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0GAK_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionCyclin g-associated kinase (ec 2.7.1.-).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004674 protein serine/threonine kinase activity (TAS)
0000074 regulation of progression through cell cycle (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 prokaryotic heat shock protein DnaJ interacts with the chaperone hsp70-like DnaK protein . Structurally.he DnaJ protein consists of an N-terminal conserved domain (called J domain) of about 70 amino acids. glycine-rich region (G domain) of about 30 residues. central domain containing four repeats of a CXXCXGXG motif (CRR domain) and a C-terminal region of 120 to 170 residues.Such a structure is shown in the following schematic representation:It is thought that the J domain of DnaJ mediates the interaction with the dnaK protein and consists of four helices.he second of which has a charged surface that includes at least one pair of basic residues that are essential for interaction with the ATPase domain of Hsp70. The J- and CRR-domains are found in many prokaryotic and eukaryotic proteins .ither together or separately. In yeast.-domains have been classified into 3 groups; the class III proteins are functionally distinct and do not appear to act as molecular chaperones .
  IPR001623:Heat shock protein DnaJ, N-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
Potassium channels are the most diverse group of the ion channel family. They are important in shaping the action potential.nd in neuronal excitability and plasticity . The potassium channel family iscomposed of several functionally distinct isoforms.hich can be broadlyseparated into 2 groups : the practically non-inactivating delayed group and the rapidly inactivating transient group.These are all highly similar proteins.ith only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism.hannel conductance and toxin binding properties. Each type of K+ channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter.ogether with intracellular kinases; and others are regulated by GTP-binding proteins orother second messengers . In eukaryotic cells.+ channelsare involved in neural signalling and generation of the cardiac rhythm.ct as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes . In prokaryotic cells.hey play a role in themaintenance of ionic homeostasis . All K+ channels discovered so far possess a core of alpha subunits.ach comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG).hich hasbeen termed the K+ selectivity sequence.In families that contain one P-domain.our subunits assemble to form a selective pathway for K+ across the membrane.However.t remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+ channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess six transmembrane (TM) domains and those that possess only two TM domains. The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+ channels; and three types of calcium (Ca)-activated K+ channels (BK.K and SK). The 2TM domain family comprises inward-rectifying K+ channels. In are K+ channel alpha-subunits that possess two P-domains. These are usually highly regulated K+ selective leak channels. The Kv family can be divided into 4 subfamilies on the basis of sequence similarity and function: Shaker (Kv1).hab (Kv2).haw (Kv3) and Shal (Kv4). All consist of pore-forming alpha subunits that associate with different types of beta subunit. Each alpha subunit comprises six hydrophobic TM domains with a P-domain between the fifth and sixth.hich partially resides in the membrane. The fourth TM domain has positively charged residues at every third residue and acts as a voltage sensor.hich triggers the conformational change that opens the channel pore in response to a displacement in membrane potential .The first Shal (Kv4) sequence was found in Drosophila melanogaster. Several vertebrate K+ channels with similar amino acid sequences were subsequently found and.ogether with the Drosophila melanogaster Shal channel.ow constitute the Shal (Kv4) family. These channels support outward K+-selective currents and are inhibited by free fatty acids . The Shal family can be further divided into 3 families.esignated Kv4.1.v4.2 and Kv4.3.
  IPR003975:Shal voltage-gated K+ channel
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
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
SequencesProtein: GAK_HUMAN (1311 aa)
mRNA: NM_005255
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords)
KO assignmentK00924
  Level 3 annotation:
  Level 2 annotation:
    Inositol phosphate metabolism
    Nicotinate and nicotinamide metabolism
    Benzoate degradation via CoA ligation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 166 residues, 833065-833562Exon2: 61 residues, 833679-833856Exon3: 51 residues, 834723-834872Exon4: 77 residues, 835537-835762Exon5: 41 residues, 843393-843510Exon6: 43 residues, 848909-849032Exon7: 59 residues, 850151-850322Exon8: 161 residues, 850743-851220Exon9: 51 residues, 852326-852473Exon10: 66 residues, 854498-854692Exon11: 28 residues, 860317-860397Exon12: 41 residues, 860877-860995Exon13: 67 residues, 861402-861597Exon14: 46 residues, 865694-865828Exon15: 43 residues, 866484-866607Exon16: 51 residues, 867102-867251Exon17: 18 residues, 867824-867874Exon18: 43 residues, 872634-872758Exon19: 32 residues, 874319-874410Exon20: 39 residues, 877164-877277Exon21: 47 residues, 877661-877797Exon22: 32 residues, 880247-880337Exon23: 44 residues, 881820-881946Exon24: 49 residues, 888424-888567Exon25: 40 residues, 895460-895575Exon26: 22 residues, 896522-896582Exon27: 22 residues, 897394-897456Exon28: 50 residues, 915830-915975Exon29: 2 residues, -Jump to GAK_HUMAN  
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Loci Cluster (Details)Loci: 4658 656225-658122 ~-2K 27158(ATP5I)(-)Loci: 4659 768745-809945 ~-41K 27171(CPLX1)(-)Loci: 4660 833065-915975 ~-83K 27175(GAK)(-)Loci: 3397 609394-654542 ~-45K 27157(PDE6B)(+)Link out to UCSC