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Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1) (Serine/threonine-protein kinase RIP)

 RIPK1_HUMAN             Reviewed;         671 AA.
Q13546; A0AV89; B2RAG1; B4E3F9; Q13180; Q59H33;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 3.
30-AUG-2017, entry version 188.
RecName: Full=Receptor-interacting serine/threonine-protein kinase 1;
EC=2.7.11.1;
AltName: Full=Cell death protein RIP;
AltName: Full=Receptor-interacting protein 1;
Short=RIP-1;
AltName: Full=Serine/threonine-protein kinase RIP;
Name=RIPK1; Synonyms=RIP, RIP1;
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), AUTOPHOSPHORYLATION,
MUTAGENESIS OF LYS-45, INTERACTION WITH TRADD; TRAF1; TRAF2 AND TRAF3,
AND VARIANT VAL-438.
TISSUE=Umbilical vein endothelial cell;
PubMed=8612133; DOI=10.1016/S1074-7613(00)80252-6;
Hsu H., Huang J., Shu H.-B., Baichwal V.R., Goeddel D.V.;
"TNF-dependent recruitment of the protein kinase RIP to the TNF
receptor-1 signaling complex.";
Immunity 4:387-396(1996).
[2]
SEQUENCE REVISION TO 120.
Huang J., Hsu H., Baichwal V.R., Goeddel D.V.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 15-671 (ISOFORM 2).
TISSUE=Adrenal gland, and Uterus;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-234.
SeattleSNPs variation discovery resource;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-438.
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-671.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 300-671, AND VARIANT VAL-438.
TISSUE=Leukemic T-cell;
PubMed=7538908; DOI=10.1016/0092-8674(95)90072-1;
Stanger B.Z., Leder P., Lee T.-H., Kim E., Seed B.;
"RIP: a novel protein containing a death domain that interacts with
Fas/APO-1 (CD95) in yeast and causes cell death.";
Cell 81:513-523(1995).
[9]
CLEAVAGE BY CASPASE-8, AND MUTAGENESIS OF ASP-324.
PubMed=10521396; DOI=10.1101/gad.13.19.2514;
Lin Y., Devin A., Rodriguez Y., Liu Z.-G.;
"Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-
induced apoptosis.";
Genes Dev. 13:2514-2526(1999).
[10]
INTERACTION WITH SQSTM1 AND TRAF2, AND DOMAIN.
PubMed=10356400; DOI=10.1093/emboj/18.11.3044;
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB
activation.";
EMBO J. 18:3044-3053(1999).
[11]
INTERACTION WITH RIPK3.
PubMed=10358032; DOI=10.1074/jbc.274.24.16871;
Sun X., Lee J., Navas T., Baldwin D.T., Stewart T.A., Dixit V.M.;
"RIP3, a novel apoptosis-inducing kinase.";
J. Biol. Chem. 274:16871-16875(1999).
[12]
INTERACTION WITH BNLF1.
PubMed=10409763; DOI=10.1128/MCB.19.8.5759;
Izumi K.M., Cahir McFarland E., Ting A.T., Riley E.A., Seed B.,
Kieff E.D.;
"The Epstein-Barr virus oncoprotein latent membrane protein 1 engages
the tumor necrosis factor receptor-associated proteins TRADD and
receptor-interacting protein (RIP) but does not induce apoptosis or
require RIP for NF-kappaB activation.";
Mol. Cell. Biol. 19:5759-5767(1999).
[13]
INTERACTION WITH IKBKG.
PubMed=9927690; DOI=10.1073/pnas.96.3.1042;
Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A.,
Wallach D., Horwitz M.S.;
"Identification of a cell protein (FIP-3) as a modulator of NF-kappaB
activity and as a target of an adenovirus inhibitor of tumor necrosis
factor alpha-induced apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999).
[14]
FUNCTION.
PubMed=11101870; DOI=10.1038/82732;
Holler N., Zaru R., Micheau O., Thome M., Attinger A., Valitutti S.,
Bodmer J.L., Schneider P., Seed B., Tschopp J.;
"Fas triggers an alternative, caspase-8-independent cell death pathway
using the kinase RIP as effector molecule.";
Nat. Immunol. 1:489-495(2000).
[15]
INTERACTION WITH EGFR.
PubMed=11116146; DOI=10.1074/jbc.M008458200;
Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S.,
Vartanian T.;
"The epidermal growth factor receptor engages receptor interacting
protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to
activate NF-kappa B. Identification of a novel receptor-tyrosine
kinase signalosome.";
J. Biol. Chem. 276:8865-8874(2001).
[16]
INTERACTION WITH RNF216.
PubMed=11854271; DOI=10.1074/jbc.M108675200;
Chen D., Li X., Zhai Z., Shu H.-B.;
"A novel zinc finger protein interacts with receptor-interacting
protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-
induced NF-kappa B activation.";
J. Biol. Chem. 277:15985-15991(2002).
[17]
RIP HOMOTYPIC INTERACTION MOTIF, AND INTERACTION WITH RIPK3.
PubMed=11734559; DOI=10.1074/jbc.M109488200;
Sun X., Yin J., Starovasnik M.A., Fairbrother W.J., Dixit V.M.;
"Identification of a novel homotypic interaction motif required for
the phosphorylation of receptor-interacting protein (RIP) by RIP3.";
J. Biol. Chem. 277:9505-9511(2002).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-384, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[19]
INTERACTION WITH ZFAND5.
PubMed=14754897; DOI=10.1074/jbc.M309491200;
Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z.,
Shu H.-B.;
"ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor
of NFkappaB activation.";
J. Biol. Chem. 279:16847-16853(2004).
[20]
UBIQUITINATION BY TRAF2, AND DEUBIQUITINATION BY TNFAIP3.
PubMed=15258597; DOI=10.1038/nature02794;
Wertz I.E., O'Rourke K.M., Zhou H., Eby M., Aravind L., Seshagiri S.,
Wu P., Wiesmann C., Baker R., Boone D.L., Ma A., Koonin E.V.,
Dixit V.M.;
"De-ubiquitination and ubiquitin ligase domains of A20 downregulate
NF-kappaB signalling.";
Nature 430:694-699(2004).
[21]
INTERACTION WITH MAVS.
PubMed=16127453; DOI=10.1038/ni1243;
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H.,
Ishii K.J., Takeuchi O., Akira S.;
"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
interferon induction.";
Nat. Immunol. 6:981-988(2005).
[22]
UBIQUITINATION AT LYS-377, AND MUTAGENESIS OF LYS-377.
PubMed=16603398; DOI=10.1016/j.molcel.2006.03.026;
Ea C.K., Deng L., Xia Z.P., Pineda G., Chen Z.J.;
"Activation of IKK by TNFalpha requires site-specific ubiquitination
of RIP1 and polyubiquitin binding by NEMO.";
Mol. Cell 22:245-257(2006).
[23]
REVIEW.
PubMed=17301840; DOI=10.1038/sj.cdd.4402085;
Festjens N., Vanden Berghe T., Cornelis S., Vandenabeele P.;
"RIP1, a kinase on the crossroads of a cell's decision to live or
die.";
Cell Death Differ. 14:400-410(2007).
[24]
FUNCTION IN PHOSPHORYLATION OF DAB2IP, AND INTERACTION WITH DAB2IP.
PubMed=17389591; DOI=10.1074/jbc.M701148200;
Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.;
"RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is
critical for tumor necrosis factor-induced ASK1-JNK/p38 activation.";
J. Biol. Chem. 282:14788-14796(2007).
[25]
INTERACTION WITH RBCK1.
PubMed=17449468; DOI=10.1074/jbc.M701913200;
Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P.,
Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.;
"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
J. Biol. Chem. 282:16776-16782(2007).
[26]
INTERACTION WITH RFFL, AND UBIQUITINATION BY RFFL.
PubMed=18450452; DOI=10.1016/j.cub.2008.04.017;
Liao W., Xiao Q., Tchikov V., Fujita K., Yang W., Wincovitch S.,
Garfield S., Conze D., El-Deiry W.S., Schuetze S., Srinivasula S.M.;
"CARP-2 is an endosome-associated ubiquitin ligase for RIP and
regulates TNF-induced NF-kappaB activation.";
Curr. Biol. 18:641-649(2008).
[27]
MUTAGENESIS OF SER-161, INHIBITION BY NECROSTATIN-1, AND
PHOSPHORYLATION AT SER-6; SER-20; SER-25; SER-161; SER-166; SER-303;
SER-320 AND SER-333.
