Version 5.4
Bos taurus Protein: RIPK2
Summary
InnateDB Protein IDBP-698078.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RIPK2
Protein Name Receptor-interacting serine/threonine-protein kinase 2
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000020312
InnateDB Gene IDBG-645358 (RIPK2)
Protein Structure
UniProt Annotation
Function Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Once recruited, autophosphorylates and undergoes 'Lys- 63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is release from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 73 interaction(s) predicted by orthology.
Predicted by orthology
Total 73 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004715 non-membrane spanning protein tyrosine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016740 transferase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0002250 adaptive immune response
GO:0002376 immune system process
GO:0006468 protein phosphorylation
GO:0006915 apoptotic process
GO:0007249 I-kappaB kinase/NF-kappaB signaling
GO:0010800 positive regulation of peptidyl-threonine phosphorylation
GO:0016310 phosphorylation
GO:0018108 peptidyl-tyrosine phosphorylation
GO:0032755 positive regulation of interleukin-6 production
GO:0032760 positive regulation of tumor necrosis factor production
GO:0033138 positive regulation of peptidyl-serine phosphorylation
GO:0042981 regulation of apoptotic process
GO:0043065 positive regulation of apoptotic process
GO:0045087 innate immune response
GO:0050731 positive regulation of peptidyl-tyrosine phosphorylation
GO:0050852 T cell receptor signaling pathway
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:0070431 nucleotide-binding oligomerization domain containing 2 signaling pathway
GO:0071225 cellular response to muramyl dipeptide
Cellular Component
GO:0005622 intracellular
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0031982 vesicle
GO:0043234 protein complex
Protein Structure and Domains
PDB ID
InterPro IPR000719 Protein kinase domain
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain
IPR001315 CARD domain
IPR002290 Serine/threonine/dual specificity protein kinase, catalytic domain
IPR011009 Protein kinase-like domain
IPR011029 Death-like domain
IPR017322 Receptor-interacting serine/threonine-protein kinase 2
IPR020635 Tyrosine-protein kinase, catalytic domain
PFAM PF00069
PF07714
PF00619
PRINTS PR00109
PIRSF PIRSF037921
SMART SM00114
SM00220
SM00219
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3SZJ2
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 534407
UniGene Bt.34596
RefSeq NP_001029782
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC102829
GenPept AAI02830

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

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Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca