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Receptor-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC 2.7.10.2)

 RIPK2_HUMAN             Reviewed;         540 AA.
O43353; B7Z748; Q6UWF0;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 2.
22-NOV-2017, entry version 191.
RecName: Full=Receptor-interacting serine/threonine-protein kinase 2;
EC=2.7.11.1;
AltName: Full=CARD-containing interleukin-1 beta-converting enzyme-associated kinase;
Short=CARD-containing IL-1 beta ICE-kinase;
AltName: Full=RIP-like-interacting CLARP kinase;
AltName: Full=Receptor-interacting protein 2;
Short=RIP-2;
AltName: Full=Tyrosine-protein kinase RIPK2;
EC=2.7.10.2;
Name=RIPK2; Synonyms=CARDIAK, RICK, RIP2;
ORFNames=UNQ277/PRO314/PRO34092;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-47.
PubMed=9575181; DOI=10.1074/jbc.273.20.12296;
Inohara N., del Peso L., Koseki T., Chen S., Nunez G.;
"RICK, a novel protein kinase containing a caspase recruitment domain,
interacts with CLARP and regulates CD95-mediated apoptosis.";
J. Biol. Chem. 273:12296-12300(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-47.
TISSUE=Endothelial cell;
PubMed=9642260; DOI=10.1074/jbc.273.27.16968;
McCarthy J.V., Ni J., Dixit V.M.;
"RIP2 is a novel NF-kappaB-activating and cell death-inducing
kinase.";
J. Biol. Chem. 273:16968-16975(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF ASP-146.
TISSUE=Pancreatic adenocarcinoma;
PubMed=9705938; DOI=10.1016/S0960-9822(07)00352-1;
Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L.,
Mattmann C., Tschopp J.;
"Identification of CARDIAK, a RIP-like kinase that associates with
caspase-1.";
Curr. Biol. 8:885-888(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[8]
FUNCTION.
PubMed=14638696; DOI=10.1074/jbc.C300460200;
Ruefli-Brasse A.A., Lee W.P., Hurst S., Dixit V.M.;
"Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-
kappaB activation.";
J. Biol. Chem. 279:1570-1574(2004).
[9]
PHOSPHORYLATION AT SER-176.
PubMed=16824733; DOI=10.1016/j.cellsig.2006.05.005;
Dorsch M., Wang A., Cheng H., Lu C., Bielecki A., Charron K.,
Clauser K., Ren H., Polakiewicz R.D., Parsons T., Li P., Ocain T.,
Xu Y.;
"Identification of a regulatory autophosphorylation site in the
serine-threonine kinase RIP2.";
Cell. Signal. 18:2223-2229(2006).
[10]
FUNCTION, INTERACTION WITH NOD1, AND MUTAGENESIS OF ARG-444; ARG-483
AND ARG-488.
PubMed=17054981; DOI=10.1016/j.jmb.2006.09.067;
Manon F., Favier A., Nunez G., Simorre J.P., Cusack S.;
"Solution structure of NOD1 CARD and mutational analysis of its
interaction with the CARD of downstream kinase RICK.";
J. Mol. Biol. 365:160-174(2007).
[11]
INTERACTION WITH MAP3K4.
PubMed=18775659; DOI=10.1016/j.cub.2008.07.084;
Clark N.M., Marinis J.M., Cobb B.A., Abbott D.W.;
"MEKK4 sequesters RIP2 to dictate NOD2 signal specificity.";
Curr. Biol. 18:1402-1408(2008).
[12]
INTERACTION WITH IKBKG/NEMO AND MAP3K7/TAK1, FUNCTION, UBIQUITINATION
AT LYS-209, AND MUTAGENESIS OF LYS-209.
PubMed=18079694; DOI=10.1038/sj.emboj.7601962;
Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G.,
Inohara N.;
"A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-
kappaB activation.";
EMBO J. 27:373-383(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-527 AND
SER-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
UBIQUITINATION BY ITCH, AND INTERACTION WITH NOD2.
PubMed=19592251; DOI=10.1016/j.cub.2009.06.038;
Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E.,
Abbott D.W.;
"ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence
inflammatory signaling pathways.";
Curr. Biol. 19:1255-1263(2009).
