Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
RIPK1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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); Protein kinase, TKL; EC 2.7.11.1; TKL group; RIPK family
Chromosomal Location of Human Ortholog: 6p25.2
Cellular Component: cytoplasm; cytosol; mitochondrion; receptor complex
Molecular Function: death receptor binding; identical protein binding; protein binding; protein complex binding; protein kinase activity; protein serine/threonine kinase activity; ubiquitin protein ligase binding
Biological Process: activation of JNK activity; activation of NF-kappaB transcription factor; apoptosis; caspase activation; cellular protein catabolic process; I-kappaB kinase/NF-kappaB cascade; negative regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of apoptosis; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interleukin-8 production; positive regulation of JNK cascade; positive regulation of macrophage differentiation; positive regulation of programmed cell death; positive regulation of protein amino acid phosphorylation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; protein amino acid autophosphorylation; protein heterooligomerization; protein homooligomerization; tumor necrosis factor-mediated signaling pathway
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
Select Structure to View Below

RIPK1

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  KinBase  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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



 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 2 S6‑p __MQPDMsLNVIKMK
2 0 S14‑p LNVIKMKssDFLEsA
2 0 S15‑p NVIKMKssDFLEsAE
1 0 S20‑p KssDFLEsAELDsGG
0 2 S25‑p LEsAELDsGGFGKVs
0 1 S32‑p sGGFGKVsLCFHRtQ
0 2 T38‑p VsLCFHRtQGLMIMK
0 2 K115‑ub MSTPLSVkGRIILEI
1 1 S161‑p IADLGLAsFKMWsKL
2 1 S166‑p LAsFKMWsKLNNEEH
0 1 K184‑ub REVDGTAkKNGGTLY
1 0 E234 PYENAICEQQLIMCI
0 2 S303‑p SVEEDVKsLKKEYSN
0 1 K306 EDVKsLKKEYSNENA
0 1 Y308 VKsLKKEYSNENAVV
1 23 N312 KKEYSNENAVVkRMQ
0 2 K316‑ub SNENAVVkRMQsLQL
0 41 S320‑p AVVkRMQsLQLdCVA
1 0 D324‑ca RMQsLQLdCVAVPss
0 4 S330‑p LdCVAVPssRsNSAT
0 4 S331‑p dCVAVPssRsNSATE
0 2 S333‑p VAVPssRsNSATEQP
4 0 K377‑ub NEPSLQSkLQDEANy
0 286 Y384‑p kLQDEANyHLyGsRM
0 211 Y387‑p DEANyHLyGsRMDRQ
0 3 S389‑p ANyHLyGsRMDRQTK
0 16 S416‑p EERRRRVsHDPFAQQ
0 34 Y426‑p PFAQQRPyENFQNTE
0 1 Q430 QRPyENFQNTEGKGT
0 1 A438 NTEGKGTAYSSAASH
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
0 1 S664‑p SRIDLLSsLIYVSQN
65746 : Phospho-RIP (Ser166) (D1L3S) Rabbit mAb
  RIPK1 iso2  
S6 __MQPDMSLNVIKMK
S14 LNVIKMKSSDFLESA
S15 NVIKMKSSDFLESAE
S20 KSSDFLESAELDSGG
S25 LESAELDSGGFGKVS
S32 SGGFGKVSLCFHRTQ
T38 VSLCFHRTQGLMIMK
- gap
S115 IADLGLASFKMWSKL
S120 LASFKMWSKLNNEEH
K138 REVDGTAKKNGGTLY
E188 PYENAICEQQLIMCI
S257 SVEEDVKSLKKEYSN
K260 EDVKSLKKEYSNENA
Y262 VKSLKKEYSNENAVV
N266 KKEYSNENAVVKRMQ
K270 SNENAVVKRMQSLQL
S274 AVVKRMQSLQLDCVA
D278 RMQSLQLDCVAVPSS
S284 LDCVAVPSSRSNSAT
S285 DCVAVPSSRSNSATE
S287 VAVPSSRSNSATEQP
K331 NEPSLQSKLQDEANY
Y338 KLQDEANYHLYGSRM
Y341 DEANYHLYGSRMDRQ
S343 ANYHLYGSRMDRQTK
S370 EERRRRVSHDPFAQQ
Y380 PFAQQRPYENFQNTE
Q384 QRPYENFQNTEGKGT
A392 NTEGKGTAYSSAASH
Y417 TSQPQVLYQNNGLYS
Y423 LYQNNGLYSSHGFGT
S424 YQNNGLYSSHGFGTR
S425 QNNGLYSSHGFGTRP
T437 TRPLDPGTAGPRVWY
Y444 TAGPRVWYRPIPSHM
N467 PETNYLGNTPTMPFS
K484 PPTDESIKYTIYNST
K525 FKEEPAAKYQAIFDN
K558 HWKNCARKLGFTQSQ
K581 ERDGLKEKVYQMLQK
K596 WVMREGIKGATVGKL
K602 IKGATVGKLAQALHQ
S618 SRIDLLSSLIYVSQN
  mouse

