TBC9B_HUMAN - dbPTM
TBC9B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC9B_HUMAN
UniProt AC Q66K14
Protein Name TBC1 domain family member 9B
Gene Name TBC1D9B
Organism Homo sapiens (Human).
Sequence Length 1250
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MWLSPEEVLVANALWVTERANPFFVLQRRRGHGRGGGLTGLLVGTLDVVLDSSARVAPYRILHQTQDSQVYWTVACGSSRKEITKHWEWLENNLLQTLSIFDSEEDITTFVKGKIHGIIAEENKNLQPQGDEDPGKFKEAELKMRKQFGMPEGEKLVNYYSCSYWKGRVPRQGWLYLTVNHLCFYSFLLGKEVSLVVQWVDITRLEKNATLLFPESIRVDTRDQELFFSMFLNIGETFKLMEQLANLAMRQLLDSEGFLEDKALPRPIRPHRNISALKRDLDARAKNECYRATFRLPRDERLDGHTSCTLWTPFNKLHIPGQMFISNNYICFASKEEDACHLIIPLREVTIVEKADSSSVLPSPLSISTKSKMTFLFANLKDRDFLVQRISDFLQKTPSKQPGSIGSRKASVVDPSTESSPAPQEGSEQPASPASPLSSRQSFCAQEAPTASQGLLKLFQKNSPMEDLGAKGAKEKMKEESWHIHFFEYGRGVCMYRTAKTRALVLKGIPESLRGELWLLFSGAWNEMVTHPGYYAELVEKSTGKYSLATEEIERDLHRSMPEHPAFQNELGIAALRRVLTAYAFRNPTIGYCQAMNIVTSVLLLYGSEEEAFWLLVALCERMLPDYYNTRVVGALVDQGIFEELTRDFLPQLSEKMQDLGVISSISLSWFLTLFLSVMPFESAVVIVDCFFYEGIKVILQVALAVLDANMEQLLGCSDEGEAMTMLGRYLDNVVNKQSVSPPIPHLRALLSSSDDPPAEVDIFELLKVSYEKFSSLRAEDIEQMRFKQRLKVIQSLEDTAKRSVVRAIPVDIGFSIEELEDLYMVFKAKHLASQYWGCSRTMAGRRDPSLPYLEQYRIDASQFRELFASLTPWACGSHTPLLAGRMFRLLDENKDSLINFKEFVTGMSGMYHGDLTEKLKVLYKLHLPPALSPEEAESALEAAHYFTEDSSSEASPLASDLDLFLPWEAQEALPQEEQEGSGSEERGEEKGTSSPDYRHYLRMWAKEKEAQKETIKDLPKMNQEQFIELCKTLYNMFSEDPMEQDLYHAIATVASLLLRIGEVGKKFSARTGRKPRDCATEEDEPPAPELHQDAARELQPPAAGDPQAKAGGDTHLGKAPQESQVVVEGGSGEGQGSPSQLLSDDETKDDMSMSSYSVVSTGSLQCEDLADDTVLVGGEACSPTARIGGTVDTDWCISFEQILASILTESVLVNFFEKRVDIGLKIKDQKKVERQFSTASDHEQPGVSG
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
34MethylationQRRRGHGRGGGLTGL
ECCCCCCCCCCHHHH
34.6054559877
39PhosphorylationHGRGGGLTGLLVGTL
CCCCCCHHHHHHHHH
29.11-
65PhosphorylationPYRILHQTQDSQVYW
CEEEEEECCCCCEEE
24.4828450419
68PhosphorylationILHQTQDSQVYWTVA
EEEECCCCCEEEEEE
16.2428450419
73PhosphorylationQDSQVYWTVACGSSR
CCCCEEEEEEECCCH
4.7928450419
78PhosphorylationYWTVACGSSRKEITK
EEEEEECCCHHHHHH
27.1828450419
79PhosphorylationWTVACGSSRKEITKH
EEEEECCCHHHHHHH
32.4328450419
114UbiquitinationITTFVKGKIHGIIAE
HHHHHHCEEEEEEEC
26.30-
124UbiquitinationGIIAEENKNLQPQGD
EEEECCCCCCCCCCC
63.41-
136UbiquitinationQGDEDPGKFKEAELK
CCCCCCCCHHHHHHH
59.66-
146AcetylationEAELKMRKQFGMPEG
HHHHHHHHHHCCCCC
46.627823187
262UbiquitinationSEGFLEDKALPRPIR
CCCCCCCCCCCCCCC
