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Protein Page:
RIPK1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RIPK1 Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) 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. 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 necroptosis-inducing complex. Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif); this interaction induces RIPK1 necroptosis-specific phosphorylation, formation of the necroptosis-inducing complex. 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. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Inhibited by necrostatin-1. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; Protein kinase, TKL; TKL group; RIPK family
Cellular Component: mitochondrion; cytosol; receptor complex; lipid raft
Molecular Function: protein serine/threonine kinase activity; identical protein binding; protein binding; ubiquitin protein ligase binding; death receptor binding; protein complex binding; ATP binding; protein kinase activity
Biological Process: protein heterooligomerization; apoptosis; positive regulation of apoptosis; protein amino acid autophosphorylation; positive regulation of JNK cascade; toll-like receptor 3 signaling pathway; activation of JNK activity; activation of NF-kappaB transcription factor; positive regulation of interleukin-8 production; tumor necrosis factor-mediated signaling pathway; positive regulation of interferon type I production; positive regulation of macrophage differentiation; toll-like receptor 4 signaling pathway; protein homooligomerization; caspase activation; positive regulation of I-kappaB kinase/NF-kappaB cascade; MyD88-independent toll-like receptor signaling pathway; negative regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of tumor necrosis factor production; positive regulation of programmed cell death; cellular protein catabolic process; toll-like receptor signaling pathway; innate immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of protein amino acid phosphorylation
Reference #:  Q13546 (UniProtKB)
Alt. Names/Synonyms: Cell death protein RIP; FLJ39204; receptor (TNFRSF)-interacting serine-threonine kinase 1; receptor interacting protein; Receptor-interacting protein 1; Receptor-interacting serine/threonine-protein kinase 1; RIP; RIP-1; RIP1; RIPK1; Serine/threonine-protein kinase RIP
Gene Symbols: RIPK1
Molecular weight: 75,931 Da
Basal Isoelectric point: 5.92  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  NF-kB Signaling  |  Regulation of P38 MAPKs  |  SAPK/JNK Signaling Cascades  |  Toll-Like Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RIPK1

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S161‑p

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 1 S6-p __MQPDMsLNVIKMK
1 0 S14-p LNVIKMKssDFLEsA
1 1 S15-p NVIKMKssDFLEsAE
1 0 S20-p KssDFLEsAELDsGG
0 1 S25-p LEsAELDsGGFGKVs
0 1 S32-p sGGFGKVsLCFHRtQ
0 2 T38-p VsLCFHRtQGLMIMK
0 2 K115-ub MSTPLSVkGRIILEI
1 1 S161-p IADLGLAsFKMWsKL
1 0 S166-p LAsFKMWsKLNNEEH
0 1 K184-ub REVDGTAkKNGGTLY
0 1 S303-p SVEEDVKsLKKEYSN
0 1 K306 EDVKsLKKEYSNENA
0 16 N312 KKEYSNENAVVkRMQ
0 1 K316-ub SNENAVVkRMQsLQL
0 33 S320-p AVVkRMQsLQLDCVA
0 3 S330-p LDCVAVPssRsNSAT
0 4 S331-p DCVAVPssRsNSATE
0 2 S333-p VAVPssRsNSATEQP
3 0 K377-ub NEPSLQSkLQDEANy
0 271 Y384-p kLQDEANyHLyGsRM
0 209 Y387-p DEANyHLyGsRMDRQ
0 2 S389-p ANyHLyGsRMDRQTK
0 14 S416-p EERRRRVsHDPFAQQ
0 34 Y426-p PFAQQRPyENFQNTE
0 1 Q430 QRPyENFQNTEGKGT
0 4 Y463-p TSQPQVLyQNNGLys
0 10 Y469-p LyQNNGLyssHGFGT
0 1 S470-p yQNNGLyssHGFGTR
0 2 S471-p QNNGLyssHGFGTRP
0 1 T483-p TRPLDPGtAGPRVWy
0 3 Y490-p tAGPRVWyRPIPSHM
0 1 N513 PETNYLGNTPTMPFS
1 0 K530-ac PPTDESIkYTIYNST
0 1 K571-ub FKEEPAAkYQAIFDN
0 1 K604-ub HWKNCARkLGFTQSQ
0 2 K627-ub ERDGLKEkVYQMLQK
0 1 K642-ac WVMREGIkGATVGkL
0 1 K648-ac IkGATVGkLAQALHQ
  mouse

