TBC15_MOUSE - dbPTM
TBC15_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC15_MOUSE
UniProt AC Q9CXF4
Protein Name TBC1 domain family member 15
Gene Name Tbc1d15
Organism Mus musculus (Mouse).
Sequence Length 671
Subcellular Localization Cytoplasm .
Protein Description Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6..
Protein Sequence MAAAGVVSGKIIYEQEGVYIHSSCGKANDQDSLISGILRVLEKDAEVIVDWRPLDDALDSSSILCAGKDSSSVVEWTQAPKERAHRGSDQQSSYEAEWDMVTTVSFKKKPHTNGDAPGHRNGKSKWSFLFSLADLKSVKQSKEGMGWSYLVFCLKDDVMLPALHFHQGDSKLLIESLEKYVVLCESPQDSRTLLVNCQNKSLSQSFENLLDEPAYGLIQKIKKDPYTATMVGFSKVTNYIFDSLRGSDPSTHQRPPSEMADFLSDAIPGLKINQQEEPGFEVITRIDLGERPVVQRREPVSLEEWNKSLDPEGRLVAVESMKQKIFRGGLSHSLRKQAWKFLLGYFPWDSTKEERTQLQKQKTDEYFRMKLQWKSVSEAQEKRNSRLRDYRSLIEKDVNRTDRTNKFYEGQDNPGLILLHDILMTYCMYDFDLGYVQGMSDLLSPLLYVMENEVDAFWCFASYMDQMHQNFEEQMQGMKTQLIQLSTLLRLLDSGFCSYLESQDSGYLYFCFRWLLIRFKREFSFLDILRLWEVMWTELPCKNFHLLLCCAILESEKQQIMAKHYGFNEILKHINELSMKIDVEDILCKAEAISLQMAQCKELPQAVCEILGLQDSEITTPDSDTDENVGSPCPVSAFPSSTLPILAASEAKDDSPTQTLASPNACRLTPA
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		13.15-
8PhosphorylationMAAAGVVSGKIIYEQ
CCCCCEEECEEEEEE		31.7827841257
23PhosphorylationEGVYIHSSCGKANDQ
CCEEEECCCCCCCCH		16.84-
26UbiquitinationYIHSSCGKANDQDSL
EEECCCCCCCCHHHH		48.63-
32PhosphorylationGKANDQDSLISGILR
CCCCCHHHHHHHHHH		23.2126824392
35PhosphorylationNDQDSLISGILRVLE
CCHHHHHHHHHHHHH		25.6928833060
70PhosphorylationILCAGKDSSSVVEWT
EEECCCCCCCCCCHH		28.18-
72PhosphorylationCAGKDSSSVVEWTQA
ECCCCCCCCCCHHCC		33.8529514104
81UbiquitinationVEWTQAPKERAHRGS
CCHHCCCHHHHCCCC		63.95-
180PhosphorylationLIESLEKYVVLCESP
HHHHHHHEEEEECCC		6.0917203969
184S-palmitoylationLEKYVVLCESPQDSR
HHHEEEEECCCCCCC		3.0828526873
186PhosphorylationKYVVLCESPQDSRTL
HEEEEECCCCCCCEE		27.1922817900
190PhosphorylationLCESPQDSRTLLVNC
EECCCCCCCEEEECC		23.1728066266
192PhosphorylationESPQDSRTLLVNCQN
CCCCCCCEEEECCCC		28.5319060867
201PhosphorylationLVNCQNKSLSQSFEN
EECCCCCCHHHHHHH		40.5827087446
203PhosphorylationNCQNKSLSQSFENLL
CCCCCCHHHHHHHHH		30.7622942356
205PhosphorylationQNKSLSQSFENLLDE
CCCCHHHHHHHHHCC		31.0227087446
215PhosphorylationNLLDEPAYGLIQKIK
HHHCCCHHHHHHHHH		24.1526060331
220UbiquitinationPAYGLIQKIKKDPYT
CHHHHHHHHHCCCCC		49.88-
226PhosphorylationQKIKKDPYTATMVGF
HHHHCCCCCEEEEEE		21.0925367039
227PhosphorylationKIKKDPYTATMVGFS
HHHCCCCCEEEEEEH		22.5025367039
235UbiquitinationATMVGFSKVTNYIFD
EEEEEEHHHHHHHHH		51.31-
243PhosphorylationVTNYIFDSLRGSDPS
HHHHHHHHHCCCCCC		14.8228066266
251PhosphorylationLRGSDPSTHQRPPSE
HCCCCCCCCCCCCHH		27.6728576409
257PhosphorylationSTHQRPPSEMADFLS
CCCCCCCHHHHHHHH		42.5630482847
264PhosphorylationSEMADFLSDAIPGLK
HHHHHHHHHHCCCCC		25.62-
322UbiquitinationLVAVESMKQKIFRGG
EEEHHHHHHHHHHCC		58.69-
331PhosphorylationKIFRGGLSHSLRKQA
HHHHCCCCHHHHHHH		17.8228066266
333PhosphorylationFRGGLSHSLRKQAWK
HHCCCCHHHHHHHHH		26.8825159016
352UbiquitinationYFPWDSTKEERTQLQ
CCCCCCCHHHHHHHH		62.62-
366PhosphorylationQKQKTDEYFRMKLQW
HHHHCHHHHHHHHHC		10.17-
396UbiquitinationDYRSLIEKDVNRTDR
HHHHHHHHHCCCCCC		61.04-
440PhosphorylationLGYVQGMSDLLSPLL
CCCCCCHHHHHHHHH		31.75-
444PhosphorylationQGMSDLLSPLLYVME
CCHHHHHHHHHHHHH		22.31-
594PhosphorylationLCKAEAISLQMAQCK
HHHHHHHHHHHHHHH		21.4228059163
623PhosphorylationSEITTPDSDTDENVG
CCCCCCCCCCCCCCC		43.5421189417
625PhosphorylationITTPDSDTDENVGSP
CCCCCCCCCCCCCCC		49.5228059163
631PhosphorylationDTDENVGSPCPVSAF
CCCCCCCCCCCCCCC		21.0323649490
636PhosphorylationVGSPCPVSAFPSSTL
CCCCCCCCCCCCCCC		14.8823649490
640PhosphorylationCPVSAFPSSTLPILA
CCCCCCCCCCCCCCC		29.5123649490
641PhosphorylationPVSAFPSSTLPILAA
CCCCCCCCCCCCCCC		33.9123649490
655PhosphorylationASEAKDDSPTQTLAS
CCCCCCCCCCCCCCC		39.7225521595
657PhosphorylationEAKDDSPTQTLASPN
CCCCCCCCCCCCCCC		37.8325619855
659PhosphorylationKDDSPTQTLASPNAC
CCCCCCCCCCCCCCC		27.1125619855
662PhosphorylationSPTQTLASPNACRLT
CCCCCCCCCCCCCCC		23.0725521595
669PhosphorylationSPNACRLTPA-----
CCCCCCCCCC-----		9.6025619855
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC15_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TBC15_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBC15_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASSSPECTROMETRY.

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