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Q9QZL0

- RIPK3_MOUSE

UniProt

Q9QZL0 - RIPK3_MOUSE

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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

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 kinase activity Source: MGI
  4. 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 NF-kappaB transcription factor activity Source: Ensembl
  11. positive regulation of oxidoreductase activity Source: MGI
  12. positive regulation of phosphatase activity Source: Ensembl
  13. positive regulation of protein deacetylation Source: MGI
  14. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  15. positive regulation of transferase activity Source: MGI
  16. protein autophosphorylation Source: UniProtKB
  17. protein heterooligomerization Source: UniProtKB
  18. protein homooligomerization Source: UniProtKB
  19. regulation of activated T cell proliferation Source: UniProtKB
  20. regulation of activation-induced cell death of T cells Source: UniProtKB
  21. regulation of adaptive immune response Source: UniProtKB
  22. regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation Source: UniProtKB
  23. regulation of interferon-gamma production Source: UniProtKB
  24. regulation of reactive oxygen species metabolic process Source: MGI
  25. regulation of T cell mediated cytotoxicity Source: UniProtKB
  26. spleen development Source: UniProtKB
  27. T cell differentiation in thymus Source: UniProtKB
  28. T cell homeostasis Source: UniProtKB
  29. thymus development Source: UniProtKB
  30. 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

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-KW
  4. plasma membrane Source: UniProtKB-KW
  5. ripoptosome Source: MGI
Complete GO annotation...

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

MaxQBiQ9QZL0.
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.
ExpressionAtlasiQ9QZL0. baseline and differential.
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 – 213Combined sources
Beta strandi22 – 3312Combined sources
Beta strandi35 – 417Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 538Combined sources
Helixi55 – 6511Combined sources
Beta strandi78 – 814Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 969Combined sources
Helixi103 – 1075Combined sources
Helixi115 – 13319Combined sources
Beta strandi135 – 1373Combined sources
Helixi146 – 1483Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi157 – 1593Combined sources
Helixi164 – 1674Combined sources
Helixi187 – 1904Combined sources
Helixi193 – 1953Combined sources
Helixi205 – 22117Combined sources
Helixi231 – 2377Combined sources
Turni238 – 2414Combined sources
Helixi247 – 2493Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 27011Combined sources
Helixi275 – 2773Combined sources
Helixi281 – 29515Combined sources
Helixi296 – 2983Combined sources
Helixi299 – 31012Combined sources

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSVKLWPTG ASAVPLVSRE ELKKLEFVGK GGFGVVFRAH HRTWNHDVAV
60 70 80 90 100
KIVNSKKISW EVKAMVNLRN ENVLLLLGVT EDLQWDFVSG QALVTRFMEN
110 120 130 140 150
GSLAGLLQPE CPRPWPLLCR LLQEVVLGMC YLHSLNPPLL HRDLKPSNIL
160 170 180 190 200
LDPELHAKLA DFGLSTFQGG SQSGSGSGSG SRDSGGTLAY LDPELLFDVN
210 220 230 240 250
LKASKASDVY SFGILVWAVL AGREAELVDK TSLIRETVCD RQSRPPLTEL
260 270 280 290 300
PPGSPETPGL EKLKELMIHC WGSQSENRPS FQDCEPKTNE VYNLVKDKVD
310 320 330 340 350
AAVSEVKHYL SQHRSSGRNL SAREPSQRGT EMDCPRETMV SKMLDRLHLE
360 370 380 390 400
EPSGPVPGKC PERQAQDTSV GPATPARTSS DPVAGTPQIP HTLPFRGTTP
410 420 430 440 450
GPVFTETPGP HPQRNQGDGR HGTPWYPWTP PNPMTGPPAL VFNNCSEVQI
460 470 480
GNYNSLVAPP RTTASSSAKY DQAQFGRGRG WQPFHK
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

MaxQBi Q9QZL0.
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.
ExpressionAtlasi Q9QZL0. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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

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