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Q9Y572

- RIPK3_HUMAN

UniProt

Q9Y572 - RIPK3_HUMAN

Protein

Receptor-interacting serine/threonine-protein kinase 3

Gene

RIPK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      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.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501ATP
    Active sitei142 – 1421Proton acceptor1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 359ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. NF-kappaB-inducing kinase activity Source: Ensembl
    4. protein binding Source: UniProtKB
    5. protein complex binding Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. protein serine/threonine kinase activity Source: UniProtKB
    8. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. activation of protein kinase activity Source: UniProtKB
    2. amyloid fibril formation Source: UniProtKB
    3. apoptotic signaling pathway Source: ProtInc
    4. cellular protein modification process Source: ProtInc
    5. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    6. innate immune response Source: Reactome
    7. lymph node development Source: UniProtKB
    8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    9. necroptotic process Source: UniProtKB
    10. positive regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    11. positive regulation of necroptotic process Source: UniProtKB
    12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    13. positive regulation of phosphatase activity Source: UniProtKB
    14. positive regulation of type I interferon production Source: Reactome
    15. protein autophosphorylation Source: UniProtKB
    16. protein heterooligomerization Source: UniProtKB
    17. protein homooligomerization Source: UniProtKB
    18. regulation of activated T cell proliferation Source: UniProtKB
    19. regulation of activation-induced cell death of T cells Source: UniProtKB
    20. regulation of adaptive immune response Source: UniProtKB
    21. regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation Source: UniProtKB
    22. regulation of interferon-gamma production Source: UniProtKB
    23. regulation of T cell mediated cytotoxicity Source: UniProtKB
    24. signal transduction Source: ProtInc
    25. spleen development Source: UniProtKB
    26. T cell differentiation in thymus Source: UniProtKB
    27. T cell homeostasis Source: UniProtKB
    28. thymus development Source: UniProtKB
    29. toll-like receptor 3 signaling pathway Source: Reactome
    30. toll-like receptor 4 signaling pathway Source: Reactome
    31. toll-like receptor signaling pathway Source: Reactome
    32. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Necrosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_150361. TRIF-mediated programmed cell death.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    SignaLinkiQ9Y572.

    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
    Gene namesi
    Name:RIPK3
    Synonyms:RIP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:10021. RIPK3.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cell membrane By similarity. Mitochondrion Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. mitochondrion Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501K → A: Abolishes kinase activity. Loss of PGAM5- and MLKL-binding. No effect on RIPK1-binding. 3 Publications
    Mutagenesisi50 – 501K → D: Abolishes kinase activity. 3 Publications
    Mutagenesisi142 – 1421D → N: Abolishes kinase activity and ability to mediate necroptosis. 1 Publication
    Mutagenesisi227 – 2271S → A: Abolishes ability to mediate necroptosis. 1 Publication

    Organism-specific databases

    PharmGKBiPA34396.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518Receptor-interacting serine/threonine-protein kinase 3PRO_0000086610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei164 – 1641PhosphoserineBy similarity
    Modified residuei170 – 1701Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei199 – 1991Phosphoserine; by autocatalysis2 Publications
    Modified residuei227 – 2271Phosphoserine1 Publication
    Modified residuei252 – 2521PhosphothreonineBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei333 – 3331PhosphothreonineBy similarity
    Modified residuei389 – 3891PhosphoserineBy similarity
    Modified residuei401 – 4011PhosphothreonineBy similarity

    Post-translational modificationi

    RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-199 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-227 is required for binding MLKL.3 Publications
    Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y572.
    PaxDbiQ9Y572.
    PRIDEiQ9Y572.

    PTM databases

    PhosphoSiteiQ9Y572.

    Expressioni

    Tissue specificityi

    Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. Isoform 3 is significantly increased in colon and lung cancers.1 Publication

    Gene expression databases

    BgeeiQ9Y572.
    CleanExiHS_RIPK3.
    GenevestigatoriQ9Y572.

    Organism-specific databases

    HPAiHPA054606.
    HPA055087.

    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 necrosis-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. Interacts with MLKL; the interaction is direct. Binds TRAF2 and is recruited to the TNFR-1 signaling complex. Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with ARHGEF2.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-298250,EBI-298250
    BIRC2Q134903EBI-298250,EBI-514538
    BIRC3Q134893EBI-298250,EBI-517709
    MLKLQ8NB1610EBI-298250,EBI-1055040
    RIPK1Q1354624EBI-298250,EBI-358507
    SIRT2Q8IXJ62EBI-298250,EBI-477232
    ZBP1Q9H1714EBI-298250,EBI-6264672

