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Protein

Receptor-interacting serine/threonine-protein kinase 1

Gene

RIPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei49ATPPROSITE-ProRule annotation1
Active sitei138Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi23 – 31ATPPROSITE-ProRule annotation9

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-containing complex binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • signal transducer activity Source: GO_Central
  • 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
  • apoptotic 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
  • I-kappaB kinase/NF-kappaB signaling Source: Reactome
  • MyD88-independent toll-like receptor signaling pathway Source: Reactome
  • necroptotic process Source: UniProtKB
  • necroptotic signaling pathway Source: BHF-UCL
  • 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 extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
  • 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 hydrogen peroxide-induced cell death Source: BHF-UCL
  • 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 necrotic cell death Source: BHF-UCL
  • 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 by RNA polymerase II Source: UniProtKB
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • protein autophosphorylation Source: BHF-UCL
  • protein deubiquitination Source: Reactome
  • 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 necroptotic process Source: Reactome
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • response to tumor necrosis factor Source: BHF-UCL
  • ripoptosome assembly Source: UniProtKB
  • ripoptosome assembly involved in necroptotic process Source: GO_Central
  • T cell apoptotic process Source: UniProtKB
  • toll-like receptor 3 signaling pathway Source: Reactome
  • TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  • tumor necrosis factor-mediated signaling pathway Source: Reactome
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processHost-virus interaction, Necrosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-140534 Ligand-dependent caspase activation
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-2562578 TRIF-mediated programmed cell death
R-HSA-3295583 TRP channels
R-HSA-3371378 Regulation by c-FLIP
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5218900 CASP8 activity is inhibited
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5675482 Regulation of necroptotic cell death
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-69416 Dimerization of procaspase-8
R-HSA-75893 TNF signaling
R-HSA-9013957 TLR3-mediated TICAM1-dependent programmed cell death
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
R-HSA-937041 IKK complex recruitment mediated by RIP1
SignaLinkiQ13546
SIGNORiQ13546

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000137275.13
HGNCiHGNC:10019 RIPK1
MIMi603453 gene
neXtProtiNX_Q13546

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45K → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi161S → A: Decreases RIPK1 kinase activity. 1 Publication1
Mutagenesisi161S → E: No effect on RIPK1 autophosphorylation. 1 Publication1
Mutagenesisi324D → K: Abolishes cleavage by caspase-8. 1 Publication1
Mutagenesisi377K → R: Abolishes RIP-mediated NF-Kappa-B activation. 1 Publication1

Organism-specific databases

DisGeNETi8737
OpenTargetsiENSG00000137275
PharmGKBiPA34394

Chemistry databases

ChEMBLiCHEMBL5464
GuidetoPHARMACOLOGYi2189

Polymorphism and mutation databases

BioMutaiRIPK1
DMDMi60393639

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866061 – 671Receptor-interacting serine/threonine-protein kinase 1Add BLAST671

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6Phosphoserine1 Publication1
Modified residuei20Phosphoserine; by autocatalysisSequence analysis1
Modified residuei25Phosphoserine1 Publication1
Modified residuei161Phosphoserine; by RIPK3 and autocatalysisSequence analysis1
Modified residuei166Phosphoserine; by autocatalysisSequence analysis1
Modified residuei303Phosphoserine1 Publication1
Modified residuei320PhosphoserineCombined sources1 Publication1
Modified residuei333Phosphoserine1 Publication1
Modified residuei384PhosphotyrosineCombined sources1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei324 – 325Cleavage; by caspase-82

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13546
MaxQBiQ13546
PaxDbiQ13546
PeptideAtlasiQ13546
PRIDEiQ13546

PTM databases

iPTMnetiQ13546
PhosphoSitePlusiQ13546

Miscellaneous databases

PMAP-CutDBiQ13546

Expressioni

Gene expression databases

BgeeiENSG00000137275
CleanExiHS_RIPK1
ExpressionAtlasiQ13546 baseline and differential
GenevisibleiQ13546 HS

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. Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436).By similarity20 Publications
(Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • death domain binding Source: BHF-UCL
  • death receptor binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114274, 86 interactors
CORUMiQ13546
DIPiDIP-433N
IntActiQ13546, 59 interactors
MINTiQ13546
STRINGi9606.ENSP00000259808

