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Q9QZL0

- RIPK3_MOUSE

UniProt

Q9QZL0 - RIPK3_MOUSE

Protein

Receptor-interacting serine/threonine-protein kinase 3

Gene

Ripk3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (19 Feb 2014)
      Previous versions | rss
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    Functioni

    Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Inhibited by necrostatin-1.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATPCurated
    Active sitei143 – 1431Proton acceptor1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. NF-kappaB-inducing kinase activity Source: MGI
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: MGI
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase activity Source: UniProtKB
    2. amyloid fibril formation Source: UniProtKB
    3. I-kappaB kinase/NF-kappaB signaling Source: MGI
    4. lymph node development Source: UniProtKB
    5. necroptotic process Source: UniProtKB
    6. NIK/NF-kappaB signaling Source: GOC
    7. positive regulation of intrinsic apoptotic signaling pathway Source: MGI
    8. positive regulation of ligase activity Source: MGI
    9. positive regulation of necroptotic process Source: UniProtKB
    10. positive regulation of oxidoreductase activity Source: MGI
    11. positive regulation of protein deacetylation Source: MGI
    12. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    13. positive regulation of transferase activity Source: MGI
    14. protein autophosphorylation Source: UniProtKB
    15. protein heterooligomerization Source: UniProtKB
    16. protein homooligomerization Source: UniProtKB
    17. regulation of activated T cell proliferation Source: UniProtKB
    18. regulation of activation-induced cell death of T cells Source: UniProtKB
    19. regulation of adaptive immune response Source: UniProtKB
    20. regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation Source: UniProtKB
    21. regulation of interferon-gamma production Source: UniProtKB
    22. regulation of reactive oxygen species metabolic process Source: MGI
    23. regulation of T cell mediated cytotoxicity Source: UniProtKB
    24. spleen development Source: UniProtKB
    25. T cell differentiation in thymus Source: UniProtKB
    26. T cell homeostasis Source: UniProtKB
    27. thymus development Source: UniProtKB
    28. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Host-virus interaction, Necrosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196636. TRIF-mediated programmed cell death.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-interacting serine/threonine-protein kinase 3 (EC:2.7.11.1)
    Alternative name(s):
    RIP-like protein kinase 3
    Receptor-interacting protein 3
    Short name:
    RIP-3
    Short name:
    mRIP3
    Gene namesi
    Name:Ripk3
    Synonyms:Rip3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2154952. Ripk3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. intracellular Source: MGI
    3. mitochondrion Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell
    5. ripoptosome Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511K → A: Complete loss of induced necrosis.
    Mutagenesisi111 – 1111C → A: No effect. 1 Publication
    Mutagenesisi143 – 1431D → N: Abolishes kinase activity and ability to mediate necroptosis. No autophosphorylation. 2 Publications
    Mutagenesisi230 – 2301K → A: Slightly affects interaction with MLKL; when associated with A-236. Affects interaction with MLKL; when associated with A-232 and A-236. 1 Publication
    Mutagenesisi231 – 2311T → A: Abolishes ability to mediate necroptosis. 1 Publication
    Mutagenesisi232 – 2321S → A: Abolishes ability to mediate necroptosis. Affects interaction with MLKL; when associated with A-230 and A-236. 3 Publications
    Mutagenesisi236 – 2361E → A: Slightly affects interaction with MLKL; when associated with A-230. Affects interaction with MLKL; when associated with A-230 and A-232. 1 Publication
    Mutagenesisi459 – 4624PPRT → AAAA: Complete loss of induced necrosis.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Receptor-interacting serine/threonine-protein kinase 3PRO_0000086611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei171 – 1711Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei204 – 2041Phosphoserine; by autocatalysisBy similarity
    Modified residuei231 – 2311Phosphothreonine1 Publication
    Modified residuei232 – 2321Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphothreonine1 Publication
    Modified residuei304 – 3041Phosphoserine1 Publication
    Modified residuei326 – 3261Phosphoserine1 Publication
    Modified residuei338 – 3381Phosphothreonine1 Publication
    Modified residuei353 – 3531Phosphoserine1 Publication
    Modified residuei369 – 3691Phosphoserine1 Publication
    Modified residuei380 – 3801Phosphoserine1 Publication
    Modified residuei392 – 3921Phosphothreonine1 Publication

    Post-translational modificationi

    RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-204 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-232 is required for binding MLKL.1 Publication
    Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9QZL0.
    PRIDEiQ9QZL0.

    PTM databases

    PhosphoSiteiQ9QZL0.

    Expressioni

    Tissue specificityi

    Expressed in embryo and in adult spleen, liver, testis, heart, brain and lung.