    Protein-protein interaction databases

    BioGridi116224. 19 interactions.
    DIPiDIP-27519N.
    IntActiQ9Y572. 12 interactions.
    MINTiMINT-1131399.
    STRINGi9606.ENSP00000216274.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y572.
    SMRiQ9Y572. Positions 11-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 287267Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi450 – 46617RIP homotypic interaction motif (RHIM)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi357 – 44892Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000035101.
    HOVERGENiHBG062538.
    InParanoidiQ9Y572.
    KOiK08847.
    OMAiVGDNNYL.
    OrthoDBiEOG7Q2N5T.
    PhylomeDBiQ9Y572.
    TreeFamiTF106506.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y572-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSCVKLWPSG APAPLVSIEE LENQELVGKG GFGTVFRAQH RKWGYDVAVK    50
    IVNSKAISRE VKAMASLDNE FVLRLEGVIE KVNWDQDPKP ALVTKFMENG 100
    SLSGLLQSQC PRPWPLLCRL LKEVVLGMFY LHDQNPVLLH RDLKPSNVLL 150
    DPELHVKLAD FGLSTFQGGS QSGTGSGEPG GTLGYLAPEL FVNVNRKAST 200
    ASDVYSFGIL MWAVLAGREV ELPTEPSLVY EAVCNRQNRP SLAELPQAGP 250
    ETPGLEGLKE LMQLCWSSEP KDRPSFQECL PKTDEVFQMV ENNMNAAVST 300
    VKDFLSQLRS SNRRFSIPES GQGGTEMDGF RRTIENQHSR NDVMVSEWLN 350
    KLNLEEPPSS VPKKCPSLTK RSRAQEEQVP QAWTAGTSSD SMAQPPQTPE 400
    TSTFRNQMPS PTSTGTPSPG PRGNQGAERQ GMNWSCRTPE PNPVTGRPLV 450
    NIYNCSGVQV GDNNYLTMQQ TTALPTWGLA PSGKGRGLQH PPPVGSQEGP 500
    KDPEAWSRPQ GWYNHSGK 518
    Length:518
    Mass (Da):56,887
    Last modified:September 2, 2008 - v2
    Checksum:iBF755F8A0B1810A1
    GO
    Isoform 2 (identifier: Q9Y572-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         220-518: VELPTEPSLV...PQGWYNHSGK → CQPNHHSCTKQCATGRTGLHWLSCPKPGLRLPA

    Show »
    Length:252
    Mass (Da):27,574
    Checksum:i20D7DFAB11AEECEF
    GO
    Isoform 3 (identifier: Q9Y572-3) [UniParc]FASTAAdd to Basket

    Also known as: Gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         222-518: LPTEPSLVYE...PQGWYNHSGK → CKTLGGFWDP

    Show »
    Length:231
    Mass (Da):25,326
    Checksum:i8E6E045EC3B11DEF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301G → D in AAD39005. (PubMed:10339433)Curated
    Sequence conflicti150 – 1501L → P in AAD39005. (PubMed:10339433)Curated
    Sequence conflicti309 – 3091R → K in AAD39005. (PubMed:10339433)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti260 – 2601E → V.
    Corresponds to variant rs7153640 [ dbSNP | Ensembl ].
    VAR_051664
    Natural varianti300 – 3001T → M.1 Publication
    Corresponds to variant rs34106261 [ dbSNP | Ensembl ].
    VAR_041048
    Natural varianti492 – 4921P → Q.1 Publication
    Corresponds to variant rs3212254 [ dbSNP | Ensembl ].
    VAR_041049

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 518299VELPT…NHSGK → CQPNHHSCTKQCATGRTGLH WLSCPKPGLRLPA in isoform 2. 1 PublicationVSP_035106Add
    BLAST
    Alternative sequencei222 – 518297LPTEP…NHSGK → CKTLGGFWDP in isoform 3. 2 PublicationsVSP_035107Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156884 mRNA. Translation: AAD39005.1.
    AY453693 mRNA. Translation: AAS16359.1.
    AY494982 mRNA. Translation: AAS75516.1.
    AY494983 mRNA. Translation: AAS75517.1.
    AL096870 Genomic DNA. No translation available.
    AK296140 mRNA. Translation: BAG58881.1.
    CH471078 Genomic DNA. Translation: EAW66021.1.
    BC062584 mRNA. Translation: AAH62584.1.
    CCDSiCCDS9628.1. [Q9Y572-1]
    RefSeqiNP_006862.2. NM_006871.3. [Q9Y572-1]
    UniGeneiHs.268551.

    Genome annotation databases

    EnsembliENST00000216274; ENSP00000216274; ENSG00000129465. [Q9Y572-1]
    ENST00000554756; ENSP00000452328; ENSG00000129465. [Q9Y572-3]
    GeneIDi11035.
    KEGGihsa:11035.
    UCSCiuc001wpa.3. human. [Q9Y572-1]

    Polymorphism databases

    DMDMi205371831.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156884 mRNA. Translation: AAD39005.1 .
    AY453693 mRNA. Translation: AAS16359.1 .
    AY494982 mRNA. Translation: AAS75516.1 .
    AY494983 mRNA. Translation: AAS75517.1 .
    AL096870 Genomic DNA. No translation available.
    AK296140 mRNA. Translation: BAG58881.1 .
    CH471078 Genomic DNA. Translation: EAW66021.1 .
    BC062584 mRNA. Translation: AAH62584.1 .
    CCDSi CCDS9628.1. [Q9Y572-1 ]
    RefSeqi NP_006862.2. NM_006871.3. [Q9Y572-1 ]
    UniGenei Hs.268551.

