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0RIPK1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionReceptor-interacting serine/threonine-protein kinase 2 (ec (serine/threonine-protein kinase rip) (cell death protein rip) (receptor interacting protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0004674 protein serine/threonine kinase activity (TAS)
0004871 signal transducer activity (IEP)
0006915 apoptosis (TAS)
0043123 positive regulation of I-kappaB kinase/NF-k... (IEP)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD is related in sequence and structure to the death effector domain ( ) and the caspase recruitment domain ( ).hich work in similar pathways and show similar interaction properties . DD bind each other forming oligomers. Mammals have numerous and diverse DD-containing proteins . Within these proteins.he DD domains can be found in combination with other domains.ncluding: CARDs.EDs.nkyrin repeats ().aspase-like folds.inase domains.eucine zippers ().eucine-rich repeats (LRR) ().IR domains ().nd ZU5 domains () .Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB.hich typically involves interactions with TNF (tumour necrosis factor) cytokine receptors . In humans.ight of the over 30 known TNF receptors contain DD in their cytoplasmic tails; several of these TNF receptors use caspase activation as a signalling mechanism. The DD mediates self-association of these receptors.hus giving the signal to downstream events that lead to apoptosis. Other DD-containing proteins.uch as ankyrin.yD88 and probably not directly involved in cell death signalling. DD-containing proteins also have links to innate immunity.ommunicating with Toll family receptors through bipartite adapter proteins such as MyD88 .
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide also family members.
  IPR001245:Tyrosine protein kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
The death domain (DD) is a conserved region of about 80 residues found on death receptors.nd which is required for death signalling.s well as a variety of non-apoptotic functions . Proteins containing this domain include the low affinity neurotrophin receptor (Fas-associated death domain protein).NF-1 (tumour necrosis factor receptor-1).elle protein kinase.nd the Tube adaptor protein .The induction of apoptosis also relies on the presence of a second domain.alled the death effector domain. The death effector domain (DED) occurs in proteins that regulate programmed cell death.ncluding both pro- and anti-apoptotic proteins; many of these proteins are also involved in controlling cellular activation and proliferation pathways . Proteins containing this domain include FADD (DED N-terminal.D C-terminal).EA-15 (phosphoproteins enriched in astrocytes 15kDa).aspases and FLIP.The induction of apoptosis results in the activation of caspases. family of aspartyl-specific cysteine proteases that are the main executioners of apoptosis. For example.he DED of FADD recruits two DED-containing caspases.aspase-8 and caspase-10.o form the death-inducing signal complex.hich initiates apoptosis. Proteins containing the caspase recruitment domain (CARD) are involved in the recruitment and activation of caspases during apoptosis . Other CARD proteins participate in NF-kappaB signalling pathways associated with innate or adaptive immune responses. Proteins containing CARD include Raidd.PAF-1 (apoptotic protease activating factor 1).rocaspase 9 and iceberg (inhibitor of interleukin-1-beta generation).The DD shows strong structural similarity to both DED and CARD. They all display a 6-helical closed bundle fold.ith greek key topology and an internal psuedo two-fold symmetry. However.espite their overall similarity in topology.ach domain forms specialised interactions.ypically only with members of its own subfamily.or example DED with DED.Please be aware that some of the proteins hit by the SSF signature may be false positives.
SequencesProtein: RIPK1_HUMAN (671 aa)
mRNA: NM_003804
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
KO assignmentK02861
  Level 3 annotation:
    receptor (TNFRSF)-interacting serine-threonine kinase 1
  Level 2 annotation:
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 55 residues, 3022056-3022220Exon2: 54 residues, 3023011-3023168Exon3: 48 residues, 3026211-3026349Exon4: 78 residues, 3028317-3028546Exon5: 52 residues, 3030491-3030641Exon6: 27 residues, 3034813-3034890Exon7: 32 residues, 3049457-3049548Exon8: 192 residues, 3050714-3051284Exon9: 53 residues, 3056035-3056188Exon10: 713 residues, 3058285-3060418Exon11: 2 residues, -Jump to RIPK1_HUMAN  
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