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O43353

- RIPK2_HUMAN

UniProt

O43353 - RIPK2_HUMAN

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Protein
Receptor-interacting serine/threonine-protein kinase 2
Gene
RIPK2, CARDIAK, RICK, RIP2, UNQ277/PRO314/PRO34092
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471ATP
Active sitei146 – 1461Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 329ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. CARD domain binding Source: UniProtKB
  3. LIM domain binding Source: UniProtKB
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: BHF-UCL
  7. protein serine/threonine kinase activity Source: ProtInc
  8. signal transducer activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  2. JNK cascade Source: Reactome
  3. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  5. T cell proliferation Source: Ensembl
  6. T cell receptor signaling pathway Source: UniProtKB
  7. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  8. activation of MAPK activity Source: Reactome
  9. adaptive immune response Source: UniProtKB
  10. apoptotic process Source: ProtInc
  11. cellular response to lipoteichoic acid Source: Ensembl
  12. cellular response to muramyl dipeptide Source: UniProtKB
  13. cellular response to peptidoglycan Source: Ensembl
  14. defense response to Gram-positive bacterium Source: Ensembl
  15. inflammatory response Source: ProtInc
  16. innate immune response Source: UniProtKB
  17. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  18. negative regulation of apoptotic process Source: Reactome
  19. neurotrophin TRK receptor signaling pathway Source: Reactome
  20. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  21. nucleotide-binding oligomerization domain containing 1 signaling pathway Source: Ensembl
  22. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: UniProtKB
  23. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  24. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  25. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  26. positive regulation of JNK cascade Source: Ensembl
  27. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  28. positive regulation of T-helper 1 cell differentiation Source: Ensembl
  29. positive regulation of T-helper 1 type immune response Source: Ensembl
  30. positive regulation of alpha-beta T cell proliferation Source: Ensembl
  31. positive regulation of apoptotic process Source: Ensembl
  32. positive regulation of chemokine production Source: Ensembl
  33. positive regulation of cytokine-mediated signaling pathway Source: Ensembl
  34. positive regulation of immature T cell proliferation Source: Ensembl
  35. positive regulation of interferon-alpha production Source: BHF-UCL
  36. positive regulation of interferon-beta production Source: BHF-UCL
  37. positive regulation of interferon-gamma production Source: Ensembl
  38. positive regulation of interleukin-12 production Source: BHF-UCL
  39. positive regulation of interleukin-2 production Source: Ensembl
  40. positive regulation of interleukin-6 production Source: Ensembl
  41. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  42. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  43. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  44. positive regulation of protein ubiquitination Source: UniProtKB
  45. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  46. positive regulation of tumor necrosis factor production Source: Ensembl
  47. response to exogenous dsRNA Source: Ensembl
  48. response to interleukin-1 Source: Ensembl
  49. response to interleukin-12 Source: Ensembl
  50. response to interleukin-18 Source: Ensembl
  51. signal transduction Source: ProtInc
  52. stress-activated MAPK cascade Source: Reactome
  53. toll-like receptor 10 signaling pathway Source: Reactome
  54. toll-like receptor 2 signaling pathway Source: MGI
  55. toll-like receptor 3 signaling pathway Source: Reactome
  56. toll-like receptor 4 signaling pathway Source: Reactome
  57. toll-like receptor 5 signaling pathway Source: Reactome
  58. toll-like receptor 9 signaling pathway Source: Reactome
  59. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  60. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  61. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Apoptosis, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_12555. Downstream TCR signaling.
REACT_13415. p75NTR recruits signalling complexes.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiO43353.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-interacting serine/threonine-protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
CARD-containing interleukin-1 beta-converting enzyme-associated kinase
Short name:
CARD-containing IL-1 beta ICE-kinase
RIP-like-interacting CLARP kinase
Receptor-interacting protein 2
Short name:
RIP-2
Tyrosine-protein kinase RIPK2 (EC:2.7.10.2)
Gene namesi
Name:RIPK2
Synonyms:CARDIAK, RICK, RIP2
ORF Names:UNQ277/PRO314/PRO34092
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:10020. RIPK2.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: Reactome
  4. protein complex Source: UniProtKB
  5. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471K → A: Abolishes kinase activity. 2 Publications
Mutagenesisi47 – 471K → M: Reduces FAS-mediated apoptosis. 2 Publications
Mutagenesisi146 – 1461D → N: Abolishes kinase activity. 1 Publication
Mutagenesisi209 – 2091K → R: Complete loss of polyubiquitination. 1 Publication
Mutagenesisi381 – 3811Y → A: Prevents phosphorylation. Reduces serine and threonine phosphorylation of ARHGEF2.
Mutagenesisi444 – 4441R → E: Abolishes interaction with NOD1. 1 Publication
Mutagenesisi474 – 4741Y → F: Decreases interaction with NOD2. 1 Publication
Mutagenesisi483 – 4831R → E: Abolishes interaction with NOD1. 1 Publication
Mutagenesisi488 – 4881R → E: Abolishes interaction with NOD1. 1 Publication