    3D structure databases

    ProteinModelPortali Q9Y572.
    SMRi Q9Y572. Positions 11-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116224. 19 interactions.
    DIPi DIP-27519N.
    IntActi Q9Y572. 12 interactions.
    MINTi MINT-1131399.
    STRINGi 9606.ENSP00000216274.

    Chemistry

    ChEMBLi CHEMBL1795199.

    PTM databases

    PhosphoSitei Q9Y572.

    Polymorphism databases

    DMDMi 205371831.

    Proteomic databases

    MaxQBi Q9Y572.
    PaxDbi Q9Y572.
    PRIDEi Q9Y572.

    Protocols and materials databases

    DNASUi 11035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216274 ; ENSP00000216274 ; ENSG00000129465 . [Q9Y572-1 ]
    ENST00000554756 ; ENSP00000452328 ; ENSG00000129465 . [Q9Y572-3 ]
    GeneIDi 11035.
    KEGGi hsa:11035.
    UCSCi uc001wpa.3. human. [Q9Y572-1 ]

    Organism-specific databases

    CTDi 11035.
    GeneCardsi GC14M024811.
    HGNCi HGNC:10021. RIPK3.
    HPAi HPA054606.
    HPA055087.
    MIMi 605817. gene.
    neXtProti NX_Q9Y572.
    PharmGKBi PA34396.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000035101.
    HOVERGENi HBG062538.
    InParanoidi Q9Y572.
    KOi K08847.
    OMAi VGDNNYL.
    OrthoDBi EOG7Q2N5T.
    PhylomeDBi Q9Y572.
    TreeFami TF106506.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_150361. TRIF-mediated programmed cell death.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    SignaLinki Q9Y572.

    Miscellaneous databases

    GeneWikii RIPK3.
    GenomeRNAii 11035.
    NextBioi 41936.
    PROi Q9Y572.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y572.
    CleanExi HS_RIPK3.
    Genevestigatori Q9Y572.

    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. "Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB."
      Yu P.W., Huang B.C.B., Shen M., Quast J., Chan E., Xu X., Nolan G.P., Payan D.G., Luo Y.
      Curr. Biol. 9:539-542(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-50, INTERACTION WITH RIPK1.
      Tissue: Cervix carcinoma and Lymphocyte.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-50.
      Tissue: Aortic endothelium and Fetal brain.
    3. "RIP3 beta and RIP3 gamma, two novel splice variants of receptor-interacting protein 3 (RIP3), downregulate RIP3-induced apoptosis."
      Yang Y., Hu W., Feng S., Ma J., Wu M.
      Biochem. Biophys. Res. Commun. 332:181-187(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Thalamus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Blood.
    8. "Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3."
      Sun X., Yin J., Starovasnik M.A., Fairbrother W.J., Dixit V.M.
      J. Biol. Chem. 277:9505-9511(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: RIP HOMOTYPIC INTERACTION MOTIF, PHOSPHORYLATION AT SER-199, INTERACTION WITH RIPK1.
    9. "RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis."
      Zhang D.W., Shao J., Lin J., Zhang N., Lu B.J., Lin S.C., Dong M.Q., Han J.
      Science 325:332-336(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PYGL; GLUL AND GLUD1.
    10. "Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha."
      He S., Wang L., Miao L., Wang T., Du F., Zhao L., Wang X.
      Cell 137:1100-1111(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-199, INTERACTION WITH RIPK1.
    11. "Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation."
      Cho Y.S., Challa S., Moquin D., Genga R., Ray T.D., Guildford M., Chan F.K.
      Cell 137:1112-1123(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The role of the kinases RIP1 and RIP3 in TNF-induced necrosis."
      Vandenabeele P., Declercq W., Van Herreweghe F., Vanden Berghe T.
      Sci. Signal. 3:RE4-RE4(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)."
      Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J., Gevaert K., Declercq W., Vandenabeele P.
      PLoS ONE 6:E22356-E22356(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY BIRC2/C-IAP1 AND BIRC3/C-IAP2, INTERACTION WITH BIRC2/C-IAP1; BIRC3/C-IAP2 AND XIAP/BIRC4.
    14. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MLKL, PHOSPHORYLATION AT SER-227, ACTIVE SITE, MUTAGENESIS OF ASP-142 AND SER-227.
    15. "The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
      Wang Z., Jiang H., Chen S., Du F., Wang X.
      Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH PGAM5; RIPK1 AND MLKL, MUTAGENESIS OF LYS-50.
    16. Cited for: INTERACTION WITH ARHGEF2.
    17. "Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis."
      Zhao J., Jitkaew S., Cai Z., Choksi S., Li Q., Luo J., Liu Z.G.
      Proc. Natl. Acad. Sci. U.S.A. 109:5322-5327(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MLKL.
    18. "Patterns of somatic mutation in human cancer genomes."
      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.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-300 AND GLN-492.

    Entry informationi

    Entry nameiRIPK3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y572
    Secondary accession number(s): B4DJL9
    , C4AM87, Q5J795, Q5J796, Q6P5Y1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3