TBC15_HUMAN - dbPTM
TBC15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC15_HUMAN
UniProt AC Q8TC07
Protein Name TBC1 domain family member 15
Gene Name TBC1D15
Organism Homo sapiens (Human).
Sequence Length 691
Subcellular Localization Cytoplasm.
Protein Description Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity)..
Protein Sequence MAAAGVVSGKIIYEQEGVYIHSSCGKTNDQDGLISGILRVLEKDAEVIVDWRPLDDALDSSSILYARKDSSSVVEWTQAPKERGHRGSEHLNSYEAEWDMVNTVSFKRKPHTNGDAPSHRNGKSKWSFLFSLTDLKSIKQNKEGMGWSYLVFCLKDDVVLPALHFHQGDSKLLIESLEKYVVLCESPQDKRTLLVNCQNKSLSQSFENLLDEPAYGLIQAGLLDRRKLLWAIHHWKKIKKDPYTATMIGFSKVTNYIFDSLRGSDPSTHQRPPSEMADFLSDAIPGLKINQQEEPGFEVITRIDLGERPVVQRREPVSLEEWTKNIDSEGRILNVDNMKQMIFRGGLSHALRKQAWKFLLGYFPWDSTKEERTQLQKQKTDEYFRMKLQWKSISQEQEKRNSRLRDYRSLIEKDVNRTDRTNKFYEGQDNPGLILLHDILMTYCMYDFDLGYVQGMSDLLSPLLYVMENEVDAFWCFASYMDQMHQNFEEQMQGMKTQLIQLSTLLRLLDSGFCSYLESQDSGYLYFCFRWLLIRFKREFSFLDILRLWEVMWTELPCTNFHLLLCCAILESEKQQIMEKHYGFNEILKHINELSMKIDVEDILCKAEAISLQMVKCKELPQAVCEILGLQGSEVTTPDSDVGEDENVVMTPCPTSAFQSNALPTLSASGARNDSPTQIPVSSDVCRLTPA
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
2Acetylation------MAAAGVVSG
------CCCCCEEEC		13.1519413330
6 (in isoform 3)Phosphorylation-2.3825850435
8PhosphorylationMAAAGVVSGKIIYEQ
CCCCCEEECEEEEEE		31.7820068231
8 (in isoform 3)Phosphorylation-31.7825850435
9 (in isoform 3)Phosphorylation-17.3625850435
10 (in isoform 3)Phosphorylation-20.5825850435
13PhosphorylationVVSGKIIYEQEGVYI
EEECEEEEEECCEEE		18.29-
14 (in isoform 3)Phosphorylation-31.5726552605
19PhosphorylationIYEQEGVYIHSSCGK
EEEECCEEEEECCCC		12.0827251275
22PhosphorylationQEGVYIHSSCGKTND
ECCEEEEECCCCCCC		20.1227251275
23PhosphorylationEGVYIHSSCGKTNDQ
CCEEEEECCCCCCCC		16.8427251275
26UbiquitinationYIHSSCGKTNDQDGL
EEEECCCCCCCCCCH		48.7821890473
34UbiquitinationTNDQDGLISGILRVL
CCCCCCHHHHHHHHH		4.3021890473
34 (in isoform 3)Ubiquitination-4.30-
43 (in isoform 2)Ubiquitination-59.06-
48UbiquitinationLEKDAEVIVDWRPLD
HHHCCCEEEECEECC		1.4321890473
48 (in isoform 1)Ubiquitination-1.4321890473
48 (in isoform 2)Ubiquitination-1.4321890473
65PhosphorylationLDSSSILYARKDSSS
CCCCCEEEEECCCCC		11.59-
68UbiquitinationSSILYARKDSSSVVE
CCEEEEECCCCCCEE		54.5121890473
68 (in isoform 2)Ubiquitination-54.51-
70PhosphorylationILYARKDSSSVVEWT
EEEEECCCCCCEEEC		27.7822167270
71PhosphorylationLYARKDSSSVVEWTQ
EEEECCCCCCEEECC		36.9722167270
72PhosphorylationYARKDSSSVVEWTQA
EEECCCCCCEEECCC		33.8522167270
73 (in isoform 3)Phosphorylation-4.9627642862
76UbiquitinationDSSSVVEWTQAPKER
CCCCCEEECCCCHHH		5.1221890473
77PhosphorylationSSSVVEWTQAPKERG
CCCCEEECCCCHHHC		11.0123403867
81UbiquitinationVEWTQAPKERGHRGS
EEECCCCHHHCCCCC		64.1621890473
81 (in isoform 2)Ubiquitination-64.16-
88PhosphorylationKERGHRGSEHLNSYE
HHHCCCCCCCHHHHH		23.0727251275
89UbiquitinationERGHRGSEHLNSYEA
HHCCCCCCCHHHHHH		56.0421890473
90UbiquitinationRGHRGSEHLNSYEAE
HCCCCCCCHHHHHHE		31.8221890473
90 (in isoform 1)Ubiquitination-31.8221890473
90 (in isoform 2)Ubiquitination-31.8221890473
93PhosphorylationRGSEHLNSYEAEWDM