Organism-specific databases

PharmGKBiPA34395.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Receptor-interacting serine/threonine-protein kinase 2
PRO_0000086608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine; by autocatalysis1 Publication
Cross-linki209 – 209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei363 – 3631Phosphoserine2 Publications
Modified residuei381 – 3811Phosphotyrosine; by CSK1 Publication
Modified residuei393 – 3931Phosphoserine1 Publication
Modified residuei474 – 4741Phosphotyrosine; by autocatalysis1 Publication
Modified residuei527 – 5271Phosphoserine2 Publications
Modified residuei529 – 5291Phosphoserine1 Publication
Modified residuei531 – 5311Phosphoserine1 Publication
Modified residuei539 – 5391Phosphoserine2 Publications

Post-translational modificationi

Autophosphorylated. Autophosphorylation at Tyr-474 is necessary for effective NOD2 signaling. Phosphorylated. Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation.3 Publications
Ubiquitinated on Lys-209; undergoes 'Lys-63'-linked polyubiquitination catalyzed by ITCH. Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Also undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation. Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent proinflammatory signaling activation of NF-kappa-B.5 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43353.
PaxDbiO43353.
PRIDEiO43353.

PTM databases

PhosphoSiteiO43353.

Expressioni

Tissue specificityi

Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node.

Gene expression databases

ArrayExpressiO43353.
BgeeiO43353.
CleanExiHS_RIPK2.
GenevestigatoriO43353.

Organism-specific databases

HPAiHPA015273.
HPA016499.

Interactioni

Subunit structurei

Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2. Interacts with ARHGEF2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK. Binds to CFLAR/CLARP and CASP1 via their CARD domains. Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6. May be a component of both the TNFRSF1A and TNRFSF5/CD40 receptor complex. Interacts with NOD1. Interacts (via CARD domain) with NOD2 (via CARD domain). Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway. Interacts with IKBKG/NEMO. The polyubiquitinated protein interacts with MAP3K7/TAK1. Interacts with XIAP/BIRC4. Interacts with NLRP10. Interacts with CARD9.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC2Q134903EBI-358522,EBI-514538
BIRC3Q134893EBI-358522,EBI-517709
MAVSQ7Z4343EBI-358522,EBI-995373
TRAF3Q131145EBI-358522,EBI-357631

Protein-protein interaction databases

BioGridi114300. 39 interactions.
DIPiDIP-27518N.
IntActiO43353. 11 interactions.
MINTiMINT-90752.
STRINGi9606.ENSP00000220751.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 173
Beta strandi18 – 269
Beta strandi28 – 3710
Turni38 – 403
Beta strandi43 – 497
Helixi56 – 7217
Beta strandi81 – 877
Beta strandi90 – 967
Helixi103 – 1086
Turni110 – 1123
Helixi118 – 13619
Beta strandi138 – 1403
Helixi149 – 1513
Beta strandi152 – 1543
Beta strandi160 – 1623
Helixi190 – 1923
Helixi195 – 1973
Helixi210 – 22415
Turni228 – 2314
Helixi235 – 2439
Turni252 – 2543
Helixi262 – 27211
Helixi277 – 2793
Helixi283 – 29513
Helixi300 – 31314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C8BX-ray2.75A/B8-317[»]
ProteinModelPortaliO43353.
SMRiO43353. Positions 9-316.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 294277Protein kinase
Add
BLAST
Domaini432 – 52493CARD
Add
BLAST

Domaini

Contains an N-terminal kinase domain and a C-terminal caspase activation and recruitment domain (CARD) that mediates the recruitment of CARD-containing proteins.

Sequence similaritiesi

Contains 1 CARD domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000136856.
HOVERGENiHBG054242.
InParanoidiO43353.
KOiK08846.
OMAiYPDVAWP.
OrthoDBiEOG78H3SS.
PhylomeDBiO43353.
TreeFamiTF106506.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017322. Rcpt-int_Ser/Thr_kinase-2.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037921. STPK_RIP2. 1 hit.
SMARTiSM00114. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50209. CARD. 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: O43353-1) [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

MNGEAICSAL PTIPYHKLAD LRYLSRGASG TVSSARHADW RVQVAVKHLH    50
IHTPLLDSER KDVLREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN 100
GSLNELLHRK TEYPDVAWPL RFRILHEIAL GVNYLHNMTP PLLHHDLKTQ 150
NILLDNEFHV KIADFGLSKW RMMSLSQSRS SKSAPEGGTI IYMPPENYEP 200
GQKSRASIKH DIYSYAVITW EVLSRKQPFE DVTNPLQIMY SVSQGHRPVI 250
NEESLPYDIP HRARMISLIE SGWAQNPDER PSFLKCLIEL EPVLRTFEEI 300
TFLEAVIQLK KTKLQSVSSA IHLCDKKKME LSLNIPVNHG PQEESCGSSQ 350
LHENSGSPET SRSLPAPQDN DFLSRKAQDC YFMKLHHCPG NHSWDSTISG 400
SQRAAFCDHK TTPCSSAIIN PLSTAGNSER LQPGIAQQWI QSKREDIVNQ 450
MTEACLNQSL DALLSRDLIM KEDYELVSTK PTRTSKVRQL LDTTDIQGEE 500
FAKVIVQKLK DNKQMGLQPY PEILVVSRSP SLNLLQNKSM 540
Length:540
Mass (Da):61,195
Last modified:November 1, 1998 - v2
Checksum:i575A692239505792
GO
Isoform 2 (identifier: O43353-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.

Show »
Length:403
Mass (Da):45,582
Checksum:i9F0DE53A01B25EF5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591I → T.1 Publication
Corresponds to variant rs2230801 [ dbSNP | Ensembl ].
VAR_041045
Natural varianti268 – 2681L → V.1 Publication
Corresponds to variant rs35004667 [ dbSNP | Ensembl ].
VAR_041046
Natural varianti313 – 3131K → N.1 Publication
Corresponds to variant rs35395048 [ dbSNP | Ensembl ].
VAR_041047

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 137137Missing in isoform 2.
VSP_013266Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711S → G in BAH13484. 1 Publication
Sequence conflicti514 – 5141Q → R in BAH13484. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF027706 mRNA. Translation: AAC34970.1.
AF078530 mRNA. Translation: AAC27722.1.
AF064824 mRNA. Translation: AAC25668.1.
AY358813 mRNA. Translation: AAQ89172.1.
AY358814 mRNA. Translation: AAQ89173.1.
AK301448 mRNA. Translation: BAH13484.1.
AC004003 Genomic DNA. Translation: AAC24561.1.
AF117829 Genomic DNA. No translation available.
BC004553 mRNA. Translation: AAH04553.1.
CCDSiCCDS6247.1. [O43353-1]
RefSeqiNP_003812.1. NM_003821.5. [O43353-1]
XP_005251149.1. XM_005251092.2. [O43353-2]
UniGeneiHs.103755.

Genome annotation databases

EnsembliENST00000220751; ENSP00000220751; ENSG00000104312. [O43353-1]
ENST00000540020; ENSP00000441623; ENSG00000104312. [O43353-2]
GeneIDi8767.
KEGGihsa:8767.
UCSCiuc003yee.3. human. [O43353-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF027706 mRNA. Translation: AAC34970.1 .
AF078530 mRNA. Translation: AAC27722.1 .
AF064824 mRNA. Translation: AAC25668.1 .
AY358813 mRNA. Translation: AAQ89172.1 .
AY358814 mRNA. Translation: AAQ89173.1 .
AK301448 mRNA. Translation: BAH13484.1 .
AC004003 Genomic DNA. Translation: AAC24561.1 .
AF117829 Genomic DNA. No translation available.
BC004553 mRNA. Translation: AAH04553.1 .
CCDSi CCDS6247.1. [O43353-1 ]
RefSeqi NP_003812.1. NM_003821.5. [O43353-1 ]
XP_005251149.1. XM_005251092.2. [O43353-2 ]
UniGenei Hs.103755.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4C8B X-ray 2.75 A/B 8-317 [» ]
ProteinModelPortali O43353.
SMRi O43353. Positions 9-316.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114300. 39 interactions.
DIPi DIP-27518N.
IntActi O43353. 11 interactions.
MINTi MINT-90752.
STRINGi 9606.ENSP00000220751.

Chemistry

BindingDBi O43353.
ChEMBLi CHEMBL5014.
GuidetoPHARMACOLOGYi 2190.

PTM databases

PhosphoSitei O43353.

Proteomic databases

MaxQBi O43353.
PaxDbi O43353.
PRIDEi O43353.

