TBD2A_HUMAN - dbPTM
TBD2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBD2A_HUMAN
UniProt AC Q9BYX2
Protein Name TBC1 domain family member 2A
Gene Name TBC1D2
Organism Homo sapiens (Human).
Sequence Length 928
Subcellular Localization Cytoplasm . Cytoplasmic vesicle . Cell junction .
Protein Description Acts as GTPase-activating protein for RAB7A. Signal effector acting as a linker between RAC1 and RAB7A, leading to RAB7A inactivation and subsequent inhibition of cadherin degradation and reduced cell-cell adhesion..
Protein Sequence MEGAGENAPESSSSAPGSEESARDPQVPPPEEESGDCARSLEAVPKKLCGYLSKFGGKGPIRGWKSRWFFYDERKCQLYYSRTAQDANPLDSIDLSSAVFDCKADAEEGIFEIKTPSRVITLKAATKQAMLYWLQQLQMKRWEFHNSPPAPPATPDAALAGNGPVLHLELGQEEAELEEFLCPVKTPPGLVGVAAALQPFPALQNISLKHLGTEIQNTMHNIRGNKQAQGTGHEPPGEDSPQSGEPQREEQPLASDASTPGREPEDSPKPAPKPSLTISFAQKAKRQNNTFPFFSEGITRNRTAQEKVAALEQQVLMLTKELKSQKELVKILHKALEAAQQEKRASSAYLAAAEDKDRLELVRHKVRQIAELGRRVEALEQERESLAHTASLREQQVQELQQHVQLLMDKNHAKQQVICKLSEKVTQDFTHPPDQSPLRPDAANRDFLSQQGKIEHLKDDMEAYRTQNCFLNSEIHQVTKIWRKVAEKEKALLTKCAYLQARNCQVESKYLAGLRRLQEALGDEASECSELLRQLVQEALQWEAGEASSDSIELSPISKYDEYGFLTVPDYEVEDLKLLAKIQALESRSHHLLGLEAVDRPLRERWAALGDLVPSAELKQLLRAGVPREHRPRVWRWLVHLRVQHLHTPGCYQELLSRGQAREHPAARQIELDLNRTFPNNKHFTCPTSSFPDKLRRVLLAFSWQNPTIGYCQGLNRLAAIALLVLEEEESAFWCLVAIVETIMPADYYCNTLTASQVDQRVLQDLLSEKLPRLMAHLGQHHVDLSLVTFNWFLVVFADSLISNILLRVWDAFLYEGTKVVFRYALAIFKYNEKEILRLQNGLEIYQYLRFFTKTISNSRKLMNIAFNDMNPFRMKQLRQLRMVHRERLEAELRELEQLKAEYLERRASRRRAVSEGCASEDEVEGEA
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-------MEGAGENA
-------CCCCCCCC		10.9322814378
40PhosphorylationESGDCARSLEAVPKK
HCCHHHHHHHHHHHH		16.4327499020
47UbiquitinationSLEAVPKKLCGYLSK
HHHHHHHHHHHHHHH		42.83-
53PhosphorylationKKLCGYLSKFGGKGP
HHHHHHHHHHCCCCC		19.9122817900
54MalonylationKLCGYLSKFGGKGPI
HHHHHHHHHCCCCCC		45.4926320211
66O-linked_GlycosylationGPIRGWKSRWFFYDE
CCCCCCCCEEEEEEC		28.3830379171
114UbiquitinationEEGIFEIKTPSRVIT
CCCCEEECCCCCEEE		47.38-
115PhosphorylationEGIFEIKTPSRVITL
CCCEEECCCCCEEEH		31.9618669648
117PhosphorylationIFEIKTPSRVITLKA
CEEECCCCCEEEHHH		44.4026270265
123UbiquitinationPSRVITLKAATKQAM
CCCEEEHHHHHHHHH		27.59-
154PhosphorylationSPPAPPATPDAALAG
CCCCCCCCCCHHHCC		27.7222468782
186PhosphorylationEFLCPVKTPPGLVGV
HHCCCCCCCCCHHHH		34.6425159151
207PhosphorylationFPALQNISLKHLGTE
CHHHHCCCHHHHCHH		38.6324719451
209MethylationALQNISLKHLGTEIQ
HHHCCCHHHHCHHHH		29.96115980159
213PhosphorylationISLKHLGTEIQNTMH
CCHHHHCHHHHHHHH		35.9528555341
218PhosphorylationLGTEIQNTMHNIRGN
HCHHHHHHHHHHHCC		11.9328555341
240PhosphorylationHEPPGEDSPQSGEPQ
CCCCCCCCCCCCCCC		22.1225159151
255PhosphorylationREEQPLASDASTPGR
CCCCCCCCCCCCCCC		41.2023312004
258PhosphorylationQPLASDASTPGREPE
CCCCCCCCCCCCCCC		39.8723312004
259PhosphorylationPLASDASTPGREPED
CCCCCCCCCCCCCCC		31.3323312004
267PhosphorylationPGREPEDSPKPAPKP
CCCCCCCCCCCCCCC		32.9126657352
283MethylationLTISFAQKAKRQNNT
EEEEHHHHHHHCCCC		53.07115980163
285MethylationISFAQKAKRQNNTFP
EEHHHHHHHCCCCCC		62.65115980171
290PhosphorylationKAKRQNNTFPFFSEG
HHHHCCCCCCCCCCC		39.9922617229
295PhosphorylationNNTFPFFSEGITRNR
CCCCCCCCCCCCCCC		34.9823403867
