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Protein

Receptor-interacting serine/threonine-protein kinase 1

Gene

RIPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) 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. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. 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 necrosis-inducing complex.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Inhibited by necrostatins, including necrostatin-1, necrostatin-3 and necrostatin-4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation
Sitei324 – 3252Cleavage; by caspase-8

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 319ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • death domain binding Source: BHF-UCL
  • death receptor binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein complex binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  • activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Reactome
  • activation of JUN kinase activity Source: BHF-UCL
  • amyloid fibril formation Source: UniProtKB
  • apoptotic process Source: UniProtKB
  • cell surface receptor signaling pathway Source: Reactome
  • cellular protein catabolic process Source: UniProtKB
  • cellular response to growth factor stimulus Source: Ensembl
  • cellular response to tumor necrosis factor Source: UniProtKB
  • death-inducing signaling complex assembly Source: Reactome
  • extrinsic apoptotic signaling pathway Source: BHF-UCL
  • innate immune response Source: Reactome
  • MyD88-independent toll-like receptor signaling pathway Source: Reactome
  • necroptotic process Source: UniProtKB
  • necroptotic signaling pathway Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  • negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • peptidyl-serine autophosphorylation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of interleukin-8 production Source: BHF-UCL
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of macrophage differentiation Source: UniProtKB
  • positive regulation of necroptotic process Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of programmed cell death Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of type I interferon production Source: Reactome
  • programmed cell death Source: Reactome
  • programmed necrotic cell death Source: Reactome
  • protein autophosphorylation Source: BHF-UCL
  • protein heterooligomerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • regulation of ATP:ADP antiporter activity Source: BHF-UCL
  • regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
  • regulation of necrotic cell death Source: Reactome
  • response to tumor necrosis factor Source: BHF-UCL
  • ripoptosome assembly Source: UniProtKB
  • ripoptosome assembly involved in necroptotic process Source: Ensembl
  • T cell apoptotic process Source: UniProtKB
  • toll-like receptor 3 signaling pathway Source: Reactome
  • toll-like receptor 4 signaling pathway Source: Reactome
  • toll-like receptor signaling pathway Source: Reactome
  • TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  • tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
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_1432. TNF signaling.
REACT_1503. Ligand-dependent caspase activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_169333. TRP channels.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_355072. TNFR1-mediated proapoptotic signaling.
REACT_355311. CASP8 activity is inhibited.
REACT_355409. RIPK1-mediated regulated necrosis.
REACT_832. Dimerization of procaspase-8.
SignaLinkiQ13546.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-interacting serine/threonine-protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
Cell death protein RIP
Receptor-interacting protein 1
Short name:
RIP-1
Serine/threonine-protein kinase RIP
Gene namesi
Name:RIPK1
Synonyms:RIP, RIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10019. RIPK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • death-inducing signaling complex Source: BHF-UCL
  • membrane raft Source: Ensembl
  • mitochondrion Source: BHF-UCL
  • receptor complex Source: BHF-UCL
  • ripoptosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451K → A: Abolishes kinase activity. 1 Publication
Mutagenesisi161 – 1611S → A: Decreases RIPK1 kinase activity. 1 Publication
Mutagenesisi161 – 1611S → E: No effect on RIPK1 autophosphorylation. 1 Publication
Mutagenesisi324 – 3241D → K: Abolishes cleavage by caspase-8. 1 Publication
Mutagenesisi377 – 3771K → R: Abolishes RIP-mediated NF-Kappa-B activation. 1 Publication

Organism-specific databases

PharmGKBiPA34394.

Polymorphism and mutation databases

BioMutaiRIPK1.
DMDMi60393639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Receptor-interacting serine/threonine-protein kinase 1PRO_0000086606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei20 – 201Phosphoserine; by autocatalysisSequence Analysis
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei161 – 1611Phosphoserine; by RIPK3 and autocatalysisSequence Analysis
Modified residuei166 – 1661Phosphoserine; by autocatalysisSequence Analysis
Modified residuei303 – 3031Phosphoserine1 Publication
Modified residuei320 – 3201Phosphoserine2 Publications
Modified residuei333 – 3331Phosphoserine1 Publication
Cross-linki377 – 377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei384 – 3841Phosphotyrosine1 Publication