CCCCCHHHHHHEEEE		30.6127251275
103UbiquitinationAEWDMVNTVSFKRKP
HEEEECCEEEECCCC		13.2021890473
103PhosphorylationAEWDMVNTVSFKRKP
HEEEECCEEEECCCC		13.2026074081
103 (in isoform 1)Ubiquitination-13.2021890473
103 (in isoform 2)Ubiquitination-13.2021890473
105PhosphorylationWDMVNTVSFKRKPHT
EEECCEEEECCCCCC		24.0228188228
107UbiquitinationMVNTVSFKRKPHTNG
ECCEEEECCCCCCCC		52.5921890473
107 (in isoform 2)Ubiquitination-52.59-
109UbiquitinationNTVSFKRKPHTNGDA
CEEEECCCCCCCCCC		41.5621906983
112PhosphorylationSFKRKPHTNGDAPSH
EECCCCCCCCCCCCC		49.8021130716
115UbiquitinationRKPHTNGDAPSHRNG
CCCCCCCCCCCCCCC		58.3321890473
125UbiquitinationSHRNGKSKWSFLFSL
CCCCCCCCCEEEEEH		50.79-
127PhosphorylationRNGKSKWSFLFSLTD
CCCCCCCEEEEEHHH		18.79-
129UbiquitinationGKSKWSFLFSLTDLK
CCCCCEEEEEHHHHH		2.0821890473
129 (in isoform 1)Ubiquitination-2.0821890473
129 (in isoform 2)Ubiquitination-2.0821890473
131PhosphorylationSKWSFLFSLTDLKSI
CCCEEEEEHHHHHHH		32.29-
131 (in isoform 1)Ubiquitination-32.2921890473
131 (in isoform 2)Ubiquitination-32.2921890473
171UbiquitinationHFHQGDSKLLIESLE
EECCCCCHHHHHHHH		52.64-
176PhosphorylationDSKLLIESLEKYVVL
CCHHHHHHHHHEEEE		34.5325693802
179UbiquitinationLLIESLEKYVVLCES
HHHHHHHHEEEEECC		48.95-
186PhosphorylationKYVVLCESPQDKRTL
HEEEEECCCCCCCEE		27.1921815630
190AcetylationLCESPQDKRTLLVNC
EECCCCCCCEEEECC		41.8727452117
190UbiquitinationLCESPQDKRTLLVNC
EECCCCCCCEEEECC		41.87-
190 (in isoform 2)Ubiquitination-41.87-
200 (in isoform 2)Ubiquitination-27.22-
201PhosphorylationLVNCQNKSLSQSFEN
EECCCCCCHHHHHHH		40.5823663014
201 (in isoform 2)Phosphorylation-40.5822167270
203PhosphorylationNCQNKSLSQSFENLL
CCCCCCHHHHHHHHH		30.7623663014
203 (in isoform 2)Phosphorylation-30.7622167270
205PhosphorylationQNKSLSQSFENLLDE
CCCCHHHHHHHHHCC		31.0223663014
205 (in isoform 2)Phosphorylation-31.0222167270
209 (in isoform 3)Phosphorylation-5.1222167270
211 (in isoform 3)Phosphorylation-64.1022167270
213 (in isoform 3)Phosphorylation-30.3722167270
215PhosphorylationNLLDEPAYGLIQAGL
HHHCCHHHHHHHHCC		24.1518707149
215 (in isoform 2)Phosphorylation-24.1525159151
220 (in isoform 2)Ubiquitination-12.01-
222 (in isoform 2)Ubiquitination-5.15-
223 (in isoform 2)Ubiquitination-4.75-
223 (in isoform 3)Phosphorylation-4.7525159151
226 (in isoform 2)Phosphorylation-33.3725159151
234 (in isoform 3)Phosphorylation-31.7525159151
235 (in isoform 2)Ubiquitination-6.89-
239UbiquitinationIHHWKKIKKDPYTAT
HHHHHHHCCCCCHHH		61.0621890473
240UbiquitinationHHWKKIKKDPYTATM
HHHHHHCCCCCHHHE		68.3721890473
242 (in isoform 2)Ubiquitination-36.9421890473
243PhosphorylationKKIKKDPYTATMIGF
HHHCCCCCHHHEEEE		21.09-
244PhosphorylationKIKKDPYTATMIGFS
HHCCCCCHHHEEEEH		22.5030631047
246PhosphorylationKKDPYTATMIGFSKV
CCCCCHHHEEEEHHH		11.0822210691
247 (in isoform 3)Phosphorylation-2.3327642862
254PhosphorylationMIGFSKVTNYIFDSL
EEEEHHHHHHHHHHH		26.4924719451
256PhosphorylationGFSKVTNYIFDSLRG
EEHHHHHHHHHHHCC		8.1329978859
260PhosphorylationVTNYIFDSLRGSDPS
HHHHHHHHHCCCCCC		14.8224719451