[16]
UBIQUITINATION BY BIRC2 AND BIRC3.
PubMed=19464198; DOI=10.1016/j.immuni.2009.04.011;
Bertrand M.J., Doiron K., Labbe K., Korneluk R.G., Barker P.A.,
Saleh M.;
"Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for
innate immunity signaling by the pattern recognition receptors NOD1
and NOD2.";
Immunity 30:789-801(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-363; SER-393;
SER-527 AND SER-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
FUNCTION, PHOSPHORYLATION AT TYR-474, AND MUTAGENESIS OF TYR-474.
PubMed=21123652; DOI=10.1101/gad.1964410;
Tigno-Aranjuez J.T., Asara J.M., Abbott D.W.;
"Inhibition of RIP2's tyrosine kinase activity limits NOD2-driven
cytokine responses.";
Genes Dev. 24:2666-2677(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
UBIQUITINATION BY BIRC2/C-IAP1 AND BIRC3/C-IAP2, AND INTERACTION WITH
BIRC2/C-IAP1; BIRC3/C-IAP2 AND XIAP/BIRC4.
PubMed=21931591; DOI=10.1371/journal.pone.0022356;
Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R.,
De Medts J., Gevaert K., Declercq W., Vandenabeele P.;
"cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin
chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).";
PLoS ONE 6:E22356-E22356(2011).
[22]
INTERACTION WITH NLRP10.
PubMed=22672233; DOI=10.1111/j.1462-5822.2012.01822.x;
Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P.,
Kremmer E., Kufer T.A.;
"NLRP10 enhances Shigella-induced pro-inflammatory responses.";
Cell. Microbiol. 14:1568-1583(2012).
[23]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ARHGEF2 AND NOD2,
INTERACTION WITH ARHGEF2 AND NOD2, AND PHOSPHORYLATION AT TYR-381.
PubMed=21887730; DOI=10.1002/ibd.21851;
Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B.,
Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.;
"Control of NOD2 and Rip2-dependent innate immune activation by GEF-
H1.";
Inflamm. Bowel Dis. 18:603-612(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-527; SER-529
AND SER-531, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
UBIQUITINATION, AND DEUBIQUITINATION.
PubMed=23806334; DOI=10.1016/j.molcel.2013.06.004;
Fiil B.K., Damgaard R.B., Wagner S.A., Keusekotten K., Fritsch M.,
Bekker-Jensen S., Mailand N., Choudhary C., Komander D.,
Gyrd-Hansen M.;
"OTULIN restricts Met1-linked ubiquitination to control innate immune
signaling.";
Mol. Cell 50:818-830(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
INTERACTION WITH INAVA.
PubMed=28436939; DOI=10.1172/JCI86282;
Yan J., Hedl M., Abraham C.;
"An inflammatory bowel disease-risk variant in INAVA decreases pattern
recognition receptor-induced outcomes.";
J. Clin. Invest. 127:2192-2205(2017).
[28]
VARIANTS [LARGE SCALE ANALYSIS] THR-259; VAL-268 AND ASN-313.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. Contributes to the tyrosine phosphorylation of the
guanine exchange factor ARHGEF2 through Src tyrosine kinase
leading to NF-kappaB activation by NOD2. Once recruited, RIPK2
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 released 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:14638696,
ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:18079694,
ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730}.
-!- 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; the interaction
mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK.
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.
Interacts with CARD9. Interacts with INAVA; the interaction takes
place upon PRR stimulation (PubMed:28436939).
{ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:18079694,
ECO:0000269|PubMed:18775659, ECO:0000269|PubMed:19592251,
ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:21931591,
ECO:0000269|PubMed:22672233, ECO:0000269|PubMed:28436939}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-358522, EBI-358522;
Q13490:BIRC2; NbExp=3; IntAct=EBI-358522, EBI-514538;
Q13489:BIRC3; NbExp=3; IntAct=EBI-358522, EBI-517709;
Q9BX69:CARD6; NbExp=2; IntAct=EBI-358522, EBI-14405242;
Q7Z434:MAVS; NbExp=3; IntAct=EBI-358522, EBI-995373;
Q9HC29:NOD2; NbExp=2; IntAct=EBI-358522, EBI-7445625;
Q13114:TRAF3; NbExp=5; IntAct=EBI-358522, EBI-357631;
P98170:XIAP; NbExp=12; IntAct=EBI-358522, EBI-517127;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43353-1; Sequence=Displayed;
Name=2;
IsoId=O43353-2; Sequence=VSP_013266;
-!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung,
peripheral blood leukocytes, spleen, kidney, testis, prostate,
pancreas and lymph node.
