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Q13546

- RIPK1_HUMAN

UniProt

Q13546 - RIPK1_HUMAN

Protein

Receptor-interacting serine/threonine-protein kinase 1

Gene

RIPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (01 Feb 2005)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW
    2. death domain binding Source: BHF-UCL
    3. death receptor binding Source: BHF-UCL
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB
    6. protein complex binding Source: UniProtKB
    7. protein kinase activity Source: UniProtKB
    8. protein serine/threonine kinase activity Source: UniProtKB
    9. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    2. activation of JUN kinase activity Source: BHF-UCL
    3. amyloid fibril formation Source: UniProtKB
    4. apoptotic process Source: UniProtKB
    5. apoptotic signaling pathway Source: Reactome
    6. cellular protein catabolic process Source: UniProtKB
    7. cellular response to tumor necrosis factor Source: UniProtKB
    8. extrinsic apoptotic signaling pathway Source: BHF-UCL
    9. innate immune response Source: Reactome
    10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    11. necroptotic process Source: UniProtKB
    12. necroptotic signaling pathway Source: BHF-UCL
    13. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    14. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    15. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    16. peptidyl-serine autophosphorylation Source: UniProtKB
    17. positive regulation of apoptotic process Source: UniProtKB
    18. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    19. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    20. positive regulation of interleukin-8 production Source: BHF-UCL
    21. positive regulation of JNK cascade Source: UniProtKB
    22. positive regulation of macrophage differentiation Source: UniProtKB
    23. positive regulation of necroptotic process Source: UniProtKB
    24. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    25. positive regulation of programmed cell death Source: UniProtKB
    26. positive regulation of protein phosphorylation Source: UniProtKB
    27. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    28. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    29. positive regulation of tumor necrosis factor production Source: BHF-UCL
    30. positive regulation of type I interferon production Source: Reactome
    31. protein autophosphorylation Source: BHF-UCL
    32. protein heterooligomerization Source: UniProtKB
    33. protein homooligomerization Source: UniProtKB
    34. regulation of ATP:ADP antiporter activity Source: BHF-UCL
    35. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
    36. response to tumor necrosis factor Source: BHF-UCL
    37. ripoptosome assembly Source: UniProtKB
    38. T cell apoptotic process Source: UniProtKB
    39. toll-like receptor 3 signaling pathway Source: Reactome
    40. toll-like receptor 4 signaling pathway Source: Reactome
    41. toll-like receptor signaling pathway Source: Reactome
    42. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    43. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL

    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. Caspase-8 activation.
    REACT_150361. TRIF-mediated programmed cell death.
    REACT_164011. Regulation by c-FLIP.
    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_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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10019. RIPK1.

    Subcellular locationi

    Cytoplasm. Cell membrane By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. death-inducing signaling complex Source: BHF-UCL
    3. membrane raft Source: Ensembl
    4. mitochondrion Source: BHF-UCL
    5. receptor complex Source: BHF-UCL
    6. ripoptosome Source: UniProtKB

    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.

    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 – 61Phosphoserine2 Publications
    Modified residuei20 – 201Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei25 – 251Phosphoserine2 Publications
    Modified residuei161 – 1611Phosphoserine; by RIPK3 and autocatalysisSequence Analysis
    Modified residuei166 – 1661Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei303 – 3031Phosphoserine2 Publications
    Modified residuei320 – 3201Phosphoserine3 Publications
    Modified residuei333 – 3331Phosphoserine2 Publications
    Cross-linki377 – 377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei384 – 3841Phosphotyrosine2 Publications

    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.4 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 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.5 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.
    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 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.By similarity18 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-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
    USP4Q131074EBI-358507,EBI-723290

    Protein-protein interaction databases

    BioGridi114274. 66 interactions.
    DIPiDIP-433N.
    IntActiQ13546. 32 interactions.
    MINTiMINT-128219.
    STRINGi9606.ENSP00000259808.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000010270.
    HOVERGENiHBG055612.
    InParanoidiQ13546.
    KOiK02861.
    OMAiSHDPFAQ.
    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. Align