261 (in isoform 1)Ubiquitination-8.4921890473
262 (in isoform 1)Ubiquitination-46.6621890473
264PhosphorylationIFDSLRGSDPSTHQR
HHHHHCCCCCCCCCC		39.6623403867
267PhosphorylationSLRGSDPSTHQRPPS
HHCCCCCCCCCCCCH		43.4423403867
268PhosphorylationLRGSDPSTHQRPPSE
HCCCCCCCCCCCCHH		27.6723403867
271 (in isoform 2)Ubiquitination-37.18-
274PhosphorylationSTHQRPPSEMADFLS
CCCCCCCHHHHHHHH		42.5628348404
281PhosphorylationSEMADFLSDAIPGLK
HHHHHHHHHHCCCCC		25.6223403867
288UbiquitinationSDAIPGLKINQQEEP
HHHCCCCCCCCCCCC		45.5921906983
293 (in isoform 2)Ubiquitination-57.2921890473
307 (in isoform 2)Ubiquitination-62.20-
310 (in isoform 1)Ubiquitination-7.7921890473
322 (in isoform 2)Ubiquitination-11.87-
324UbiquitinationVSLEEWTKNIDSEGR
CCHHHHHCCCCCCCC		53.6421906983
329 (in isoform 2)Ubiquitination-49.0621890473
330UbiquitinationTKNIDSEGRILNVDN
HCCCCCCCCEECCCC		26.3621890473
339UbiquitinationILNVDNMKQMIFRGG
EECCCCHHHHHHHCC		42.8621890473
344UbiquitinationNMKQMIFRGGLSHAL
CHHHHHHHCCHHHHH		27.6121890473
344 (in isoform 2)Ubiquitination-27.6121890473
346 (in isoform 1)Ubiquitination-21.5421890473
352 (in isoform 2)Ubiquitination-29.80-
361 (in isoform 1)Ubiquitination-24.9621890473
369UbiquitinationYFPWDSTKEERTQLQ
CCCCCCCHHHHHHHH		62.6221906983
374 (in isoform 2)Ubiquitination-48.3821890473
379UbiquitinationRTQLQKQKTDEYFRM
HHHHHHHHCHHHHHH		66.05-
383PhosphorylationQKQKTDEYFRMKLQW
HHHHCHHHHHHHHHH		10.1722817900
387UbiquitinationTDEYFRMKLQWKSIS
CHHHHHHHHHHHCCC		33.02-
391UbiquitinationFRMKLQWKSISQEQE
HHHHHHHHCCCHHHH		25.58-
391 (in isoform 1)Ubiquitination-25.5821890473
394PhosphorylationKLQWKSISQEQEKRN
HHHHHCCCHHHHHHH		34.4527251275
396 (in isoform 2)Ubiquitination-54.65-
399UbiquitinationSISQEQEKRNSRLRD
CCCHHHHHHHHHHHH		57.48-
409PhosphorylationSRLRDYRSLIEKDVN
HHHHHHHHHHHHHCC		27.7224719451
413UbiquitinationDYRSLIEKDVNRTDR
HHHHHHHHHCCCCCC		61.0421906983
418 (in isoform 2)Ubiquitination-25.3221890473
435 (in isoform 1)Ubiquitination-4.1221890473
497PhosphorylationEQMQGMKTQLIQLST
HHHHHHHHHHHHHHH		21.5121406692
503PhosphorylationKTQLIQLSTLLRLLD
HHHHHHHHHHHHHHH		10.7121406692
504PhosphorylationTQLIQLSTLLRLLDS
HHHHHHHHHHHHHHH		38.1021406692
571UbiquitinationLLCCAILESEKQQIM
HHHHHHHHHHHHHHH		51.2221890473
572 (in isoform 2)Ubiquitination-46.80-
573 (in isoform 3)Phosphorylation-45.5727642862
580UbiquitinationEKQQIMEKHYGFNEI
HHHHHHHHHCCHHHH		25.4221890473
580UbiquitinationEKQQIMEKHYGFNEI
HHHHHHHHHCCHHHH		25.4221890473
582PhosphorylationQQIMEKHYGFNEILK
HHHHHHHCCHHHHHH		34.1825159151
585UbiquitinationMEKHYGFNEILKHIN
HHHHCCHHHHHHHHH		30.9121890473
585 (in isoform 2)Ubiquitination-30.9121890473
589UbiquitinationYGFNEILKHINELSM
CCHHHHHHHHHHHCC		48.3721890473
594UbiquitinationILKHINELSMKIDVE
HHHHHHHHCCCCCHH		5.3921890473
594 (in isoform 2)Ubiquitination-5.3921890473
597UbiquitinationHINELSMKIDVEDIL
HHHHHCCCCCHHHHH		32.17-
602 (in isoform 1)Ubiquitination-38.7221890473
606UbiquitinationDVEDILCKAEAISLQ
CHHHHHHHHHHHHHE		45.90-
611PhosphorylationLCKAEAISLQMVKCK
