TBL2_HUMAN - dbPTM
TBL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBL2_HUMAN
UniProt AC Q9Y4P3
Protein Name Transducin beta-like protein 2
Gene Name TBL2
Organism Homo sapiens (Human).
Sequence Length 447
Subcellular Localization
Protein Description
Protein Sequence MELSQMSELMGLSVLLGLLALMATAAVARGWLRAGEERSGRPACQKANGFPPDKSSGSKKQKQYQRIRKEKPQQHNFTHRLLAAALKSHSGNISCMDFSSNGKYLATCADDRTIRIWSTKDFLQREHRSMRANVELDHATLVRFSPDCRAFIVWLANGDTLRVFKMTKREDGGYTFTATPEDFPKKHKAPVIDIGIANTGKFIMTASSDTTVLIWSLKGQVLSTINTNQMNNTHAAVSPCGRFVASCGFTPDVKVWEVCFGKKGEFQEVVRAFELKGHSAAVHSFAFSNDSRRMASVSKDGTWKLWDTDVEYKKKQDPYLLKTGRFEEAAGAAPCRLALSPNAQVLALASGSSIHLYNTRRGEKEECFERVHGECIANLSFDITGRFLASCGDRAVRLFHNTPGHRAMVEEMQGHLKRASNESTRQRLQQQLTQAQETLKSLGALKK
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
4Phosphorylation----MELSQMSELMG
----CCHHHHHHHHH		15.5524043423
7Phosphorylation-MELSQMSELMGLSV
-CCHHHHHHHHHHHH		21.6824719451
13PhosphorylationMSELMGLSVLLGLLA
HHHHHHHHHHHHHHH		12.6524719451
24PhosphorylationGLLALMATAAVARGW
HHHHHHHHHHHHHHH		10.9424043423
44S-palmitoylationERSGRPACQKANGFP
CCCCCCCHHHCCCCC		4.7721044946
55PhosphorylationNGFPPDKSSGSKKQK
CCCCCCCCCCCHHHH		47.5121712546
69UbiquitinationKQYQRIRKEKPQQHN
HHHHHHHHHCCCCCC		68.65-
71UbiquitinationYQRIRKEKPQQHNFT
HHHHHHHCCCCCCHH		51.68-
88PhosphorylationLLAAALKSHSGNISC
HHHHHHHHCCCCEEE		24.6030622161
90PhosphorylationAAALKSHSGNISCMD
HHHHHHCCCCEEEEE		40.4030622161
94PhosphorylationKSHSGNISCMDFSSN
HHCCCCEEEEECCCC		13.8530622161
99PhosphorylationNISCMDFSSNGKYLA
CEEEEECCCCCCEEE		20.7327251275
103AcetylationMDFSSNGKYLATCAD
EECCCCCCEEEEECC		41.1426051181
103UbiquitinationMDFSSNGKYLATCAD
EECCCCCCEEEEECC		41.14-
104PhosphorylationDFSSNGKYLATCADD
ECCCCCCEEEEECCC		11.7228152594
107PhosphorylationSNGKYLATCADDRTI
CCCCEEEEECCCCEE		12.9628102081
112MethylationLATCADDRTIRIWST
EEEECCCCEEEEEEH		32.38115918293
113PhosphorylationATCADDRTIRIWSTK
EEECCCCEEEEEEHH		22.9228857561
120UbiquitinationTIRIWSTKDFLQREH
EEEEEEHHHHHHHHH		40.7521890473
120AcetylationTIRIWSTKDFLQREH
EEEEEEHHHHHHHHH		40.7526051181
167PhosphorylationTLRVFKMTKREDGGY
EEEEEEEEECCCCCE		27.7822468782
168SumoylationLRVFKMTKREDGGYT
EEEEEEEECCCCCEE		50.7428112733
174PhosphorylationTKREDGGYTFTATPE
EECCCCCEEEEECHH		12.2928152594
175PhosphorylationKREDGGYTFTATPED
ECCCCCEEEEECHHH		20.1325072903
177PhosphorylationEDGGYTFTATPEDFP
CCCCEEEEECHHHCC		23.0925072903
179PhosphorylationGGYTFTATPEDFPKK
CCEEEEECHHHCCCC		24.9325072903
185UbiquitinationATPEDFPKKHKAPVI
ECHHHCCCCCCCCEE		68.45-
188UbiquitinationEDFPKKHKAPVIDIG
HHCCCCCCCCEEEEE		64.36-
207PhosphorylationGKFIMTASSDTTVLI
CCEEEEECCCCEEEE		21.4125332170
208PhosphorylationKFIMTASSDTTVLIW
CEEEEECCCCEEEEE		36.1925332170
210PhosphorylationIMTASSDTTVLIWSL
EEEECCCCEEEEEEE		22.2825332170
238PhosphorylationNNTHAAVSPCGRFVA
CCCEEEECCCHHHHH		15.1127251275
262MalonylationVWEVCFGKKGEFQEV
EEEEECCCCCCHHHH		37.0432601280
2622-HydroxyisobutyrylationVWEVCFGKKGEFQEV