 
S6 __MQPDMSLDNIKMA
S14 LDNIKMASsDLLEKT
S15-p DNIKMASsDLLEKTD
K20 ASsDLLEKTDLDSGG
S25 LEKTDLDSGGFGKVS
S32 SGGFGKVSLCYHRSH
S38 VSLCYHRSHGFVILK
K115-ub IDVPLSLkGRIIVEA
S161 IADLGVASFKTWSKL
S166 VASFKTWSKLTKEKD
K184 KEVSSTTKKNNGGTL
S304 YVEEDVASLKkEYPD
K307-ub EDVASLKkEYPDQsP
S313-p KkEYPDQsPVLQRMF
Q317 PDQsPVLQRMFsLQH
S321-p PVLQRMFsLQHDCVP
P331 HDCVPLPPsRsNSEQ
S332-p DCVPLPPsRsNSEQP
S334-p VPLPPsRsNSEQPGS
K376 NDRSVQAKLQEEASY
Y383 KLQEEASYHAFGIFA
F386 EEASYHAFGIFAEKQ
I388 ASYHAFGIFAEKQTK
S415-p EERKRRVsHDPFAQQ
R425 PFAQQRARENIkSAG
K429-ac QRARENIkSAGARGH
V459 SWPATQTVWNNGLYN
Y465 TVWNNGLYNQHGFGT
N466 VWNNGLYNQHGFGTT
Q467 WNNGLYNQHGFGTTG
T472 YNQHGFGTTGTGVWY
Y479 TTGTGVWYPPNLSQM
S502 PETNIPGSTPTMPYF
K519 PVADDLIKYTIFNSS
R556 CKEESTSRHQAIFDN
K589 QWKNCARKLGFTESQ
K612-ub ERDGLKEkVYQMLQK
K627 WLMREGTKGATVGKL
K633 TKGATVGKLAQALHQ
  rat

 
S6 __MQPDMSLDNIKMA
S14 LDNIKMASDDLLERK
D15 DNIKMASDDLLERKD
R20 ASDDLLERKDLDSGG
S25 LERKDLDSGGFGKVS
S32 SGGFGKVSLCFHRTH
T38 VSLCFHRTHGFVILK
K115 ESVPLSVKGRIIVEI
S161 IADLGVASFKTWSKL
S166 VASFKTWSKLTKEEH
K184 REASSVTKKNGGTLY
S303 YVEEDVASLKKEYPS
K306 EDVASLKKEYPSQSP
S312 KKEYPSQSPVLKRMF
K316 PSQSPVLKRMFSLQH
S320 PVLKRMFSLQHDCVP
P330 HDCVPLPPSRSNSEQ
S331 DCVPLPPSRSNSEQP
S333 VPLPPSRSNSEQPGS
K375 NERSVQAKLQEEASY
Y382 KLQEEASYHAFGIFA
F385 EEASYHAFGIFAEKQ
I387 ASYHAFGIFAEKQTK
S414-p EERKRRVsHDPFAQQ
H424 PFAQQRVHENVKSAG
K428 QRVHENVKSAGAKGL
L461 ASQIKVPLWNNGVYN
Y467 PLWNNGVYNHHGFGA
N468 LWNNGVYNHHGFGAT
H469 WNNGVYNHHGFGATG
A474 YNHHGFGATGTGVWY
Y481 ATGTGVWYGPSVSQS
S504-p PETNLPGsIPTMPYI
R521 APPDDSIRCTIYNSS
R558 CKVESTSRHQAVFAN
K591 QWKNCARKLGFTESQ
K614 ERDGLKEKVYQMLQK
K629 WLMREGTKGATVGKL
K635 TKGATVGKLAQALHQ
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