    Gene expression databases

    CleanExiMM_RIPK3.
    GenevestigatoriQ9QZL0.

    Interactioni

    Subunit structurei

    Interacts (via RIP homotypic interaction motif) with RIPK1 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex. 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 By similarity. Binds TRAF2 and is recruited to the TNFR-1 signaling complex By similarity. Interacts with MLKL; the interaction is direct. Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes. Interacts (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation; this interaction disrupts RIP3-RIP1 interactions characteristic of TNF-alpha induced necroptosis, thereby suppressing this death pathway. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 By similarity. Interacts with ARHGEF2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAXXQ9UER72EBI-2367423,EBI-77321From a different organism.
    RIPK1Q135462EBI-2367423,EBI-358507From a different organism.
    Ripk1Q608557EBI-2367423,EBI-529119

    Protein-protein interaction databases

    DIPiDIP-54883N.
    IntActiQ9QZL0. 15 interactions.
    STRINGi10090.ENSMUSP00000022830.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 213
    Beta strandi22 – 3312
    Beta strandi35 – 417
    Turni42 – 454
    Beta strandi46 – 538
    Helixi55 – 6511
    Beta strandi78 – 814
    Beta strandi83 – 853
    Beta strandi88 – 969
    Helixi103 – 1075
    Helixi115 – 13319
    Beta strandi135 – 1373
    Helixi146 – 1483
    Beta strandi149 – 1513
    Beta strandi157 – 1593
    Helixi164 – 1674
    Helixi187 – 1904
    Helixi193 – 1953
    Helixi205 – 22117
    Helixi231 – 2377
    Turni238 – 2414
    Helixi247 – 2493
    Beta strandi255 – 2573
    Helixi260 – 27011
    Helixi275 – 2773
    Helixi281 – 29515
    Helixi296 – 2983
    Helixi299 – 31012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M66X-ray2.40A/B1-313[»]
    4M69X-ray2.50A1-313[»]
    ProteinModelPortaliQ9QZL0.
    SMRiQ9QZL0. Positions 12-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 292271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi440 – 46122RIP homotypic interaction motif (RHIM)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi352 – 43887Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG274817.
    GeneTreeiENSGT00550000074536.
    HOGENOMiHOG000035101.
    HOVERGENiHBG062538.
    InParanoidiQ9QZL0.
    KOiK08847.
    OMAiVGDNNYL.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR025735. RHIM_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF12721. RHIM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QZL0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSVKLWPTG ASAVPLVSRE ELKKLEFVGK GGFGVVFRAH HRTWNHDVAV    50
    KIVNSKKISW EVKAMVNLRN ENVLLLLGVT EDLQWDFVSG QALVTRFMEN 100
    GSLAGLLQPE CPRPWPLLCR LLQEVVLGMC YLHSLNPPLL HRDLKPSNIL 150
    LDPELHAKLA DFGLSTFQGG SQSGSGSGSG SRDSGGTLAY LDPELLFDVN 200
    LKASKASDVY SFGILVWAVL AGREAELVDK TSLIRETVCD RQSRPPLTEL 250
    PPGSPETPGL EKLKELMIHC WGSQSENRPS FQDCEPKTNE VYNLVKDKVD 300
    AAVSEVKHYL SQHRSSGRNL SAREPSQRGT EMDCPRETMV SKMLDRLHLE 350
    EPSGPVPGKC PERQAQDTSV GPATPARTSS DPVAGTPQIP HTLPFRGTTP 400
    GPVFTETPGP HPQRNQGDGR HGTPWYPWTP PNPMTGPPAL VFNNCSEVQI 450
    GNYNSLVAPP RTTASSSAKY DQAQFGRGRG WQPFHK 486
    Length:486
    Mass (Da):53,322
    Last modified:February 19, 2014 - v2
    Checksum:i31C5EEE77F55778B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361N → D in AAF03133. (PubMed:10490590)Curated
    Sequence conflicti136 – 1361N → D in BAE32636. (PubMed:16141072)Curated
    Sequence conflicti198 – 1981D → K in AAF03133. (PubMed:10490590)Curated
    Sequence conflicti198 – 1981D → K in BAE32636. (PubMed:16141072)Curated
    Sequence conflicti198 – 1981D → N in AAH29210. (PubMed:15489334)Curated
    Sequence conflicti283 – 2831D → G in BAE32636. (PubMed:16141072)Curated
    Sequence conflicti471 – 4711D → G in BAE32636. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF178953 mRNA. Translation: AAF03133.1.
    AK154505 mRNA. Translation: BAE32636.1.
    AC098877 Genomic DNA. No translation available.
    CH466535 Genomic DNA. Translation: EDL36236.1.
    BC029210 mRNA. Translation: AAH29210.1.
    CCDSiCCDS27131.1.
    RefSeqiNP_064339.2. NM_019955.2.
    UniGeneiMm.46612.