Post-translational modificationi

Proteolytically cleaved by caspase-8 during TNF-induced apoptosis. Cleavage abolishes NF-kappa-B activation and enhances pro-apoptotic signaling through the TRADD-FADD interaction.1 Publication
RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex.2 Publications
Ubiquitinated by 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin. Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex. Deubiquitination of 'Lys-63'-linked chains and polyubiquitination with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal degradation and consequently down-regulates TNF-alpha-induced NFkappa-B signaling. 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-alpha-induced NFkappa-B signaling. Linear polyubiquitinated; the head-to-tail polyubiquitination is mediated by the LUBAC complex. LPS-mediated activation of NF-kappa-B. Also ubiquitinated with 'Lys-11'-linked chains. Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.6 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13546.
PaxDbiQ13546.
PRIDEiQ13546.

PTM databases

PhosphoSiteiQ13546.

Miscellaneous databases

PMAP-CutDBQ13546.

Expressioni

Gene expression databases

BgeeiQ13546.
CleanExiHS_RIPK1.
ExpressionAtlasiQ13546. baseline and differential.
GenevestigatoriQ13546.

Organism-specific databases

HPAiCAB010302.
HPA015257.

Interactioni

Subunit structurei

Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif). 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 (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 (By similarity). Interacts with ZBP1 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK3 and MLKL. Interacts (via kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts with ARHGEF2. Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination. Interacts with RNF34; involved in RIPK1 ubiquitination.By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-358507,EBI-358507
ANXA1P040835EBI-358507,EBI-354007
BIRC2Q134903EBI-358507,EBI-514538
BIRC3Q134893EBI-358507,EBI-517709
CASP10Q928512EBI-358507,EBI-495095
CASP8Q1479023EBI-358507,EBI-78060
CCDC50Q8IVM02EBI-358507,EBI-723996
CSNK1A1P487295EBI-358507,EBI-1383726
FADDQ131585EBI-358507,EBI-494804
IKBKGQ9Y6K97EBI-358507,EBI-81279
RIPK3Q9Y57224EBI-358507,EBI-298250
Ripk3Q9QZL02EBI-358507,EBI-2367423From a different organism.
TNFRSF1AP194386EBI-358507,EBI-299451
TRAF1Q130773EBI-358507,EBI-359224
TRAF2Q129334EBI-358507,EBI-355744
USP4Q131074EBI-358507,EBI-723290

Protein-protein interaction databases

BioGridi114274. 74 interactions.
DIPiDIP-433N.
IntActiQ13546. 33 interactions.
MINTiMINT-128219.
STRINGi9606.ENSP00000259808.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Beta strandi17 – 237Combined sources
Turni26 – 283Combined sources
Beta strandi30 – 367Combined sources
Turni37 – 393Combined sources
Beta strandi40 – 5112Combined sources
Helixi54 – 563Combined sources
Helixi57 – 6812Combined sources
Beta strandi78 – 847Combined sources
Beta strandi87 – 937Combined sources
Helixi100 – 1045Combined sources
Beta strandi106 – 1083Combined sources
Helixi112 – 13120Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi152 – 1543Combined sources
Helixi163 – 1686Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 1973Combined sources
Beta strandi201 – 2033Combined sources
Helixi207 – 22317Combined sources
Helixi234 – 2429Combined sources
Helixi249 – 2513Combined sources
Helixi258 – 26710Combined sources
Helixi272 – 2743Combined sources
Helixi278 – 29215Combined sources
Helixi294 – 2963Combined sources
Helixi297 – 30913Combined sources
Turni310 – 3123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ITHX-ray2.25A/B1-294[»]
4ITIX-ray2.86A/B1-294[»]
4ITJX-ray1.80A/B1-294[»]
4NEUX-ray2.57A/B1-324[»]
ProteinModelPortaliQ13546.
SMRiQ13546. Positions 7-327, 579-661.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 289273Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini583 – 66987DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 582293Interaction with SQSTM1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi531 – 54717RIP homotypic interaction motif (RHIM)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi411 – 4144Poly-Arg

Domaini

Contains a C-terminal death domain (DD) that engages other DD-containing proteins as well as a central (intermediate) region important for NF-kB activation and RHIM-dependent signaling.1 Publication

