DPTOR_HUMAN - dbPTM
DPTOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPTOR_HUMAN
UniProt AC Q8TB45
Protein Name DEP domain-containing mTOR-interacting protein
Gene Name DEPTOR
Organism Homo sapiens (Human).
Sequence Length 409
Subcellular Localization
Protein Description Negative regulator of the mTORC1 and mTORC2 signaling pathways. Inhibits the kinase activity of both complexes..
Protein Sequence MEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPLDNEVKAFMRGQRLYEKLMSPENTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMEHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNEKSPSSQETHDSPFCLRKQSHDNRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLHVDYRTVSNLILTGPRTIVMEVMEELEC
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
1Acetylation-------MEEGGSTG
-------CCCCCCCC		10.7722814378
6Phosphorylation--MEEGGSTGSAGSD
--CCCCCCCCCCCCC		40.2123401153
7Phosphorylation-MEEGGSTGSAGSDS
-CCCCCCCCCCCCCC		38.1327251275
9PhosphorylationEEGGSTGSAGSDSST
CCCCCCCCCCCCCCC		29.5523401153
12PhosphorylationGSTGSAGSDSSTSGS
CCCCCCCCCCCCCCC		33.7523401153
14PhosphorylationTGSAGSDSSTSGSGG
CCCCCCCCCCCCCCH		36.8923401153
15PhosphorylationGSAGSDSSTSGSGGA
CCCCCCCCCCCCCHH		31.4225627689
17PhosphorylationAGSDSSTSGSGGAQQ
CCCCCCCCCCCHHHH		32.6724719451
19PhosphorylationSDSSTSGSGGAQQRE
CCCCCCCCCHHHHHH		33.5425849741
58UbiquitinationKDRRHHLKTYPNCFV
HCCHHHHHHCCCCHH		41.4729967540
59PhosphorylationDRRHHLKTYPNCFVA
CCHHHHHHCCCCHHH		51.0427251275
91UbiquitinationTAIKLMQKLADRGII
HHHHHHHHHHHCCCH		31.51-
131UbiquitinationFPLDNEVKAFMRGQR
CCCCHHHHHHHHHHH		29.7229967540
142UbiquitinationRGQRLYEKLMSPENT
HHHHHHHHHCCCCCC		35.61-
145PhosphorylationRLYEKLMSPENTLLQ
HHHHHHCCCCCCCCC		39.2328188228
149PhosphorylationKLMSPENTLLQPREE
HHCCCCCCCCCCCHH		27.4728188228
160UbiquitinationPREEEGVKYERTFMA
CCHHHCCCCEEEEEH		52.85-
164PhosphorylationEGVKYERTFMASEFL
HCCCCEEEEEHHHHH		13.0632142685
168PhosphorylationYERTFMASEFLDWLV
CEEEEEHHHHHHHHH		19.6622017875
234UbiquitinationLMELLNEKSPSSQET
HHHHHHCCCCCCCCC		67.60-
235PhosphorylationMELLNEKSPSSQETH
HHHHHCCCCCCCCCC		24.6823401153
237PhosphorylationLLNEKSPSSQETHDS
HHHCCCCCCCCCCCC		52.3123401153
238PhosphorylationLNEKSPSSQETHDSP
HHCCCCCCCCCCCCC		35.1122167270
241PhosphorylationKSPSSQETHDSPFCL
CCCCCCCCCCCCCCE		24.2823401153
244PhosphorylationSSQETHDSPFCLRKQ
CCCCCCCCCCCEEEC		16.5723401153
258PhosphorylationQSHDNRKSTSFMSVS
CCCCCCCCCCCEECC		26.5023401153
259PhosphorylationSHDNRKSTSFMSVSP
CCCCCCCCCCEECCC		29.0825159151
260PhosphorylationHDNRKSTSFMSVSPS
CCCCCCCCCEECCCC		26.4923401153
263PhosphorylationRKSTSFMSVSPSKEI
CCCCCCEECCCCCCE		19.8930278072
265PhosphorylationSTSFMSVSPSKEIKI
CCCCEECCCCCCEEE		19.0223401153
267PhosphorylationSFMSVSPSKEIKIVS
CCEECCCCCCEEEEE		35.1025159151
279PhosphorylationIVSAVRRSSMSSCGS
EEEEEHHHHCCCCCC		21.5923401153
280PhosphorylationVSAVRRSSMSSCGSS
EEEEHHHHCCCCCCC		22.3723401153
282PhosphorylationAVRRSSMSSCGSSGY
EEHHHHCCCCCCCCC		25.1526657352
283PhosphorylationVRRSSMSSCGSSGYF
EHHHHCCCCCCCCCC		17.5423401153
286PhosphorylationSSMSSCGSSGYFSSS
HHCCCCCCCCCCCCC		25.5626657352
287PhosphorylationSMSSCGSSGYFSSSP
HCCCCCCCCCCCCCC		23.8528348404
289PhosphorylationSSCGSSGYFSSSPTL
CCCCCCCCCCCCCCC		11.3923401153