EEEEECCCCCCHHHH		37.04-
263MalonylationWEVCFGKKGEFQEVV
EEEECCCCCCHHHHH		65.1426320211
263AcetylationWEVCFGKKGEFQEVV
EEEECCCCCCHHHHH		65.1426051181
263UbiquitinationWEVCFGKKGEFQEVV
EEEECCCCCCHHHHH		65.14-
279PhosphorylationAFELKGHSAAVHSFA
HEEECCCCEEEEEEE		26.9620873877
284PhosphorylationGHSAAVHSFAFSNDS
CCCEEEEEEECCCCC		16.2120873877
288PhosphorylationAVHSFAFSNDSRRMA
EEEEEECCCCCCCCE		35.9820873877
291PhosphorylationSFAFSNDSRRMASVS
EEECCCCCCCCEEEC		26.4920873877
299UbiquitinationRRMASVSKDGTWKLW
CCCEEECCCCCEEEC		59.00-
302PhosphorylationASVSKDGTWKLWDTD
EEECCCCCEEECCCC		29.5628857561
304UbiquitinationVSKDGTWKLWDTDVE
ECCCCCEEECCCCCC		39.27-
308PhosphorylationGTWKLWDTDVEYKKK
CCEEECCCCCCHHHC		30.29-
313AcetylationWDTDVEYKKKQDPYL
CCCCCCHHHCCCCCE		39.7326051181
313UbiquitinationWDTDVEYKKKQDPYL
CCCCCCHHHCCCCCE		39.73-
314AcetylationDTDVEYKKKQDPYLL
CCCCCHHHCCCCCEE		55.5619608861
314UbiquitinationDTDVEYKKKQDPYLL
CCCCCHHHCCCCCEE		55.5619608861
315AcetylationTDVEYKKKQDPYLLK
CCCCHHHCCCCCEEE		56.6419608861
315UbiquitinationTDVEYKKKQDPYLLK
CCCCHHHCCCCCEEE		56.6419608861
319PhosphorylationYKKKQDPYLLKTGRF
HHHCCCCCEEECCCH		32.7228152594
322UbiquitinationKQDPYLLKTGRFEEA
CCCCCEEECCCHHHH		46.462190698
323PhosphorylationQDPYLLKTGRFEEAA
CCCCEEECCCHHHHC		33.2927251275
335GlutathionylationEAAGAAPCRLALSPN
HHCCCCCCEEEECCC		4.8322555962
340PhosphorylationAPCRLALSPNAQVLA
CCCEEEECCCCEEEE		15.5322617229
350PhosphorylationAQVLALASGSSIHLY
CEEEEECCCCEEEEE		39.8125693802
352PhosphorylationVLALASGSSIHLYNT
EEEECCCCEEEEEEC		24.5125693802
353PhosphorylationLALASGSSIHLYNTR
EEECCCCEEEEEECC		19.9728857561
357PhosphorylationSGSSIHLYNTRRGEK
CCCEEEEEECCCCCH		10.5825693802
359PhosphorylationSSIHLYNTRRGEKEE
CEEEEEECCCCCHHH		14.2625693802
364UbiquitinationYNTRRGEKEECFERV
EECCCCCHHHHHHHH		62.73-
364AcetylationYNTRRGEKEECFERV
EECCCCCHHHHHHHH		62.7325953088
394MethylationFLASCGDRAVRLFHN
HHHHCCCHHHHHHCC		21.92115918297
402PhosphorylationAVRLFHNTPGHRAMV
HHHHHCCCCCHHHHH		23.2927251275
417MalonylationEEMQGHLKRASNEST
HHHHHHHHHHCCHHH		40.0026320211
417UbiquitinationEEMQGHLKRASNEST
HHHHHHHHHHCCHHH		40.00-
417MethylationEEMQGHLKRASNEST
HHHHHHHHHHCCHHH		40.0054424575
433PhosphorylationQRLQQQLTQAQETLK
HHHHHHHHHHHHHHH		19.9528112733
438PhosphorylationQLTQAQETLKSLGAL
HHHHHHHHHHHCCCC		27.6624173317
440UbiquitinationTQAQETLKSLGALKK
HHHHHHHHHCCCCCC		51.56-
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
433TPhosphorylationKinaseATMQ13315
Uniprot
433TPhosphorylationKinaseATRQ13535
Uniprot
433TPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBL2_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 TBL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TBL2_HUMAN !!
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 TBL2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-314 AND LYS-315, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.

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