PubMed=18408713; DOI=10.1038/nchembio.83;
Degterev A., Hitomi J., Germscheid M., Ch'en I.L., Korkina O.,
Teng X., Abbott D., Cuny G.D., Yuan C., Wagner G., Hedrick S.M.,
Gerber S.A., Lugovskoy A., Yuan J.;
"Identification of RIP1 kinase as a specific cellular target of
necrostatins.";
Nat. Chem. Biol. 4:313-321(2008).
[28]
INTERACTION WITH MURID HERPESVIRUS 1 VIRAL INHIBITOR OF RIP
ACTIVATION.
PubMed=18442983; DOI=10.1074/jbc.C800051200;
Upton J.W., Kaiser W.J., Mocarski E.S.;
"Cytomegalovirus M45 cell death suppression requires receptor-
interacting protein (RIP) homotypic interaction motif (RHIM)-dependent
interaction with RIP1.";
J. Biol. Chem. 283:16966-16970(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, 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).
[30]
FUNCTION, AND PHOSPHORYLATION.
PubMed=19524513; DOI=10.1016/j.cell.2009.05.037;
Cho Y.S., Challa S., Moquin D., Genga R., Ray T.D., Guildford M.,
Chan F.K.;
"Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates
programmed necrosis and virus-induced inflammation.";
Cell 137:1112-1123(2009).
[31]
FUNCTION, AND INTERACTION WITH RIPK3.
PubMed=19524512; DOI=10.1016/j.cell.2009.05.021;
He S., Wang L., Miao L., Wang T., Du F., Zhao L., Wang X.;
"Receptor interacting protein kinase-3 determines cellular necrotic
response to TNF-alpha.";
Cell 137:1100-1111(2009).
[32]
INTERACTION WITH RNF34, AND UBIQUITINATION BY RNF34.
DOI=10.1016/j.cub.2008.11.041;
Liao W., Fujita K., Xiao Q., Tchikov V., Yang W., Gunsor M.,
Garfield S., Goldsmith P., El-Deiry W.S., Schuetze S.,
Srinivasula S.M.;
"Response: CARP1 regulates induction of NF-kappaB by TNFalpha.";
Curr. Biol. 19:R17-R19(2009).
[33]
REVIEW.
PubMed=20354226; DOI=10.1126/scisignal.3115re4;
Vandenabeele P., Declercq W., Van Herreweghe F., Vanden Berghe T.;
"The role of the kinases RIP1 and RIP3 in TNF-induced necrosis.";
Sci. Signal. 3:RE4-RE4(2010).
[34]
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).
[35]
UBIQUITINATION BY THE LUBAC COMPLEX.
PubMed=21455173; DOI=10.1038/nature09816;
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E.,
Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W.,
Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J.,
Walczak H.;
"Linear ubiquitination prevents inflammation and regulates immune
signalling.";
Nature 471:591-596(2011).
[36]
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).
[37]
IDENTIFICATION IN COMPLEX WITH PGAM5; RIPK3 AND MLKL.
PubMed=22265414; DOI=10.1016/j.cell.2011.11.030;
Wang Z., Jiang H., Chen S., Du F., Wang X.;
"The mitochondrial phosphatase PGAM5 functions at the convergence
point of multiple necrotic death pathways.";
Cell 148:228-243(2012).
[38]
INTERACTION WITH ARHGEF2.
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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[40]
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).
[41]
INTERACTION WITH TICAM1.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[42]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-294 IN COMPLEXES WITH
NECROSTATIN-TYPE INHIBITORS, CATALYTIC ACTIVITY, ENZYME REGULATION,
AND AUTOPHOSPHORYLATION.
PubMed=23473668; DOI=10.1016/j.str.2013.01.016;
Xie T., Peng W., Liu Y., Yan C., Maki J., Degterev A., Yuan J.,
Shi Y.;
"Structural basis of RIP1 inhibition by necrostatins.";
Structure 21:493-499(2013).
[43]
VARIANTS [LARGE SCALE ANALYSIS] VAL-64; ILE-81; VAL-220; SER-404;
VAL-443 AND VAL-569.
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 kinase which transduces inflammatory
and cell-death signals (programmed necrosis) following death
receptors ligation, activation of pathogen recognition receptors
(PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha
family cytokines, TRADD and TRAF2 are recruited to the receptor.
Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent
manner, and thereby activates the MAP3K5-JNK apoptotic cascade.
Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a
critical enhancer of communication with downstream signal
transducers in the mitogen-activated protein kinase pathway and
the NF-kappa-B pathway, which in turn mediate downstream events
including the activation of genes encoding inflammatory molecules.
Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory
subunit of the IKK complex, a critical event for NF-kappa-B
activation. Interaction with other cellular RHIM-containing
adapters initiates gene activation and cell death. RIPK1 and RIPK3
association, in particular, forms a necrosis-inducing complex.
{ECO:0000269|PubMed:11101870, ECO:0000269|PubMed:17389591,
ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:23473668}.
-!- ENZYME REGULATION: Inhibited by necrostatins, including
necrostatin-1, necrostatin-3 and necrostatin-4.
{ECO:0000269|PubMed:23473668}.
-!- SUBUNIT: Interacts (via RIP homotypic interaction motif) with
RIPK3 (via RIP homotypic interaction motif). Upon TNF-induced
necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and
MLKL; the formation of this complex leads to PGAM5 phosphorylation
and increase in PGAM5 phosphatase activity. Interacts (via the
death domain) with TNFRSF6 (via the death domain) and TRADD (via
the death domain). Is recruited by TRADD to TNFRSF1A in a TNF-
dependent process. Binds RNF216, EGFR, IKBKG, TRAF1, TRAF2 and
TRAF3. Interacts with BNLF1. Interacts with SQSTM1 upon TNF-alpha
stimulation. May interact with MAVS/IPS1. Interacts with ZFAND5.
Interacts with RBCK1 (By similarity). Interacts with ZBP1 (By
similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and
XIAP/BIRC4. Upon TNF-induced necrosis, forms in complex with
PGAM5, RIPK3 and MLKL. Interacts (via kinase domain) with DAB2IP
(via Ras-GAP domain); the interaction occurs in a TNF-alpha-
dependent manner. Interacts with ARHGEF2. Interacts (via protein
kinase domain) with RFFL; involved in RIPK1 ubiquitination.
Interacts with RNF34; involved in RIPK1 ubiquitination. Interacts
with TICAM1 and this interaction is enhanced in the presence of
WDFY1 (PubMed:25736436). {ECO:0000250|UniProtKB:Q60855,
ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10358032,
ECO:0000269|PubMed:10409763, ECO:0000269|PubMed:11116146,
ECO:0000269|PubMed:11734559, ECO:0000269|PubMed:11854271,
ECO:0000269|PubMed:14754897, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:17449468,
ECO:0000269|PubMed:18442983, ECO:0000269|PubMed:18450452,
ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:21887730,
ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:22265414,
ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:8612133,
ECO:0000269|PubMed:9927690, ECO:0000269|Ref.32}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-358507, EBI-358507;
P04083:ANXA1; NbExp=5; IntAct=EBI-358507, EBI-354007;
Q13490:BIRC2; NbExp=3; IntAct=EBI-358507, EBI-514538;
Q13489:BIRC3; NbExp=3; IntAct=EBI-358507, EBI-517709;
Q92851:CASP10; NbExp=2; IntAct=EBI-358507, EBI-495095;
Q14790:CASP8; NbExp=24; IntAct=EBI-358507, EBI-78060;
Q8IVM0:CCDC50; NbExp=2; IntAct=EBI-358507, EBI-723996;
P48729:CSNK1A1; NbExp=5; IntAct=EBI-358507, EBI-1383726;
Q13158:FADD; NbExp=11; IntAct=EBI-358507, EBI-494804;
Q9Y6K9:IKBKG; NbExp=7; IntAct=EBI-358507, EBI-81279;
Q9ULZ3:PYCARD; NbExp=2; IntAct=EBI-358507, EBI-751215;
Q9Y572:RIPK3; NbExp=26; IntAct=EBI-358507, EBI-298250;
Q9QZL0:Ripk3 (xeno); NbExp=2; IntAct=EBI-358507, EBI-2367423;
P19438:TNFRSF1A; NbExp=6; IntAct=EBI-358507, EBI-299451;
Q13077:TRAF1; NbExp=5; IntAct=EBI-358507, EBI-359224;
Q12933:TRAF2; NbExp=6; IntAct=EBI-358507, EBI-355744;
U5TQE9:UL39 (xeno); NbExp=3; IntAct=EBI-358507, EBI-11894787;
Q13107:USP4; NbExp=4; IntAct=EBI-358507, EBI-723290;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13546-1; Sequence=Displayed;
Name=2;
IsoId=Q13546-2; Sequence=VSP_037690;
Note=No experimental confirmation available.;
-!- DOMAIN: Contains a C-terminal death domain (DD) that engages other
DD-containing proteins as well as a central (intermediate) region
important for NF-kB activation and RHIM-dependent signaling.
