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Q9Y572

- RIPK3_HUMAN

UniProt

Q9Y572 - RIPK3_HUMAN

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Protein
Receptor-interacting serine/threonine-protein kinase 3
Gene
RIPK3, RIP3
Organism
Homo sapiens (Human)
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.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 359ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. NF-kappaB-inducing kinase activity Source: Ensembl
  3. identical protein binding Source: IntAct
  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
Complete GO annotation...

GO - Biological processi

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

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. Cell membrane By similarity. Mitochondrion Reviewed prediction 1 Publication

GO - Cellular componenti

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

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 3
PRO_0000086610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei164 – 1641Phosphoserine By similarity
Modified residuei170 – 1701Phosphoserine; by autocatalysis Reviewed prediction
Modified residuei199 – 1991Phosphoserine; by autocatalysis2 Publications
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei252 – 2521Phosphothreonine By similarity
Modified residuei299 – 2991Phosphoserine By similarity
Modified residuei333 – 3331Phosphothreonine By similarity
Modified residuei389 – 3891Phosphoserine By similarity
Modified residuei401 – 4011Phosphothreonine By 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.
Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 287267Protein kinase
Add
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-rich
Add
BLAST

Sequence similaritiesi

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

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.
VSP_035106Add
BLAST
Alternative sequencei222 – 518297LPTEP…NHSGK → CKTLGGFWDP in isoform 3.
VSP_035107Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301G → D in AAD39005. 1 Publication
Sequence conflicti150 – 1501L → P in AAD39005. 1 Publication
Sequence conflicti309 – 3091R → K in AAD39005. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 141 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

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