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General Information
Symbol
Dmel\Sh
Species
D. melanogaster
Name
Shaker
Annotation Symbol
CG12348
Feature Type
FlyBase ID
FBgn0003380
Gene Model Status
Stock Availability
Gene Snapshot
Shaker (Sh) encodes the structural alpha subunit of a voltage-gated potassium channel. It plays a key role in maintaining electrical excitability in neurons and muscle cells, as well as regulating neurotransmitter release at the synapse. [Date last reviewed: 2019-03-14]
Also Known As

EKO, Shw

Key Links
Genomic Location
Cytogenetic map
Sequence location
X:17,924,307..18,063,247 [-]
Recombination map

1-59

RefSeq locus
NC_004354 REGION:17924307..18063247
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Protein Family (UniProt)
Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Shaker sub-subfamily. (P08510)
Summaries
Gene Group (FlyBase)
VOLTAGE-GATED POTASSIUM CHANNEL - ALPHA SUBUNITS -
Voltage-gated potassium α subunits form homo- or heterotetrameric transmembrane channels specific for potassium which are activated by changes in membrane potential. Kv channel α subunits possess six or seven transmembrane domains. (Adapted from FBrf0224790).
Protein Function (UniProtKB)
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A-type currents (PubMed:2448636). Plays a role in the regulation of sleep need or efficiency (PubMed:15858564).
(UniProt, P08510)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Sh: Shaker (M. Tanouye)
Under moderate ether anesthesia, legs shake abnormally, antennae twitch, abdomen pulsates; wings scissor in some alleles; very little effect in deeply etherized flies; unetherized mutants twitch and shudder occasionally; severed legs shake (Kaplan and Trout, 1969, Genetics 61: 399-409; Trout and Kaplan, 1973; Tanouye, Ferrus, and Fujita, 1981; Ganetzky and Wu, 1982a, Genetics 100: 597-614; Tanouye and Ferrus, 1985, J. Neurogenet. 2: 253-71). Structural gene for several types of potassium channel (Iverson, Tanouye, Lester, Davidson, and Rudy, 1988, Proc. Nat. Acad. Sci. USA 85: 5723-27; Timpe, Schwarz, Tempel, Papazian, Jan, and Jan, 1988, Nature 331: 143-45). Abnormal action potential repolarization of adult giant fiber; repetitive firing of action potentials in larval nerves; prolonged transmitter release at larval neuromuscular junction (Jan, Jan, and Dennis, 1977; Tanouye, Ferrus, and Fujita, 1981; Ganetzky and Wu, 1982b, J. Neurophysiol. 47: 501-14; Tanouye and Ferrus, 1985). Abnormal in one class of potassium channel (A channel) present in embryonic myocytes, larval and pupal muscle (Salkoff and Wyman, 1981; Salkoff, 1983, Cold Spring Harbor Symp. Quant. Biol. 48: 221-31; Wu and Haugland, 1985, J. Neurosci. 5: 2626-40; Timpe and Jan, 1987, J. Neurosci. 7: 1307-17; Haugland and Wu, 1990, J. Neurosci.). Sh mutations do not affect four other distinct potassium-channel types (KD, K1, A2, Calcium-gated) (Salkoff and Wyman, 1981; Salkoff, 1983, Nature 302: 249-51; Wu, Ganetzky, Haugland, and Liu, 1983, Science 220: 1076-78; Solc, Zagotta, and Aldrich, 1987, Science 236: 1094-98; Solc and Aldrich, 1988, J. Neurosci. 8: 2556-70). Males carrying hemizygous deletions of Sh are viable (Tanouye, Ferrus, and Fujita, 1981). Abnormal associative learning in some paradigms (Tully); activity patterns high, but show normal circadian rhythmicity (Konopka). RK1.
Summary (Interactive Fly)

Integral membrane voltage-gated potassium ion channel - carries type-A potassium current responsible for the repolarization of the cell - regulates neurotransmitter release at the synapse - regulates sleep - neuromuscular junction

Gene Model and Products
Number of Transcripts
15
Number of Unique Polypeptides
11

Please see the GBrowse view of Dmel\Sh or the JBrowse view of Dmel\Sh for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model

Gene model reviewed during 5.55

Gene model reviewed during 5.45

Low-frequency RNA-Seq exon junction(s) not annotated.

Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.

Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated

Gene model reviewed during 6.02

gene_with_non_canonical_start_codon ; SO:0001739

Unconventional translation start (AUU) postulated; FlyBase analysis.

