TBCD9_HUMAN - dbPTM
TBCD9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBCD9_HUMAN
UniProt AC Q6ZT07
Protein Name TBC1 domain family member 9
Gene Name TBC1D9
Organism Homo sapiens (Human).
Sequence Length 1266
Subcellular Localization
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MWVNPEEVLLANALWITERANPYFILQRRKGHAGDGGGGGGLAGLLVGTLDVVLDSSARVAPYRILYQTPDSLVYWTIACGGSRKEITEHWEWLEQNLLQTLSIFENENDITTFVRGKIQGIIAEYNKINDVKEDDDTEKFKEAIVKFHRLFGMPEEEKLVNYYSCSYWKGKVPRQGWMYLSINHLCFYSFLMGREAKLVIRWVDITQLEKNATLLLPDVIKVSTRSSEHFFSVFLNINETFKLMEQLANIAMRQLLDNEGFEQDRSLPKLKRKSPKKVSALKRDLDARAKSERYRALFRLPKDEKLDGHTDCTLWTPFNKMHILGQMFVSTNYICFTSKEENLCSLIIPLREVTIVEKADSSSVLPSPLSISTRNRMTFLFANLKDRDFLVQRISDFLQQTTSKIYSDKEFAGSYNSSDDEVYSRPSSLVSSSPQRSTSSDADGERQFNLNGNSVPTATQTLMTMYRRRSPEEFNPKLAKEFLKEQAWKIHFAEYGQGICMYRTEKTRELVLKGIPESMRGELWLLLSGAINEKATHPGYYEDLVEKSMGKYNLATEEIERDLHRSLPEHPAFQNEMGIAALRRVLTAYAFRNPNIGYCQAMNIVTSVLLLYAKEEEAFWLLVALCERMLPDYYNTRVVGALVDQGVFEELARDYVPQLYDCMQDLGVISTISLSWFLTLFLSVMPFESAVVVVDCFFYEGIKVIFQLALAVLDANVDKLLNCKDDGEAMTVLGRYLDSVTNKDSTLPPIPHLHSLLSDDVEPYPEVDIFRLIRTSYEKFGTIRADLIEQMRFKQRLKVIQTLEDTTKRNVVRTIVTETSFTIDELEELYALFKAEHLTSCYWGGSSNALDRHDPSLPYLEQYRIDFEQFKGMFALLFPWACGTHSDVLASRLFQLLDENGDSLINFREFVSGLSAACHGDLTEKLKLLYKMHVLPEPSSDQDEPDSAFEATQYFFEDITPECTHVVGLDSRSKQGADDGFVTVSLKPDKGKRANSQENRNYLRLWTPENKSKSKNAKDLPKLNQGQFIELCKTMYNMFSEDPNEQELYHATAAVTSLLLEIGEVGKLFVAQPAKEGGSGGSGPSCHQGIPGVLFPKKGPGQPYVVESVEPLPASLAPDSEEHSLGGQMEDIKLEDSSPRDNGACSSMLISDDDTKDDSSMSSYSVLSAGSHEEDKLHCEDIGEDTVLVRSGQGTAALPRSTSLDRDWAITFEQFLASLLTEPALVKYFDKPVCMMARITSAKNIRMMGKPLTSASDYEISAMSG
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
267PhosphorylationEGFEQDRSLPKLKRK
CCCCCCCCCHHHCCC		58.2625849741
280PhosphorylationRKSPKKVSALKRDLD
CCCHHHHHHHHHHHH		36.44-
355PhosphorylationIIPLREVTIVEKADS
EEEECEEEEEEECCC		17.98-
362PhosphorylationTIVEKADSSSVLPSP
EEEEECCCCCCCCCC		29.40-
402PhosphorylationISDFLQQTTSKIYSD
HHHHHHHHHHHHCCC		21.7828348404
403PhosphorylationSDFLQQTTSKIYSDK
HHHHHHHHHHHCCCH		24.5528348404
404PhosphorylationDFLQQTTSKIYSDKE
HHHHHHHHHHCCCHH		22.0528348404
405UbiquitinationFLQQTTSKIYSDKEF
HHHHHHHHHCCCHHH		43.5032015554
415PhosphorylationSDKEFAGSYNSSDDE
CCHHHCCCCCCCCCC		20.0825849741
416PhosphorylationDKEFAGSYNSSDDEV
CHHHCCCCCCCCCCC		20.3922199227
418PhosphorylationEFAGSYNSSDDEVYS
HHCCCCCCCCCCCCC		27.2325849741
419PhosphorylationFAGSYNSSDDEVYSR
HCCCCCCCCCCCCCC		45.5020363803
424PhosphorylationNSSDDEVYSRPSSLV
CCCCCCCCCCCHHHC		9.2728450419
425PhosphorylationSSDDEVYSRPSSLVS
CCCCCCCCCCHHHCC		42.7827251275
428PhosphorylationDEVYSRPSSLVSSSP
CCCCCCCHHHCCCCC		34.8827251275
429PhosphorylationEVYSRPSSLVSSSPQ
CCCCCCHHHCCCCCC		35.1627251275
432PhosphorylationSRPSSLVSSSPQRST
CCCHHHCCCCCCCCC		30.3229255136
433PhosphorylationRPSSLVSSSPQRSTS
CCHHHCCCCCCCCCC		38.2625849741
434PhosphorylationPSSLVSSSPQRSTSS
CHHHCCCCCCCCCCC		19.9725849741
438PhosphorylationVSSSPQRSTSSDADG
CCCCCCCCCCCCCCC		27.65-
441PhosphorylationSPQRSTSSDADGERQ
CCCCCCCCCCCCCEE		36.59-
458PhosphorylationLNGNSVPTATQTLMT
CCCCCCCCHHHHHHH		39.9329978859
460PhosphorylationGNSVPTATQTLMTMY
CCCCCCHHHHHHHHH		25.2729978859
462PhosphorylationSVPTATQTLMTMYRR
CCCCHHHHHHHHHHH		17.7229978859
465PhosphorylationTATQTLMTMYRRRSP
