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Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)

 RIPK2_MOUSE             Reviewed;         539 AA.
P58801;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 1.
23-MAY-2018, entry version 161.
RecName: Full=Receptor-interacting serine/threonine-protein kinase 2;
EC=2.7.11.1;
AltName: Full=Tyrosine-protein kinase RIPK2;
EC=2.7.10.2;
Name=Ripk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=11894097; DOI=10.1038/416190a;
Chin A.I., Dempsey P.W., Bruhn K., Miller J.F., Xu Y., Cheng G.;
"Involvement of receptor-interacting protein 2 in innate and adaptive
immune responses.";
Nature 416:190-194(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
DISRUPTION PHENOTYPE.
PubMed=17277144; DOI=10.4049/jimmunol.178.4.2380;
Park J.H., Kim Y.G., McDonald C., Kanneganti T.D., Hasegawa M.,
Body-Malapel M., Inohara N., Nunez G.;
"RICK/RIP2 mediates innate immune responses induced through Nod1 and
Nod2 but not TLRs.";
J. Immunol. 178:2380-2386(2007).
[4]
INTERACTION WITH CARD9.
PubMed=17187069; DOI=10.1038/ni1426;
Hsu Y.M., Zhang Y., You Y., Wang D., Li H., Duramad O., Qin X.F.,
Dong C., Lin X.;
"The adaptor protein CARD9 is required for innate immune responses to
intracellular pathogens.";
Nat. Immunol. 8:198-205(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21469090; DOI=10.1002/eji.201040827;
Magalhaes J.G., Lee J., Geddes K., Rubino S., Philpott D.J.,
Girardin S.E.;
"Essential role of Rip2 in the modulation of innate and adaptive
immunity triggered by Nod1 and Nod2 ligands.";
Eur. J. Immunol. 41:1445-1455(2011).
-!- 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. {ECO:0000269|PubMed:21469090}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- SUBUNIT: Found in a signaling complex consisting of at least
ARHGEF2, NOD2 and RIPK2. Interacts with ARHGEF2. Binds to
CFLAR/CLARP and CASP1 via their CARD domains. Binds to BIRC3/c-
IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6. May be a
component of both the TNFRSF1A and TNRFSF5/CD40 receptor complex.
Interacts with NOD1. Interacts (via CARD domain) with NOD2 (via
CARD domain). Interacts with MAP3K4; this interaction sequesters
RIPK2 from the NOD2 signaling pathway. Interacts with IKBKG/NEMO.
The polyubiquitinated protein interacts with MAP3K7/TAK1.
Interacts with XIAP/BIRC4. Interacts with NLRP10 (By similarity).
Interacts with CARD9. Interacts with INAVA; the interaction takes
place upon PRR stimulation (By similarity).
{ECO:0000250|UniProtKB:P51617, ECO:0000269|PubMed:17187069}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- DOMAIN: Contains an N-terminal kinase domain and a C-terminal
caspase activation and recruitment domain (CARD) that mediates the
recruitment of CARD-containing proteins.
{ECO:0000250|UniProtKB:P51617}.
-!- PTM: Autophosphorylated. Autophosphorylation at Tyr-473 is
necessary for effective NOD2 signaling.
{ECO:0000250|UniProtKB:P51617}.
-!- PTM: Ubiquitinated on Lys-209; undergoes 'Lys-63'-linked
polyubiquitination catalyzed by ITCH. Polyubiquitinated with 'Lys-
48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2,
leading to activation of NF-kappa-B. Also undergoes 'Met-1'-linked
polyubiquitination; the head-to-tail linear polyubiquitination is
mediated by the LUBAC complex in response to NOD2 stimulation.
Linear polyubiquitination is restricted by FAM105B/otulin,
probably to limit NOD2-dependent proinflammatory signaling
activation of NF-kappa-B (By similarity).
{ECO:0000250|UniProtKB:P51617}.
-!- DISRUPTION PHENOTYPE: Mice show a lack of chemokine production
induced by bacterial peptidoglycans. RIPK2 deficiency affects
cellular signaling and cytokine responses triggered by NOD1 and
NOD2 ligands, but not TLR ligands. {ECO:0000269|PubMed:17277144,
ECO:0000269|PubMed:21469090}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF461040; AAL96436.1; -; mRNA.
