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0PTK6_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePTK6
DescriptionTyrosine-protein kinase 6 (ec 2.7.1.112) (breast tumor kinase) (tyrosine-protein kinase brk).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004715 non-membrane spanning protein tyrosine kina... (TAS)
0006468 protein amino acid phosphorylation (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:
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide receptor.re also family members.
  IPR001245:Tyrosine 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
The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps . Similar sequences were later found in many other intracellular signal-transducing proteins . SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific.H2 domains recognize between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs fromone SH2 domain to another.nd strictly phosphorylation-dependent manner . They are found in a wide variety of protein contexts e.g..n association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules..e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the alpha+beta class.ts overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel beta-sheet.lanked by 2 short alpha-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand.nd is hence designated the phosphate binding loop.he phosphorylated ligand binds perpendicular to the beta-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins .
  IPR000980:SH2 motif
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
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
IPR001245:TyrKc 
Evalue:-136.0268721464 
Location:191-441IPR000980:SH2 
Evalue:-30.0809219076239 
Location:76-161IPR001452:SH3 
Evalue:-14.0705810742857 
Location:11-71
SequencesProtein: PTK6_HUMAN (451 aa)
mRNA: NM_005975
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
KO assignmentK08253
  Level 3 annotation:
    non-specific protein-tyrosine kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 434 residues, 61630221-61631520Exon2: 53 residues, 61631874-61632028Exon3: 62 residues, 61632542-61632724Exon4: 56 residues, 61634322-61634484Exon5: 53 residues, 61635347-61635501Exon6: 56 residues, 61635948-61636112Exon7: 42 residues, 61636734-61636856Exon8: 92 residues, 61638881-61639151Exon9: 2 residues, -Jump to PTK6_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3279 60906621-60915796 ~-9K 23505(OGFR)(+)Loci: 3280 61337720-61342298 ~-5K 23526(BIRC7)(+)Loci: 4537 61448389-61463100 ~-15K 23536(CHRNA4)(-)Loci: 4538 61507985-61574437 ~-66K 23542(KCNQ2)(-)Loci: 4539 61630221-61639151 ~-9K 23549(PTK6)(-)Loci: 4540 61642606-61649301 ~-7K 23550(SRMS)(-)Loci: 4541 61659883-61676033 ~-16K 23552(PRIC285)(-)Loci: 4542 61689398-61721673 ~-32K 23556(GMEB2)(-)Loci: 3281 61996961-62035838 ~-39K 23585(DNAJC5)(+)Loci: 3282 62082900-62134895 ~-52K 23593(C20orf14)(+)Loci: 3283 62181931-62202435 ~-21K 23600(OPRL1)(+)Loci: 3278 60810633-60864567 ~-54K 23503(NTSR1)(+)Link out to UCSC