Gene model reviewed during 6.08

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0089659
1814
304
FBtr0089658
7860
616
FBtr0089661
12181
643
FBtr0089660
2442
571
FBtr0089657
2781
655
FBtr0089663
1774
349
FBtr0301955
1286
304
FBtr0302902
6786
643
FBtr0302903
4135
643
FBtr0308199
2221
297
FBtr0308200
4138
644
FBtr0332299
3578
337
FBtr0346703
2843
616
FBtr0346705
3836
604
FBtr0346706
2781
655
Additional Transcript Data and Comments
Reported size (kB)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0088601
34.9
304
4.69
FBpp0088600
70.3
616
6.02
FBpp0088603
72.5
643
5.86
FBpp0088602
64.7
571
5.74
FBpp0088599
74.2
655
5.89
FBpp0088605
40.5
349
4.93
FBpp0291167
34.9
304
4.69
FBpp0292033
72.5
643
5.86
FBpp0292034
72.5
643
5.86
FBpp0300519
34.2
297
4.52
FBpp0300520
72.6
644
5.86
FBpp0304578
38.8
337
4.87
FBpp0312316
70.3
616
6.02
FBpp0312318
68.6
604
5.51
FBpp0312319
74.2
655
6.02
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

643 aa isoforms: Sh-PC, Sh-PI, Sh-PJ
616 aa isoforms: Sh-PB, Sh-PQ
304 aa isoforms: Sh-PA, Sh-PH
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Subunit Structure (UniProtKB)

Homotetramer or heterotetramer of potassium channel proteins.

(UniProt, P08510)
Domain

The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.

(UniProt, P08510)
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Sh using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Gene Ontology (24 terms)
Molecular Function (3 terms)
Terms Based on Experimental Evidence (1 term)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000898862
(assigned by GO_Central )
traceable author statement
non-traceable author statement
inferred from biological aspect of ancestor with PANTHER:PTN000164970
(assigned by GO_Central )
Biological Process (19 terms)
Terms Based on Experimental Evidence (12 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (7 terms)
CV Term
Evidence
References
non-traceable author statement
traceable author statement
non-traceable author statement
non-traceable author statement
inferred from biological aspect of ancestor with PANTHER:PTN000164970
(assigned by GO_Central )
inferred from electronic annotation with InterPro:IPR003131
(assigned by InterPro )
non-traceable author statement
Cellular Component (2 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000164970
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001355853
(assigned by GO_Central )
traceable author statement
non-traceable author statement
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

Sh is expressed in a group of visual projection neurons (VPN fibers) that send processes to the lobula plate.

Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\Sh in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 54 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 25 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Sh
Transgenic constructs containing regulatory region of Sh
Deletions and Duplications ( 9 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
axon & motor neuron | conditional ts
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (28)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
13 of 15
Yes
Yes
 
12 of 15
No
Yes
 
12 of 15
No
Yes
9 of 15
No
Yes
9 of 15
No
Yes
 
8 of 15
No
Yes
 
7 of 15
No
Yes
7 of 15
No
Yes
 
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
 
1 of 15
No
No
1 of 15
No
No
 
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
 
1 of 15
No
No
 
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
 
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (27)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
13 of 15
Yes
Yes
12 of 15
No
Yes
12 of 15
No
Yes
9 of 15
No
Yes
9 of 15
No
Yes
8 of 15
No
Yes
7 of 15
No
Yes
7 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Rattus norvegicus (Norway rat) (24)
11 of 13
Yes
Yes
11 of 13
Yes
Yes
10 of 13
No
Yes
9 of 13
No
Yes
8 of 13
No
Yes
7 of 13
No
Yes
6 of 13
No
Yes
6 of 13
No
Yes
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
Xenopus tropicalis (Western clawed frog) (9)
10 of 12
Yes
Yes
10 of 12
Yes
Yes
8 of 12
No
Yes
7 of 12
No
Yes
5 of 12
No
Yes
5 of 12
No
Yes
4 of 12
No
Yes
1 of 12
No
Yes
1 of 12
No
No
Danio rerio (Zebrafish) (35)
12 of 15
Yes
Yes
12 of 15
Yes
Yes
12 of 15
Yes
Yes
12 of 15
Yes
Yes
8 of 15
No
Yes
8 of 15
No
Yes
6 of 15
No
Yes
5 of 15
No
Yes
5 of 15
No
Yes
5 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (13)
13 of 15
Yes
Yes
1 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Arabidopsis thaliana (thale-cress) (4)
1 of 9
Yes
No
1 of 9
Yes
No
1 of 9
Yes
Yes
1 of 9
Yes
No
Saccharomyces cerevisiae (Brewer's yeast) (0)
No records found.
Schizosaccharomyces pombe (Fission yeast) (0)
No records found.
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG091906VY )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091504WK )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W04RM )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Rhodnius prolixus
Kissing bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X04NX )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G10NU )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (6)
3 of 10
3 of 10
2 of 10
2 of 10
1 of 10
1 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Model Summary Ribbon
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 3 )
    Modifiers Based on Experimental Evidence ( 1 )
    Allele
    Disease
    Interaction
    References
    DOES NOT ameliorate  brain cancer
    Disease Associations of Human Orthologs (via DIOPT v7.1 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Show neighbor-neighbor interactions:
    Select Layout:
    Legend:
    Protein
    RNA
    Selected Interactor(s)
    Interactions Browser