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000010270.
HOVERGENiHBG055612.
InParanoidiQ13546.
KOiK02861.
OMAiVVKRMQS.
OrthoDBiEOG7MPRDN.
PhylomeDBiQ13546.
TreeFamiTF106506.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR025735. RHIM_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
PF12721. RHIM. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13546-1) [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

        10         20         30         40         50
MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG
60 70 80 90 100
PNCIEHNEAL LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL
110 120 130 140 150
MHVLKAEMST PLSVKGRIIL EIIEGMCYLH GKGVIHKDLK PENILVDNDF
160 170 180 190 200
HIKIADLGLA SFKMWSKLNN EEHNELREVD GTAKKNGGTL YYMAPEHLND
210 220 230 240 250
VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC IKSGNRPDVD
260 270 280 290 300
DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED
310 320 330 340 350
VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG
360 370 380 390 400
MGPVEESWFA PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR
410 420 430 440 450
QNVAYNREEE RRRRVSHDPF AQQRPYENFQ NTEGKGTAYS SAASHGNAVH
460 470 480 490 500
QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD PGTAGPRVWY RPIPSHMPSL
510 520 530 540 550
HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ IGAYNYMEIG
560 570 580 590 600
GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN
610 620 630 640 650
CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA
660 670
QALHQCSRID LLSSLIYVSQ N
Length:671
Mass (Da):75,931
Last modified:February 1, 2005 - v3
Checksum:i976E2428D525A9B2
GO
Isoform 2 (identifier: Q13546-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-153: Missing.

Note: No experimental confirmation available.

Show »
Length:625
Mass (Da):70,733
Checksum:i4D3780FB4A93FDB1
GO

Sequence cautioni

The sequence BAG65471.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581R → I in BAG36858 (PubMed:14702039).Curated
Sequence conflicti286 – 2861R → S in BAG36858 (PubMed:14702039).Curated
Sequence conflicti514 – 5141T → S in AAC50137 (PubMed:7538908).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041039
Natural varianti81 – 811V → I in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041040
Natural varianti220 – 2201A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041041
Natural varianti234 – 2341E → K.1 Publication
Corresponds to variant rs17548383 [ dbSNP | Ensembl ].
VAR_021109
Natural varianti404 – 4041A → S.1 Publication
Corresponds to variant rs34872409 [ dbSNP | Ensembl ].
VAR_041042
Natural varianti438 – 4381A → V.3 Publications
Corresponds to variant rs3173519 [ dbSNP | Ensembl ].
VAR_058285
Natural varianti443 – 4431A → V.1 Publication
Corresponds to variant rs35722193 [ dbSNP | Ensembl ].
VAR_041043
Natural varianti569 – 5691A → V.1 Publication
Corresponds to variant rs55861377 [ dbSNP | Ensembl ].
VAR_041044

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei108 – 15346Missing in isoform 2. 1 PublicationVSP_037690Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50062 mRNA. Translation: AAC32232.1.
AK314176 mRNA. Translation: BAG36858.1.
AK304701 mRNA. Translation: BAG65471.1. Different initiation.
AY682848 Genomic DNA. Translation: AAT74626.1.
AL031963 Genomic DNA. Translation: CAD70625.1.
BC126254 mRNA. Translation: AAI26255.1.
BC126256 mRNA. Translation: AAI26257.1.
AB208926 mRNA. Translation: BAD92163.1.
U25994 mRNA. Translation: AAC50137.1.
CCDSiCCDS4482.1. [Q13546-1]
PIRiT09479.
RefSeqiNP_003795.2. NM_003804.3. [Q13546-1]
XP_005249514.2. XM_005249457.3.
XP_005249515.1. XM_005249458.1. [Q13546-1]
UniGeneiHs.519842.