42.31-
275PhosphorylationIRPHRNISALKRDLD
CCCCCCHHHHHHHHH
30.9723401153
278UbiquitinationHRNISALKRDLDARA
CCCHHHHHHHHHHHH
43.51-
350PhosphorylationIIPLREVTIVEKADS
EEECCEEEEEEECCC
17.9830206219
357PhosphorylationTIVEKADSSSVLPSP
EEEEECCCCCCCCCC
29.4030206219
358PhosphorylationIVEKADSSSVLPSPL
EEEECCCCCCCCCCC
25.6430206219
359PhosphorylationVEKADSSSVLPSPLS
EEECCCCCCCCCCCE
31.4630206219
363PhosphorylationDSSSVLPSPLSISTK
CCCCCCCCCCEECCC
34.0230206219
366PhosphorylationSVLPSPLSISTKSKM
CCCCCCCEECCCCCE
20.2030206219
368PhosphorylationLPSPLSISTKSKMTF
CCCCCEECCCCCEEE
26.8030206219
369PhosphorylationPSPLSISTKSKMTFL
CCCCEECCCCCEEEE
37.3530206219
371PhosphorylationPLSISTKSKMTFLFA
CCEECCCCCEEEEEC
27.96-
374PhosphorylationISTKSKMTFLFANLK
ECCCCCEEEEECCCC
22.4130576142
391PhosphorylationDFLVQRISDFLQKTP
HHHHHHHHHHHHHCC
25.2123927012
396AcetylationRISDFLQKTPSKQPG
HHHHHHHHCCCCCCC
65.6319815011
397PhosphorylationISDFLQKTPSKQPGS
HHHHHHHCCCCCCCC
21.6023927012
399PhosphorylationDFLQKTPSKQPGSIG
HHHHHCCCCCCCCCC
49.5123403867
400AcetylationFLQKTPSKQPGSIGS
HHHHCCCCCCCCCCC
62.8119815021
400UbiquitinationFLQKTPSKQPGSIGS
HHHHCCCCCCCCCCC
62.81-
404PhosphorylationTPSKQPGSIGSRKAS
CCCCCCCCCCCCEEE
30.3823927012
407PhosphorylationKQPGSIGSRKASVVD
CCCCCCCCCEEEECC
29.0123927012
411PhosphorylationSIGSRKASVVDPSTE
CCCCCEEEECCCCCC
26.2129255136
416PhosphorylationKASVVDPSTESSPAP
EEEECCCCCCCCCCC
40.1029255136
417PhosphorylationASVVDPSTESSPAPQ
EEECCCCCCCCCCCC
45.3229255136
419PhosphorylationVVDPSTESSPAPQEG
ECCCCCCCCCCCCCC
41.5330266825
420PhosphorylationVDPSTESSPAPQEGS
CCCCCCCCCCCCCCC
20.8830266825
427PhosphorylationSPAPQEGSEQPASPA
CCCCCCCCCCCCCCC
32.1030266825
432PhosphorylationEGSEQPASPASPLSS
CCCCCCCCCCCCCCC
27.9029255136
435PhosphorylationEQPASPASPLSSRQS
CCCCCCCCCCCCCCC
29.7429255136
438PhosphorylationASPASPLSSRQSFCA
CCCCCCCCCCCCHHC
27.1930266825
439PhosphorylationSPASPLSSRQSFCAQ
CCCCCCCCCCCHHCC
41.8629255136
442PhosphorylationSPLSSRQSFCAQEAP
CCCCCCCCHHCCCCC
22.6025159151
450PhosphorylationFCAQEAPTASQGLLK
HHCCCCCCHHHHHHH
46.0930377224
452PhosphorylationAQEAPTASQGLLKLF
CCCCCCHHHHHHHHH
27.5330377224
463PhosphorylationLKLFQKNSPMEDLGA
HHHHHCCCCHHHHCC
32.4329255136
512PhosphorylationVLKGIPESLRGELWL
HHCCCCHHHHHHHHH
20.2920068231
545UbiquitinationLVEKSTGKYSLATEE
HHHHCCCCCEECHHH
31.58-