    Please see the Physical Interaction reports below for full details
    protein-protein
    Physical Interaction
    Assay
    References
    Summary of Genetic Interactions
    esyN Network Diagram
    esyN Network Key:
    Suppression
    Enhancement

    Please look at the allele data for full details of the genetic interactions
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Subunit Structure (UniProtKB)
    Homotetramer or heterotetramer of potassium channel proteins.
    (UniProt, P08510 )
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (genetic) - An integrated Molecular Interaction Database
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Signaling Pathways (FlyBase)
    Metabolic Pathways
    External Data
    Linkouts
    Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    X
    Recombination map

    1-59

    Cytogenetic map
    Sequence location
    X:17,924,307..18,063,247 [-]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    16F3-16F6
    Limits computationally determined from genome sequence between P{EP}EP970 and P{EP}ari-1EP317
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    16F1-16F4
    (determined by in situ hybridisation)
    16F-16F
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Location

    1-53.3 +/- 0.7

    1-57.6

    Left of (cM)
    Notes
    Stocks and Reagents
    Stocks (34)
    Genomic Clones (52)
    cDNA Clones (51)
     

    Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

    cDNA clones, fully sequences
    BDGP DGC clones
    Drosophila Genomics Resource Center cDNA clones

    For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

    cDNA Clones, End Sequenced (ESTs)
    RNAi and Array Information
    Linkouts
    DRSC - Results frm RNAi screens
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    Antibody Information
    Laboratory Generated Antibodies
     

    polyclonal

    Commercially Available Antibodies
     
    Other Information
    Relationship to Other Genes
    Source for database identify of
    Source for database merge of

    Source for merge of: Sh BcDNA:GH03046

    Source for merge of: Sh CG17860 CG7640

    Additional comments

    Annotations CG12348, CG17860 and CG7640 merged as CG12348 (which corresponds to Sh) in release 3 of the genome annotation.

    Other Comments

    Sh K+ conductance is important for neural coding precision and as a mechanism for selectively amplifying graded signals in neurons.

    The intracellular gate of Sh channels is capable of regulating access even by the small cations Cd2+ and Ag+. It can exclude small neutral or negatively charged molecules, suggesting that the gate operates by steric exclusion rather than electrostatically.

    Mutants are hypersensitive to paraquat.

    qvr and Sh may share the same pathway in the regulation of synaptic transmission.

    The Sh gene product may be a major target for PKG modulation.

    Three permeant ion binding-sites in the pore of Sh channel are studied. Pore-lining resides are identified that appear to contribute to the formation of two deeper sites. Results are consistent with a mechanism of gating that operates by pinching off access of the deep pore to the internal or external solution.

    The membrane potential plays a crucial role in the loss of conductance. There is a close connection between the gating and conduction function of the membrane.

    Slob, identified as a protein that binds to the carboxy-terminal domain of slo, does not co-immunoprecipitate with Sh.

    Fluorescent labeling allows the examination of voltage-dependent conformational changes in different regions of the Sh channel. The S2 segment may undergo voltage sensitive conformational changes that precede those in the S4 segment. Fluorescence changes in the pore correlate with the voltage dependence and time course of ionic activation and slow inactivation.

    Incorporation of Npg (an unnatural amino acid (2-nitrophenyl)glycine) produces peptide backbone cleavage at the site of the novel residue, by analogy with other 2-nitrobenzyl systems.

    Analysis of Sh-Ecol\lacZ reporter constructs suggests that tissue-specific alternative splicing of Sh transcripts results from distinct modes of regulating 3' splice choice in different tissues.

    Recovery from inactivation in Sh K+ channels begins with no delay on repolarisation. Hyperpolarisation hastens only the initial phase of recovery, yet retards the later phase of recovery by increasing the proportion of slow components. The fast and slow components primarily correspond to recovery via the open state and via the closed state, respectively. Sh K+ channel deactivation hinders, rather than facilitates, the unbinding of the inactivating particle and therefore retards recovery from inactivation, whereas external K+ may enhance unbinding of the particle by binding to a site located near the external entrance of the pore.

    A series of positions in the S6 transmembrane regions are found to react rapidly with water soluble thiol reagents in the open state but not the closed state. An open-channel blocker can protect several of these Cys residues, showing that they lie in the ion-conduction pore. Results suggest the channels open and close by the movement of an intracellular gate, distinct from the selectivity filter, that regulates access to the pore.

    The spatio-temporal expression of Sh protein in the developing and adult nervous system has been analysed.

    Probing the boundary of the electric field with protons indicates that the voltage-sensing residue 365 lies on an internally faced narrow crevice in the resting state, while the sensing charge at position 368 sits in an externally faced crevice in the open state of the channel. Both residues move entirely from the internal to external medium in each stroke of the voltage sensor. The translocation of the two residues accounts for 66% of the total gating charge.

    The dlg1 product colocalises with Sh K+ channels, which are clustered at glutamatergic synapses at the larval neuromuscular junction.

    The C-terminal sequences of Fas2 and Sh are both necessary and sufficient for targeting to the subsynaptic muscle membrane at the larval neuromuscular junction, and this localization depends on the product of dlg1.

