TX1B3_HUMAN - dbPTM
TX1B3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TX1B3_HUMAN
UniProt AC O14907
Protein Name Tax1-binding protein 3
Gene Name TAX1BP3 {ECO:0000312|HGNC:HGNC:30684}
Organism Homo sapiens (Human).
Sequence Length 124
Subcellular Localization Cytoplasm. Nucleus. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Recruited to the cell membrane by interaction with membrane proteins.
Protein Description May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6..
Protein Sequence MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS
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
2Phosphorylation------MSYIPGQPV
------CCCCCCCCE
31.5930576142
2Acetylation------MSYIPGQPV
------CCCCCCCCE
31.5922223895
3Phosphorylation-----MSYIPGQPVT
-----CCCCCCCCEE
15.1625394399
10PhosphorylationYIPGQPVTAVVQRVE
CCCCCCEEEEEEEEE
22.0324043423
32PhosphorylationENLILGFSIGGGIDQ
CCEEEEEEECCCCCC
20.6528348404
42PhosphorylationGGIDQDPSQNPFSED
CCCCCCCCCCCCCCC
51.3728348404
532-HydroxyisobutyrylationFSEDKTDKGIYVTRV
CCCCCCCCCEEEEEE
53.06-
53UbiquitinationFSEDKTDKGIYVTRV
CCCCCCCCCEEEEEE
53.06-
56PhosphorylationDKTDKGIYVTRVSEG
CCCCCCEEEEEECCC
12.3930576142
58PhosphorylationTDKGIYVTRVSEGGP
CCCCEEEEEECCCCC
14.3722617229
61PhosphorylationGIYVTRVSEGGPAEI
CEEEEEECCCCCCEE
27.5130266825
86PhosphorylationQVNGWDMTMVTHDQA
EECCCEEEEECHHHH
13.1526552605
89PhosphorylationGWDMTMVTHDQARKR
CCEEEEECHHHHHHH
14.6526552605
110PhosphorylationEVVRLLVTRQSLQKA
HHHHHHHHHHHHHHH
23.9822496350
113PhosphorylationRLLVTRQSLQKAVQQ
HHHHHHHHHHHHHHH
29.4929978859
116UbiquitinationVTRQSLQKAVQQSML
HHHHHHHHHHHHHHC
56.68-
121PhosphorylationLQKAVQQSMLS----
HHHHHHHHHCC----
12.4720068231
124PhosphorylationAVQQSMLS-------
HHHHHHCC-------
29.5422496350

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 TX1B3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TX1B3_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 TX1B3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
18835279
CK5P3_HUMANCDK5RAP3physical
23028987
UB2D2_HUMANUBE2D2physical
22939629
VAMP2_HUMANVAMP2physical
22939629
DTX1_HUMANDTX1physical
23395680
STAU1_HUMANSTAU1physical
23395680
RN183_HUMANRNF183physical
25416956

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 TX1B3_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-61, AND MASSSPECTROMETRY.

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