Chemistry databases

BindingDBiQ13546

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 16Combined sources3
Beta strandi17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Turni26 – 28Combined sources3
Beta strandi30 – 36Combined sources7
Turni37 – 39Combined sources3
Beta strandi40 – 51Combined sources12
Helixi54 – 56Combined sources3
Helixi57 – 68Combined sources12
Beta strandi78 – 84Combined sources7
Beta strandi87 – 93Combined sources7
Helixi100 – 104Combined sources5
Beta strandi106 – 108Combined sources3
Helixi112 – 131Combined sources20
Helixi141 – 143Combined sources3
Beta strandi144 – 146Combined sources3
Beta strandi152 – 154Combined sources3
Helixi163 – 168Combined sources6
Beta strandi171 – 173Combined sources3
Helixi188 – 190Combined sources3
Beta strandi191 – 193Combined sources3
Helixi195 – 197Combined sources3
Beta strandi201 – 203Combined sources3
Helixi207 – 223Combined sources17
Helixi234 – 242Combined sources9
Helixi249 – 251Combined sources3
Helixi258 – 267Combined sources10
Helixi272 – 274Combined sources3
Helixi278 – 292Combined sources15
Helixi294 – 296Combined sources3
Helixi297 – 309Combined sources13
Turni310 – 312Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ITHX-ray2.25A/B1-294[»]
4ITIX-ray2.86A/B1-294[»]
4ITJX-ray1.80A/B1-294[»]
4NEUX-ray2.57A/B1-324[»]
5HX6X-ray2.23A/B1-294[»]
5TX5X-ray2.56A/B1-294[»]
ProteinModelPortaliQ13546
SMRiQ13546
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 289Protein kinasePROSITE-ProRule annotationAdd BLAST273
Domaini583 – 669DeathPROSITE-ProRule annotationAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni290 – 582Interaction with SQSTM11 PublicationAdd BLAST293

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi531 – 547RIP homotypic interaction motif (RHIM)Add BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi411 – 414Poly-Arg4

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

Phylogenomic databases

eggNOGiKOG0192 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00550000074536
HOGENOMiHOG000010270
HOVERGENiHBG055612
InParanoidiQ13546
KOiK02861
OMAiVMEYMEK
OrthoDBiEOG091G0479
PhylomeDBiQ13546
TreeFamiTF106506

Family and domain databases

CDDicd08777 Death_RIP1, 1 hit
InterProiView protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR025735 RHIM_dom
IPR037934 RIP1_Death
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00531 Death, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF12721 RHIM, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00005 DEATH, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti258R → I in BAG36858 (PubMed:14702039).Curated1
Sequence conflicti286R → S in BAG36858 (PubMed:14702039).Curated1
Sequence conflicti514T → S in AAC50137 (PubMed:7538908).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04103964A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs774996232Ensembl.1
Natural variantiVAR_04104081V → I in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs758268804Ensembl.1
Natural variantiVAR_041041220A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs759012409Ensembl.1
Natural variantiVAR_021109234E → K1 PublicationCorresponds to variant dbSNP:rs17548383Ensembl.1
Natural variantiVAR_041042404A → S1 PublicationCorresponds to variant dbSNP:rs34872409Ensembl.1
Natural variantiVAR_058285438A → V3 PublicationsCorresponds to variant dbSNP:rs3173519Ensembl.1
Natural variantiVAR_041043443A → V1 PublicationCorresponds to variant dbSNP:rs35722193Ensembl.1
Natural variantiVAR_041044569A → V1 PublicationCorresponds to variant dbSNP:rs55861377Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_037690108 – 153Missing in isoform 2. 1 PublicationAdd BLAST46

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 No translation available.
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_003804.4 [Q13546-1]
XP_005249514.2, XM_005249457.3
UniGeneiHs.519842

Genome annotation databases

EnsembliENST00000259808; ENSP00000259808; ENSG00000137275 [Q13546-1]
ENST00000380409; ENSP00000369773; ENSG00000137275 [Q13546-1]
GeneIDi8737
KEGGihsa:8737
UCSCiuc003mux.4 human [Q13546-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRIPK1_HUMAN
AccessioniPrimary (citable) accession number: Q13546
Secondary accession number(s): A0AV89
, B2RAG1, B4E3F9, Q13180, Q59H33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 2005
Last modified: April 25, 2018
This is version 196 of the entry and version 3 of the sequence. See 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
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Main funding by: National Institutes of Health