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0PAK7_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePAK7
DescriptionSerine/threonine-protein kinase pak 7 (ec 2.7.1.37) (p21-activated kinase 7) (pak-7) (pak-5).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
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
The molecular bases of the versatile functions of Rho-like GTPases are still unknown.Small domains that bind Cdc42p- and/or Rho-like small GTPases.Also known as the Cdc42/Rac interactive binding (CRIB). The Cdc42/Rac interactive binding (CRIB) region has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway . In fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating .
  IPR000095:PAK-box/P21-Rho-binding
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
The Rho-family GTPase.dc42.an regulate the actin cytoskeleton through activation of Wiskott-Aldrich syndrome protein (WASP) family members . Mutations in WASP lead to the Wiskott-Aldrich syndrome. paediatric disorder characterized by actin cytoskeletal defects in haematopoietic cells.eading clinically to thrombocytopenia.czema and immunodeficiency. The WASP proteins signal to the cytoskeleton through the Arp2/3 complex.n actin-nucleating assembly that regulates the structure and dynamics of actin filament networks at the leading edge of the cell.WASP family members have unique N-terminal regions.ollowed by a central segment rich in proline.nd a common C-terminal region. The C-terminal region contains the VCA region that binds the Arp2/3 complex and actin.hile the distinct N-terminal region enables family members to activate Arp2/3 in response to different upstream signals.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011026:Wiscott-Aldrich syndrome, C-terminal
IPR002290:S_TKc 
Evalue:-89.7212463990472 
Location:449-700IPR000095:PBD 
Evalue:-20.8860569000244 
Location:10-67IPR011026:WASP_C 
Evalue:0 
Location:338-376IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: PAK7_HUMAN (719 aa)
mRNA: NM_020341
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK05736
  Level 3 annotation:
    p21-activated kinase 7
  Level 2 annotation:
    Regulation of actin cytoskeleton
    Focal adhesion
    T cell receptor signaling pathway
    Axon guidance
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 743 residues, 9466036-9468264Exon2: 47 residues, 9471232-9471367Exon3: 44 residues, 9473015-9473141Exon4: 44 residues, 9486254-9486381Exon5: 46 residues, 9491537-9491671Exon6: 166 residues, 9494539-9495031Exon7: 264 residues, 9508791-9509577Exon8: 73 residues, 9572772-9572987Exon9: 52 residues, 9639933-9640083Exon10: 51 residues, 9713005-9713154Exon11: 39 residues, 9767409-9767522Exon12: 2 residues, -Jump to PAK7_HUMAN  
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