Lys644
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.0.1
Powered by Cell Signaling Technology
Home > Ubiquitylation Site Page: > Lys644  -  MALT1 (human)

Site Information
LDLDIDPkDANkGTP   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 2134705

In vivo Characterization
Methods used to characterize site in vivo:
electrophoretic mobility shift ( 3 ) , immunoprecipitation ( 1 , 3 ) , mass spectrometry ( 3 ) , mutation of modification site ( 1 , 2 , 3 , 4 ) , western blotting ( 1 , 2 , 3 )
Disease tissue studied:
breast cancer ( 3 ) , leukemia ( 1 , 2 , 3 , 4 ) , T cell leukemia ( 1 , 2 , 3 , 4 ) , lymphoma ( 3 ) , B cell lymphoma ( 3 ) , Burkitt's lymphoma ( 3 ) , non-Hodgkin's lymphoma ( 3 ) , follicular lymphoma ( 3 )
Relevant cell line - cell type - tissue:
293 (epithelial) ( 2 ) , BJAB (B lymphocyte) ( 3 ) , HBL-100 (breast cell) ( 3 ) , HEK293T (epithelial) ( 1 , 3 , 4 ) , Jurkat (T lymphocyte) ( 1 , 2 , 3 , 4 ) , lymphocyte ( 2 ) , lymphocyte-blood ( 1 ) , OCI-ly10 (B lymphocyte) ( 3 ) , OCI-ly3 (B lymphocyte) ( 3 ) , Raji (B lymphocyte) ( 3 ) , T lymphocyte-lymph node ( 4 ) , T lymphocyte-spleen ( 4 )

Upstream Regulation
Regulatory protein:
USP2 (human) ( 2 )
Treatments:
ionomycin ( 3 ) , phorbol_ester ( 3 ) , Z-VAD-FMK ( 2 )

Downstream Regulation
Effects of modification on MALT1:
enzymatic activity, induced ( 1 , 2 , 3 ) , molecular association, regulation ( 4 ) , protein conformation ( 1 ) , protein degradation ( 2 , 4 ) , protein processing ( 2 ) , protein stabilization ( 3 )
Effects of modification on biological processes:
carcinogenesis, induced ( 3 ) , cell growth, induced ( 3 ) , transcription, induced ( 1 , 2 , 3 )
Induce interaction with:
IKKA (human) ( 4 ) , MALT1 (human) ( 3 )

References 

1

Schairer R, et al. (2020) Allosteric activation of MALT1 by its ubiquitin-binding Ig3 domain. Proc Natl Acad Sci U S A 117, 3093-3102
31980531   Curated Info

2

Ginster S, et al. (2017) Two Antagonistic MALT1 Auto-Cleavage Mechanisms Reveal a Role for TRAF6 to Unleash MALT1 Activation. PLoS One 12, e0169026
28052131   Curated Info

3

Pelzer C, et al. (2013) The protease activity of the paracaspase MALT1 is controlled by monoubiquitination. Nat Immunol 14, 337-45
23416615   Curated Info

4

Oeckinghaus A, et al. (2007) Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation. EMBO J 26, 4634-45
17948050   Curated Info

Developed with grants from  NIH Logo and literature mining with Linguamatics  I2E Logo Creative Commons License PhosphoSite, created by Cell Signaling Technology is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License.

©2003-2019 Cell Signaling Technology, Inc.