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Reviewed, UniProtKB/Swiss-Prot Q13546 (RIPK1_HUMAN)

Last modified February 9, 2010. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Receptor-interacting serine/threonine-protein kinase 1
    EC=2.7.11.1
Alternative name(s):
    Serine/threonine-protein kinase RIP
    Cell death protein RIP
    Receptor-interacting protein 1
      Short name=RIP-1
Gene names
Name: RIPK1
Synonyms: RIP, RIP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the transduction of TNF signaling. TNF stimulation induces binding of RIPK1-TRADD-TRAF2-TRAF5 complex to TNFR1. TRAF proteins then catalyze the 'Lys-63'-linked polyubiquitination of RIPK1, inducing RIPK1 association with the IKK complex, which is subsequently activated, leading ultimately to the activation of NF-kappa-B. The inflammatory response is kept transient by the action of the NF-kappa-B target gene product TNFAIP3. TNFAIP3 is recruited to RIPK1 within a complex comprising also RNF11, ITCH and TAX1BP1. TNFAIP3 deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteosomal degradation and consequently to the termination of the TNF- or LPS-mediated activation of NF-kappa-B.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Binds to the death domain of TNFRSF6 and TRADD. Is recruited by TRADD to TNFRSF1A in a TNF-dependent process. Binds RIPK3, UBCE7IP1 isoform 3 (ZIN), EGFR, IKBKG, TRAF1, TRAF2 and TRAF3. Interacts with BNLF1. Interacts with SQSTM1 upon TNF-alpha stimulation. May interacts with MAVS/IPS1. Interacts with ZFAND5. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19

Subcellular location

Cytoplasm.

Post-translational modification

Proteolytically cleaved by caspase-8 during TNF-induced apoptosis. Cleavage abolishes NF-kappa-B activation and enhances pro-apototic signaling through the TRADD-FADD interaction. Ref.9

Autophosphorylated on serine and threonine residues. Ref.1 Ref.16 Ref.20

Undergoes 'Lys-63'-polyubiquitination catalyzed by TRAF2 after TNF stimulation. Down-regulated by 'Lys-63'-deubiquitination and 'Lys-48'-ubiquitination, both reactions being catalyzed by TNFAIP3. 'Lys-48'-ubiquitination leads to proteasomal degradation.

Sequence similarities

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

Contains 1 death domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processI-kappaB kinase/NF-kappaB cascade

Inferred from Experiment. Source: Reactome

activation of JUN kinase activity

Traceable author statement. Source: UniProtKB

activation of pro-apoptotic gene products

Inferred from Experiment. Source: Reactome

induction of apoptosis Ref.1 Ref.9

Inferred from mutant phenotype. Source: UniProtKB

induction of necroptosis by extracellular signals

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from expression pattern. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity Ref.1 Ref.9

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of anti-apoptosis

Traceable author statement. Source: UniProtKB

protein amino acid autophosphorylation Ref.1

Inferred from direct assay. Source: UniProtKB

regulation of oxygen and reactive oxygen species metabolic process

Traceable author statement. Source: UniProtKB

response to tumor necrosis factor Ref.9

Inferred from mutant phenotype. Source: UniProtKB

tumor necrosis factor-mediated signaling pathway Ref.1

Inferred by curator. Source: UniProtKB

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

death-inducing signaling complex

Inferred from direct assay. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: UniProtKB

receptor complex Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

death domain binding Ref.1

Inferred from physical interaction. Source: UniProtKB

death receptor binding Ref.8

Inferred from physical interaction. Source: UniProtKB

protein serine/threonine kinase activity Ref.1

Inferred from direct assay. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13546-1)

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.
Isoform 2 (identifier: Q13546-2)

The sequence of this isoform differs from the canonical sequence as follows:
     108-153: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 671671Receptor-interacting serine/threonine-protein kinase 1
PRO_0000086606

Regions

Domain17 – 289273Protein kinase
Domain583 – 66987Death
Nucleotide binding23 – 319ATP By similarity
Region290 – 582293Interaction with SQSTM1
Compositional bias411 – 4144Poly-Arg

Sites

Active site1381Proton acceptor By similarity
Binding site491ATP By similarity
Site324 – 3252Cleavage; by caspase-8

Amino acid modifications

Modified residue3201Phosphoserine Ref.20
Modified residue3841Phosphotyrosine Ref.16
Modified residue3871Phosphotyrosine Ref.16
Modified residue3891Phosphoserine Ref.16

Natural variations

Alternative sequence108 – 15346Missing in isoform 2.
VSP_037690
Natural variant641A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.21
VAR_041039
Natural variant811V → I in a colorectal adenocarcinoma sample; somatic mutation. Ref.21
VAR_041040
Natural variant2201A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.21
VAR_041041
Natural variant2341E → K: dbSNP rs17548383. Ref.4
VAR_021109
Natural variant4041A → S: dbSNP rs34872409. Ref.21
VAR_041042
Natural variant4381A → V: dbSNP rs3173519. Ref.1 Ref.6 Ref.8
VAR_058285
Natural variant4431A → V: dbSNP rs35722193. Ref.21
VAR_041043
Natural variant5691A → V: dbSNP rs55861377. Ref.21
VAR_041044

