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0M4K4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAP4K4
DescriptionMitogen-activated protein kinase kinase kinase kinase 4 (ec 2.7.1.37) (mapk/erk kinase kinase kinase 4) (mek kinase kinase 4) (mekkk 4) (hpk/gck-like kinase hgk) (nck interacting kinase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005524 ATP binding (IDA)
0004674 protein serine/threonine kinase activity (IDA)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0006950 response to stress (IDA)

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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:
Based on sequence similarities a domain of homology has been identified in the following proteins :Citron and Citron kinase. These two proteins interact with the GTP-bound forms of the small GTPases Rho and Rac but not with Cdc42.Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCKalpha). This serine/threonine kinase interacts with the GTP-bound form of the small GTPase Cdc42 and to a lesser extent with that of Rac.NCK Interacting Kinase (NIK). serine/threonine protein kinase.ROM-1 and ROM-2.rom yeast. These proteins are GDP/GTP exchange proteins (GEPs) for the small GTP binding protein Rho1.This domain.alled the citron homology domain.s often found after cysteine rich and pleckstrin homology (PH) domains at the C-terminal end of the proteins . It acts as a regulatory domain and could be involved in macromolecular interactions .
  IPR001180:Citron-like
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
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
IPR001180:CNH 
Evalue:-126.376750709602 
Location:921-1219IPR002290:S_TKc 
Evalue:-94.1549019599857 
Location:25-289
SequencesProtein: M4K4_HUMAN (1239 aa)
mRNA: AY212247 NM_145686
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK04407
  Level 3 annotation:
    mitogen-activated protein kinase kinase kinase kinase 4
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 38 residues, 101680919-101681031Exon2: 24 residues, 101681366-101681432Exon3: 21 residues, 101773613-101773670Exon4: 44 residues, 101806821-101806947Exon5: 39 residues, 101808212-101808323Exon6: 32 residues, 101812397-101812488Exon7: 45 residues, 101814614-101814745Exon8: 20 residues, 101817302-101817357Exon9: 28 residues, 101818793-101818872Exon10: 60 residues, 101822712-101822888Exon11: 26 residues, 101825502-101825575Exon12: 72 residues, 101826994-101827205Exon13: 56 residues, 101838870-101839032Exon14: 31 residues, 101841889-101841976Exon15: 76 residues, 101842536-101842758Exon16: 56 residues, 101843718-101843880Exon17: 79 residues, 101846714-101846945Exon18: 37 residues, 101847823-101847930Exon19: 52 residues, 101849321-101849473Exon20: 34 residues, 101850105-101850203Exon21: 5 residues, 101850922-101850931Exon22: 60 residues, 101852515-101852691Exon23: 42 residues, 101853188-101853309Exon24: 41 residues, 101856540-101856658Exon25: 59 residues, 101856975-101857146Exon26: 50 residues, 101859896-101860040Exon27: 47 residues, 101865444-101865579Exon28: 35 residues, 101868080-101868181Exon29: 52 residues, 101869981-101870131Exon30: 55 residues, 101870671-101870831Exon31: 48 residues, 101871689-101871829Exon32: 1176 residues, 101874059-101877583Exon33: 2 residues, -Jump to M4K4_HUMANExon1: 20 residues, 101680974-101681031Exon2: 24 residues, 101681366-101681432Exon3: 21 residues, 101773613-101773670Exon4: 44 residues, 101806821-101806947Exon5: 39 residues, 101808212-101808323Exon6: 32 residues, 101812397-101812488Exon7: 45 residues, 101814614-101814745Exon8: 20 residues, 101817302-101817357Exon9: 28 residues, 101818793-101818872Exon10: 60 residues, 101822712-101822888Exon11: 26 residues, 101825502-101825575Exon12: 72 residues, 101826994-101827205Exon13: 56 residues, 101838870-101839032Exon14: 31 residues, 101841889-101841976Exon15: 76 residues, 101842536-101842758Exon16: 56 residues, 101843718-101843880Exon17: 37 residues, 101847823-101847930Exon18: 51 residues, 101849324-101849473Exon19: 34 residues, 101850105-101850203Exon20: 60 residues, 101852515-101852691Exon21: 42 residues, 101853188-101853309Exon22: 41 residues, 101856540-101856658Exon23: 59 residues, 101856975-101857146Exon24: 50 residues, 101859896-101860040Exon25: 47 residues, 101865444-101865579Exon26: 35 residues, 101868080-101868181Exon27: 52 residues, 101869981-101870131Exon28: 55 residues, 101870671-101870831Exon29: 48 residues, 101871689-101871829Exon30: 54 residues, 101874059-101874215Exon31: 2 residues, -Jump to M4K4_HUMAN  
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