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Q9Y572 (RIPK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RIPK3
Synonyms:RIP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

Cytoplasmcytosol. Cell membrane By similarity. Mitochondrion Potential Ref.14.

Tissue specificity

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. Ref.3

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processNecrosis
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell differentiation in thymus

Inferred from sequence or structural similarity. Source: UniProtKB

T cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of protein kinase activity

Inferred from mutant phenotype PubMed 22817896. Source: UniProtKB

amyloid fibril formation

Inferred from mutant phenotype PubMed 22817896. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement Ref.1. Source: ProtInc

cellular protein modification process

Traceable author statement Ref.2. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

lymph node development

Inferred from sequence or structural similarity. Source: UniProtKB

necroptotic process

Inferred from mutant phenotype PubMed 21737330Ref.14. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of necroptotic process

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of phosphatase activity

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

protein autophosphorylation

Inferred from direct assay Ref.15. Source: UniProtKB

protein heterooligomerization

Inferred from mutant phenotype PubMed 22817896. Source: UniProtKB

protein homooligomerization

Inferred from direct assay PubMed 22817896. Source: UniProtKB

regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of activated T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of activation-induced cell death of T cells

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of adaptive immune response

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

spleen development

Inferred from sequence or structural similarity. Source: UniProtKB

thymus development

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay Ref.14. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NF-kappaB-inducing kinase activity

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 22817896. Source: IntAct

protein complex binding

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.14. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y572-1)

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.
Isoform 2 (identifier: Q9Y572-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     220-518: VELPTEPSLV...PQGWYNHSGK → CQPNHHSCTKQCATGRTGLHWLSCPKPGLRLPA
Isoform 3 (identifier: Q9Y572-3)

Also known as: Gamma;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Receptor-interacting serine/threonine-protein kinase 3
PRO_0000086610

Regions

Domain21 – 287267Protein kinase
Nucleotide binding27 – 359ATP By similarity
Motif450 – 46617RIP homotypic interaction motif (RHIM)
Compositional bias357 – 44892Pro-rich

Sites

Active site1421Proton acceptor Probable
Binding site501ATP

Amino acid modifications

Modified residue21Phosphoserine By similarity
Modified residue1641Phosphoserine By similarity
Modified residue1701Phosphoserine; by autocatalysis Potential
Modified residue1991Phosphoserine; by autocatalysis Ref.8 Ref.10
Modified residue2271Phosphoserine Ref.14
Modified residue2521Phosphothreonine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3331Phosphothreonine By similarity
Modified residue3891Phosphoserine By similarity
Modified residue4011Phosphothreonine By similarity

Natural variations

Alternative sequence220 – 518299VELPT…NHSGK → CQPNHHSCTKQCATGRTGLH WLSCPKPGLRLPA in isoform 2.
VSP_035106
Alternative sequence222 – 518297LPTEP…NHSGK → CKTLGGFWDP in isoform 3.
VSP_035107
Natural variant2601E → V.
Corresponds to variant rs7153640 [ dbSNP | Ensembl ].
VAR_051664
Natural variant3001T → M. Ref.18
Corresponds to variant rs34106261 [ dbSNP | Ensembl ].
VAR_041048
Natural variant4921P → Q. Ref.18
Corresponds to variant rs3212254 [ dbSNP | Ensembl ].
VAR_041049

Experimental info

Mutagenesis501K → A: Abolishes kinase activity. Loss of PGAM5- and MLKL-binding. No effect on RIPK1-binding. Ref.1 Ref.2 Ref.15
Mutagenesis501K → D: Abolishes kinase activity. Ref.1 Ref.2 Ref.15
Mutagenesis1421D → N: Abolishes kinase activity and ability to mediate necroptosis. Ref.14
Mutagenesis2271S → A: Abolishes ability to mediate necroptosis. Ref.14
Sequence conflict301G → D in AAD39005. Ref.1
Sequence conflict1501L → P in AAD39005. Ref.1
Sequence conflict3091R → K in AAD39005. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: BF755F8A0B1810A1