Experimental info

Mutagenesis451K → A: Abolishes kinase activity. Ref.1
Mutagenesis3241D → K: Abolishes cleavage by caspase-8. Ref.9
Sequence conflict2581R → I in BAG36858. Ref.3
Sequence conflict2861R → S in BAG36858. Ref.3
Sequence conflict5141T → S in AAC50137. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 2005. Version 3.
Checksum: 976E2428D525A9B2

FASTA67175,931
        10         20         30         40         50         60 
MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG PNCIEHNEAL 

        70         80         90        100        110        120 
LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL MHVLKAEMST PLSVKGRIIL 

       130        140        150        160        170        180 
EIIEGMCYLH GKGVIHKDLK PENILVDNDF HIKIADLGLA SFKMWSKLNN EEHNELREVD 

       190        200        210        220        230        240 
GTAKKNGGTL YYMAPEHLND VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC 

       250        260        270        280        290        300 
IKSGNRPDVD DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED 

       310        320        330        340        350        360 
VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG MGPVEESWFA 

       370        380        390        400        410        420 
PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR QNVAYNREEE RRRRVSHDPF 

       430        440        450        460        470        480 
AQQRPYENFQ NTEGKGTAYS SAASHGNAVH QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD 

       490        500        510        520        530        540 
PGTAGPRVWY RPIPSHMPSL HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ 

       550        560        570        580        590        600 
IGAYNYMEIG GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN 

       610        620        630        640        650        660 
CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA QALHQCSRID 

       670 
LLSSLIYVSQ N 

« Hide

Isoform 2.

Checksum: 4D3780FB4A93FDB1
Show »

FASTA62570,733

References

« Hide 'large scale' references
[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: 8612133] [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. expand/collapse author list , 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: 14702039] [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. expand/collapse author list , 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: 14574404] [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: 15489334] [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: 7538908] [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: 10521396] [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: 10356400] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND TRAF2, DOMAIN.
[11]"RIP3, a novel apoptosis-inducing kinase."
Sun X., Lee J., Navas T., Baldwin D.T., Stewart T.A., Dixit V.M.
J. Biol. Chem. 274:16871-16875(1999) [PubMed: 10358032] [Abstract]
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: 10409763] [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: 9927690] [Abstract]
Cited for: INTERACTION WITH IKBKG.
[14]"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: 11116146] [Abstract]
Cited for: INTERACTION WITH EGFR.
[15]"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: 11854271] [Abstract]
Cited for: INTERACTION WITH UBCE7IP1.
[16]"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: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-384; TYR-387 AND SER-389, MASS SPECTROMETRY.
Tissue: T-cell.
[17]"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: 14754897] [Abstract]
Cited for: INTERACTION WITH ZFAND5.
[18]"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: 15258597] [Abstract]
Cited for: UBIQUITINATION BY TRAF2, DEUBIQUITINATION BY TNFAIP3.
[19]"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: 16127453] [Abstract]
Cited for: INTERACTION WITH MAVS.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY.
[21]"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. expand/collapse author list , 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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-64; ILE-81; VAL-220; SER-404; VAL-443 AND VAL-569.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00013773.
IPI00939198.
PIRT09479.
RefSeqNP_003795.2.
UniGeneHs.519842

3D structure databases

SMRQ13546. Positions 13-291, 578-666.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-433N.
IntActQ13546. 29 interactions.
STRINGQ13546.

PTM databases

PhosphoSiteQ13546.

Proteomic databases

PRIDEQ13546.

Genome annotation databases

EnsemblENST00000259808; ENSP00000259808; ENSG00000137275; Homo sapiens. [Genome view]
ENST00000380409; ENSP00000369773; ENSG00000137275; Homo sapiens. [Genome view]
GeneID8737.
KEGGhsa:8737.
UCSCuc003mux.1. human.

Organism-specific databases

CTD8737.
GeneCardsGC06P003022.
H-InvDBHIX0005535.
HGNCHGNC:10019. RIPK1.
HPACAB010302.
HPA015257.
MIM603453. gene.
PharmGKBPA34394.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05953.
HOGENOMHBG445889.
HOVERGENQ13546.
InParanoidQ13546.
OMASHDPFAQ.
OrthoDBEOG9VDSJ8.
PhylomeDBQ13546.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
2.7.11.1. 247.
Pathway_Interaction_DBcaspase_pathway. Caspase cascade in apoptosis.
ceramidepathway. Ceramide signaling pathway.
faspathway. FAS signaling pathway (CD95).
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.
ReactomeREACT_578. Apoptosis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressQ13546.
BgeeQ13546.
CleanExHS_RIPK1.
GenevestigatorQ13546.

Family and domain databases

InterProIPR000488. Death.
IPR011029. DEATH-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
[Graphical view]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
PfamPF00531. Death. 1 hit.
[Graphical view]
SMARTSM00005. DEATH. 1 hit.
[Graphical view]
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32775.
PMAP-CutDBQ13546.
SOURCESearch...

Entry information

Entry nameRIPK1_HUMAN
AccessionPrimary (citable) accession number: Q13546
Secondary accession number(s): A0AV89 expand/collapse secondary AC list , B2RAG1, B4E3F9, Q13180, Q59H33
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 2005
Last modified: February 9, 2010
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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