TBL1R_HUMAN - dbPTM
TBL1R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBL1R_HUMAN
UniProt AC Q9BZK7
Protein Name F-box-like/WD repeat-containing protein TBL1XR1
Gene Name TBL1XR1
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Nucleus .
Protein Description F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation..
Protein Sequence MSISSDEVNFLVYRYLQESGFSHSAFTFGIESHISQSNINGALVPPAALISIIQKGLQYVEAEVSINEDGTLFDGRPIESLSLIDAVMPDVVQTRQQAYRDKLAQQQAAAAAAAAAAASQQGSAKNGENTANGEENGAHTIANNHTDMMEVDGDVEIPPNKAVVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLSENSTSGSTQLVLRHCIREGGQDVPSNKDVTSLDWNSEGTLLATGSYDGFARIWTKDGNLASTLGQHKGPIFALKWNKKGNFILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQSNNTFASCSTDMCIHVCKLGQDRPIKTFQGHTNEVNAIKWDPTGNLLASCSDDMTLKIWSMKQDNCVHDLQAHNKEIYTIKWSPTGPGTNNPNANLMLASASFDSTVRLWDVDRGICIHTLTKHQEPVYSVAFSPDGRYLASGSFDKCVHIWNTQTGALVHSYRGTGGIFEVCWNAAGDKVGASASDGSVCVLDLRK
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
2Acetylation------MSISSDEVN
------CCCCHHHHH		31.0422223895
2Phosphorylation------MSISSDEVN
------CCCCHHHHH		31.0424043423
4Phosphorylation----MSISSDEVNFL
----CCCCHHHHHHH		25.1624043423
5Phosphorylation---MSISSDEVNFLV
---CCCCHHHHHHHH		35.8024043423
13PhosphorylationDEVNFLVYRYLQESG
HHHHHHHHHHHHHCC		8.8324043423
13NitrationDEVNFLVYRYLQESG
HHHHHHHHHHHHHCC		8.83-
15UbiquitinationVNFLVYRYLQESGFS
HHHHHHHHHHHCCCC		8.6121963094
102AcetylationRQQAYRDKLAQQQAA
HHHHHHHHHHHHHHH		36.4023954790
102UbiquitinationRQQAYRDKLAQQQAA
HHHHHHHHHHHHHHH		36.4021906983
119PhosphorylationAAAAAAASQQGSAKN
HHHHHHHHHHCCCCC		20.5017525332
123PhosphorylationAAASQQGSAKNGENT
HHHHHHCCCCCCCCC		31.5629255136
170PhosphorylationVVLRGHESEVFICAW
EEECCCCCCEEEEEC		33.1327080861
179UbiquitinationVFICAWNPVSDLLAS
EEEEECCCHHHHHHC		19.1129967540
186UbiquitinationPVSDLLASGSGDSTA
CHHHHHHCCCCCCCE		33.2023000965
189UbiquitinationDLLASGSGDSTARIW
HHHHCCCCCCCEEEE		36.0923000965
190UbiquitinationLLASGSGDSTARIWN
HHHCCCCCCCEEEEE		44.5023000965
199PhosphorylationTARIWNLSENSTSGS
CEEEEECCCCCCCCC		31.3618374649
202PhosphorylationIWNLSENSTSGSTQL
EEECCCCCCCCCHHH		21.6527067055
203PhosphorylationWNLSENSTSGSTQLV
EECCCCCCCCCHHHH		49.0018374649
204PhosphorylationNLSENSTSGSTQLVL
ECCCCCCCCCHHHHH		30.4818374649
254AcetylationGFARIWTKDGNLAST
CEEEEEECCCCHHHH		48.9519608861
256UbiquitinationARIWTKDGNLASTLG
EEEEECCCCHHHHHC		32.3829967540
260PhosphorylationTKDGNLASTLGQHKG
ECCCCHHHHHCCCCC		27.6027251275
261PhosphorylationKDGNLASTLGQHKGP
CCCCHHHHHCCCCCC		29.3327251275
266UbiquitinationASTLGQHKGPIFALK
HHHHCCCCCCEEEEE		59.5029967540
273UbiquitinationKGPIFALKWNKKGNF
CCCEEEEEECCCCCE		45.3423000965
