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Q60855

- RIPK1_MOUSE

UniProt

Q60855 - RIPK1_MOUSE

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Protein
Receptor-interacting serine/threonine-protein kinase 1
Gene
Ripk1, Rinp, Rip
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

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 – 461ATP By similarity
Active sitei138 – 1381Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 319ATP By similarity

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine By similarity
Modified residuei25 – 251Phosphoserine By similarity
Modified residuei161 – 1611Phosphoserine; by RIPK3 and autocatalysis Reviewed prediction
Modified residuei166 – 1661Phosphoserine; by autocatalysis Reviewed prediction
Modified residuei304 – 3041Phosphoserine By similarity
Modified residuei321 – 3211Phosphoserine By similarity
Modified residuei334 – 3341Phosphoserine By similarity
Modified residuei383 – 3831Phosphotyrosine By 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.
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.
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.

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.2 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 290274Protein kinase
Add
BLAST
Domaini568 – 65487Death
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 567277Interaction with SQSTM1
Add
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.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661M → K in BAC27194. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

Similar proteinsi