{ECO:0000269|PubMed:10356400}.
-!- PTM: Proteolytically cleaved by caspase-8 during TNF-induced
apoptosis. Cleavage abolishes NF-kappa-B activation and enhances
pro-apoptotic signaling through the TRADD-FADD interaction.
{ECO:0000269|PubMed:10521396}.
-!- PTM: RIPK1 and RIPK3 undergo reciprocal auto- and trans-
phosphorylation. Phosphorylation of Ser-161 by RIPK3 is necessary
for the formation of the necroptosis-inducing complex.
{ECO:0000269|PubMed:18408713, ECO:0000269|PubMed:19524513}.
-!- PTM: Ubiquitinated by 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-
linked type ubiquitin. Polyubiquitination with 'Lys-63'-linked
chains by TRAF2 induces association with the IKK complex.
Deubiquitination of 'Lys-63'-linked chains and polyubiquitination
with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal
degradation and consequently down-regulates TNF-alpha-induced
NFkappa-B signaling. 'Lys-48'-linked polyubiquitination by RFFL or
RNF34 also promotes proteasomal degradation and negatively
regulates TNF-alpha-induced NFkappa-B signaling. Linear
polyubiquitinated; the head-to-tail polyubiquitination is mediated
by the LUBAC complex. LPS-mediated activation of NF-kappa-B. Also
ubiquitinated with 'Lys-11'-linked chains. Polyubiquitinated with
'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-
IAP2, leading to activation of NF-kappa-B.
{ECO:0000269|PubMed:15258597, ECO:0000269|PubMed:16603398,
ECO:0000269|PubMed:18450452, ECO:0000269|PubMed:21455173,
ECO:0000269|PubMed:21931591, ECO:0000269|Ref.32}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG65471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ripk1/";
-----------------------------------------------------------------------
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EMBL; U50062; AAC32232.1; -; mRNA.
EMBL; AK314176; BAG36858.1; -; mRNA.
EMBL; AK304701; BAG65471.1; ALT_INIT; mRNA.
EMBL; AY682848; AAT74626.1; -; Genomic_DNA.
EMBL; AL031963; CAD70625.1; -; Genomic_DNA.
EMBL; BC126254; AAI26255.1; -; mRNA.
EMBL; BC126256; AAI26257.1; -; mRNA.
EMBL; AB208926; BAD92163.1; -; mRNA.
EMBL; U25994; AAC50137.1; -; mRNA.
CCDS; CCDS4482.1; -. [Q13546-1]
PIR; T09479; T09479.
RefSeq; NP_001303990.1; NM_001317061.1.
RefSeq; NP_003795.2; NM_003804.4. [Q13546-1]
RefSeq; XP_005249514.2; XM_005249457.3. [Q13546-1]
UniGene; Hs.519842; -.
PDB; 4ITH; X-ray; 2.25 A; A/B=1-294.
PDB; 4ITI; X-ray; 2.86 A; A/B=1-294.
PDB; 4ITJ; X-ray; 1.80 A; A/B=1-294.
PDB; 4NEU; X-ray; 2.57 A; A/B=1-324.
PDB; 5HX6; X-ray; 2.23 A; A/B=1-294.
PDBsum; 4ITH; -.
PDBsum; 4ITI; -.
PDBsum; 4ITJ; -.
PDBsum; 4NEU; -.
PDBsum; 5HX6; -.
ProteinModelPortal; Q13546; -.
SMR; Q13546; -.
BioGrid; 114274; 85.
DIP; DIP-433N; -.
IntAct; Q13546; 39.
MINT; MINT-128219; -.
STRING; 9606.ENSP00000259808; -.
BindingDB; Q13546; -.
ChEMBL; CHEMBL5464; -.
GuidetoPHARMACOLOGY; 2189; -.
iPTMnet; Q13546; -.
PhosphoSitePlus; Q13546; -.
BioMuta; RIPK1; -.
DMDM; 60393639; -.