276UbiquitinationIFALKWNKKGNFILS
EEEEEECCCCCEEEE		62.0323000965
277SumoylationFALKWNKKGNFILSA
EEEEECCCCCEEEEE		56.74-
277SumoylationFALKWNKKGNFILSA
EEEEECCCCCEEEEE		56.7428112733
277AcetylationFALKWNKKGNFILSA
EEEEECCCCCEEEEE		56.7426051181
277MalonylationFALKWNKKGNFILSA
EEEEECCCCCEEEEE		56.7426320211
277UbiquitinationFALKWNKKGNFILSA
EEEEECCCCCEEEEE		56.7423000965
287UbiquitinationFILSAGVDKTTIIWD
EEEEECCCCEEEEEE		41.4823000965
292UbiquitinationGVDKTTIIWDAHTGE
CCCCEEEEEECCCCC		2.2721890473
305UbiquitinationGEAKQQFPFHSAPAL
CCCHHCCCCCCCCCC		23.0029967540
343UbiquitinationLGQDRPIKTFQGHTN
HCCCCCCEEECCCCC		46.0729967540
374UbiquitinationCSDDMTLKIWSMKQD
CCCCCEEEEEEECCC		32.7223000965
379UbiquitinationTLKIWSMKQDNCVHD
EEEEEEECCCCCEEE		49.3223000965
379AcetylationTLKIWSMKQDNCVHD
EEEEEEECCCCCEEE		49.3225953088
392UbiquitinationHDLQAHNKEIYTIKW
EEHHHCCCEEEEEEE		35.3129967540
395PhosphorylationQAHNKEIYTIKWSPT
HHCCCEEEEEEECCC		11.9628064214
431MethylationVRLWDVDRGICIHTL
EEEEECCCCEEEEEE		35.90115918289
446PhosphorylationTKHQEPVYSVAFSPD
CCCCCCEEEEEECCC		14.2428152594
447PhosphorylationKHQEPVYSVAFSPDG
CCCCCEEEEEECCCC		13.7528152594
459PhosphorylationPDGRYLASGSFDKCV
CCCCCEECCCCCCEE		32.1620873877
461PhosphorylationGRYLASGSFDKCVHI
CCCEECCCCCCEEEE		27.9820873877
464MethylationLASGSFDKCVHIWNT
EECCCCCCEEEEEEC		35.83-
497SumoylationCWNAAGDKVGASASD
EECCCCCCCCCCCCC		41.47-
497SumoylationCWNAAGDKVGASASD
EECCCCCCCCCCCCC		41.47-
501PhosphorylationAGDKVGASASDGSVC
CCCCCCCCCCCCCEE		23.5223403867
503PhosphorylationDKVGASASDGSVCVL
CCCCCCCCCCCEEEE		39.7523403867
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
123SPhosphorylationKinasePRKCDQ05655
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBL1R_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 TBL1R_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOR1_HUMANNCOR1physical
12628926
H2B2E_HUMANHIST2H2BEphysical
12628926
NCOR1_HUMANNCOR1physical
18202150
HDAC3_HUMANHDAC3physical
18202150
UB2E3_HUMANUBE2E3physical
18202150
EMD_HUMANEMDphysical
17620012
UB2D1_HUMANUBE2D1physical
14980219
CTNB1_HUMANCTNNB1physical
18193033
TAB2_HUMANTAB2physical
16469706
KDM1A_HUMANKDM1Aphysical
21258344
HDAC3_HUMANHDAC3physical
21258344
GPS2_HUMANGPS2physical
21258344
NCOR1_HUMANNCOR1physical
21258344
TBL1X_HUMANTBL1Xphysical
21258344
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 TBL1R_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-254, AND MASS SPECTROMETRY.
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 SER-119, AND MASSSPECTROMETRY.

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