FASTA51856,887
        10         20         30         40         50         60 
MSCVKLWPSG APAPLVSIEE LENQELVGKG GFGTVFRAQH RKWGYDVAVK IVNSKAISRE 

        70         80         90        100        110        120 
VKAMASLDNE FVLRLEGVIE KVNWDQDPKP ALVTKFMENG SLSGLLQSQC PRPWPLLCRL 

       130        140        150        160        170        180 
LKEVVLGMFY LHDQNPVLLH RDLKPSNVLL DPELHVKLAD FGLSTFQGGS QSGTGSGEPG 

       190        200        210        220        230        240 
GTLGYLAPEL FVNVNRKAST ASDVYSFGIL MWAVLAGREV ELPTEPSLVY EAVCNRQNRP 

       250        260        270        280        290        300 
SLAELPQAGP ETPGLEGLKE LMQLCWSSEP KDRPSFQECL PKTDEVFQMV ENNMNAAVST 

       310        320        330        340        350        360 
VKDFLSQLRS SNRRFSIPES GQGGTEMDGF RRTIENQHSR NDVMVSEWLN KLNLEEPPSS 

       370        380        390        400        410        420 
VPKKCPSLTK RSRAQEEQVP QAWTAGTSSD SMAQPPQTPE TSTFRNQMPS PTSTGTPSPG 

       430        440        450        460        470        480 
PRGNQGAERQ GMNWSCRTPE PNPVTGRPLV NIYNCSGVQV GDNNYLTMQQ TTALPTWGLA 

       490        500        510 
PSGKGRGLQH PPPVGSQEGP KDPEAWSRPQ GWYNHSGK 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 20D7DFAB11AEECEF
Show »

FASTA25227,574
Isoform 3 (Gamma) [UniParc].

Checksum: 8E6E045EC3B11DEF
Show »

FASTA23125,326

References

« Hide 'large scale' references
[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]"RIP3, a novel apoptosis-inducing kinase."
Sun X., Lee J., Navas T., Baldwin D.T., Stewart T.A., Dixit V.M.
J. Biol. Chem. 274:16871-16875(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1."
Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B., Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.
Inflamm. Bowel Dis. 18:603-612(2012) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006862.2. NM_006871.3.
UniGeneHs.268551.

3D structure databases

ProteinModelPortalQ9Y572.
SMRQ9Y572. Positions 11-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116224. 19 interactions.
IntActQ9Y572. 12 interactions.
MINTMINT-1131399.
STRING9606.ENSP00000216274.

Chemistry

ChEMBLCHEMBL1795199.

PTM databases

PhosphoSiteQ9Y572.

Polymorphism databases

DMDM205371831.

Proteomic databases

PaxDbQ9Y572.
PRIDEQ9Y572.

Protocols and materials databases

DNASU11035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216274; ENSP00000216274; ENSG00000129465. [Q9Y572-1]
ENST00000554756; ENSP00000452328; ENSG00000129465. [Q9Y572-3]
GeneID11035.
KEGGhsa:11035.
UCSCuc001wpa.3. human. [Q9Y572-1]

Organism-specific databases

CTD11035.
GeneCardsGC14M024811.
HGNCHGNC:10021. RIPK3.
HPAHPA054606.
HPA055087.
MIM605817. gene.
neXtProtNX_Q9Y572.
PharmGKBPA34396.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000035101.
HOVERGENHBG062538.
InParanoidQ9Y572.
KOK08847.
OMAVGDNNYL.
OrthoDBEOG7Q2N5T.
PhylomeDBQ9Y572.
TreeFamTF106506.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_6900. Immune System.
SignaLinkQ9Y572.

Gene expression databases

BgeeQ9Y572.
CleanExHS_RIPK3.
GenevestigatorQ9Y572.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR025735. RHIM_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF12721. RHIM. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRIPK3.
GenomeRNAi11035.
NextBio41936.
PROQ9Y572.
SOURCESearch...

Entry information

Entry nameRIPK3_HUMAN
AccessionPrimary (citable) accession number: Q9Y572
Secondary accession number(s): B4DJL9 expand/collapse secondary AC list , C4AM87, Q5J795, Q5J796, Q6P5Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM