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Q60855

- RIPK1_MOUSE

UniProt

Q60855 - RIPK1_MOUSE

Protein

Receptor-interacting serine/threonine-protein kinase 1

Gene

Ripk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    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 By similarity. Interacts with ARHGEF2 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Inhibited by necrostatin-1.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATPPROSITE-ProRule annotation
    Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 319ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein kinase activity Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. amyloid fibril formation Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. cellular protein catabolic process Source: UniProtKB
    4. cellular response to growth factor stimulus Source: UniProtKB
    5. cellular response to tumor necrosis factor Source: UniProtKB
    6. extrinsic apoptotic signaling pathway Source: Ensembl
    7. necroptotic process Source: MGI
    8. necroptotic signaling pathway Source: UniProtKB
    9. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
    10. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
    11. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    12. peptidyl-serine autophosphorylation Source: UniProtKB
    13. positive regulation of apoptotic process Source: UniProtKB
    14. positive regulation of extrinsic apoptotic signaling pathway Source: MGI
    15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    16. positive regulation of interleukin-8 production Source: Ensembl
    17. positive regulation of JNK cascade Source: UniProtKB
    18. positive regulation of macrophage differentiation Source: Ensembl
    19. positive regulation of MAPK cascade Source: UniProtKB
    20. positive regulation of necroptotic process Source: Ensembl
    21. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    22. positive regulation of phosphorylation Source: UniProtKB
    23. positive regulation of protein phosphorylation Source: UniProtKB
    24. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    25. positive regulation of transferase activity Source: MGI
    26. positive regulation of tumor necrosis factor production Source: Ensembl
    27. protein heterooligomerization Source: UniProtKB
    28. protein homooligomerization Source: UniProtKB
    29. regulation of ATP:ADP antiporter activity Source: Ensembl
    30. regulation of reactive oxygen species metabolic process Source: MGI
    31. ripoptosome assembly Source: UniProtKB
    32. ripoptosome assembly involved in necroptotic process Source: MGI
    33. T cell apoptotic process Source: UniProtKB
    34. 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

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_196636. TRIF-mediated programmed cell death.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_215122. Regulation by c-FLIP.
    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 1 (EC:2.7.11.1)
    Alternative name(s):
    Cell death protein RIP
    Receptor-interacting protein 1
    Short name:
    RIP-1
    Serine/threonine-protein kinase RIP
    Gene namesi
    Name:Ripk1
    Synonyms:Rinp, Rip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:108212. Ripk1.

    Subcellular locationi

    GO - Cellular componenti

    1. death-inducing signaling complex Source: Ensembl
    2. membrane raft Source: Ensembl
    3. mitochondrion Source: Ensembl
    4. receptor complex Source: Ensembl
    5. ripoptosome Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 656656Receptor-interacting serine/threonine-protein kinase 1PRO_0000086607Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61PhosphoserineBy similarity
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei161 – 1611Phosphoserine; by RIPK3 and autocatalysisSequence Analysis
    Modified residuei166 – 1661Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei304 – 3041PhosphoserineBy similarity
    Modified residuei321 – 3211PhosphoserineBy similarity
    Modified residuei334 – 3341PhosphoserineBy similarity
    Modified residuei383 – 3831PhosphotyrosineBy similarity

    Post-translational modificationi

    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 By similarity.By similarity
    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 By similarity.By similarity
    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 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 By similarity. 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.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ60855.
    PaxDbiQ60855.
    PRIDEiQ60855.

    PTM databases

    PhosphoSiteiQ60855.

    Expressioni

    Tissue specificityi

    Found at low levels in all tissues.

    Inductioni

    In concanavalin A-treated splenocytes.

    Gene expression databases

    BgeeiQ60855.
    GenevestigatoriQ60855.

    Interactioni

    Subunit structurei

    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 kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-alpha-dependent manner By similarity. 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 (via RIP homotypic interaction motif) with murid herpesvirus 1 viral inhibitor of RIP activation; this interaction inhibits RIPK1 ubiquitination. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 By similarity. Interacts with ARHGEF2 By similarity. Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTRA2O434642EBI-529119,EBI-517086From a different organism.
    Ripk3Q9QZL07EBI-529119,EBI-2367423
    Tnfrsf1aP251183EBI-529119,EBI-518014