    Opening of a Sh channel is associated with a displacement of 13.6 electron charge units. Mutational analysis reveals that movement of the amino-terminal half but not the carboxy-terminal end of the S4 segment underlies gating charge, and this portion of the S4 segment appears to move across the entire transmembrane voltage difference in association with channel activation.

    When applied to Sh channels expressed in mammalian cells, quaternary ammonium blockers produce use-dependent inhibition by promoting an intrinsic conformational change, C-type inactivation, from which recovery is slow.

    Subunits from eag and Sh functionally interact in Xenopus oocytes, most likely as heteromultimeric channels. Site directed mutagenesis indicates the eag carboxyl terminus is crucial for the interaction with Sh.

    eag coexpression with Sh in Xenopus oocytes accelerates the inactivation and slows the recovery from inactivation of the transient Sh current.

    The effects of amino acid replacements on AgTx2 affinity define the eccentricity of amino acids in the pore entryway and imply a different secondary structure for the amino and carboxyl ends of the pore loop.

    Mutations in Khc enhance the para and mel and suppress the Sh and eag mutant phenotypes.

    The putative voltage-sensing charges of S4 actually reside in the membrane and move outward when channels open.

    The S4 domain contains the gating charge. Activation consists of the movement of the outer portion of S4 into the extracellular fluid from a position that is buried in the resting state, thus generating the gating current.

    Triple mutation can convert the outwardly rectifying Sh channel to an inward rectifier. The conversion does not rely on a difference in sign or direction of charge movement of the voltage sensor, since activation of the Sh outward rectifier is due to a different gate than activation of the mutant inward rectifier.

    Charybdotoxin insensitivity maps to residue 449 of the Sh K+ channel.

    Studies of the interaction of Agitoxin2 with Sh channels reveals a shallow vestibule formed by the pore loops at the Sh channel entryway. The selectivity filter is located at the center of the vestibule close to (around 5 Angstroms from) the extracellular solution.

    Alteration of the rate of aging and life span using Sh and Hk hyperactive mutants shows that the timing of type I Ecol\lacZ2216 expression is independent of metabolic rate.

    Fas2 is necessary for the synaptic sprouting induced by increased activity (eag Sh double mutants) or increased cAMP (dnc).

    Voltage sensing residues have been mapped to the S2 and S4 segments of the Sh K+ channel.

    Hk β subunit modulates a wide range of the Sh K+ current properties, inducing its amplitude, activation and inactivation, temperature dependence and drug sensitivity. Modulation is thought to occur via hydrophobic interactions, Hk β subunits modulate Sh channel formation in the cytoplasmic pore region.

    The monkey Cos cell line is a reasonable system for transient expression of K+ channels, particularly those with fast inactivation kinetics.

    Hk encodes a K+ channel β subunit with distinctive effects on Sh channel function.

    Synthetic inactivating and synthetic noninactivating peptides are used to investigate whether the single amino acid change in the peptide sequence determines alteration in the conformation of the "ball" peptide that might explain the loss of function. The two peptides have a different potential capacity to become structured into a given conformation.

    Modulation of Sh channels using serotonin has been studied in a semi-intact preparation of the retina.

    Using Ecol\lacZ reporter gene for accurate splicing of variable Sh 3' domains the expression pattern in transgenic animals indicates both temporal and spatial regulation of 3' splice choice. Tissue-specific expression of functionally distinct Sh K+ channels is regulated, in part, at the level of pre-mRNA splicing and implicates sequences in or around the 3' splice sites in regulating the choice of 3' domain.

    Mutations conveying both strong and weak suppression of the primary S4 neutralisation mutations K374Q and R377Q have been obtained identifying likely short- and long range electrostatic interactions among transmembrane charged residues.

    Immunochemical techniques have identified so called short Sh cDNAs. Genetic criteria determines a good part of the protein variety is generated by alternative splicing. The expression pattern of Sh splice variants changes dramatically throughout development.

    The entire adult temporal pattern of expression of an enhancer trap element, P{lacW}1085, scales to life span in Hk1 and Sh5 mutants.

    Sh currents are not detectable in embryonic neurons.

    Coimmunoprecipitation and yeast two-hybrid system studies demonstrate the association of the hydrophilic N-terminal domains of the genes encoding channel proteins plays an important role in determining the specificity of α subunit association to form heteromultimeric potassium channels.

    Abnormal function of Sh K+ channels at motor nerves specifically abolishes post-tetanic potentiation (PTP) in the larval neuromuscular junction.

    The time course of N-type inactivation of Sh K+ channels is prolonged upon exposure of the cytoplasmic face to phosphatases and this effect is completely reversed by subsequent application of the purified catalytic subunit of the cAMP-dependent protein kinase (PKA) and ATP.

    The functional consequences of introducing point mutations into the signature sequence of Sh channel is studied.