299PhosphorylationPFFSEGITRNRTAQE
CCCCCCCCCCCCHHH		32.5227080861
330UbiquitinationKSQKELVKILHKALE
HCHHHHHHHHHHHHH		52.77-
334MalonylationELVKILHKALEAAQQ
HHHHHHHHHHHHHHH		51.7426320211
334UbiquitinationELVKILHKALEAAQQ
HHHHHHHHHHHHHHH		51.74-
343UbiquitinationLEAAQQEKRASSAYL
HHHHHHHHHHCHHHH		49.26-
346PhosphorylationAQQEKRASSAYLAAA
HHHHHHHCHHHHHHH		21.3823312004
347PhosphorylationQQEKRASSAYLAAAE
HHHHHHCHHHHHHHC		21.6823312004
349PhosphorylationEKRASSAYLAAAEDK
HHHHCHHHHHHHCCC		9.9827642862
356UbiquitinationYLAAAEDKDRLELVR
HHHHHCCCHHHHHHH		35.93-
385PhosphorylationALEQERESLAHTASL
HHHHHHHHHHHHHHH		36.7628555341
410UbiquitinationHVQLLMDKNHAKQQV
HHHHHHCCCHHHHHH		36.35-
4142-HydroxyisobutyrylationLMDKNHAKQQVICKL
HHCCCHHHHHHHHHH		33.44-
414UbiquitinationLMDKNHAKQQVICKL
HHCCCHHHHHHHHHH		33.44-
424UbiquitinationVICKLSEKVTQDFTH
HHHHHHHHHHCCCCC		47.40-
426PhosphorylationCKLSEKVTQDFTHPP
HHHHHHHHCCCCCCC		33.2325850435
430PhosphorylationEKVTQDFTHPPDQSP
HHHHCCCCCCCCCCC		41.5925850435
436PhosphorylationFTHPPDQSPLRPDAA
CCCCCCCCCCCCCCC		33.0322167270
453UbiquitinationDFLSQQGKIEHLKDD
HHHHHHCCHHHHHHH		40.35-
458UbiquitinationQGKIEHLKDDMEAYR
HCCHHHHHHHHHHHH		54.30-
464PhosphorylationLKDDMEAYRTQNCFL
HHHHHHHHHHHCCCC		10.8228787133
466PhosphorylationDDMEAYRTQNCFLNS
HHHHHHHHHCCCCCH		16.0928787133
490UbiquitinationRKVAEKEKALLTKCA
HHHHHHHHHHHHHHH		56.24-
495UbiquitinationKEKALLTKCAYLQAR
HHHHHHHHHHHHHHH		19.48-
560PhosphorylationELSPISKYDEYGFLT
EECCCCCCCCCCCEE		13.7627642862
563PhosphorylationPISKYDEYGFLTVPD
CCCCCCCCCCEECCC		15.4127642862
571PhosphorylationGFLTVPDYEVEDLKL
CCEECCCCCHHHHHH		18.7922817900
577UbiquitinationDYEVEDLKLLAKIQA
CCCHHHHHHHHHHHH		54.50-
581UbiquitinationEDLKLLAKIQALESR
HHHHHHHHHHHHHHC		35.01-
619UbiquitinationLVPSAELKQLLRAGV
CCCHHHHHHHHHCCC		30.33-
657PhosphorylationGCYQELLSRGQAREH
CHHHHHHHCCCCCCC		47.1724719451
768PhosphorylationRVLQDLLSEKLPRLM
HHHHHHHHCHHHHHH		39.7324719451
834MalonylationAIFKYNEKEILRLQN
HHHHCCHHHHHHHHC		46.5526320211
846PhosphorylationLQNGLEIYQYLRFFT
HHCHHHHHHHHHHHH		5.03-
857PhosphorylationRFFTKTISNSRKLMN
HHHHHHHCCCHHHHH		33.70-
859PhosphorylationFTKTISNSRKLMNIA
HHHHHCCCHHHHHHH		24.81-
900UbiquitinationLRELEQLKAEYLERR
HHHHHHHHHHHHHHH		38.58-
903PhosphorylationLEQLKAEYLERRASR
HHHHHHHHHHHHHHH		20.7927642862
904PhosphorylationEQLKAEYLERRASRR
HHHHHHHHHHHHHHH		2.8824719451
909PhosphorylationEYLERRASRRRAVSE
HHHHHHHHHHHHHHC		25.2217081983
915PhosphorylationASRRRAVSEGCASED
HHHHHHHHCCCCCCC		27.5625159151
920PhosphorylationAVSEGCASEDEVEGE
HHHCCCCCCCCCCCC		50.0525159151
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 TBD2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBD2A_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 TBD2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INT9_HUMANINTS9physical
22863883
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 TBD2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-436 AND SER-920, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186; SER-915 ANDSER-920, 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 AT SER-920, AND MASS SPECTROMETRY.

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