CHHHHHHHHHHHCCH		17.7329978859
467PhosphorylationTQTLMTMYRRRSPEE
HHHHHHHHHHCCHHH		7.5729978859
471PhosphorylationMTMYRRRSPEEFNPK
HHHHHHCCHHHHCHH		34.5523927012
4812-HydroxyisobutyrylationEFNPKLAKEFLKEQA
HHCHHHHHHHHHHCC		60.48-
496PhosphorylationWKIHFAEYGQGICMY
CEEEEHHCCCCEEEE		16.00-
552UbiquitinationLVEKSMGKYNLATEE
HHHHHHCCCCCCHHH		23.4821890473
588PhosphorylationAALRRVLTAYAFRNP
HHHHHHHHHHHHHCC		18.1122210691
608PhosphorylationQAMNIVTSVLLLYAK
HHHHHHHHHHHHHHC		10.4022210691
613PhosphorylationVTSVLLLYAKEEEAF
HHHHHHHHHCHHHHH		18.6522210691
725UbiquitinationVDKLLNCKDDGEAMT
HHHHHCCCCCHHHHH		58.7532015554
809UbiquitinationQTLEDTTKRNVVRTI
HHHCHHCHHCCEEEE		44.0332142685
847PhosphorylationTSCYWGGSSNALDRH
CCCCCCCCCCCHHCC		19.2425849741
974PhosphorylationVVGLDSRSKQGADDG
EEECCCCCCCCCCCC		33.0324719451
975UbiquitinationVGLDSRSKQGADDGF
EECCCCCCCCCCCCC		52.2029967540
988UbiquitinationGFVTVSLKPDKGKRA
CCEEEEECCCCCCCC		43.6032142685
997PhosphorylationDKGKRANSQENRNYL
CCCCCCCCHHCCCCH		37.5815302935
1008PhosphorylationRNYLRLWTPENKSKS
CCCHHCCCCCCCCCC		25.8926270265
1012UbiquitinationRLWTPENKSKSKNAK
HCCCCCCCCCCCCHH		58.5632015554
1121PhosphorylationPASLAPDSEEHSLGG
CCCCCCCCCCCCCCC		43.7728348404
1125PhosphorylationAPDSEEHSLGGQMED
CCCCCCCCCCCCCEE		31.8028348404
1138PhosphorylationEDIKLEDSSPRDNGA
EEEECCCCCCCCCCC		32.6329255136
1139PhosphorylationDIKLEDSSPRDNGAC
EEECCCCCCCCCCCC		35.9525849741
1152PhosphorylationACSSMLISDDDTKDD
CCCCEEECCCCCCCC		30.9025849741
1160PhosphorylationDDDTKDDSSMSSYSV
CCCCCCCCCCCCEEE		37.7728348404
1161PhosphorylationDDTKDDSSMSSYSVL
CCCCCCCCCCCEEEH		29.6728348404
1163PhosphorylationTKDDSSMSSYSVLSA
CCCCCCCCCEEEHHC		28.2428348404
1164PhosphorylationKDDSSMSSYSVLSAG
CCCCCCCCEEEHHCC		16.8828348404
1166PhosphorylationDSSMSSYSVLSAGSH
CCCCCCEEEHHCCCC		20.6628348404
1172PhosphorylationYSVLSAGSHEEDKLH
EEEHHCCCCCCCCCC		27.6925849741
1192PhosphorylationEDTVLVRSGQGTAAL
CCEEEEECCCCCEEC		28.1725849741
1196PhosphorylationLVRSGQGTAALPRST
EEECCCCCEECCCCC		10.8129449344
1254PhosphorylationRMMGKPLTSASDYEI
CCCCCCCCCHHHHCH		30.6727251275
1255PhosphorylationMMGKPLTSASDYEIS
CCCCCCCCHHHHCHH		33.2027251275
1257PhosphorylationGKPLTSASDYEISAM
CCCCCCHHHHCHHCC		40.2627251275
1259PhosphorylationPLTSASDYEISAMSG
CCCCHHHHCHHCCCC		16.8024719451
1262PhosphorylationSASDYEISAMSG---
CHHHHCHHCCCC---		13.1324719451
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 TBCD9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBCD9_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 TBCD9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRIC3_HUMANPRICKLE3physical
26496610
SRSF2_HUMANSRSF2physical
26496610
RUXE_HUMANSNRPEphysical
26496610
LA_HUMANSSBphysical
26496610
YMEL1_HUMANYME1L1physical
26496610
DDX41_HUMANDDX41physical
26496610
PR38B_HUMANPRPF38Bphysical
26496610
ABHGA_HUMANABHD16Aphysical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
PP4P2_HUMANTMEM55Aphysical
28514442
MRS2_HUMANMRS2physical
28514442
CPT1A_HUMANCPT1Aphysical
28514442
MUL1_HUMANMUL1physical
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 TBCD9_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-997, AND MASSSPECTROMETRY.

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