    Physical dimensions and biochemical characteristics of Sh channels expressed in Sf9 cells studied using electron microscopy demonstrates they have a tetrameric subunit composition. Negative staining reveals a four-fold symmetric tetramer with a large, central vestibule that presumably constitutes part of the pathway for ions.

    4-AP binds to an internally accessible site of Sh and alters channel gating. The binding is state-dependent and when bound 4-AP prevents channels from opening and blocks distinct conformational rearrangements.

    Ion permeation of Sh channels appears to have many of the properties consistent with multi-ion pores.

    S4 mutations alter gating currents of Sh K channels.

    Expression of Sh using a mammalian transient transfection system allows N-ethlymaleamide-labelled charybdotoxin (NEM-CTX) quantification and characterisation of assembled tetrameric channels in both isolated membrane fragments and detergent extracts. The channels produced can be functionally reconstituted into model membranes accessible to direct electrical recording.

    Double mutant combinations and gene dosage experiments suggest that tta interacts with the viable region (V) of the Sh complex.

    Ion channel mutants alter synaptic activity at the embryonic neuromuscular junction (NMJ). GluRIIA expression in the postsynaptic membrane is reduced by changes in presynaptic electrical activity. The size of the synaptic domain depends on the level of neural activity during embryonic synaptogenesis.

    Mutations in two regions of Sh, the pore region and the last transmembrane sequence, appear to alter quaternary ammonium (QA) compound binding and inhibition of Sh.

    The conduction properties of the cloned Sh channel are characteristic of those traditionally found in other K+ channels.

    Electrophysiological measurements and numerical simulation studies of channels expressed in transfected cells reveals that the slow properties of the encoded channel help to determine the voltage trajectories in the synthetic neurons. Slow inactivation of transient K+ currents could play a role in the encoding properties of real neurons.

    In eag,Sh hyperexcitable double mutants nerve/muscle synaptic ultrastructure is dramatically altered. Two types of synaptic vesicle are depleted and a third is altered in appearance, and there are changes in number and appearance of synaptic densities, and multivesicular bodies.

    The role of conserved L370 residue is investigated. Substitutions result in alteration in the relative stabilities of open, closed and inactivated conformational states, corresponding to the size and hydrophobicity of the substituted residue. Data suggests that nonconservative substitutions of L370 influence the ability of Sh subunits to assemble into functional channel complexes. All observations are consistent with the idea that L370 and other residues in the region undergo protein interactions that are important determinants in the formational structure of the channel.

    In mutant channels that have completely abolished ion conduction the channel can still undergo the closed-open conformation in response to voltage changes.

    The effect of mutations that decrease the steepness of the conductance-voltage relationship is to alter the kinetics and equilibria of charge-moving transitions.

    A 20 amino acid synthetic peptide corresponding to the amino terminal of the B splice variant of the Sh K+ channel, and responsible for its fast inactivation, can block large conductance Ca2+-dependent K+ channels from rat brain and muscle, in two kinetically distinct types of blocking, "long" and "short". Pharmacological experiments indicate the peptide induces short block by binding in the pore of Ca2+-dependent K+ channels. This short block and the inactivation of Sh exhibit similar characteristics, therefore the binding region for the peptide in the pore regions is conserved in these very different K+ channels.

    Effects of potassium channel blocking drugs on the presynaptic action potential repolarization after electrotonic stimulation was studied. At least four K+ currents contribute to repolarization of the nerve terminal.

    The effects of mutations where the pore sequences mimic those of the cyclic nucleotide gated channels were tested in the Xenopus oocyte expression system. These channels behave as cyclic nucleotide gated channels, demonstrating that the two physiologically distinct types of channel are actually closely related.

    Channel gating is investigated.

    Inactivation mechanism of Sh channels is investigated.

    Cell-free protein translation, microsomal membrane processing of nascent channel protein, and reconstitution of newly synthesised ion channels into planar lipid bilayers generated glycosylated, active, functional Shaker potassium channels.

    Sh, Shal, Shab and Shaw encode independent channel systems that function independently in Xenopus oocytes.

    Shaker splice variant B 20 amino acid inactivating peptide (known as "ball peptide" BP) interacts with Ca2+-activated K+ channels in porcine coronary smooth muscle from cytoplasmic side only, producing inhibition of channel activity. Effect is reversible and dose- and voltage-dependent. BP binds KCa channels in a bimolecular reaction, and results suggest that Ca-dependent K+ channels and the Sh channels have the same receptor for "BP".

    Inactivation of Sh channel during a prolonged depolarisation lasting many seconds must occur by a distinct mechanism from the rapid inactivation of the wild type Sh channel.

    Subunit assembly of Sh does not depend on the leucine heptad repeat. Substitutions of the Leu residues in the repeat produce large effects on the observed voltage dependence of conductance voltage and prepulse inactivation curves. Results suggest the Leu residues mediate interactions that play an important role in the transduction of charge movement into channel opening and closing.

    Site directed mutagenesis of the S4 sequence of the Sh potassium channel and electrophysiological analysis suggest that voltage-dependent activation involves the S4 sequence but it is not solely due to electrostatic interactions.

