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Protein Page:
RIPK3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RIPK3 Promotes apoptosis. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Binds TRAF2 and RIPK1 and is recruited to the TNFR-1 signaling complex. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, TKL; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; TKL group; RIPK family
Cellular Component: mitochondrion; plasma membrane; cytosol
Molecular Function: NF-kappaB-inducing kinase activity; identical protein binding; protein serine/threonine kinase activity; protein binding; transcription coactivator activity; ATP binding; protein kinase activity
Biological Process: I-kappaB kinase/NF-kappaB cascade; protein heterooligomerization; induction of apoptosis; activation of protein kinase activity; positive regulation of interferon type I production; innate immune response; protein modification process; signal transduction; protein homooligomerization; activation of NF-kappaB transcription factor
Reference #:  Q9Y572 (UniProtKB)
Alt. Names/Synonyms: receptor interacting protein 3; Receptor-interacting protein 3; receptor-interacting serine-threonine kinase 3; Receptor-interacting serine/threonine-protein kinase 3; RIP-3; RIP-like protein kinase 3; RIP3; RIPK3
Gene Symbols: RIPK3
Molecular weight: 56,887 Da
Basal Isoelectric point: 6.08  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  NF-kB Signaling  |  SAPK/JNK Signaling Cascades  |  Signaling Pathways Activating p38 MAPK
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RIPK3

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 P179 SGTGSGEPGGTLGYL
1 0 S227-p VELPTEPsLVYEAVC
0 14 S316-p RSSNRRFsIPEsGQG
0 1 S320-p RRFsIPEsGQGGtEM
0 1 G321 RFsIPEsGQGGtEMD
0 2 T325-p PEsGQGGtEMDGFRR
0 2 S339-p RTIENQHsRNDVMVS
0 1 S359-p LNLEEPPsSVPKKCP
0 1 S372-p CPSLTKRsRAQEEQV
0 2 W383 EEQVPQAWTAGTSSD
0 1 T398-p SMAQPPQtPETSTFR
0 2 S410-p TFRNQMPsPtSTGTP
1 1 - gap
0 1 T412-p RNQMPsPtSTGTPSP
0 3 R508 KDPEAWSRPQGWYNH
0 1 R508 KDPEAWSRPQGWYNH
0 1 Q510 PEAWSRPQGWYNHSG
0 1 Q510 PEAWSRPQGWYNHSG
  mouse

 
S184-p SGSGSRDsGGTLAYL
S232-p AELVDKTsLIRETVC
S321 RSSGRNLSAREPsQR
P325 RNLSAREPsQRGTEM
S326-p NLSAREPsQRGTEMD
T330 REPsQRGTEMDCPRE
- gap
G354 LHLEEPSGPVPGKCP
- gap
T374-p DTSVGPAtPARTSSD
I389 PVAGTPQIPHTLPFR
- gap
T399-p TLPFRGTtPGPVFTE
- gap
R477-m1 YDQAQFGrGrGWQPF
R477-m2 YDQAQFGrGrGWQPF
R479 QAQFGrGRGWQPFHK
R479-m2 QAQFGrGrGWQPFHK
  rat

 
S182 SGSGSRDSGGTLAYL
S229 AEVVDKTSLIRGAVC
S318 RSSDTKLSARESSQK
S322 TKLSARESSQKGTEV
S323 KLSARESSQKGTEVD
T327 RESSQKGTEVDCPRE
- gap
G351 LHLEEPSGSVPERLT
- gap
T374 EASFGHATPAGTSSD
I389 TLAGTPQIPHTLPSR
- gap
T399 TLPSRGTTPRPAFTE
- gap
R474-m1 KEPAQFGrGrGW___
R474 KEPAQFGRGrGW___
R476-m1 PAQFGrGrGW_____
R476 PAQFGrGRGW_____
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