TBC16_HUMAN - dbPTM
TBC16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC16_HUMAN
UniProt AC Q8TBP0
Protein Name TBC1 domain family member 16
Gene Name TBC1D16
Organism Homo sapiens (Human).
Sequence Length 767
Subcellular Localization
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MSLGRLLRRASSKASDLLTLTPGGSGSGSPSVLDGEIIYSKNNVCVHPPEGLQGLGEHHPGYLCLYMEKDEMLGATLILAWVPNSRIQRQDEEALRYITPESSPVRKAPRPRGRRTRSSGASHQPSPTELRPTLTPKDEDILVVAQSVPDRMLASPAPEDEEKLAQGLGVDGAQPASQPACSPSGILSTVSPQDVTEEGREPRPEAGEEDGSLELSAEGVSRDSSFDSDSDTFSSPFCLSPISAALAESRGSVFLESDSSPPSSSDAGLRFPDSNGLLQTPRWDEPQRVCALEQICGVFRVDLGHMRSLRLFFSDEACTSGQLVVASRESQYKVFHFHHGGLDKLSDVFQQWKYCTEMQLKDQQVAPDKTCMQFSIRRPKLPSSETHPEESMYKRLGVSAWLNHLNELGQVEEEYKLRKAIFFGGIDVSIRGEVWPFLLRYYSHESTSEEREALRLQKRKEYSEIQQKRLSMTPEEHRAFWRNVQFTVDKDVVRTDRNNQFFRGEDNPNVESMRRILLNYAVYNPAVGYSQGMSDLVAPILAEVLDESDTFWCFVGLMQNTIFVSSPRDEDMEKQLLYLRELLRLTHVRFYQHLVSLGEDGLQMLFCHRWLLLCFKREFPEAEALRIWEACWAHYQTDYFHLFICVAIVAIYGDDVIEQQLATDQMLLHFGNLAMHMNGELVLRKARSLLYQFRLLPRIPCSLHDLCKLCGSGMWDSGSMPAVECTGHHPGSESCPYGGTVEMPSPKSLREGKKGPKTPQDGFGFRR
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
11PhosphorylationGRLLRRASSKASDLL
HHHHHHHHHCCHHCE		30.4728857561
12PhosphorylationRLLRRASSKASDLLT
HHHHHHHHCCHHCEE		31.1233259812
15PhosphorylationRRASSKASDLLTLTP
HHHHHCCHHCEEECC		32.3128857561
19PhosphorylationSKASDLLTLTPGGSG
HCCHHCEEECCCCCC		35.5630624053
21PhosphorylationASDLLTLTPGGSGSG
CHHCEEECCCCCCCC		18.0430624053
22PhosphorylationSDLLTLTPGGSGSGS
HHCEEECCCCCCCCC		48.5432142685
25PhosphorylationLTLTPGGSGSGSPSV
EEECCCCCCCCCCCC		35.3827732954
27PhosphorylationLTPGGSGSGSPSVLD
ECCCCCCCCCCCCCC		37.4830624053
29PhosphorylationPGGSGSGSPSVLDGE
CCCCCCCCCCCCCCE		18.7230624053
31PhosphorylationGSGSGSPSVLDGEII
CCCCCCCCCCCCEEE		36.6927732954
39PhosphorylationVLDGEIIYSKNNVCV
CCCCEEEEECCCEEE		21.1827732954
40PhosphorylationLDGEIIYSKNNVCVH
CCCEEEEECCCEEEC		20.6427732954
85UbiquitinationILAWVPNSRIQRQDE
EEEECCCHHHHCCCH		25.3729967540
97PhosphorylationQDEEALRYITPESSP
CCHHHHHHCCCCCCC		15.2528450419
98UbiquitinationDEEALRYITPESSPV
CHHHHHHCCCCCCCC		4.1329967540
99PhosphorylationEEALRYITPESSPVR
HHHHHHCCCCCCCCC		16.4522167270
102PhosphorylationLRYITPESSPVRKAP
HHHCCCCCCCCCCCC		40.9429255136
103PhosphorylationRYITPESSPVRKAPR
HHCCCCCCCCCCCCC		26.2529255136
116PhosphorylationPRPRGRRTRSSGASH
CCCCCCCCCCCCCCC		33.2823312004
118PhosphorylationPRGRRTRSSGASHQP
CCCCCCCCCCCCCCC		32.2930266825
119PhosphorylationRGRRTRSSGASHQPS
CCCCCCCCCCCCCCC		34.7830266825
122PhosphorylationRTRSSGASHQPSPTE
CCCCCCCCCCCCCCC		26.6130266825
126PhosphorylationSGASHQPSPTELRPT
CCCCCCCCCCCCCCC		37.5721406692
128PhosphorylationASHQPSPTELRPTLT
CCCCCCCCCCCCCCC		52.5728857561
133PhosphorylationSPTELRPTLTPKDED
CCCCCCCCCCCCCCC		36.5128857561
135PhosphorylationTELRPTLTPKDEDIL
CCCCCCCCCCCCCEE		30.6728857561
147PhosphorylationDILVVAQSVPDRMLA
CEEEEEECCCCHHCC		26.3625921289