EPD; Q13546; -.
MaxQB; Q13546; -.
PaxDb; Q13546; -.
PeptideAtlas; Q13546; -.
PRIDE; Q13546; -.
DNASU; 8737; -.
Ensembl; ENST00000259808; ENSP00000259808; ENSG00000137275. [Q13546-1]
Ensembl; ENST00000380409; ENSP00000369773; ENSG00000137275. [Q13546-1]
GeneID; 8737; -.
KEGG; hsa:8737; -.
UCSC; uc003mux.4; human. [Q13546-1]
CTD; 8737; -.
DisGeNET; 8737; -.
GeneCards; RIPK1; -.
HGNC; HGNC:10019; RIPK1.
HPA; CAB010302; -.
HPA; HPA015257; -.
MIM; 603453; gene.
neXtProt; NX_Q13546; -.
OpenTargets; ENSG00000137275; -.
PharmGKB; PA34394; -.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00550000074536; -.
HOGENOM; HOG000010270; -.
HOVERGEN; HBG055612; -.
InParanoid; Q13546; -.
KO; K02861; -.
OMA; VMEYMEK; -.
OrthoDB; EOG091G0479; -.
PhylomeDB; Q13546; -.
TreeFam; TF106506; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75893; TNF signaling.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
SignaLink; Q13546; -.
SIGNOR; Q13546; -.
ChiTaRS; RIPK1; human.
GeneWiki; RIPK1; -.
GenomeRNAi; 8737; -.
PMAP-CutDB; Q13546; -.
PRO; PR:Q13546; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137275; -.
CleanEx; HS_RIPK1; -.
ExpressionAtlas; Q13546; baseline and differential.
Genevisible; Q13546; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031264; C:death-inducing signaling complex; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0070513; F:death domain binding; IPI:BHF-UCL.
GO; GO:0005123; F:death receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0007257; P:activation of JUN kinase activity; TAS:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0044257; P:cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0070266; P:necroptotic process; IMP:UniProtKB.
GO; GO:0097527; P:necroptotic signaling pathway; IMP:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1905206; P:positive regulation of hydrogen peroxide-induced cell death; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:UniProtKB.
GO; GO:0060545; P:positive regulation of necroptotic process; IMP:UniProtKB.
GO; GO:0010940; P:positive regulation of necrotic cell death; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; TAS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051291; P:protein heterooligomerization; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0070926; P:regulation of ATP:ADP antiporter activity; IMP:BHF-UCL.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0034612; P:response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0097343; P:ripoptosome assembly; IMP:UniProtKB.
GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; IBA:GO_Central.
GO; GO:0070231; P:T cell apoptotic process; ISS:UniProtKB.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR000488; Death_domain.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR025735; RHIM_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00531; Death; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF12721; RHIM; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00005; DEATH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Kinase; Membrane; Necrosis;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 671 Receptor-interacting serine/threonine-
protein kinase 1.
/FTId=PRO_0000086606.
DOMAIN 17 289 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 583 669 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
NP_BIND 23 31 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 290 582 Interaction with SQSTM1.
{ECO:0000269|PubMed:10356400}.
MOTIF 531 547 RIP homotypic interaction motif (RHIM).
COMPBIAS 411 414 Poly-Arg.
ACT_SITE 138 138 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 324 325 Cleavage; by caspase-8.
MOD_RES 6 6 Phosphoserine.
{ECO:0000269|PubMed:18408713}.
MOD_RES 20 20 Phosphoserine; by autocatalysis.
{ECO:0000255}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000269|PubMed:18408713}.
MOD_RES 161 161 Phosphoserine; by RIPK3 and
autocatalysis. {ECO:0000255}.
MOD_RES 166 166 Phosphoserine; by autocatalysis.
{ECO:0000255}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000269|PubMed:18408713}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18408713}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000269|PubMed:18408713}.
MOD_RES 384 384 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
VAR_SEQ 108 153 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037690.
VARIANT 64 64 A -> V (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs774996232).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041039.
VARIANT 81 81 V -> I (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs758268804).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041040.
VARIANT 220 220 A -> V (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs759012409).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041041.
VARIANT 234 234 E -> K (in dbSNP:rs17548383).
{ECO:0000269|Ref.4}.
/FTId=VAR_021109.
VARIANT 404 404 A -> S (in dbSNP:rs34872409).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041042.