Genome annotation databases

EnsembliENST00000259808; ENSP00000259808; ENSG00000137275. [Q13546-1]
ENST00000380409; ENSP00000369773; ENSG00000137275. [Q13546-1]
GeneIDi8737.
KEGGihsa:8737.
UCSCiuc003muv.4. human. [Q13546-1]
uc011dhs.2. human. [Q13546-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50062 mRNA. Translation: AAC32232.1.
AK314176 mRNA. Translation: BAG36858.1.
AK304701 mRNA. Translation: BAG65471.1. Different initiation.
AY682848 Genomic DNA. Translation: AAT74626.1.
AL031963 Genomic DNA. Translation: CAD70625.1.
BC126254 mRNA. Translation: AAI26255.1.
BC126256 mRNA. Translation: AAI26257.1.
AB208926 mRNA. Translation: BAD92163.1.
U25994 mRNA. Translation: AAC50137.1.
CCDSiCCDS4482.1. [Q13546-1]
PIRiT09479.
RefSeqiNP_003795.2. NM_003804.3. [Q13546-1]
XP_005249514.2. XM_005249457.3.
XP_005249515.1. XM_005249458.1. [Q13546-1]
UniGeneiHs.519842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ITHX-ray2.25A/B1-294[»]
4ITIX-ray2.86A/B1-294[»]
4ITJX-ray1.80A/B1-294[»]
4NEUX-ray2.57A/B1-324[»]
ProteinModelPortaliQ13546.
SMRiQ13546. Positions 7-327, 579-661.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114274. 74 interactions.
DIPiDIP-433N.
IntActiQ13546. 33 interactions.
MINTiMINT-128219.
STRINGi9606.ENSP00000259808.

Chemistry

BindingDBiQ13546.
ChEMBLiCHEMBL5464.
GuidetoPHARMACOLOGYi2189.

PTM databases

PhosphoSiteiQ13546.

Polymorphism and mutation databases

BioMutaiRIPK1.
DMDMi60393639.

Proteomic databases

MaxQBiQ13546.
PaxDbiQ13546.
PRIDEiQ13546.

Protocols and materials databases

DNASUi8737.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259808; ENSP00000259808; ENSG00000137275. [Q13546-1]
ENST00000380409; ENSP00000369773; ENSG00000137275. [Q13546-1]
GeneIDi8737.
KEGGihsa:8737.
UCSCiuc003muv.4. human. [Q13546-1]
uc011dhs.2. human. [Q13546-2]

Organism-specific databases

CTDi8737.
GeneCardsiGC06P003064.
HGNCiHGNC:10019. RIPK1.
HPAiCAB010302.
HPA015257.
MIMi603453. gene.
neXtProtiNX_Q13546.
PharmGKBiPA34394.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074536.
HOGENOMiHOG000010270.
HOVERGENiHBG055612.
InParanoidiQ13546.
KOiK02861.
OMAiVVKRMQS.
OrthoDBiEOG7MPRDN.
PhylomeDBiQ13546.
TreeFamiTF106506.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_1432. TNF signaling.
REACT_1503. Ligand-dependent caspase activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_164011. Regulation by c-FLIP.
REACT_169333. TRP channels.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_355072. TNFR1-mediated proapoptotic signaling.
REACT_355311. CASP8 activity is inhibited.
REACT_355409. RIPK1-mediated regulated necrosis.
REACT_832. Dimerization of procaspase-8.
SignaLinkiQ13546.

Miscellaneous databases

ChiTaRSiRIPK1. human.
GeneWikiiRIPK1.
GenomeRNAii8737.
NextBioi32775.
PMAP-CutDBQ13546.
PROiQ13546.
SOURCEiSearch...