546PhosphorylationVEKSTGKYSLATEEI
HHHCCCCCEECHHHH
15.4023312004
547PhosphorylationEKSTGKYSLATEEIE
HHCCCCCEECHHHHH
18.2728857561
550PhosphorylationTGKYSLATEEIERDL
CCCCEECHHHHHHHH
39.1723312004
560PhosphorylationIERDLHRSMPEHPAF
HHHHHHHHCCCCHHH
28.1327251275
718PhosphorylationMEQLLGCSDEGEAMT
HHHHHCCCCHHHHHH
36.5824043423
725PhosphorylationSDEGEAMTMLGRYLD
CCHHHHHHHHHHHHH
19.1124043423
730PhosphorylationAMTMLGRYLDNVVNK
HHHHHHHHHHHCCCC
19.3324043423
739PhosphorylationDNVVNKQSVSPPIPH
HHCCCCCCCCCCCHH
26.6020068231
741PhosphorylationVVNKQSVSPPIPHLR
CCCCCCCCCCCHHHH
30.1525159151
752PhosphorylationPHLRALLSSSDDPPA
HHHHHHHHCCCCCCH
28.7530278072
753PhosphorylationHLRALLSSSDDPPAE
HHHHHHHCCCCCCHH
37.4425849741
754PhosphorylationLRALLSSSDDPPAEV
HHHHHHCCCCCCHHC
42.5328450419
775PhosphorylationKVSYEKFSSLRAEDI
HHHHHHHHCCCHHHH
39.2622210691
776PhosphorylationVSYEKFSSLRAEDIE
HHHHHHHCCCHHHHH
25.6324719451
796PhosphorylationQRLKVIQSLEDTAKR
HHHHHHHCHHHHHHH
23.7029514088
800PhosphorylationVIQSLEDTAKRSVVR
HHHCHHHHHHHHHHE
25.3829514088
802UbiquitinationQSLEDTAKRSVVRAI
HCHHHHHHHHHHEEE
47.50-
824PhosphorylationIEELEDLYMVFKAKH
HHHHHHHHHHHHHHH
11.98-
834PhosphorylationFKAKHLASQYWGCSR
HHHHHHHHHHCCCCC
30.1128857561
836PhosphorylationAKHLASQYWGCSRTM
HHHHHHHHCCCCCHH
10.9823917254
850PhosphorylationMAGRRDPSLPYLEQY
HCCCCCCCCHHHHHH
46.3928857561
853PhosphorylationRRDPSLPYLEQYRID
CCCCCCHHHHHHCCC
28.32-
857PhosphorylationSLPYLEQYRIDASQF
CCHHHHHHCCCHHHH
10.52-
897PhosphorylationLLDENKDSLINFKEF
HHCCCCCCCCCHHHH
32.5321214269
912PhosphorylationVTGMSGMYHGDLTEK
HHCCCCCCCCCHHHH
13.2321214269
917PhosphorylationGMYHGDLTEKLKVLY
CCCCCCHHHHHHHHH
35.4921214269
946PhosphorylationSALEAAHYFTEDSSS
HHHHHHHHHCCCCCC
13.89-
965 (in isoform 2)Phosphorylation-8.4328348404
967 (in isoform 2)Phosphorylation-21.3727251275
982PhosphorylationPQEEQEGSGSEERGE
CHHHHCCCCCCCCCC
38.0924275569
993PhosphorylationERGEEKGTSSPDYRH
CCCCCCCCCCHHHHH
36.7823403867
994PhosphorylationRGEEKGTSSPDYRHY
CCCCCCCCCHHHHHH
48.8425159151
995PhosphorylationGEEKGTSSPDYRHYL
CCCCCCCCHHHHHHH
22.9416964243
998PhosphorylationKGTSSPDYRHYLRMW
CCCCCHHHHHHHHHH
11.5923403867
1001PhosphorylationSSPDYRHYLRMWAKE
CCHHHHHHHHHHHHH
6.2321406692
1033PhosphorylationQFIELCKTLYNMFSE
HHHHHHHHHHHHCCC
33.2226434552
1053PhosphorylationDLYHAIATVASLLLR
HHHHHHHHHHHHHHH
