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0KLC1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameKNS2
DescriptionKinesin light chain 1 (klc 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005871 kinesin complex (TAS)
0003774 motor activity (TAS)
0005515 protein binding (IPI)

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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 tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR013026:Tetratricopeptide region
Kinesin is a microtubule-associated force-producing molecular motor protein that transports numerous organelles along mirotubules. Kinesin is an oligomeric complex composed of two heavy chains and two identical light chains. The light chain has been proposed to function in the coupling of cargo to the heavy chain or in the modulation of its ATPase activity. The specificity of kinesin-cargo binding is thought to depend on the type of light chain that a kinesin molecule contains.here different isoforms of kinesin light chains are associated with different types of cargo.itochondria and membranes of the Golgi complex .The structure of Drosophila kinesin light chain was shown to have a core composed of a coiled-coil domain followed by five imperfect tandem repeats and a sixth shorter motif . These repeats are highly conserved across species. The N and C termini are more variable and alternative splicing is responsible for the production of isoforms that differ in those two regions.
  IPR002151:Kinesin light chain
Pentatricopeptide repeat proteins are characterised by the presence of a tandem array of repeats.here the number of PPR motifs controls the affinity and specificity of the PPR protein for RNA. These proteins occur predominantly in plants.here they appear to play essential roles in RNA/DNA metabolism in mitochondria and chloroplasts . It has been suggested that each of the highly variable PPR proteins is a gene-specific regulator of plant organellar RNA metabolism. PPR proteins may also play a role in organelle biogenesis.robably via binding to organellar transcripts . Examples of PPR repeat-containing proteins include PET309 .hich may be involved in RNA stabilisation .nd crp1.hich is involved in RNA processing . The repeat is associated with a predicted plant protein that has a domain organization similar to the human BRCA1 protein.
  IPR002885:Pentatricopeptide repeat
Protein prenyltransferases catalyze the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D structure of a mammalian Ras farnesyltransferases (Ftase).oth subunits are largely composed of alpha-helices. The alpha-2 to alpha-15 helices in the alpha subunit fold into a novel helical hairpin structure.esulting in a crescent-shape domain that envelopes part of the subunit. The 12 helices of the beta-subunit form an alpha-alpha barrel. Six additional helices connect the inner core of helices and form the outside of the helical barrel. A deep cleft surrounded by hydrophobic amino acids in the centre of the barrel is proposed as the FPP-binding pocket. A single Zn2+ ion is located at the junction between the hydrophilic surface groove near the subunit interface. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008940:Protein prenyltransferase
The death domain (DD) is a conserved region of about 80 residues found on death receptors.nd which is required for death signalling.s well as a variety of non-apoptotic functions . Proteins containing this domain include the low affinity neurotrophin receptor p73.as.ADD (Fas-associated death domain protein).NF-1 (tumour necrosis factor receptor-1).elle protein kinase.nd the Tube adaptor protein .The induction of apoptosis also relies on the presence of a second domain.alled the death effector domain. The death effector domain (DED) occurs in proteins that regulate programmed cell death.ncluding both pro- and anti-apoptotic proteins; many of these proteins are also involved in controlling cellular activation and proliferation pathways . Proteins containing this domain include FADD (DED N-terminal.D C-terminal).EA-15 (phosphoproteins enriched in astrocytes 15kDa).aspases and FLIP.The induction of apoptosis results in the activation of caspases. family of aspartyl-specific cysteine proteases that are the main executioners of apoptosis. For example.he DED of FADD recruits two DED-containing caspases.aspase-8 and caspase-10.o form the death-inducing signal complex.hich initiates apoptosis. Proteins containing the caspase recruitment domain (CARD) are involved in the recruitment and activation of caspases during apoptosis . Other CARD proteins participate in NF-kappaB signalling pathways associated with innate or adaptive immune responses. Proteins containing CARD include Raidd.PAF-1 (apoptotic protease activating factor 1).rocaspase 9 and iceberg (inhibitor of interleukin-1-beta generation).The DD shows strong structural similarity to both DED and CARD. They all display a 6-helical closed bundle fold.ith greek key topology and an internal psuedo two-fold symmetry. However.espite their overall similarity in topology.ach domain forms specialised interactions.ypically only with members of its own subfamily.or example DED with DED.Please be aware that some of the proteins hit by the SSF signature may be false positives.
  IPR011029:DEATH-like
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR001440:TPR_1 
Evalue:-6.619788646698 
Location:293-326IPR001440:TPR_1 
Evalue:-4.44369745254517 
Location:335-368IPR001440:TPR_1 
Evalue:-3.60206007957458 
Location:377-410IPR001440:TPR_1 
Evalue:-1.50863826274872 
Location:460-480IPR001440:TPR_1 
Evalue:-1.42021644115448 
Location:251-284IPR011029:DEATH_like 
Evalue:0 
Location:7-66IPR013026:TPR 
Evalue:0 
Location:209-242IPR002151:KINESINLIGHT 
Evalue:0 
Location:104-121IPR008940:Prenyl_trans 
Evalue:0 
Location:126-138
SequencesProtein: KLC1_HUMAN (569 aa)
mRNA: NM_182923
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 87 residues, 103165326-103165584Exon2: 89 residues, 103190653-103190915Exon3: 79 residues, 103193635-103193866Exon4: 28 residues, 103198205-103198284Exon5: 77 residues, 103198791-103199017Exon6: 31 residues, 103205600-103205688Exon7: 36 residues, 103206271-103206373Exon8: 60 residues, 103209103-103209277Exon9: 35 residues, 103209421-103209521Exon10: 18 residues, 103211641-103211691Exon11: 24 residues, 103211778-103211846Exon12: 38 residues, 103213504-103213613Exon13: 56 residues, 103215473-103215635Exon14: 26 residues, 103236744-103236817Exon15: 106 residues, 103237290-103237604Exon16: 2 residues, -Jump to KLC1_HUMANExon1: 85 residues, 103165330-103165584Exon2: 89 residues, 103190653-103190915Exon3: 79 residues, 103193635-103193866Exon4: 28 residues, 103198205-103198284Exon5: 77 residues, 103198791-103199017Exon6: 31 residues, 103205600-103205688Exon7: 36 residues, 103206271-103206373Exon8: 60 residues, 103209103-103209277Exon9: 35 residues, 103209421-103209521Exon10: 18 residues, 103211641-103211691Exon11: 24 residues, 103211778-103211846Exon12: 38 residues, 103213504-103213613Exon13: 56 residues, 103215473-103215635Exon14: 46 residues, 103223170-103223302Exon15: 26 residues, 103236747-103236821Exon16: 41 residues, 103238163-103238280Exon17: 107 residues, 103247146-103247461Exon18: 2 residues, -Jump to KLC1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2865 103165326-103247461 ~-82K 11833(KNS2)(+)Loci: 4154 103269841-103383555 ~-114K 11841(PPP1R13B)(-)Loci: 2864 102921523-103039917 ~-118K 11819(MARK3)(+)Link out to UCSC