    Genome annotation databases

    EnsembliENSMUST00000022830; ENSMUSP00000022830; ENSMUSG00000022221.
    GeneIDi56532.
    KEGGimmu:56532.
    UCSCiuc007uav.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF178953 mRNA. Translation: AAF03133.1 .
    AK154505 mRNA. Translation: BAE32636.1 .
    AC098877 Genomic DNA. No translation available.
    CH466535 Genomic DNA. Translation: EDL36236.1 .
    BC029210 mRNA. Translation: AAH29210.1 .
    CCDSi CCDS27131.1.
    RefSeqi NP_064339.2. NM_019955.2.
    UniGenei Mm.46612.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M66 X-ray 2.40 A/B 1-313 [» ]
    4M69 X-ray 2.50 A 1-313 [» ]
    ProteinModelPortali Q9QZL0.
    SMRi Q9QZL0. Positions 12-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-54883N.
    IntActi Q9QZL0. 15 interactions.
    STRINGi 10090.ENSMUSP00000022830.

    PTM databases

    PhosphoSitei Q9QZL0.

    Proteomic databases

    PaxDbi Q9QZL0.
    PRIDEi Q9QZL0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022830 ; ENSMUSP00000022830 ; ENSMUSG00000022221 .
    GeneIDi 56532.
    KEGGi mmu:56532.
    UCSCi uc007uav.2. mouse.

    Organism-specific databases

    CTDi 11035.
    MGIi MGI:2154952. Ripk3.

    Phylogenomic databases

    eggNOGi NOG274817.
    GeneTreei ENSGT00550000074536.
    HOGENOMi HOG000035101.
    HOVERGENi HBG062538.
    InParanoidi Q9QZL0.
    KOi K08847.
    OMAi VGDNNYL.

    Enzyme and pathway databases

    Reactomei REACT_196636. TRIF-mediated programmed cell death.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Miscellaneous databases

    NextBioi 312886.
    PROi Q9QZL0.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_RIPK3.
    Genevestigatori Q9QZL0.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR025735. RHIM_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF12721. RHIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse receptor interacting protein 3 does not contain a caspase-recruiting or a death domain but induces apoptosis and activates NF-kappaB."
      Pazdernik N.J., Donner D.B., Goebl M.G., Harrington M.A.
      Mol. Cell. Biol. 19:6500-6508(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACTIVE SITE, MUTAGENESIS OF ASP-143.
      Tissue: Embryo.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    6. "Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1."
      Upton J.W., Kaiser W.J., Mocarski E.S.
      J. Biol. Chem. 283:16966-16970(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MURID HERPESVIRUS 1 VIRAL INHIBITOR OF RIP ACTIVATION.
    7. "DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB."
      Rebsamen M., Heinz L.X., Meylan E., Michallet M.C., Schroder K., Hofmann K., Vazquez J., Benedict C.A., Tschopp J.
      EMBO Rep. 10:916-922(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZBP1.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase."
      Sun L., Wang H., Wang Z., He S., Chen S., Liao D., Wang L., Yan J., Liu W., Lei X., Wang X.
      Cell 148:213-227(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-232.
    10. Cited for: FUNCTION.
    11. Cited for: FUNCTION, MUTAGENESIS OF ASP-143, INTERACTION WITH MLKL.
    12. "Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling."
      Chen W., Zhou Z., Li L., Zhong C.Q., Zheng X., Wu X., Zhang Y., Ma H., Huang D., Li W., Xia Z., Han J.
      J. Biol. Chem. 288:16247-16261(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2; SER-165; THR-231; SER-232; THR-257; SER-304; SER-326; THR-338; SER-353; SER-369; SER-380 AND THR-392, INTERACTION WITH MLKL, MUTAGENESIS OF THR-231 AND SER-232.
    13. "Structural insights into RIP3-mediated necroptotic signaling."
      Xie T., Peng W., Yan C., Wu J., Gong X., Shi Y.
      Cell Rep. 5:70-78(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-313 OF MUTANT ALA-111 IN COMPLEX WITH MLKL, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-111; LYS-230; SER-232 AND GLU-236.

    Entry informationi

    Entry nameiRIPK3_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZL0
    Secondary accession number(s): G3X8V8, Q3U3Z9, Q8K2Y2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: February 19, 2014
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3