-!- 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.
-!- PTM: Autophosphorylated. Autophosphorylation at Tyr-474 is
necessary for effective NOD2 signaling. Phosphorylated.
Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-
dependent manner and is required for NOD2-dependent innate immune
activation. {ECO:0000269|PubMed:16824733,
ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730}.
-!- 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. {ECO:0000269|PubMed:18079694,
ECO:0000269|PubMed:19464198, ECO:0000269|PubMed:19592251,
ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23806334}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; AF027706; AAC34970.1; -; mRNA.
EMBL; AF078530; AAC27722.1; -; mRNA.
EMBL; AF064824; AAC25668.1; -; mRNA.
EMBL; AY358813; AAQ89172.1; -; mRNA.
EMBL; AY358814; AAQ89173.1; -; mRNA.
EMBL; AK301448; BAH13484.1; -; mRNA.
EMBL; AC004003; AAC24561.1; -; Genomic_DNA.
EMBL; AF117829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004553; AAH04553.1; -; mRNA.
CCDS; CCDS6247.1; -. [O43353-1]
RefSeq; NP_003812.1; NM_003821.5. [O43353-1]
RefSeq; XP_005251149.1; XM_005251092.3. [O43353-2]
UniGene; Hs.103755; -.
PDB; 2N7Z; NMR; -; A=434-539.
PDB; 2N83; NMR; -; B=434-539.
PDB; 4C8B; X-ray; 2.75 A; A/B=8-317.
PDB; 5AR2; X-ray; 2.44 A; A/B=1-310.
PDB; 5AR3; X-ray; 3.23 A; A/B=1-310.
PDB; 5AR4; X-ray; 2.70 A; A/B=1-310.
PDB; 5AR5; X-ray; 2.66 A; A/B=1-310.
PDB; 5AR7; X-ray; 2.71 A; A/B=1-310.
PDB; 5AR8; X-ray; 2.79 A; A/B=1-310.
PDB; 5J79; X-ray; 2.69 A; A/B=1-310.
PDB; 5J7B; X-ray; 2.53 A; A/B=1-310.
PDB; 5NG0; X-ray; 2.00 A; A/B=1-300.
PDB; 5NG2; X-ray; 2.80 A; A/B=1-300.
PDB; 5NG3; X-ray; 2.60 A; A/B/C/D=1-300.
PDBsum; 2N7Z; -.
PDBsum; 2N83; -.
PDBsum; 4C8B; -.
PDBsum; 5AR2; -.
PDBsum; 5AR3; -.
PDBsum; 5AR4; -.
PDBsum; 5AR5; -.
PDBsum; 5AR7; -.
PDBsum; 5AR8; -.
PDBsum; 5J79; -.
PDBsum; 5J7B; -.
PDBsum; 5NG0; -.
PDBsum; 5NG2; -.
PDBsum; 5NG3; -.
ProteinModelPortal; O43353; -.
SMR; O43353; -.
BioGrid; 114300; 47.
DIP; DIP-27518N; -.
IntAct; O43353; 15.
MINT; MINT-90752; -.
STRING; 9606.ENSP00000220751; -.
BindingDB; O43353; -.
ChEMBL; CHEMBL5014; -.
GuidetoPHARMACOLOGY; 2190; -.
iPTMnet; O43353; -.
PhosphoSitePlus; O43353; -.
BioMuta; RIPK2; -.
EPD; O43353; -.
MaxQB; O43353; -.
PaxDb; O43353; -.
PeptideAtlas; O43353; -.
PRIDE; O43353; -.
DNASU; 8767; -.
