Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q13546 (RIPK1_HUMAN)

Entry version 220 (10 Feb 2021)
Sequence version 3 (01 Feb 2005)
Previous versions | rss
Add a publicationFeedback
Protein

Receptor-interacting serine/threonine-protein kinase 1

Gene

RIPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:31827280, PubMed:31827281). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity).By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Serine-threonine kinase activity is inhibited by linear polyubiquitination ('Met-1'-linked) by the LUBAC complex (By similarity). Inhibited by necrostatins, including necrostatin-1, necrostatin-3 and necrostatin-4 (PubMed:23473668).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei45ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei138Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi23 – 31ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Host-virus interaction, Inflammatory response, Necrosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.2, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q13546

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-140534, Caspase activation via Death Receptors in the presence of ligand
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
R-HSA-9679191, Potential therapeutics for SARS
R-HSA-9686347, Microbial modulation of RIPK1-mediated regulated necrosis
R-HSA-9693928, Defective RIPK1-mediated regulated necrosis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q13546

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13546

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Receptor-interacting serine/threonine-protein kinase 1 (EC:2.7.11.14 Publications)
Alternative name(s):
Cell death protein RIP1 Publication
Receptor-interacting protein 11 Publication
Short name:
RIP-11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RIPK1Imported
Synonyms:RIP1 Publication, RIP11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:10019, RIPK1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603453, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13546

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000137275.13

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Immunodeficiency 57 with autoinflammation (IMD57)1 Publication
The disease is caused by variants affecting the gene represented in this entry. RIPK1-deficient immune cells from IMD57 patients have impaired proinflammatory signaling leading to dysregulated cytokine secretion and are prone to necroptosis.1 Publication
Disease descriptionAn autosomal recessive primary immunodeficiency characterized by lymphopenia and recurrent viral, bacterial, and fungal infections. Patients exhibit early-onset inflammatory bowel disease involving the upper and lower gastrointestinal tract, and develop progressive polyarthritis.
Related information in OMIM
Autoinflammation with episodic fever and lymphadenopathy (AIEFL)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant immunologic disorder characterized by early onset of recurrent episodes of unexplained fever, lymphadenopathy, hepatosplenomegaly, and increased levels of inflammatory cytokines and chemokines in patient serum.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_083518324D → H in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response. 2 Publications1
Natural variantiVAR_083519324D → N in AIEFL; prevents cleavage by CASP8; changed inflammatory response. 1 Publication1
Natural variantiVAR_084135324D → V in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response. 1 Publication1
Natural variantiVAR_083520324D → Y in AIEFL; prevents cleavage by CASP8; changed inflammatory response. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi25S → D: Phophomimetic mutant. Significant loss of kinase activity. 1 Publication1
Mutagenesisi45K → A: Abolishes kinase activity. 2 Publications1
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
Mutagenesisi536S → C: Strongly reduced homodimerization and interaction with RIPK3. 1 Publication1
Mutagenesisi599K → R: Blocks homodimerization, necroptosis and apoptosis. 1 Publication1

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		8737

MalaCards human disease database

More...MalaCardsi		RIPK1
MIMi618108, phenotype
618852, phenotype

Open Targets

More...OpenTargetsi		ENSG00000137275

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34394

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13546, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5464

Drug and drug target database

More...DrugBanki		DB12010, Fostamatinib

DrugCentral

More...DrugCentrali		Q13546

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2189

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RIPK1

Domain mapping of disease mutations (DMDM)

More...DMDMi		60393639

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000866061 – 671Receptor-interacting serine/threonine-protein kinase 1Add BLAST671

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6Phosphoserine; by IKKA and IKKB1 Publication1
Modified residuei20Phosphoserine; by autocatalysisSequence analysis1
Modified residuei25Phosphoserine; by IKKA and IKKB2 Publications1
Modified residuei161Phosphoserine; by RIPK3 and autocatalysisSequence analysis1
Modified residuei166Phosphoserine; by autocatalysisSequence analysis2 Publications1
Modified residuei303Phosphoserine1 Publication1
Modified residuei320Phosphoserine; by MAP3K7Combined sources1 Publication1
Modified residuei331Phosphoserine; by MAP3K7By similarity1
Modified residuei333Phosphoserine; by MAP3K71 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei384PhosphotyrosineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically cleaved by CASP8 at Asp-324 (PubMed:10521396, PubMed:31827281, PubMed:31827280). Cleavage is crucial for limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827281, PubMed:31827280). Cleavage abolishes NF-kappa-B activation and enhances the interaction of TRADD with FADD (PubMed:10521396).By similarity3 Publications
RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:18408713, PubMed:19524513, PubMed:31827280). Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex (PubMed:18408713). Phosphorylation at Ser-25 represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (PubMed:30988283). Phosphorylated at Ser-320 by MAP3K7 which requires prior ubiquitination with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 (By similarity). This phosphorylation positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).By similarity4 Publications
Ubiquitinated with 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin (PubMed:15258597, PubMed:16603398, PubMed:18450452, PubMed:21455173, PubMed:21931591, PubMed:29883609, Ref. 33). Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex (PubMed:15258597). 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 NF-kappa-B signaling (PubMed:15258597). 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-alpha-induced NF-kappa-B signaling (PubMed:18450452, Ref. 33). Linear polyubiquitinated; the head-to-tail linear polyubiquitination ('Met-1'-linked) is mediated by the LUBAC complex and decreases protein kinase activity (PubMed:21455173). Deubiquitination of linear polyubiquitin by CYLD promotes the kinase activity (By similarity). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B (PubMed:21931591). Ubiquitinated with 'Lys-63'-linked chains by PELI1 (PubMed:29883609). Ubiquitination at Lys-377 with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 is essential for its phosphorylation at Ser-320 mediated by MAP3K7 (By similarity). This ubiquitination is required for NF-kB activation, suppresses RIPK1 kinase activity and plays a critical role in preventing cell death during embryonic development (By similarity).By similarity7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei324 – 325Cleavage; by CASP83 Publications2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1053
CPTAC-900
CPTAC-901
CPTAC-902

