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0KS6A5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRPS6KA5
DescriptionRibosomal protein s6 kinase alpha 5 (ec 2.7.1.37) (nuclear mitogen-and stress-activated protein kinase 1) (90 kda ribosomal protein s6 kinase 5) (rsk-like protein kinase) (rlsk).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (IEP)
0005524 ATP binding (IDA)
0005515 protein binding (IPI)
0004674 protein serine/threonine kinase activity (IDA)
0007173 epidermal growth factor receptor signaling ... (TAS)
0016572 histone phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0006355 regulation of transcription, DNA-dependent (IDA)
0042221 response to chemical substance (IEP)
0009605 response to external stimulus (IEP)
0006950 response to stress (IEP)

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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:
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 . CAUTION: Despite SMART having created two different HMMs for Serine/Threonine protein kinase and for Tyrosine protein kinase.arge number of proteins match both signatures.s SMART considers it to be natural for these two closely related families.
  IPR002290:Serine/threonine protein kinase
Protein kinases are responsible for the phosphorylation of proteins.otentially for regulating their activity. This domain is found in a large variety of protein kinases with different functions and dependencies. Protein kinase C.or example.s a calcium-activated.hospholipid-dependent serine- and threonine-specific enzyme. It is activated by diacylglycerol which.n turn.hosphorylates a range ofcellular proteins. This domain is most often found associated with .
  IPR000961:Protein kinase, C-terminal
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 () 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
IPR002290:S_TKc 
Evalue:-103.38721614328 
Location:49-318IPR002290:S_TKc 
Evalue:-96.1426675035687 
Location:426-687IPR000961:S_TK_X 
Evalue:-14.5528419686578 
Location:319-379
SequencesProtein: KS6A5_HUMAN (802 aa)
mRNA: NM_004755
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK04445
  Level 3 annotation:
    mitogen-,stress activated protein kinases
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 499 residues, 90406924-90408419Exon2: 56 residues, 90409728-90409892Exon3: 55 residues, 90411297-90411457Exon4: 66 residues, 90426583-90426775Exon5: 59 residues, 90430509-90430680Exon6: 33 residues, 90435425-90435519Exon7: 46 residues, 90436204-90436338Exon8: 44 residues, 90436707-90436833Exon9: 56 residues, 90438904-90439066Exon10: 52 residues, 90442245-90442396Exon11: 36 residues, 90456302-90456406Exon12: 30 residues, 90459209-90459293Exon13: 38 residues, 90479174-90479282Exon14: 40 residues, 90483531-90483647Exon15: 75 residues, 90514402-90514621Exon16: 26 residues, 90537184-90537256Exon17: 108 residues, 90596428-90596746Exon18: 2 residues, -Jump to KS6A5_HUMAN  
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Loci Cluster (Details)Loci: 2858 90650466-90761449 ~-111K 11612(C14orf159)(+)Loci: 4145 90406924-90596746 ~-190K 11609(RPS6KA5)(-)Link out to UCSC