (in isoform 2)Ubiquitination-35.11-
330PhosphorylationACQGQYETIERLRSL
HCCCHHHHHHHHHHC		24.1728796482
335PhosphorylationYETIERLRSLSPKIM
HHHHHHHHHCCHHHH		41.6027642862
336PhosphorylationETIERLRSLSPKIMQ
HHHHHHHHCCHHHHH		37.4826074081
338PhosphorylationIERLRSLSPKIMQEA
HHHHHHCCHHHHHHH		25.9526074081
357PhosphorylationEVVELPVTERQIERE
HHHCCCCCHHHHHHH		24.4228165663
383PhosphorylationRGELQCRSPPRLHGA
HCCCCCCCCCCCCCC		47.0523401153
390PhosphorylationSPPRLHGAKAILDAE
CCCCCCCCEEEECCC		6.3327251275
407PhosphorylationPRPALQPSPSIRLPL
CCCCCCCCCCEECCC		20.5129255136
409PhosphorylationPALQPSPSIRLPLDA
CCCCCCCCEECCCCC		25.3619664994
411MethylationLQPSPSIRLPLDAPL
CCCCCCEECCCCCCC		34.29115918261
414PhosphorylationSPSIRLPLDAPLPGS
CCCEECCCCCCCCCC		11.8227251275
416PhosphorylationSIRLPLDAPLPGSKA
CEECCCCCCCCCCCC		18.4027251275
421PhosphorylationLDAPLPGSKAKPKPP
CCCCCCCCCCCCCCC		27.7422199227
422UbiquitinationDAPLPGSKAKPKPPK
CCCCCCCCCCCCCCH		67.36-
433AcetylationKPPKQAQKEQRKQMK
CCCHHHHHHHHHHHC		59.857707179
437AcetylationQAQKEQRKQMKGRGQ
HHHHHHHHHHCCCCC		55.217707191
440AcetylationKEQRKQMKGRGQLEK
HHHHHHHCCCCCCCC		42.857707203
447AcetylationKGRGQLEKPPAPNQA
CCCCCCCCCCCCCCE		65.967460735
479PhosphorylationKDSAPKDSAPQDLAP
CCCCCCCCCCCCHHH		48.2325002506
489PhosphorylationQDLAPQVSAHHRSQE
CCHHHHHHHHHCCHH		19.3523312004
494PhosphorylationQVSAHHRSQESLTSQ
HHHHHHCCHHHCCCC		33.6622617229
496PhosphorylationSAHHRSQESLTSQES
HHHHCCHHHCCCCCC		49.3027251275
497PhosphorylationAHHRSQESLTSQESE
HHHCCHHHCCCCCCC		29.3425159151
499PhosphorylationHRSQESLTSQESEDT
HCCHHHCCCCCCCCC		37.3322115753
500PhosphorylationRSQESLTSQESEDTY
CCHHHCCCCCCCCCC		36.9225159151
501PhosphorylationSQESLTSQESEDTYL
CHHHCCCCCCCCCCC		53.6627251275
503PhosphorylationESLTSQESEDTYL--
HHCCCCCCCCCCC--		32.8925159151
504PhosphorylationSLTSQESEDTYL---
HCCCCCCCCCCC---		54.3327251275
506PhosphorylationTSQESEDTYL-----
CCCCCCCCCC-----		23.7530108239
507PhosphorylationSQESEDTYL------
CCCCCCCCC------		23.8030108239
510PhosphorylationSEDTYL---------
CCCCCC---------		27251275
514PhosphorylationYL-------------
CC-------------		27642862
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 TB10A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TB10A_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 TB10A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TB10A_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 TB10A_HUMAN

loading...

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-40 AND SER-503, AND MASSSPECTROMETRY.
"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-40 AND SER-43, 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-407, AND MASSSPECTROMETRY.

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