Protocols and materials databases

DNASUi 8767.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220751 ; ENSP00000220751 ; ENSG00000104312 . [O43353-1 ]
ENST00000540020 ; ENSP00000441623 ; ENSG00000104312 . [O43353-2 ]
GeneIDi 8767.
KEGGi hsa:8767.
UCSCi uc003yee.3. human. [O43353-1 ]

Organism-specific databases

CTDi 8767.
GeneCardsi GC08P090769.
HGNCi HGNC:10020. RIPK2.
HPAi HPA015273.
HPA016499.
MIMi 603455. gene.
neXtProti NX_O43353.
PharmGKBi PA34395.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000136856.
HOVERGENi HBG054242.
InParanoidi O43353.
KOi K08846.
OMAi YPDVAWP.
OrthoDBi EOG78H3SS.
PhylomeDBi O43353.
TreeFami TF106506.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_12555. Downstream TCR signaling.
REACT_13415. p75NTR recruits signalling complexes.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki O43353.

Miscellaneous databases

GeneWikii RIPK2.
GenomeRNAii 8767.
NextBioi 32880.
PROi O43353.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43353.
Bgeei O43353.
CleanExi HS_RIPK2.
Genevestigatori O43353.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017322. Rcpt-int_Ser/Thr_kinase-2.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00619. CARD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF037921. STPK_RIP2. 1 hit.
SMARTi SM00114. CARD. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50209. CARD. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis."
    Inohara N., del Peso L., Koseki T., Chen S., Nunez G.
    J. Biol. Chem. 273:12296-12300(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-47.
  2. "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."
    McCarthy J.V., Ni J., Dixit V.M.
    J. Biol. Chem. 273:16968-16975(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-47.
    Tissue: Endothelial cell.
  3. "Identification of CARDIAK, a RIP-like kinase that associates with caspase-1."
    Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L., Mattmann C., Tschopp J.
    Curr. Biol. 8:885-888(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-146.
    Tissue: Pancreatic adenocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  5. "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 2).
    Tissue: Synovium.
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Skin.
  8. "Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-kappaB activation."
    Ruefli-Brasse A.A., Lee W.P., Hurst S., Dixit V.M.
    J. Biol. Chem. 279:1570-1574(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Identification of a regulatory autophosphorylation site in the serine-threonine kinase RIP2."
    Dorsch M., Wang A., Cheng H., Lu C., Bielecki A., Charron K., Clauser K., Ren H., Polakiewicz R.D., Parsons T., Li P., Ocain T., Xu Y.
    Cell. Signal. 18:2223-2229(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-176.
  10. "Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK."
    Manon F., Favier A., Nunez G., Simorre J.P., Cusack S.
    J. Mol. Biol. 365:160-174(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOD1, MUTAGENESIS OF ARG-444; ARG-483 AND ARG-488.
  11. "MEKK4 sequesters RIP2 to dictate NOD2 signal specificity."
    Clark N.M., Marinis J.M., Cobb B.A., Abbott D.W.
    Curr. Biol. 18:1402-1408(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K4.
  12. "A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation."
    Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G., Inohara N.
    EMBO J. 27:373-383(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKG/NEMO AND MAP3K7/TAK1, FUNCTION, UBIQUITINATION AT LYS-209, MUTAGENESIS OF LYS-209.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363; SER-527 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways."
    Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E., Abbott D.W.
    Curr. Biol. 19:1255-1263(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY ITCH, INTERACTION WITH NOD2.
  16. "Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2."
    Bertrand M.J., Doiron K., Labbe K., Korneluk R.G., Barker P.A., Saleh M.
    Immunity 30:789-801(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY BIRC2 AND BIRC3.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-363; SER-393; SER-527 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Inhibition of RIP2's tyrosine kinase activity limits NOD2-driven cytokine responses."
    Tigno-Aranjuez J.T., Asara J.M., Abbott D.W.
    Genes Dev. 24:2666-2677(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-474, MUTAGENESIS OF TYR-474.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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.
  22. Cited for: INTERACTION WITH NLRP10.
  23. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ARHGEF2 AND NOD2, INTERACTION WITH ARHGEF2 AND NOD2, PHOSPHORYLATION AT TYR-381.
  24. Cited for: UBIQUITINATION, DEUBIQUITINATION.
  25. "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] THR-259; VAL-268 AND ASN-313.

Entry informationi

Entry nameiRIPK2_HUMAN
AccessioniPrimary (citable) accession number: O43353
Secondary accession number(s): B7Z748, Q6UWF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 158 of the entry and version 2 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 8
    Human chromosome 8: 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

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