HHHHHHHHHEEECCC		21.4220068231
611 (in isoform 1)Ubiquitination-21.4221890473
616UbiquitinationAISLQMVKCKELPQA
HHHHEEECCCHHHHH		33.96-
618UbiquitinationSLQMVKCKELPQAVC
HHEEECCCHHHHHHH		57.47-
633PhosphorylationEILGLQGSEVTTPDS
HHHCCCCCEEECCCC		18.8820068231
636PhosphorylationGLQGSEVTTPDSDVG
CCCCCEEECCCCCCC		28.6728348404
637PhosphorylationLQGSEVTTPDSDVGE
CCCCEEECCCCCCCC		30.2127251275
640PhosphorylationSEVTTPDSDVGEDEN
CEEECCCCCCCCCCC		35.0927251275
651PhosphorylationEDENVVMTPCPTSAF
CCCCEEEEECCCHHH		15.3228348404
660PhosphorylationCPTSAFQSNALPTLS
CCCHHHHCCCCCCCC		20.02-
665PhosphorylationFQSNALPTLSASGAR
HHCCCCCCCCCCCCC		33.9125332170
669PhosphorylationALPTLSASGARNDSP
CCCCCCCCCCCCCCC		29.6125332170
675PhosphorylationASGARNDSPTQIPVS
CCCCCCCCCCCCCCC		33.1419664994
677PhosphorylationGARNDSPTQIPVSSD
CCCCCCCCCCCCCCC		42.9822167270
682O-linked_GlycosylationSPTQIPVSSDVCRLT
CCCCCCCCCCCCCCC		18.5730379171
682PhosphorylationSPTQIPVSSDVCRLT
CCCCCCCCCCCCCCC		18.5723927012
683PhosphorylationPTQIPVSSDVCRLTP
CCCCCCCCCCCCCCC		34.0125159151
689PhosphorylationSSDVCRLTPA-----
CCCCCCCCCC-----		9.6025159151
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 TBC15_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC15_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 TBC15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB5A_HUMANRAB5Aphysical
16923123
RAB5B_HUMANRAB5Bphysical
16923123
RAB5C_HUMANRAB5Cphysical
16923123
FIS1_HUMANFIS1physical
23077178
ARFP1_HUMANARFIP1physical
22863883
VATC1_HUMANATP6V1C1physical
22863883
DNM1L_HUMANDNM1Lphysical
22863883
IDE_HUMANIDEphysical
22863883
PSMG3_HUMANPSMG3physical
22863883
GLYM_HUMANSHMT2physical
22863883
SNX2_HUMANSNX2physical
22863883
STAT3_HUMANSTAT3physical
22863883
VP26A_HUMANVPS26Aphysical
22863883
CEP63_HUMANCEP63physical
25416956
CEP63_HUMANCEP63physical
21516116
UBXN8_HUMANUBXN8physical
26389662
GRAM4_HUMANGRAMD4physical
28514442
TBC17_HUMANTBC1D17physical
28514442
ATF6B_HUMANATF6Bphysical
28514442
MRS2_HUMANMRS2physical
28514442
DYN1_HUMANDNM1physical
28514442
UTP15_HUMANUTP15physical
28514442
ZNT9_HUMANSLC30A9physical
28514442
UBXN8_HUMANUBXN8physical
28514442
DYN2_HUMANDNM2physical
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 TBC15_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-675, AND MASS SPECTROMETRY.
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-70; SER-205 AND TYR-215,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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-675, AND MASS SPECTROMETRY.
"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-70; SER-675 AND THR-689,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND THR-689, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, 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-675, 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-675, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215, AND MASSSPECTROMETRY.

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