    Sh RNA expression in pupae and adults has been studied.

    An amino acid residue that specifically affects the affinity for the intracellular tetraethylammonium (TEA) has been identified and is in the middle of a conserved stretch of 18 amino acids. Results suggest this conserved region is intimately involved in the formation of the ion conduction pore of the channel.

    Molecular region of Sh has been identified that influences ionic selectivity. H5 (fifth hydrophobic region) is likely to line th pore of the potassium channel.

    Variations in amino acid sequence in a small region of Sh near the amino terminus can cause changes in channel inactivation rates.

    The effect of Ca2+ removal causes a nonselective leak of expressed K+ channels due to a massive functional alteration of the channel.

    Although Sh, Shal, Shab and Shaw proteins share a conserved structral organisation, their potassium channel currents (expressed in Xenopus oocytes) differ greatly in individual kinetic properties and voltage sensitivity.

    The Sh locus can be dissected by means of aneuploids into three regions: maternal effect (ME), viable (V) and haplolethal (HL). Mutations of the ME region of the Sh locus affect oogenesis and the differentiation of the hypoderm and/or the physiology of the CGF.

    Expression of mutated Sh potassium channels in Xenopus oocytes has identified a region near the amino terminus that has an important role in inactivation of the channel.

    Cloning and characterisation of Sh has identified structural elements involved in potassium channel gating. The amino and carboxy terminus are specialised for, and appear to interact in, inactivation gating.

    Analysis of Sh polypeptides expressed in Xenopus oocytes suggests that they assemble to form multimeric channels.

    Both the 5' and 3' variable domains of the Sh gene product influence the kinetics of macroscopic inactivation. The amino domain dictates a general range of inactivation properties. Chimaeric Sh cDNAs exhibit variable time constants for inactivation, variable incomplete inactivation and variable recovery from inactivation.

    Specific amino acid residues have been identified that affect channel blockade by an external source tetraethylammonium (tetraethylammonium (TEA)), as well as conductance of ions through the pore.

    Coinjection of different Sh RNAs into Xenopus oocytes indicates the formation of heteromultimeric Sh channels.

    The distribution of Sh proteins in the brain of the adult fly has been determined.

    The presence of A2-type potassium channels in Sh deficiency flies indicates that these channels are not encoded by the Sh gene.

    Studies of two Sh proteins that differ only in their amino termini suggests that the amino terminus of Sh proteins affects potassium channel structures on both sides of the membrane.

    Sh, Shal, Shab and Shaw encode voltage gated potassium channels with widely varying kinetics (rate of macroscopic current activation and inactivation) and voltage sensitivity of steady state inactivation.

    Potassium channel diversity could result from an extended gene family as well as from alternate splicing of the Sh primary transcript.

    The Glu residue at position 422 is near or in the externally facing mouth of the potassium conduction pathway. The positively charged toxin charybdotoxin (CTX) is electrostatically focused toward its blocking site by the negative potential set up by Glu-422.

    P-element mediated germline transformation has been used to express ShB channel in Sh mutants. The transformant A-current inactivates rapidly and recovers from inactivation similarly to ShB channels expressed in Xenopus oocytes. Unlike channels in oocytes the transformant A-current is insensitive to charybdotoxin (CTX).

    The molecular transition rates leading to the first opening of ShB and ShD channels are voltage-dependent. All further transitions are independent of voltage. The difference in macroscopic current between the channels is due to the quantitative difference in transition rates. Voltage dependence of macroscopic currents is determined by the voltage dependency on the time to first opening.

    A Sh cDNA has been used as a probe to isolate a homologous rat brain cDNA.

    Transcripts synthesised in vitro from Sh cDNA express A-type K+ currents when injected into Xenopus oocytes.

    Two basic forms of conceptual proteins are encoded by Sh cDNA: the more common form containing seven potential membrane spanning domains and the other form containing 3 potential membrane spanning domains. The cDNAs contain variable 5' and 3' ends joined to a constant central region. The different cDNAs encode proteins with distinct structural features.

    At least four probable components of potassium channels are encoded at the Sh locus by a family of alternatively spliced transcripts.

    Sh gene encodes the A potassium ion channel or one of its subunits.

    Four different Sh mRNAs have been tested and found to produce A currents in Xenopus oocytes. The four currents differ in kinetics of inactivation indicating that the Sh products may contribute to kinetic diversity in A-channels. Sequences in both the amino- and carboxy-terminal regions are important for inactivation.

    Sh has been isolated as part of a chromosomal walk. Sh corresponds to a large transcription unit encompassing 95kb of genomic DNA and split by a major 85kb intron.

    The Sh genomic region has been cloned and the transcription pattern of this region has been analysed.

    Sh encodes a structural component of a voltage-dependent K+ channel.