155PhosphorylationVPDRMLASPAPEDEE
CCCHHCCCCCCCCHH		20.0329255136
216PhosphorylationEDGSLELSAEGVSRD
CCCCEEECEECCCCC		18.2026471730
221PhosphorylationELSAEGVSRDSSFDS
EECEECCCCCCCCCC		41.0226471730
224PhosphorylationAEGVSRDSSFDSDSD
EECCCCCCCCCCCCC		31.6228102081
225PhosphorylationEGVSRDSSFDSDSDT
ECCCCCCCCCCCCCC		37.0428102081
228PhosphorylationSRDSSFDSDSDTFSS
CCCCCCCCCCCCCCC		36.6828348404
230PhosphorylationDSSFDSDSDTFSSPF
CCCCCCCCCCCCCCC		42.3728348404
232PhosphorylationSFDSDSDTFSSPFCL
CCCCCCCCCCCCCCC		29.3928348404
234PhosphorylationDSDSDTFSSPFCLSP
CCCCCCCCCCCCCCH		38.9128348404
235PhosphorylationSDSDTFSSPFCLSPI
CCCCCCCCCCCCCHH		20.1528348404
240PhosphorylationFSSPFCLSPISAALA
CCCCCCCCHHHHHHH		22.7427251275
252PhosphorylationALAESRGSVFLESDS
HHHHHCCCEEEECCC		14.4823090842
257PhosphorylationRGSVFLESDSSPPSS
CCCEEEECCCCCCCC		44.9628985074
259PhosphorylationSVFLESDSSPPSSSD
CEEEECCCCCCCCCC		54.7629255136
260PhosphorylationVFLESDSSPPSSSDA
EEEECCCCCCCCCCC		45.9129255136
263PhosphorylationESDSSPPSSSDAGLR
ECCCCCCCCCCCCCC		45.9529255136
264PhosphorylationSDSSPPSSSDAGLRF
CCCCCCCCCCCCCCC		37.7029978859
265PhosphorylationDSSPPSSSDAGLRFP
CCCCCCCCCCCCCCC		35.5026699800
375PhosphorylationDKTCMQFSIRRPKLP
CCCCEEEEECCCCCC		9.7828857561
383PhosphorylationIRRPKLPSSETHPEE
ECCCCCCCCCCCCCH		51.7722617229
384PhosphorylationRRPKLPSSETHPEES
CCCCCCCCCCCCCHH		44.5723403867
386PhosphorylationPKLPSSETHPEESMY
CCCCCCCCCCCHHHH		44.6823403867
391PhosphorylationSETHPEESMYKRLGV
CCCCCCHHHHHHHCH		26.2525002506
393PhosphorylationTHPEESMYKRLGVSA
CCCCHHHHHHHCHHH		11.3921214269
394UbiquitinationHPEESMYKRLGVSAW
CCCHHHHHHHCHHHH		32.29-
429PhosphorylationFFGGIDVSIRGEVWP
HCCCCCEEECCCHHH		11.65-
460UbiquitinationALRLQKRKEYSEIQQ
HHHHHHHHHHHHHHH		68.9529967540
463PhosphorylationLQKRKEYSEIQQKRL
HHHHHHHHHHHHHHH		29.3427135362
471PhosphorylationEIQQKRLSMTPEEHR
HHHHHHHCCCHHHHH		25.3322964224
473PhosphorylationQQKRLSMTPEEHRAF
HHHHHCCCHHHHHHH		24.9522964224
490UbiquitinationNVQFTVDKDVVRTDR
HCEEEECCCCEECCC		48.35-
566PhosphorylationQNTIFVSSPRDEDME
CCEEEECCCCCHHHH		20.7424719451
745PhosphorylationGGTVEMPSPKSLREG
CCEEECCCCHHHCCC		43.5827422710
758PhosphorylationEGKKGPKTPQDGFGF
CCCCCCCCCCCCCCC		29.3421815630
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 TBC16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC16_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 TBC16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C40_HUMANKRT40physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CATC_HUMANCTSCphysical
26496610
TIM_HUMANTIMELESSphysical
26496610
SYNE2_HUMANSYNE2physical
26496610
TTLL6_HUMANTTLL6physical
26496610
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 TBC16_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-99 AND SER-103, AND MASSSPECTROMETRY.

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