Encyclopedia of Proteome Dynamics

More...EPDi		Q13546

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13546

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13546

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13546

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13546

PeptideAtlas

More...PeptideAtlasi		Q13546

PRoteomics IDEntifications database

More...PRIDEi		Q13546

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59527 [Q13546-1]
59528 [Q13546-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13546

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q13546

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13546

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000137275, Expressed in sural nerve and 199 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13546, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13546, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000137275, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:29440439, PubMed:29681455).

Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex (PubMed:11734559, PubMed:29883609, PubMed:19524512, PubMed:10358032, PubMed:29681455). 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 (PubMed:22265414).

Interacts (via the death domain) with TNFRSF6 (via the death domain) and TRADD (via the death domain) (PubMed:8612133). Is recruited by TRADD to TNFRSF1A in a TNF-dependent process (PubMed:24130170). Binds RNF216, EGFR, IKBKG, TRAF1, TRAF2 and TRAF3 (PubMed:8612133, PubMed:9927690, PubMed:11854271, PubMed:11116146).

Interacts with BNLF1 (PubMed:10409763).

Interacts with SQSTM1 upon TNF-alpha stimulation (PubMed:10356400). May interact with MAVS/IPS1 (PubMed:16127453).

Interacts with ZFAND5 (PubMed:14754897).

Interacts with RBCK1 (PubMed:17449468).

Interacts with ZBP1 (By similarity).

Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (PubMed:21931591).

Interacts (via kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-alpha-dependent manner (PubMed:17389591).

Interacts with ARHGEF2 (PubMed:21887730).

Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination (PubMed:18450452).

Interacts with RNF34; involved in RIPK1 ubiquitination (Ref. 33).

Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436).

Interacts with PELI1 (PubMed:29883609).

Interacts (via death domain) with CRADD (via death domain); the interaction is direct (PubMed:9044836).

Component of complex IIa composed of at least RIPK1, FADD and CASP8 (By similarity).

Interacts with MAP3K7, CFLAR, CASP8, FADD and NEMO (By similarity).

By similarity24 Publications

(Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation.

1 Publication

(Microbial infection) Interacts with Murid herpesvirus 1 protein RIR1.

1 Publication

(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 1/HHV-1 protein RIR1/ICP6 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation.

1 Publication

(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 2/HHV-2 protein RIR1/ICP10 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114274, 132 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1907, Ripoptosome

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13546

Database of interacting proteins

More...DIPi		DIP-433N

Protein interaction database and analysis system

More...IntActi		Q13546, 76 interactors

Molecular INTeraction database

More...MINTi		Q13546

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000259808

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13546

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q13546, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q13546

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13546

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 289Protein kinasePROSITE-ProRule annotationAdd BLAST273
Domaini583 – 669DeathPROSITE-ProRule annotationAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni290 – 582Interaction with SQSTM11 PublicationAdd BLAST293

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi531 – 547RIP homotypic interaction motif (RHIM)2 PublicationsAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi411 – 414Poly-Arg4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The RIP homotypic interaction motif (RHIM) mediates interaction with the RHIM motif of RIPK1. Both motifs form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and featuring an unusual Cys-Ser ladder of alternating Ser (from RIPK1) and Cys (from RIPK3).1 Publication
The death domain mediates dimerization and activation of its kinase activity during necroptosis and apoptosis (PubMed:29440439). It engages other DD-containing proteins as well as a central (intermediate) region important for NF-kB activation and RHIM-dependent signaling (PubMed:10356400).2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0192, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159347

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_017229_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13546

Identification of Orthologs from Complete Genome Data

More...OMAi		NDFHIKI

Database of Orthologous Groups

More...OrthoDBi		346354at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13546

