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0K2C6D_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameKRT6D
DescriptionKeratin, type ii cytoskeletal 6d (cytokeratin 6d) (ck 6d) (k6d keratin) (fragment).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005200 structural constituent of cytoskeleton (NAS)
0030154 cell differentiation (NAS)
0008284 positive regulation of cell proliferation (NAS)

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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 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 proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide. Type II keratins are the basic or neutral courterparts to the acidic type I keratins. Each type II keratin forms a heterodimer with a specific acidic keratin.nd the heterodimers are organised into tetramers and then into chains . Type II keratins consist of head-.od- and tail-like structures.he rod being constructed from three linked coils: 1A.B and 2. The head and tail structures of the type 2 keratins are highly variable low-complexity regions.
  IPR003054:Type II keratin
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:-147.769546508789 
Location:1-295
SequencesProtein: K2C6D_HUMAN (384 aa)
mRNA: NM_173086
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:keywords,domains)
intermediate filaments of the presynaptic compartments. Both microtubles and intermediate filaments represent the main structural scaffold of axons.
sdb:0086 intermediate filaments  (Evidence:keywords,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:keywords,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:keywords,domains)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
KO assignmentK07605
  Level 3 annotation:
    type II keratin, basic
  Level 2 annotation:
    Membrane and intracellular structural molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 163 residues, 51148861-51149348Exon2: 13 residues, 51149461-51149496Exon3: 75 residues, 51149720-51149941Exon4: 44 residues, 51150555-51150681Exon5: 57 residues, 51151182-51151347Exon6: 34 residues, 51151471-51151567Exon7: 22 residues, 51151722-51151783Exon8: 73 residues, 51152116-51152331Exon9: 194 residues, 51153248-51153824Exon10: 2 residues, -Jump to K2C6D_HUMAN  
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Loci Cluster (Details)Loci: 2755 50587468-50601120 ~-14K 8882(ACVRL1)(+)Loci: 2756 50631752-50677126 ~-45K 8883(ACVR1B)(+)Loci: 2757 50687014-50695938 ~-9K 8886(GRASP)(+)Loci: 4034 50965965-50971566 ~-6K 8896(KRTHB1)(-)Loci: 2758 50981917-50988684 ~-7K 8897(KRTHB6)(+)Loci: 4035 50994358-51001438 ~-7K 8898(KRTHB3)(-)Loci: 4036 51040058-51047576 ~-8K 8899(KRTHB5)(-)Loci: 4037 51057862-51065684 ~-8K 8900(KRTHB4)(-)Loci: 4038 51104120-51114373 ~-10K 8902(-)Loci: 4039 51148861-51153824 ~-5K 8903(KRT6D)(-)Loci: 4040 51167243-51173287 ~-6K 8904(KRT6A)(-)Loci: 4041 51194627-51200510 ~-6K 8905(KRT5)(-)Loci: 4042 51265639-51281559 ~-16K 8909(-)Loci: 4043 51448205-51457372 ~-9K 8917(KRT2P)(-)Loci: 4044 51486600-51494602 ~-8K 8920(KRT4)(-)Loci: 4045 51577237-51585127 ~-8K 8924(KRT8)(-)Loci: 2759 51629109-51632951 ~-4K 8926(KRT18)(+)Loci: 2761 51948817-51973697 ~-25K 8948(ESPL1)(+)Loci: 4046 52160546-52179538 ~-19K 8970(MAP3K12)(-)Loci: 4047 52186740-52187689 ~-1K 8973(NPFF)(-)Loci: 4048 52345211-52356779 ~-12K 8978(ATP5G2)(-)Loci: 2754 50271286-50488365 ~-217K 8878(SCN8A)(+)Link out to UCSC