Ensembl; ENST00000220751; ENSP00000220751; ENSG00000104312. [O43353-1]
GeneID; 8767; -.
KEGG; hsa:8767; -.
UCSC; uc003yee.4; human. [O43353-1]
CTD; 8767; -.
DisGeNET; 8767; -.
EuPathDB; HostDB:ENSG00000104312.7; -.
GeneCards; RIPK2; -.
HGNC; HGNC:10020; RIPK2.
HPA; HPA015273; -.
HPA; HPA016499; -.
MIM; 603455; gene.
neXtProt; NX_O43353; -.
OpenTargets; ENSG00000104312; -.
PharmGKB; PA34395; -.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00550000074536; -.
HOGENOM; HOG000136856; -.
HOVERGEN; HBG054242; -.
InParanoid; O43353; -.
KO; K08846; -.
OMA; QWIQSKR; -.
OrthoDB; EOG091G0505; -.
PhylomeDB; O43353; -.
TreeFam; TF106506; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
SignaLink; O43353; -.
SIGNOR; O43353; -.
ChiTaRS; RIPK2; human.
GeneWiki; RIPK2; -.
GenomeRNAi; 8767; -.
PRO; PR:O43353; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104312; -.
CleanEx; HS_RIPK2; -.
ExpressionAtlas; O43353; baseline and differential.
Genevisible; O43353; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050700; F:CARD domain binding; IDA:MGI.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030274; F:LIM domain binding; IPI:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl.
GO; GO:0071225; P:cellular response to muramyl dipeptide; IDA:UniProtKB.
GO; GO:0071224; P:cellular response to peptidoglycan; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0033091; P:positive regulation of immature T cell proliferation; IEA:Ensembl.
GO; GO:0032727; P:positive regulation of interferon-alpha production; NAS:BHF-UCL.
GO; GO:0032728; P:positive regulation of interferon-beta production; NAS:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; NAS:BHF-UCL.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IMP:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; NAS:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0070671; P:response to interleukin-12; IEA:Ensembl.
GO; GO:0070673; P:response to interleukin-18; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IDA:MGI.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
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;
3D-structure; Adaptive immunity; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Cytoplasm; Immunity; Innate immunity;
Isopeptide bond; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 540 Receptor-interacting serine/threonine-
protein kinase 2.
/FTId=PRO_0000086608.
DOMAIN 18 294 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 432 524 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
NP_BIND 24 32 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 146 146 Proton acceptor.
BINDING 47 47 ATP.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 176 176 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16824733}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 381 381 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:21887730}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 474 474 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:21123652}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
CROSSLNK 209 209 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18079694}.
VAR_SEQ 1 137 Missing (in isoform 2).
{ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_013266.
VARIANT 259 259 I -> T (in dbSNP:rs2230801).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041045.
VARIANT 268 268 L -> V (in dbSNP:rs35004667).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041046.
VARIANT 313 313 K -> N (in dbSNP:rs35395048).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041047.
MUTAGEN 47 47 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:9575181,
ECO:0000269|PubMed:9642260}.
MUTAGEN 47 47 K->M: Reduces FAS-mediated apoptosis.
{ECO:0000269|PubMed:9575181,
ECO:0000269|PubMed:9642260}.
MUTAGEN 146 146 D->N: Abolishes kinase activity.
{ECO:0000269|PubMed:9705938}.
MUTAGEN 209 209 K->R: Complete loss of
polyubiquitination.
{ECO:0000269|PubMed:18079694}.
MUTAGEN 381 381 Y->A: Prevents phosphorylation. Reduces
serine and threonine phosphorylation of
ARHGEF2.
MUTAGEN 444 444 R->E: Abolishes interaction with NOD1.
{ECO:0000269|PubMed:17054981}.
MUTAGEN 474 474 Y->F: Decreases interaction with NOD2.
{ECO:0000269|PubMed:21123652}.
MUTAGEN 483 483 R->E: Abolishes interaction with NOD1.
{ECO:0000269|PubMed:17054981}.
MUTAGEN 488 488 R->E: Abolishes interaction with NOD1.
{ECO:0000269|PubMed:17054981}.
CONFLICT 271 271 S -> G (in Ref. 5; BAH13484).