Gene expression databases

BgeeiQ13546.
CleanExiHS_RIPK1.
ExpressionAtlasiQ13546. baseline and differential.
GenevestigatoriQ13546.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR025735. RHIM_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00069. Pkinase. 1 hit.
PF12721. RHIM. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex."
    Hsu H., Huang J., Shu H.-B., Baichwal V.R., Goeddel D.V.
    Immunity 4:387-396(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-45, INTERACTION WITH TRADD; TRAF1; TRAF2 AND TRAF3, VARIANT VAL-438.
    Tissue: Umbilical vein endothelial cell.
  2. Huang J., Hsu H., Baichwal V.R., Goeddel D.V.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 120.
  3. "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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-671 (ISOFORM 2).
    Tissue: Adrenal gland and Uterus.
  4. SeattleSNPs variation discovery resource
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-234.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT VAL-438.
  7. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-671.
    Tissue: Brain.
  8. "RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death."
    Stanger B.Z., Leder P., Lee T.-H., Kim E., Seed B.
    Cell 81:513-523(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 300-671, VARIANT VAL-438.
    Tissue: Leukemic T-cell.
  9. "Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis."
    Lin Y., Devin A., Rodriguez Y., Liu Z.-G.
    Genes Dev. 13:2514-2526(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY CASPASE-8, MUTAGENESIS OF ASP-324.
  10. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
    Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
    EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND TRAF2, DOMAIN.
  11. Cited for: INTERACTION WITH RIPK3.
  12. "The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation."
    Izumi K.M., Cahir McFarland E., Ting A.T., Riley E.A., Seed B., Kieff E.D.
    Mol. Cell. Biol. 19:5759-5767(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BNLF1.
  13. "Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis."
    Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A., Wallach D., Horwitz M.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKG.
  14. "Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule."
    Holler N., Zaru R., Micheau O., Thome M., Attinger A., Valitutti S., Bodmer J.L., Schneider P., Seed B., Tschopp J.
    Nat. Immunol. 1:489-495(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome."
    Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., Vartanian T.
    J. Biol. Chem. 276:8865-8874(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EGFR.
  16. "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation."
    Chen D., Li X., Zhai Z., Shu H.-B.
    J. Biol. Chem. 277:15985-15991(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF216.
  17. "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, INTERACTION WITH RIPK3.
  18. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation."
    Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z., Shu H.-B.
    J. Biol. Chem. 279:16847-16853(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFAND5.
  20. "De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling."
    Wertz I.E., O'Rourke K.M., Zhou H., Eby M., Aravind L., Seshagiri S., Wu P., Wiesmann C., Baker R., Boone D.L., Ma A., Koonin E.V., Dixit V.M.
    Nature 430:694-699(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY TRAF2, DEUBIQUITINATION BY TNFAIP3.
  21. "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
    Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
    Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAVS.
  22. "Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO."
    Ea C.K., Deng L., Xia Z.P., Pineda G., Chen Z.J.
    Mol. Cell 22:245-257(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-377, MUTAGENESIS OF LYS-377.
  23. "RIP1, a kinase on the crossroads of a cell's decision to live or die."
    Festjens N., Vanden Berghe T., Cornelis S., Vandenabeele P.
    Cell Death Differ. 14:400-410(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
    Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
    J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DAB2IP, INTERACTION WITH DAB2IP.
  25. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
    Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
    J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBCK1.
  26. "CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation."
    Liao W., Xiao Q., Tchikov V., Fujita K., Yang W., Wincovitch S., Garfield S., Conze D., El-Deiry W.S., Schuetze S., Srinivasula S.M.
    Curr. Biol. 18:641-649(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFFL, UBIQUITINATION BY RFFL.
  27. Cited for: MUTAGENESIS OF SER-161, INHIBITION BY NECROSTATIN-1, PHOSPHORYLATION AT SER-6; SER-20; SER-25; SER-161; SER-166; SER-303; SER-320 AND SER-333.
  28. "Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1."
    Upton J.W., Kaiser W.J., Mocarski E.S.
    J. Biol. Chem. 283:16966-16970(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MURID HERPESVIRUS 1 VIRAL INHIBITOR OF RIP ACTIVATION.
  29. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "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, PHOSPHORYLATION.
  31. "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, INTERACTION WITH RIPK3.
  32. Cited for: INTERACTION WITH RNF34, UBIQUITINATION BY RNF34.
  33. "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.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
  36. "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.
  37. "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: IDENTIFICATION IN COMPLEX WITH PGAM5; RIPK3 AND MLKL.
  38. Cited for: INTERACTION WITH ARHGEF2.
  39. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  40. "Structural basis of RIP1 inhibition by necrostatins."
    Xie T., Peng W., Liu Y., Yan C., Maki J., Degterev A., Yuan J., Shi Y.
    Structure 21:493-499(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-294 IN COMPLEXES WITH NECROSTATIN-TYPE INHIBITORS, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION.
  41. "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] VAL-64; ILE-81; VAL-220; SER-404; VAL-443 AND VAL-569.

Entry informationi

Entry nameiRIPK1_HUMAN
AccessioniPrimary (citable) accession number: Q13546
Secondary accession number(s): A0AV89
, B2RAG1, B4E3F9, Q13180, Q59H33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 2005
Last modified: May 27, 2015
This is version 166 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.