    Some Sh phenotypes are suppressed by nap and para alleles; i.e., in double mutant combinations, abnormal leg-shaking, repetitive firing of larval action potentials, and transmitter release at larval neuromuscular junction are nearly normal; the interactions are not allele-specific (Ganetzky and Wu, 1982a; Ganetzky and Wu, 1982b). Some Sh phenotypes are enhanced by eag; i.e., in double mutant combinations, abnormal leg-shaking, repetitive firing of larval action potentials and transmitter release are more extreme; also, adults have down-turned wings and dented-in thoraces at the sites of the dorsal longitudinal muscle insertions; the interactions are not allele-specific (Ganetzky and Wu, 1983). Some Sh phenotypes are enhanced by dnc; i.e., in double mutant combinations, abnormal leg-shaking is more extreme; abnormal spontaneous activity is seen in the giant fiber (Ferrus and Tanouye). The breakpoint of T(1;2)B27, induced in a Sh14 background, causes an alteration in the pattern of leg-shaking (Tanouye and Ferrus).

    Under moderate ether anesthesia, legs shake abnormally, antennae twitch, abdomen pulsates; wings scissor in some alleles; very little effect in deeply etherized flies; unetherized mutants twitch and shudder occasionally; severed legs shake (Kaplan and Trout, 1969; Trout and Kaplan, 1973; Tanouye, Ferrus and Fujita, 1981; Ganetzky and Wu, 1982a; Tanouye and Ferrus, 1985). Structural gene for several types of potassium channel (Iverson et al., 1988; Timpe et al. Jan, 1988). Abnormal action potential repolarization of adult giant fiber; repetitive firing of action potentials in larval nerves; prolonged transmitter release at larval neuromuscular junction (Jan, Jan and Dennis, 1977; Tanouye, Ferrus and Fujita, 1981; Ganetzky and Wu, 1982b; Tanouye and Ferrus, 1985). Abnormal in one class of potassium channel (A channel) present in embryonic myocytes, larval and pupal muscle (Salkoff and Wyman, 1981; Salkoff, 1983; Wu and Haugland, 1985; Timpe and Jan, 1987; Haugland and Wu, 1990). Sh mutations do not affect four other distinct potassium-channel types (KD, K1, A2, Calcium-gated) (Salkoff and Wyman, 1981; Salkoff, 1983; Wu et al., 1983; Solc et al., 1987; Solc and Aldrich, 1988). Males carrying hemizygous deletions of Sh are viable (Tanouye, Ferrus and Fujita, 1981). Abnormal associative learning in some paradigms (Tully); activity patterns high, but show normal circadian rhythmicity (Konopka).

    Origin and Etymology
    Discoverer

    Catsch, 1944.