 
S6 __MQPDMSLDNIKMA
S14‑p LDNIKMAssDLLEKT
S15‑p DNIKMAssDLLEKTD
K20 AssDLLEKTDLDSGG
S25 LEKTDLDSGGFGKVS
S32 SGGFGKVSLCYHRSH
S38 VSLCYHRSHGFVILK
K115‑ub IDVPLSLkGRIIVEA
S161 IADLGVASFKTWSKL
S166 VASFKTWSKLTKEKD
K185 EVSSTTKKNNGGTLY
T235‑p PYENVICtEQFVICI
S304 YVEEDVASLKkEyPD
K307‑ub EDVASLKkEyPDQsP
Y309‑p VASLKkEyPDQsPVL
S313‑p KkEyPDQsPVLQRMF
Q317 PDQsPVLQRMFsLQH
S321‑p PVLQRMFsLQHDCVP
D325 RMFsLQHDCVPLPPs
P331 HDCVPLPPsRsNSEQ
S332‑p DCVPLPPsRsNSEQP
S334‑p VPLPPsRsNSEQPGS
K376 NDRSVQAKLQEEASY
Y383 KLQEEASYHAFGIFA
F386 EEASYHAFGIFAEKQ
I388 ASYHAFGIFAEKQTK
S415‑p EERKRRVsHDPFAQQ
R425 PFAQQRARENIkSAG
K429‑ac QRARENIkSAGARGH
S437‑p SAGARGHsDPSTTSR
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
H649 CRIDLLNHLIRASQS
31122 : Phospho-RIP (Ser166) Antibody (Rodent Specific)
  rat

 
S6 __MQPDMSLDNIKMA
S14 LDNIKMASDDLLERK
D15 DNIKMASDDLLERKD
R20 ASDDLLERKDLDSGG
S25 LERKDLDSGGFGKVS
S32 SGGFGKVSLCFHRTH
T38 VSLCFHRTHGFVILK
K115 ESVPLSVKGRIIVEI
S161 IADLGVASFKTWSKL
S166 VASFKTWSKLTKEEH
K184 REASSVTKKNGGTLY
T234 PYENVICTEQFLVCI
S303 YVEEDVASLKKEYPS
K306 EDVASLKKEYPSQsP
Y308 VASLKKEYPSQsPVL
S312‑p KKEYPSQsPVLKRMF
K316 PSQsPVLKRMFSLQH
S320 PVLKRMFSLQHDCVP
D324 RMFSLQHDCVPLPPS
P330 HDCVPLPPSRSNSEQ
S331 DCVPLPPSRSNSEQP
S333 VPLPPSRSNSEQPGS
K375 NERSVQAKLQEEASY
Y382 KLQEEASYHAFGIFA
F385 EEASYHAFGIFAEKQ
I387 ASYHAFGIFAEKQTK
S414‑p EERKRRVsHDPFAQQ
H424 PFAQQRVHENVKSAG
K428 QRVHENVKSAGAKGL
P436 SAGAKGLPYPSTTSH
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
Q651 CRTDLLNQLIQASQS
31122 : Phospho-RIP (Ser166) Antibody (Rodent Specific)
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.