VARIANT 438 438 A -> V (in dbSNP:rs3173519).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7538908,
ECO:0000269|PubMed:8612133}.
/FTId=VAR_058285.
VARIANT 443 443 A -> V (in dbSNP:rs35722193).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041043.
VARIANT 569 569 A -> V (in dbSNP:rs55861377).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041044.
MUTAGEN 45 45 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:8612133}.
MUTAGEN 161 161 S->A: Decreases RIPK1 kinase activity.
{ECO:0000269|PubMed:18408713}.
MUTAGEN 161 161 S->E: No effect on RIPK1
autophosphorylation.
{ECO:0000269|PubMed:18408713}.
MUTAGEN 324 324 D->K: Abolishes cleavage by caspase-8.
{ECO:0000269|PubMed:10521396}.
MUTAGEN 377 377 K->R: Abolishes RIP-mediated NF-Kappa-B
activation.
{ECO:0000269|PubMed:16603398}.
CONFLICT 258 258 R -> I (in Ref. 3; BAG36858).
{ECO:0000305}.
CONFLICT 286 286 R -> S (in Ref. 3; BAG36858).
{ECO:0000305}.
CONFLICT 514 514 T -> S (in Ref. 8; AAC50137).
{ECO:0000305}.
HELIX 14 16 {ECO:0000244|PDB:4ITJ}.
STRAND 17 19 {ECO:0000244|PDB:5HX6}.
STRAND 20 22 {ECO:0000244|PDB:4ITJ}.
TURN 26 28 {ECO:0000244|PDB:4ITI}.
STRAND 30 36 {ECO:0000244|PDB:4ITJ}.
TURN 37 39 {ECO:0000244|PDB:4ITJ}.
STRAND 40 51 {ECO:0000244|PDB:4ITJ}.
HELIX 54 56 {ECO:0000244|PDB:4ITJ}.
HELIX 57 68 {ECO:0000244|PDB:4ITJ}.
STRAND 78 84 {ECO:0000244|PDB:4ITJ}.
STRAND 87 93 {ECO:0000244|PDB:4ITJ}.
HELIX 100 104 {ECO:0000244|PDB:4ITJ}.
STRAND 106 108 {ECO:0000244|PDB:4ITJ}.
HELIX 112 131 {ECO:0000244|PDB:4ITJ}.
HELIX 141 143 {ECO:0000244|PDB:4ITJ}.
STRAND 144 146 {ECO:0000244|PDB:4ITJ}.
STRAND 152 154 {ECO:0000244|PDB:4ITJ}.
HELIX 163 168 {ECO:0000244|PDB:4ITJ}.
STRAND 171 173 {ECO:0000244|PDB:4ITH}.
HELIX 190 192 {ECO:0000244|PDB:4NEU}.
HELIX 195 197 {ECO:0000244|PDB:4ITJ}.
STRAND 201 203 {ECO:0000244|PDB:4ITJ}.
HELIX 207 223 {ECO:0000244|PDB:4ITJ}.
HELIX 234 242 {ECO:0000244|PDB:4ITJ}.
HELIX 249 251 {ECO:0000244|PDB:4ITJ}.
HELIX 258 267 {ECO:0000244|PDB:4ITJ}.
HELIX 272 274 {ECO:0000244|PDB:4ITJ}.
HELIX 278 292 {ECO:0000244|PDB:4ITJ}.
HELIX 294 296 {ECO:0000244|PDB:4NEU}.
HELIX 297 309 {ECO:0000244|PDB:4NEU}.
TURN 310 312 {ECO:0000244|PDB:4NEU}.
SEQUENCE 671 AA; 75931 MW; 976E2428D525A9B2 CRC64;
MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG PNCIEHNEAL
LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL MHVLKAEMST PLSVKGRIIL
EIIEGMCYLH GKGVIHKDLK PENILVDNDF HIKIADLGLA SFKMWSKLNN EEHNELREVD
GTAKKNGGTL YYMAPEHLND VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC
IKSGNRPDVD DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED
VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG MGPVEESWFA
PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR QNVAYNREEE RRRRVSHDPF
AQQRPYENFQ NTEGKGTAYS SAASHGNAVH QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD
PGTAGPRVWY RPIPSHMPSL HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ
IGAYNYMEIG GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN
CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA QALHQCSRID
LLSSLIYVSQ N


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