291PhosphorylationCGSSGYFSSSPTLSS
CCCCCCCCCCCCCCC		22.7926657352
292PhosphorylationGSSGYFSSSPTLSSS
CCCCCCCCCCCCCCC		30.3628450419
293PhosphorylationSSGYFSSSPTLSSSP
CCCCCCCCCCCCCCC		22.2428450419
295PhosphorylationGYFSSSPTLSSSPPV
CCCCCCCCCCCCCCC		41.0228450419
297PhosphorylationFSSSPTLSSSPPVLC
CCCCCCCCCCCCCCC		31.1128450419
298PhosphorylationSSSPTLSSSPPVLCN
CCCCCCCCCCCCCCC		50.4028450419
299PhosphorylationSSPTLSSSPPVLCNP
CCCCCCCCCCCCCCC		29.8211230166
311UbiquitinationCNPKSVLKRPVTSEE
CCCHHHHCCCCCCHH		53.12-
315PhosphorylationSVLKRPVTSEELLTP
HHHCCCCCCHHHCCC		32.8626657352
316PhosphorylationVLKRPVTSEELLTPG
HHCCCCCCHHHCCCC		29.3428348404
321PhosphorylationVTSEELLTPGAPYAR
CCCHHHCCCCCCCCC		32.0924247654
348UbiquitinationGFVVRGSKPCHIQAV
CEEEECCCCCEEEEE		55.26-
387PhosphorylationVLHVDYRTVSNLILT
EEECEEEECCCCCCC		23.2723312004
389PhosphorylationHVDYRTVSNLILTGP
ECEEEECCCCCCCCC		25.8823312004
394PhosphorylationTVSNLILTGPRTIVM
ECCCCCCCCCCEEEE		37.8423312004
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
149TPhosphorylationKinaseCSNK1A1P48729
GPS
263SPhosphorylationKinaseCSNK1A1P48729
GPS
265SPhosphorylationKinaseMTORP42345
PSP
286SPhosphorylationKinaseCSNK1A1P48729
GPS
286SPhosphorylationKinaseRPS6KA1Q15418
GPS
286SPhosphorylationKinaseRPS6KB1P23443
GPS
286SPhosphorylationKinaseMTORP42345
PSP
287SPhosphorylationKinaseCSNK1A1P48729
GPS
287SPhosphorylationKinaseRPS6KA1Q15418
GPS
287SPhosphorylationKinaseRPS6KB1P23443
GPS
291SPhosphorylationKinaseCSNK1A1P48729
GPS
291SPhosphorylationKinaseRPS6KA1Q15418
GPS
291SPhosphorylationKinaseRPS6KB1P23443
GPS
293SPhosphorylationKinaseMTORP42345
PSP
295TPhosphorylationKinaseMTORP42345
PSP
299SPhosphorylationKinaseMTORP42345
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseSAGP10523
PMID:23136067
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPTOR_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 DPTOR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBW1A_HUMANBTRCphysical
22017877
MTOR_HUMANMTORphysical
22017877
MTOR_HUMANMTORphysical
22017875
LST8_HUMANMLST8physical
22017875
FBW1B_HUMANFBXW11physical
22017875
FBW1A_HUMANBTRCphysical
22017875
A4_HUMANAPPphysical
21832049
MTOR_HUMANMTORphysical
19446321
RPTOR_HUMANRPTORphysical
19446321
RICTR_HUMANRICTORphysical
19446321
CC110_HUMANCCDC110physical
25416956
FBW1A_HUMANBTRCphysical
21516116
TRI41_HUMANTRIM41physical
21516116
FBXW7_HUMANFBXW7physical
22017876
FBW1B_HUMANFBXW11physical
22017876
FBW1A_HUMANBTRCphysical
22017876
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 DPTOR_HUMAN

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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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"DEPTOR is an mTOR inhibitor frequently overexpressed in multiplemyeloma cells and required for their survival.";
Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A.,Kuehl W.M., Gray N.S., Sabatini D.M.;
Cell 137:873-886(2009).
Cited for: FUNCTION, INTERACTION WITH MTOR, INDUCTION, PHOSPHORYLATION ATTHR-241; SER-244; SER-258; THR-259; SER-263; SER-265; SER-282;SER-283; SER-287; SER-293; SER-297; SER-298 AND SER-299, AND MASSSPECTROMETRY.

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