    Etymology
    Identification
    External Crossreferences and Linkouts ( 137 )
    Sequence Crossreferences
    NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
    GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
    UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
    Other crossreferences
    BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
    Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
    Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
    Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
    Flygut - An atlas of the Drosophila adult midgut
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
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    FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
    FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
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    Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
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    Synonyms and Secondary IDs (22)
    Reported As
    Symbol Synonym
    BcDNA:GH03046
    F-c
    Sh
    (Harbison et al., 2019, Hill et al., 2019, Kasuya et al., 2019, Kulik et al., 2019, Kumar Chaudhary and Rizvi, 2019, Davis et al., 2018, Feng et al., 2018, Fernández-Mariño et al., 2018, Hall et al., 2018, Lee et al., 2018, Li et al., 2018, Walcott et al., 2018, Wang et al., 2018, Xing and Wu, 2018, Agrawal et al., 2017, Kline et al., 2017, Transgenic RNAi Project members, 2017-, Carbone et al., 2016, Saur et al., 2016, Ugur et al., 2016, Wang et al., 2016, Dialynas et al., 2015, Gene Disruption Project members, 2015-, Huang et al., 2015, Kern et al., 2015, Kroll et al., 2015, Pan et al., 2015, Wang et al., 2015, Zandany et al., 2015, Ashwal-Fluss et al., 2014, Ford and Davis, 2014, Iyengar and Wu, 2014, Lee et al., 2014, Takayama et al., 2014, Vernes, 2014, Wolfram et al., 2014, Wu et al., 2014, Joiner et al., 2013, Stocker et al., 2013, Timmerman et al., 2013, Beck et al., 2012, Hazelett et al., 2012, Houot et al., 2012, Owald et al., 2012, Pfeiffenberger and Allada, 2012, Rodriguez et al., 2012, Senthilan et al., 2012, Tsai et al., 2012, Tsubouchi et al., 2012, Winbush et al., 2012, Yoshihara and Ito, 2012, Abruzzi et al., 2011, Ellis and Carney, 2011, Graveley et al., 2011, Guan et al., 2011, Koon et al., 2011, Leiserson and Keshishian, 2011, Leiserson et al., 2011, Ping et al., 2011, Banovic et al., 2010, Carrillo et al., 2010, Fergestad et al., 2010, Friedman et al., 2010, Keene et al., 2010, Lorbeck et al., 2010, Mosca and Schwarz, 2010, Singh et al., 2010, Wang and Wu, 2010, Wu et al., 2010, Chiang et al., 2009, de Bivort et al., 2009, Ruedi and Hughes, 2009, Ryglewski and Duch, 2009, Weber et al., 2009, Anaka et al., 2008, Ataman et al., 2008, Duch et al., 2008, Hartwig et al., 2008, Howlett et al., 2008, Johnson and Bennett, 2008, Koh et al., 2008, Lee et al., 2008, Ueda and Wu, 2008, Beuchle et al., 2007, Bushey et al., 2007, Haerty et al., 2007, Joiner et al., 2007, Junion et al., 2007, Magidovich et al., 2007, Peng and Wu, 2007, Peng and Wu, 2007, Peng et al., 2007, Berke et al., 2006, Cardnell et al., 2006, Hebbar et al., 2006, Lee and Wu, 2006, Meyer and Aberle, 2006, Pielage et al., 2006, Ueda and Wu, 2006, Yuan et al., 2006, Glazov et al., 2005, Hodge et al., 2005, Honjo and Furukubo-Tokunaga, 2005, Laviolette et al., 2005, Xu et al., 2005, Yang et al., 2005, Bogdanik et al., 2004, Choi et al., 2004, Feng et al., 2004, Girardot et al., 2004, Hebbar and Fernandes, 2004, Niven et al., 2004, Wang et al., 2004, Zhong and Wu, 2004, Hall, 2003, Juusola et al., 2003, Niven et al., 2003, Huang and Stern, 2002, Wang et al., 2002, Kuebler et al., 2001, Walcourt et al., 2001, Yao and Wu, 2001, Brenner et al., 2000, Madhavan et al., 2000, Schmidt et al., 2000)
    minisleep
    Name Synonyms
    F-c transcription unit
    Shaker
    (Davis et al., 2018, Kalstrup and Blunck, 2018, Ly et al., 2018, Allada et al., 2017, Donlea et al., 2017, Sheng et al., 2017, Tomita et al., 2017, Pimentel et al., 2016, Ugur et al., 2016, Wang et al., 2016, Dissel et al., 2015, Huang et al., 2015, Kalstrup and Blunck, 2015, Kroll et al., 2015, Ping et al., 2015, Wangler et al., 2015, Zandany et al., 2015, Ford and Davis, 2014, Frank, 2014, Ghezzi et al., 2014, Iyengar and Wu, 2014, Lee et al., 2014, Scott and Panin, 2014, Singh et al., 2014, Wolfram et al., 2014, Castellanos et al., 2013, Kalstrup and Blunck, 2013, Mahdavi and Kuyucak, 2013, Neckameyer and Argue, 2013, Robertson and Keene, 2013, Stocker et al., 2013, Xu et al., 2013, Frolov et al., 2012, Henrion et al., 2012, Houot et al., 2012, Jan and Jan, 2012, Jepson et al., 2012, Savva et al., 2012, Schaper et al., 2012, Tsubouchi et al., 2012, Graveley et al., 2011, Guan et al., 2011, Leiserson et al., 2011, Pandey and Nichols, 2011, Sehgal and Mignot, 2011, Crocker et al., 2010, Diao et al., 2010, Fergestad et al., 2010, Liu et al., 2010, Lorbeck et al., 2010, Singh et al., 2010, Wang and Wu, 2010, Wu et al., 2010, Ben-Abu et al., 2009, de Bivort et al., 2009, Diao et al., 2009, Ingleby et al., 2009, Ruedi and Hughes, 2009, Ryglewski and Duch, 2009, Weber et al., 2009, Camacho, 2008, Duch et al., 2008, Hartwig et al., 2008, Johnson and Bennett, 2008, Lee et al., 2008, Ueda and Wu, 2008, Alabi et al., 2007, Bushey et al., 2007, Joiner et al., 2007, Magidovich et al., 2007, Peng and Wu, 2007, Zhang et al., 2007, Berke et al., 2006, Lee and Wu, 2006, Middleton et al., 2006, Nakayama et al., 2006, Pielage et al., 2006, Burnette et al., 2005, Glazov et al., 2005, Hodge et al., 2005, Honjo and Furukubo-Tokunaga, 2005, Marques, 2005, Rasse et al., 2005, Xu et al., 2005, Bhalla et al., 2004, Feng et al., 2004, Hebbar and Fernandes, 2004, Niven et al., 2004, Rivlin et al., 2004, Wang et al., 2004, Hall, 2003, Juusola et al., 2003, McCormack, 2003, Niven et al., 2003, Silverman et al., 2003, Wang et al., 2002, Kuebler et al., 2001, Walcourt et al., 2001, Yao and Wu, 2001, Blaustein et al., 2000, Brenner et al., 2000, Madhavan et al., 2000, Schwarz, 1993.3.26, Barbas, 1992.6.29)
    Shaker-downheld
    Secondary FlyBase IDs
    • FBgn0030885
    • FBgn0030888
    • FBgn0064981
    Datasets (0)
    Study focus (0)
    Experimental Role
    Project
    Project Type
    Title
    References (806)