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1Q5TCI8_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionLamin a/c.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005198 structural molecule activity (IEA)
Domain Architecture (Details)
InterPro domains assigned to SynO:
Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an alpha-helical coiled-coil domain called the SNARE motif . These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classification scheme defines R-SNAREs and Q-SNAREs.s based on the conserved arginine or glutamine residue in the centre of the SNARE motif. SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways.nd contribute to the specificity of intracellular membrane fusion processes.The t-SNARE domain consists of a 4-helical bundle with a coiled-coil twist. The SNARE motif contributes to the fusion of two membranes. SNARE motifs fall into four classes: homologues of syntaxin 1a (t-SNARE).AMP-2 (v-SNARE).nd the N- and C-terminal SNARE motifs of SNAP-25. It is thought that one member from each class interacts to form a SNARE complex.The SNARE motif represented in this entry is found in the N-terminal domains of certain syntaxin family members: syntaxin 1a.hich is required for neurotransmitter release.yntaxin 6.hich is found in endosomal transport vesicles .east Sso1p .nd Vam3p. yeast syntaxin essential for vacuolar fusion . The SNARE motifs in these proteins share structural similarity.espite having a low level of sequence similarity.
  IPR010989:t-snare
InterPro domains unassigned to SynO:
Intermediate filaments (IF) are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide.IF proteins are members of a very large multigene family of proteins which has been subdivided in five major subgroups:Type I: Acidic cytokeratins.Type II: Basic cytokeratins.Type III: Vimentin.esmin.lial fibrillary acidic protein (GFAP).eripherin.nd plasticin.Type IV: Neurofilaments L. and M.lpha-internexin and nestin.Type V: Nuclear lamins A.1.2 and C.All IF proteins are structurally similar in that they consist of: a central rod domain comprising some 300 to 350 residues which is arranged in coiled-coiled alpha-helices.ith at least two short characteristic interruptions; a N-terminal non-helical domain (head) of variable length; and a C-terminal domain (tail) which is also non-helical.nd which shows extreme length variation between different IF proteins.While IF proteins are evolutionary and structurally related.hey have limited sequence homologies except in several regions of the rod domain.
  IPR001664:Intermediate filament protein
Intermediate filaments (IF) are primordial components of the cytoskeleton and the nuclear envelope . They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of a very large multigene family of proteins which has been subdivided in five major subgroups.ype I: acidic cytokeratins.ype II: basic cytokeratins.ype III: vimentin.esmin.lial fibrillary acidic protein (GFAP).eripherin.nd plasticin.ype IV: neurofilaments L. and M.lpha-internexin and nestin.nd type V: nuclear lamins A.1.2 and C. The lamins are components of thenuclear lamina. fibrous layer on the nucleoplasmic side of the inner nuclear membranethat may provide a framework for the nuclear envelope and may interact with chromatin.All IF proteins are structurally similar in that they consist of a central rod domain arranged in coiled-coil alpha-helices.ith at least two short characteristic interruptions; a N-terminal non-helical domain (head) of variable length; and a C-terminaldomain (tail) which is also non-helical.nd which shows extreme length variation between different IF proteins. The C-terminal domain has been charcterised for the lamins.
  IPR001322:Intermediate filament, C-terminal
This domain consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011000:Apolipophorin III-like
IPR001664:Filament 
Evalue:-80.7958831787109 
Location:1-305IPR001322:IF_tail 
Evalue:-74.3372421264648 
Location:344-464
SequencesProtein: Q5TCI8_HUMAN (491 aa)
mRNA: AK097801
Local Annotation
Synapse Ontology
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:domains)
?
sdb:0328 transmitters release and endocytosis  (Evidence:domains)
KO assignmentK07611
  Level 3 annotation:
    lamin
  Level 2 annotation:
    Membrane and intracellular structural molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 12 residues, 154362603-154362638Exon2: 62 residues, 154363150-154363330Exon3: 54 residues, 154367031-154367188Exon4: 44 residues, 154370817-154370943Exon5: 59 residues, 154371219-154371390Exon6: 44 residues, 154371601-154371727Exon7: 75 residues, 154372315-154372536Exon8: 76 residues, 154372628-154372851Exon9: 38 residues, 154373335-154373443Exon10: 42 residues, 154373527-154373647Exon11: 72 residues, 154374068-154374280Exon12: 2 residues, -Jump to Q5TCI8_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3833 152220753-152225430 ~-5K 2681(RAB13)(-)Loci: 2551 152511662-152514973 ~-3K 2706(HAX1)(+)Loci: 2552 152806880-152815707 ~-9K 2720(CHRNB2)(+)Loci: 3834 152821158-152847306 ~-26K 2722(ADAR)(-)Loci: 3835 153201398-153209847 ~-8K 2739(SHC1)(-)Loci: 2553 153412983-153424069 ~-11K 2783(TRIM46)(+)Loci: 2554 153513997-153526262 ~-12K 2831(HCN3)(+)Loci: 3836 153526253-153537835 ~-12K 2833(PKLR)(-)Loci: 2555 153669594-153670676 ~-1K 2846(POU5FLC1)(+)Loci: 2556 154095923-154121459 ~-26K 2875(SYT11)(+)Loci: 3837 154183269-154214942 ~-32K 2882(ARHGEF2)(-)Loci: 2557 154297589-154306917 ~-9K 2890(RAB25)(+)Loci: 2558 154362603-154374280 ~-12K 2897(+)Loci: 2559 154855709-154862142 ~-6K 2944(HAPLN2)(+)Loci: 2560 154878363-154895942 ~-18K 2945(BCAN)(+)Loci: 3838 154905181-154913813 ~-9K 2947(NES)(-)Loci: 2561 155097294-155118266 ~-21K 2961(NTRK1)(+)Loci: 3839 155171256-155281786 ~-111K 2965(ARHGEF11)(-)Loci: 2550 151897823-151900928 ~-3K 2658(SNAPAP)(+)Link out to UCSC