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
0LCK_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLCK
DescriptionProto-oncogene tyrosine-protein kinase lck (ec 2.7.1.112) (p56-lck) (lsk) (t cell-specific protein-tyrosine kinase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0004713 protein-tyrosine kinase activity (TAS)
0007242 intracellular signaling cascade (TAS)
0006468 protein amino acid phosphorylation (TAS)
0007265 Ras protein signal transduction (TAS)
0000074 regulation of progression through cell cycle (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/784045695.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:
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
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
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
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:Pkinase_Tyr 
Evalue:-154.091522216797 
Location:244-493IPR000980:SH2 
Evalue:-43.6197891235352 
Location:126-208IPR001452:SH3_1 
Evalue:-19.0132274627686 
Location:63-118
SequencesProtein: LCK_HUMAN (508 aa)
mRNA: BC013200 NM_005356 U23852
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
KO assignmentK05856
  Level 3 annotation:
    lymphocyte-specific protein tyrosine kinase
  Level 2 annotation:
    CAM ligands
    Natural killer cell mediated cytotoxicity
    T cell receptor signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 19 residues, 32489505-32489559Exon2: 38 residues, 32512512-32512622Exon3: 29 residues, 32512924-32513006Exon4: 32 residues, 32513180-32513271Exon5: 35 residues, 32513508-32513607Exon6: 36 residues, 32513756-32513860Exon7: 52 residues, 32514101-32514251Exon8: 53 residues, 32514524-32514677Exon9: 62 residues, 32514794-32514974Exon10: 110 residues, 32517858-32518182Exon11: 46 residues, 32518266-32518398Exon12: 217 residues, 32523701-32524348Exon13: 2 residues, -Jump to LCK_HUMANExon1: 14 residues, 32489518-32489559Exon2: 38 residues, 32512512-32512622Exon3: 29 residues, 32512924-32513006Exon4: 32 residues, 32513180-32513271Exon5: 35 residues, 32513508-32513607Exon6: 37 residues, 32513756-32513862Exon7: 50 residues, 32514106-32514251Exon8: 53 residues, 32514524-32514677Exon9: 62 residues, 32514794-32514974Exon10: 27 residues, 32517858-32517935Exon11: 53 residues, 32518028-32518182Exon12: 46 residues, 32518266-32518398Exon13: 217 residues, 32523701-32524348Exon14: 2 residues, -Jump to LCK_HUMANExon1: 32 residues, 32512319-32512414Exon2: 38 residues, 32512512-32512622Exon3: 29 residues, 32512924-32513006Exon4: 32 residues, 32513180-32513271Exon5: 35 residues, 32513508-32513607Exon6: 36 residues, 32513756-32513860Exon7: 52 residues, 32514101-32514251Exon8: 53 residues, 32514524-32514677Exon9: 62 residues, 32514794-32514974Exon10: 57 residues, 32517768-32517935Exon11: 53 residues, 32518028-32518182Exon12: 46 residues, 32518266-32518398Exon13: 218 residues, 32523701-32524350Exon14: 2 residues, -Jump to LCK_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3788 31965305-32002223 ~-37K 944(BAI2)(-)Loci: 2501 32417931-32436472 ~-19K 964(TXLNA)(+)Loci: 2502 32489505-32524350 ~-35K 978(LCK)(+)Loci: 3789 32572027-32574410 ~-2K 982(MARCKSL1)(-)Loci: 2500 31857227-31865301 ~-8K 939(HCRTR1)(+)Link out to UCSC