    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

    MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG    50
    PNCIEHNEAL LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL 100
    MHVLKAEMST PLSVKGRIIL EIIEGMCYLH GKGVIHKDLK PENILVDNDF 150
    HIKIADLGLA SFKMWSKLNN EEHNELREVD GTAKKNGGTL YYMAPEHLND 200
    VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC IKSGNRPDVD 250
    DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED 300
    VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG 350
    MGPVEESWFA PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR 400
    QNVAYNREEE RRRRVSHDPF AQQRPYENFQ NTEGKGTAYS SAASHGNAVH 450
    QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD PGTAGPRVWY RPIPSHMPSL 500
    HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ IGAYNYMEIG 550
    GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN 600
    CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA 650
    QALHQCSRID LLSSLIYVSQ N 671
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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_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]

    Polymorphism databases

    DMDMi60393639.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4482.1. [Q13546-1 ]
    PIRi T09479.
    RefSeqi NP_003795.2. NM_003804.3. [Q13546-1 ]
    XP_005249515.1. XM_005249458.1. [Q13546-1 ]
    UniGenei Hs.519842.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4ITH X-ray 2.25 A/B 1-294 [» ]
    4ITI X-ray 2.86 A/B 1-294 [» ]
    4ITJ X-ray 1.80 A/B 1-294 [» ]
    4NEU X-ray 2.57 A/B 1-324 [» ]
    ProteinModelPortali Q13546.
    SMRi Q13546. Positions 7-327, 579-661.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114274. 66 interactions.
    DIPi DIP-433N.
    IntActi Q13546. 32 interactions.
    MINTi MINT-128219.
    STRINGi 9606.ENSP00000259808.

    Chemistry

    BindingDBi Q13546.
    ChEMBLi CHEMBL5464.
    GuidetoPHARMACOLOGYi 2189.

    PTM databases

    PhosphoSitei Q13546.

    Polymorphism databases

    DMDMi 60393639.

    Proteomic databases

    MaxQBi Q13546.
    PaxDbi Q13546.
    PRIDEi Q13546.

    Protocols and materials databases

    DNASUi 8737.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259808 ; ENSP00000259808 ; ENSG00000137275 . [Q13546-1 ]
    ENST00000380409 ; ENSP00000369773 ; ENSG00000137275 . [Q13546-1 ]
    GeneIDi 8737.
    KEGGi hsa:8737.
    UCSCi uc003muv.4. human. [Q13546-1 ]
    uc011dhs.2. human. [Q13546-2 ]

    Organism-specific databases

    CTDi 8737.
    GeneCardsi GC06P003064.
    HGNCi HGNC:10019. RIPK1.
    HPAi CAB010302.
    HPA015257.
    MIMi 603453. gene.
    neXtProti NX_Q13546.
    PharmGKBi PA34394.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000010270.
    HOVERGENi HBG055612.
    InParanoidi Q13546.
    KOi K02861.
    OMAi SHDPFAQ.
    OrthoDBi EOG7MPRDN.
    PhylomeDBi Q13546.
    TreeFami TF106506.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_1432. TNF signaling.
    REACT_1503. Caspase-8 activation.
    REACT_150361. TRIF-mediated programmed cell death.
    REACT_164011. Regulation by c-FLIP.
    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_832. Dimerization of procaspase-8.
    SignaLinki Q13546.

    Miscellaneous databases

    GeneWikii RIPK1.
    GenomeRNAii 8737.
    NextBioi 32775.
    PMAP-CutDB Q13546.
    PROi Q13546.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13546.
    CleanExi HS_RIPK1.
    Genevestigatori Q13546.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    InterProi IPR011029. 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 ]
    Pfami PF00531. Death. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF12721. RHIM. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00005. DEATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
    35. "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.
    36. "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.
    37. Cited for: INTERACTION WITH ARHGEF2.
    38. "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.
    39. "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: October 1, 2014
    This is version 158 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