TreeFam database of animal gene trees

More...TreeFami		TF106506

Family and domain databases

Conserved Domains Database

More...CDDi		cd08777, Death_RIP1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View 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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00531, Death, 1 hit
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF12721, RHIM, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00109, TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00005, DEATH, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47986, SSF47986, 1 hit
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50017, DEATH_DOMAIN, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q13546-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAG65471 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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_083518324D → H in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response. 2 Publications1
Natural variantiVAR_083519324D → N in AIEFL; prevents cleavage by CASP8; changed inflammatory response. 1 Publication1
Natural variantiVAR_084135324D → V in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response. 1 Publication1
Natural variantiVAR_083520324D → Y in AIEFL; prevents cleavage by CASP8; changed inflammatory response. 1 Publication1
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
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_037690108 – 153Missing in isoform 2. 1 PublicationAdd BLAST46

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4482.1 [Q13546-1]

Protein sequence database of the Protein Information Resource

More...PIRi		T09479

NCBI Reference Sequences

More...RefSeqi		NP_003795.2, NM_003804.4 [Q13546-1]
XP_005249514.2, XM_005249457.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000259808; ENSP00000259808; ENSG00000137275 [Q13546-1]
ENST00000380409; ENSP00000369773; ENSG00000137275 [Q13546-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8737

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8737

UCSC genome browser

More...UCSCi		uc003mux.4, human [Q13546-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
5V7ZNMR-B/D/F/H532-549[»]
6AC5X-ray1.45A561-671[»]
6C3EX-ray2.60A/B2-294[»]
6C4DX-ray2.52A/B/C/D2-294[»]
6HHOX-ray3.49A/B1-294[»]
6NW2X-ray2.00A/B1-294[»]
6NYHX-ray2.10A/B1-294[»]
6OCQX-ray2.79A/B1-294[»]
6R5FX-ray3.25A/B/C/D1-294[»]
6RLNX-ray2.87A/B1-294[»]
BMRBiQ13546
SMRiQ13546
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114274, 132 interactors
ComplexPortaliCPX-1907, Ripoptosome
CORUMiQ13546
DIPiDIP-433N
IntActiQ13546, 76 interactors
MINTiQ13546
STRINGi9606.ENSP00000259808

Chemistry databases

BindingDBiQ13546
ChEMBLiCHEMBL5464
DrugBankiDB12010, Fostamatinib
DrugCentraliQ13546
GuidetoPHARMACOLOGYi2189

PTM databases

iPTMnetiQ13546
MetOSiteiQ13546
PhosphoSitePlusiQ13546

Genetic variation databases

BioMutaiRIPK1
DMDMi60393639

Proteomic databases

CPTACiCPTAC-1053
CPTAC-900
CPTAC-901
CPTAC-902
EPDiQ13546
jPOSTiQ13546
MassIVEiQ13546
MaxQBiQ13546
PaxDbiQ13546
PeptideAtlasiQ13546
PRIDEiQ13546
ProteomicsDBi59527 [Q13546-1]
59528 [Q13546-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4145, 600 antibodies

The DNASU plasmid repository

More...DNASUi		8737

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8737
DisGeNETi8737

GeneCards: human genes, protein and diseases

More...GeneCardsi		RIPK1
HGNCiHGNC:10019, RIPK1
HPAiENSG00000137275, Low tissue specificity
MalaCardsiRIPK1
MIMi603453, gene
618108, phenotype
618852, phenotype
neXtProtiNX_Q13546
OpenTargetsiENSG00000137275
PharmGKBiPA34394
VEuPathDBiHostDB:ENSG00000137275.13

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0192, Eukaryota
GeneTreeiENSGT00940000159347
HOGENOMiCLU_017229_0_0_1
InParanoidiQ13546
OMAiNDFHIKI
OrthoDBi346354at2759
PhylomeDBiQ13546
TreeFamiTF106506

Enzyme and pathway databases

BRENDAi2.7.10.2, 2681
PathwayCommonsiQ13546
ReactomeiR-HSA-140534, Caspase activation via Death Receptors in the presence of ligand
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
R-HSA-9679191, Potential therapeutics for SARS
R-HSA-9686347, Microbial modulation of RIPK1-mediated regulated necrosis
R-HSA-9693928, Defective RIPK1-mediated regulated necrosis
SignaLinkiQ13546
SIGNORiQ13546

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8737, 18 hits in 904 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RIPK1, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RIPK1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8737
PharosiQ13546, Tchem

Protein Ontology

More...PROi		PR:Q13546
RNActiQ13546, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000137275, Expressed in sural nerve and 199 other tissues
ExpressionAtlasiQ13546, baseline and differential
GenevisibleiQ13546, HS

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, PK_Tyr_Ser-Thr, 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRIPK1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13546
Secondary accession number(s): A0AV89
, B2RAG1, B4E3F9, Q13180, Q59H33
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 2005
Last modified: February 10, 2021
This is version 220 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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. SIMILARITY comments
    Index of protein domains and families
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again