    Protein-protein interaction databases

    BioGridi202896. 16 interactions.
    DIPiDIP-34962N.
    IntActiQ60855. 12 interactions.
    MINTiMINT-144784.
    STRINGi10090.ENSMUSP00000021844.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60855.
    SMRiQ60855. Positions 7-404, 577-655.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 290274Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini568 – 65487DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni291 – 567277Interaction with SQSTM1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi520 – 53617RIP homotypic interaction motif (RHIM)Add
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074536.
    HOGENOMiHOG000010270.
    HOVERGENiHBG055612.
    InParanoidiQ60855.
    KOiK02861.
    OMAiSHDPFAQ.
    OrthoDBiEOG7MPRDN.
    PhylomeDBiQ60855.
    TreeFamiTF106506.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR025735. RHIM_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF12721. RHIM. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00005. DEATH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60855-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPDMSLDNI KMASSDLLEK TDLDSGGFGK VSLCYHRSHG FVILKKVYTG    50
    PNRAEYNEVL LEEGKMMHRL RHSRVVKLLG IIIEEGNYSL VMEYMEKGNL 100
    MHVLKTQIDV PLSLKGRIIV EAIEGMCYLH DKGVIHKDLK PENILVDRDF 150
    HIKIADLGVA SFKTWSKLTK EKDNKQKEVS STTKKNNGGT LYYMAPEHLN 200
    DINAKPTEKS DVYSFGIVLW AIFAKKEPYE NVICTEQFVI CIKSGNRPNV 250
    EEILEYCPRE IISLMERCWQ AIPEDRPTFL GIEEEFRPFY LSHFEEYVEE 300
    DVASLKKEYP DQSPVLQRMF SLQHDCVPLP PSRSNSEQPG SLHSSQGLQM 350
    GPVEESWFSS SPEYPQDEND RSVQAKLQEE ASYHAFGIFA EKQTKPQPRQ 400
    NEAYNREEER KRRVSHDPFA QQRARENIKS AGARGHSDPS TTSRGIAVQQ 450
    LSWPATQTVW NNGLYNQHGF GTTGTGVWYP PNLSQMYSTY KTPVPETNIP 500
    GSTPTMPYFS GPVADDLIKY TIFNSSGIQI GNHNYMDVGL NSQPPNNTCK 550
    EESTSRHQAI FDNTTSLTDE HLNPIRENLG RQWKNCARKL GFTESQIDEI 600
    DHDYERDGLK EKVYQMLQKW LMREGTKGAT VGKLAQALHQ CCRIDLLNHL 650
    IRASQS 656
    Length:656
    Mass (Da):74,854
    Last modified:November 1, 1997 - v1
    Checksum:iABB350B523879933
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661M → K in BAC27194. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti473 – 4731T → I.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25995 mRNA. Translation: AAB60487.1.
    AK030959 mRNA. Translation: BAC27194.1.
    AK156803 mRNA. Translation: BAE33860.1.
    BC050905 mRNA. Translation: AAH50905.2.
    BC054542 mRNA. Translation: AAH54542.1.
    BC058162 mRNA. Translation: AAH58162.1.
    CCDSiCCDS26443.1.
    PIRiI49299.
    RefSeqiNP_033094.3. NM_009068.3.
    XP_006516670.1. XM_006516607.1.
    XP_006516671.1. XM_006516608.1.
    XP_006516672.1. XM_006516609.1.
    UniGeneiMm.374799.

    Genome annotation databases

    EnsembliENSMUST00000021844; ENSMUSP00000021844; ENSMUSG00000021408.
    ENSMUST00000167374; ENSMUSP00000129831; ENSMUSG00000021408.
    GeneIDi19766.
    KEGGimmu:19766.
    UCSCiuc007qax.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25995 mRNA. Translation: AAB60487.1 .
    AK030959 mRNA. Translation: BAC27194.1 .
    AK156803 mRNA. Translation: BAE33860.1 .
    BC050905 mRNA. Translation: AAH50905.2 .
    BC054542 mRNA. Translation: AAH54542.1 .
    BC058162 mRNA. Translation: AAH58162.1 .
    CCDSi CCDS26443.1.
    PIRi I49299.
    RefSeqi NP_033094.3. NM_009068.3.
    XP_006516670.1. XM_006516607.1.
    XP_006516671.1. XM_006516608.1.
    XP_006516672.1. XM_006516609.1.
    UniGenei Mm.374799.

    3D structure databases

    ProteinModelPortali Q60855.
    SMRi Q60855. Positions 7-404, 577-655.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202896. 16 interactions.
    DIPi DIP-34962N.
    IntActi Q60855. 12 interactions.
    MINTi MINT-144784.
    STRINGi 10090.ENSMUSP00000021844.

    PTM databases

    PhosphoSitei Q60855.

    Proteomic databases

    MaxQBi Q60855.
    PaxDbi Q60855.
    PRIDEi Q60855.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021844 ; ENSMUSP00000021844 ; ENSMUSG00000021408 .
    ENSMUST00000167374 ; ENSMUSP00000129831 ; ENSMUSG00000021408 .
    GeneIDi 19766.
    KEGGi mmu:19766.
    UCSCi uc007qax.1. mouse.

    Organism-specific databases

    CTDi 8737.
    MGIi MGI:108212. Ripk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074536.
    HOGENOMi HOG000010270.
    HOVERGENi HBG055612.
    InParanoidi Q60855.
    KOi K02861.
    OMAi SHDPFAQ.
    OrthoDBi EOG7MPRDN.
    PhylomeDBi Q60855.
    TreeFami TF106506.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_196636. TRIF-mediated programmed cell death.
    REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
    REACT_215122. Regulation by c-FLIP.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Miscellaneous databases

    NextBioi 297220.
    PROi Q60855.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q60855.
    Genevestigatori Q60855.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR025735. RHIM_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF12721. RHIM. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00005. DEATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death."
      Stanger B.Z., Leder P., Lee T.-H., Kim E., Seed B.
      Cell 81:513-523(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
      Tissue: Thymus.
    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: C57BL/6J and NOD.
      Tissue: Spleen and Thymus.
    3. "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: C57BL/6.
      Tissue: Brain and Liver.
    4. "The death domain kinase RIP has an essential role in DNA damage-induced NF-kappa B activation."
      Hur G.M., Lewis J., Yang Q., Lin Y., Nakano H., Nedospasov S., Liu Z.G.
      Genes Dev. 17:873-882(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "RIP1, a kinase on the crossroads of a cell's decision to live or die."
      Festjens N., Vanden Berghe T., Cornelis S., Vandenabeele P.
      Cell Death Differ. 14:400-410(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    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.

    Entry informationi

    Entry nameiRIPK1_MOUSE
    AccessioniPrimary (citable) accession number: Q60855
    Secondary accession number(s): Q3U0J3, Q8CD90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3