{ECO:0000305}.
CONFLICT 514 514 Q -> R (in Ref. 5; BAH13484).
{ECO:0000305}.
STRAND 7 9 {ECO:0000244|PDB:5NG0}.
HELIX 15 17 {ECO:0000244|PDB:5NG0}.
STRAND 18 26 {ECO:0000244|PDB:5NG0}.
STRAND 31 37 {ECO:0000244|PDB:5NG0}.
TURN 38 40 {ECO:0000244|PDB:5NG0}.
STRAND 43 48 {ECO:0000244|PDB:5NG0}.
STRAND 51 53 {ECO:0000244|PDB:5NG0}.
HELIX 57 72 {ECO:0000244|PDB:5NG0}.
STRAND 81 87 {ECO:0000244|PDB:5NG0}.
STRAND 90 96 {ECO:0000244|PDB:5NG0}.
HELIX 103 108 {ECO:0000244|PDB:5NG0}.
TURN 110 112 {ECO:0000244|PDB:5NG0}.
HELIX 118 136 {ECO:0000244|PDB:5NG0}.
STRAND 138 140 {ECO:0000244|PDB:5NG0}.
HELIX 149 151 {ECO:0000244|PDB:5NG0}.
STRAND 152 154 {ECO:0000244|PDB:5NG0}.
STRAND 160 162 {ECO:0000244|PDB:5NG0}.
HELIX 168 176 {ECO:0000244|PDB:5NG3}.
HELIX 190 192 {ECO:0000244|PDB:5J79}.
HELIX 195 197 {ECO:0000244|PDB:5NG0}.
TURN 202 204 {ECO:0000244|PDB:5AR4}.
HELIX 210 224 {ECO:0000244|PDB:5NG0}.
TURN 228 231 {ECO:0000244|PDB:5NG0}.
HELIX 235 243 {ECO:0000244|PDB:5NG0}.
TURN 252 254 {ECO:0000244|PDB:5NG0}.
HELIX 262 272 {ECO:0000244|PDB:5NG0}.
HELIX 277 279 {ECO:0000244|PDB:5NG0}.
HELIX 283 295 {ECO:0000244|PDB:5NG0}.
HELIX 299 307 {ECO:0000244|PDB:5AR2}.
HELIX 436 450 {ECO:0000244|PDB:2N7Z}.
HELIX 453 465 {ECO:0000244|PDB:2N7Z}.
HELIX 471 476 {ECO:0000244|PDB:2N7Z}.
HELIX 483 497 {ECO:0000244|PDB:2N7Z}.
HELIX 501 511 {ECO:0000244|PDB:2N7Z}.
STRAND 526 528 {ECO:0000244|PDB:2N7Z}.
TURN 530 532 {ECO:0000244|PDB:2N83}.
SEQUENCE 540 AA; 61195 MW; 575A692239505792 CRC64;
MNGEAICSAL PTIPYHKLAD LRYLSRGASG TVSSARHADW RVQVAVKHLH IHTPLLDSER
KDVLREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN GSLNELLHRK TEYPDVAWPL
RFRILHEIAL GVNYLHNMTP PLLHHDLKTQ NILLDNEFHV KIADFGLSKW RMMSLSQSRS
SKSAPEGGTI IYMPPENYEP GQKSRASIKH DIYSYAVITW EVLSRKQPFE DVTNPLQIMY
SVSQGHRPVI NEESLPYDIP HRARMISLIE SGWAQNPDER PSFLKCLIEL EPVLRTFEEI
TFLEAVIQLK KTKLQSVSSA IHLCDKKKME LSLNIPVNHG PQEESCGSSQ LHENSGSPET
SRSLPAPQDN DFLSRKAQDC YFMKLHHCPG NHSWDSTISG SQRAAFCDHK TTPCSSAIIN
PLSTAGNSER LQPGIAQQWI QSKREDIVNQ MTEACLNQSL DALLSRDLIM KEDYELVSTK
PTRTSKVRQL LDTTDIQGEE FAKVIVQKLK DNKQMGLQPY PEILVVSRSP SLNLLQNKSM


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