EMBL; BC069878; AAH69878.1; -; mRNA.
CCDS; CCDS17988.1; -.
RefSeq; NP_620402.1; NM_138952.4.
UniGene; Mm.112765; -.
ProteinModelPortal; P58801; -.
SMR; P58801; -.
BioGrid; 228697; 7.
CORUM; P58801; -.
IntAct; P58801; 2.
STRING; 10090.ENSMUSP00000038833; -.
iPTMnet; P58801; -.
PhosphoSitePlus; P58801; -.
EPD; P58801; -.
PaxDb; P58801; -.
PeptideAtlas; P58801; -.
PRIDE; P58801; -.
Ensembl; ENSMUST00000037035; ENSMUSP00000038833; ENSMUSG00000041135.
GeneID; 192656; -.
KEGG; mmu:192656; -.
UCSC; uc008sbr.1; mouse.
CTD; 8767; -.
MGI; MGI:1891456; Ripk2.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00550000074536; -.
HOGENOM; HOG000136856; -.
HOVERGEN; HBG054242; -.
InParanoid; P58801; -.
KO; K08846; -.
OMA; QWIQSKR; -.
OrthoDB; EOG091G0505; -.
PhylomeDB; P58801; -.
TreeFam; TF106506; -.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
PRO; PR:P58801; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000041135; -.
ExpressionAtlas; P58801; baseline and differential.
Genevisible; P58801; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050700; F:CARD domain binding; ISO:MGI.
GO; GO:0089720; F:caspase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030274; F:LIM domain binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:MGI.
GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
GO; GO:0071224; P:cellular response to peptidoglycan; IMP:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IMP:MGI.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:MGI.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI.
GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:0033091; P:positive regulation of immature T cell proliferation; IMP:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISO:MGI.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:MGI.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IMP:MGI.
GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IMP:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:1904417; P:positive regulation of xenophagy; IMP:MGI.
GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
GO; GO:0070555; P:response to interleukin-1; IMP:MGI.
GO; GO:0070671; P:response to interleukin-12; IMP:MGI.
GO; GO:0070673; P:response to interleukin-18; IMP:MGI.
GO; GO:0042098; P:T cell proliferation; IMP:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISO:MGI.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:MGI.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017322; Rcpt-int_Ser/Thr_kinase-2.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00619; CARD; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF037921; STPK_RIP2; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Adaptive immunity; Apoptosis; ATP-binding; Complete proteome;
Cytoplasm; Immunity; Innate immunity; Isopeptide bond; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 539 Receptor-interacting serine/threonine-
protein kinase 2.
/FTId=PRO_0000086609.
DOMAIN 18 294 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 431 523 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
NP_BIND 24 32 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 146 146 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 47 47 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 176 176 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 473 473 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000250|UniProtKB:O43353}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000250|UniProtKB:O43353}.
CROSSLNK 209 209 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O43353}.
SEQUENCE 539 AA; 60400 MW; 42951BF97CA15DFA CRC64;
MNGDAICSAL PPIPYHKLAD LHYLSRGASG TVSSARHADW RVRVAVKHLH IHTPLLDSER
NDILREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN GSLNELLHRK TEYPDIAWPL
RFRILHEIAL GVNYLHNMNP PLLHHDLKTQ NILLDNEFHV KIADFGLSKW RMMSLSQSRS
YKSAPEGGTI IYMPPENYEP GQKSRASVKH DIYSYAVIMW EVLSRKQPFE EVTNPLQIMY
SVSQGHRPDT SEENLPFDIP HRGLMISLIQ SGWAQNPDER PSFLKCLIEL EPVLRTFEDI
TFLEAVIQLK KAKIQSSSST IHLCDKKMDL SLNIPANHPP QEESCGSSLL SRNTGSPGPS
RSLSAPQDKG FLSGAPQDCS SLKAHHCPGN HSWDGIVSVP PGAAFCDRRA SSCSLAVISP
FLVEKGSERP PIGIAQQWIQ SKREAIVSQM TEACLNQSLD ALLSRDLIMK EDYELISTKP
TRTSKVRQLL DTSDIQGEEF AKVVVQKLKD NKQLGLQPYP EVPVLSKAPP SNFPQNKSL


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