15.5326434552
1056PhosphorylationHAIATVASLLLRIGE
HHHHHHHHHHHHHHH
18.4026434552
1081PhosphorylationRKPRDCATEEDEPPA
CCCCCCCCCCCCCCC
46.3630624053
1132PhosphorylationQVVVEGGSGEGQGSP
CEEEECCCCCCCCCH
44.5229514088
1138PhosphorylationGSGEGQGSPSQLLSD
CCCCCCCCHHHCCCC
17.3125159151
1140PhosphorylationGEGQGSPSQLLSDDE
CCCCCCHHHCCCCCC
34.8525850435
1144PhosphorylationGSPSQLLSDDETKDD
CCHHHCCCCCCCCCC
52.1618691976
1148PhosphorylationQLLSDDETKDDMSMS
HCCCCCCCCCCCCCC
46.9327732954
1164PhosphorylationYSVVSTGSLQCEDLA
EEEEECCCEEEECCC
18.5026657352
1191PhosphorylationPTARIGGTVDTDWCI
CCCCCCCCCCCCHHC
15.2522673903
1194PhosphorylationRIGGTVDTDWCISFE
CCCCCCCCCHHCCHH
27.3622673903
1199PhosphorylationVDTDWCISFEQILAS
CCCCHHCCHHHHHHH
21.4222673903
1206PhosphorylationSFEQILASILTESVL
CHHHHHHHHCCHHHH
18.0622673903
1209PhosphorylationQILASILTESVLVNF
HHHHHHCCHHHHHHH
25.2522673903
1211PhosphorylationLASILTESVLVNFFE
HHHHCCHHHHHHHHH
18.6022673903
1238PhosphorylationKKVERQFSTASDHEQ
HHHHHHHCCCCCCCC
18.0927273156
1239PhosphorylationKVERQFSTASDHEQP
HHHHHHCCCCCCCCC
31.3127273156
1241PhosphorylationERQFSTASDHEQPGV
HHHHCCCCCCCCCCC
39.3227273156
1249PhosphorylationDHEQPGVSG------
CCCCCCCCC------
44.7125159151

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 TBC9B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC9B_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 TBC9B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
LMBL2_HUMANL3MBTL2physical
25416956
CLK2_HUMANCLK2physical
26496610
SEC62_HUMANSEC62physical
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 TBC9B_HUMAN

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Related Literatures of Post-Translational Modification
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-411; SER-432 ANDSER-435, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASSSPECTROMETRY.
"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 SER-432 AND SER-435, ANDMASS 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-411; SER-420; SER-432;SER-435 AND SER-463, 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-420; SER-432; SER-435AND SER-463, AND MASS SPECTROMETRY.
"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-411 AND SER-435, ANDMASS SPECTROMETRY.

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