SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0M4K5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAP4K5
DescriptionMitogen-activated protein kinase kinase kinase kinase 5 (ec 2.7.1.37) (mapk/erk kinase kinase kinase 5) (mek kinase kinase 5) (mekkk 5) (kinase homologous to sps1/ste20) (khs).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IDA)
0005524 ATP binding (IDA)
0005515 protein binding (IPI)
0004674 protein serine/threonine kinase activity (IDA)
0007257 activation of JNK activity (TAS)
0006468 protein amino acid phosphorylation (IDA)
0007243 protein kinase cascade (IDA)
0006950 response to stress (IDA)

Warning: fopen(/home/kongl/syndb/www/temp/1294982554.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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:-142.552841968658 
Location:511-826IPR002290:S_TKc 
Evalue:-87.4685210829577 
Location:20-277IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: M4K5_HUMAN (846 aa)
mRNA: NM_198794
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 527 residues, 49954996-49956574Exon2: 20 residues, 49959588-49959644Exon3: 25 residues, 49962374-49962445Exon4: 33 residues, 49965129-49965222Exon5: 25 residues, 49965659-49965728Exon6: 61 residues, 49970861-49971039Exon7: 36 residues, 49971429-49971533Exon8: 21 residues, 49973943-49974002Exon9: 41 residues, 49974361-49974479Exon10: 22 residues, 49976480-49976541Exon11: 28 residues, 49976829-49976909Exon12: 30 residues, 49979199-49979284Exon13: 16 residues, 49980196-49980238Exon14: 34 residues, 49980406-49980504Exon15: 53 residues, 49981508-49981662Exon16: 16 residues, 49982546-49982589Exon17: 24 residues, 49983881-49983949Exon18: 21 residues, 49985241-49985300Exon19: 28 residues, 49992983-49993062Exon20: 41 residues, 49999132-49999249Exon21: 29 residues, 50000519-50000601Exon22: 23 residues, 50003050-50003113Exon23: 46 residues, 50005118-50005250Exon24: 26 residues, 50011544-50011617Exon25: 16 residues, 50012595-50012638Exon26: 18 residues, 50012726-50012774Exon27: 20 residues, 50018828-50018884Exon28: 23 residues, 50022045-50022110Exon29: 32 residues, 50022571-50022662Exon30: 21 residues, 50041267-50041325Exon31: 74 residues, 50068409-50068626Exon32: 88 residues, 50068867-50069126Exon33: 2 residues, -Jump to M4K5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2835 49429588-49431484 ~-2K 11111(ARF6)(+)Loci: 2836 49848796-49862418 ~-14K 11116(ATP5S)(+)Loci: 4130 49954996-50069126 ~-114K 11120(MAP4K5)(-)Loci: 2837 50096499-50169140 ~-73K 11121(SPG3A)(+)Loci: 2834 49304536-49319605 ~-15K 11105(KLHDC2)(+)Link out to UCSC