Q9NEL2 · SSL1_CAEEL

  • Protein
    Helicase ssl-1
  • Gene
    ssl-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Probable catalytic component of a chromatin-remodeling complex which mediates the ATP-dependent exchange of histone H2A variant H2AV/htz-1 for H2A, leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in foregut development, and may be involved in vulval development.

Features

Showing features for binding site.

123952004006008001,0001,2001,4001,6001,8002,0002,200
TypeIDPosition(s)Description
Binding site583-590ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentSwr1 complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent chromatin remodeler activity
Molecular FunctionDNA binding
Molecular Functionhelicase activity
Molecular Functionhistone binding
Biological Processchromatin remodeling
Biological Processnegative regulation of cell fate specification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Helicase ssl-1
  • EC number
  • Alternative names
    • Swi/snf2-like protein 1

Gene names

    • Name
      ssl-1
    • ORF names
      Y111B2A.22

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q9NEL2
  • Secondary accessions
    • E0R7L4
    • E0R7L5
    • E0R7L6
    • Q6Q9H2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Defects in feminization. Embryonic arrest.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003112371-2395Helicase ssl-1

Proteomic databases

Expression

Gene expression databases

    • WBGene00007027Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, coiled coil.

Type
IDPosition(s)Description
Compositional bias1-31Polar residues
Region1-62Disordered
Compositional bias48-62Basic and acidic residues
Domain227-300HSA
Region354-404Disordered
Compositional bias363-404Basic and acidic residues
Coiled coil388-464
Compositional bias444-469Basic and acidic residues
Region444-504Disordered
Compositional bias470-491Polar residues
Domain570-735Helicase ATP-binding
Region963-982Disordered
Domain1196-1342Helicase C-terminal
Coiled coil1452-1476
Compositional bias1615-1670Polar residues
Region1615-1706Disordered
Compositional bias1977-2041Polar residues
Region1977-2073Disordered
Compositional bias2050-2073Polar residues
Region2092-2143Disordered
Region2276-2306Disordered
Compositional bias2350-2385Polar residues
Region2350-2395Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q9NEL2-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    2,395
  • Mass (Da)
    268,727
  • Last updated
    2006-06-13 v4
  • MD5 Checksum
    56DBCE1671F32F6D7B446B0538F36A5A
MPATPVRASSTRISRRTSSRSVADDQPSTSSAVAPPPSPIAIETDEDAVVEEEKKKKKTSDDLEIITPRTPVDRRIPYICSILLTENRSIRDKLVLSSGPVRQEDHEEQIARAQRIQPVVDQIQRVEQIILNGSVEDILKDPRFAVMADLTKEPPPTPAPPPPIQKTMQPIEVKIEDSEGSNTAQPSVLPSCGGGETNVERAAKREAHVLARIAELRKNGLWSNSRLPKCVEPERNKTHWDYLLEEVKWMAVDFRTETNTKRKIAKVIAHAIAKQHRDKQIEIERAAEREIKEKRKMCAGIAKMVRDFWSSTDKVVDIRAKEVLESRLRKARNKHLMFVIGQVDEMSNIVQEGLVSSSKSPSIASDRDDKDEEFKAPGSDSESDDEQTIANAEKSQKKEDVRQEVDALQNEATVDMDDFLYTLPPEYLKAYGLTQEDLEEMKREKLEEQKARKEACGDNEEKMEIDESPSSDAQKPSTSSSDLTAEQLQDPTAEDGNGDGHGVLENVDYVKLNSQDSDERQQELANIAEEALKFQPKGYTLETTQVKTPVPFLIRGQLREYQMVGLDWMVTLYEKNLNGILADEMGLGKTIQTISLLAHMACSESIWGPHLIVVPTSVILNWEMEFKKWCPALKILTYFGTAKERAEKRKGWMKPNCFHVCITSYKTVTQDIRAFKQRAWQYLILDEAQNIKNWKSQRWQALLNVRARRRLLLTGTPLQNSLMELWSLMHFLMPTIFSSHDDFKDWFSNPLTGMMEGNMEFNAPLIGRLHKVLRPFILRRLKKEVEKQLPEKTEHIVNCSLSKRQRYLYDDFMSRRSTKENLKSGNMMSVLNIVMQLRKCCNHPNLFEPRPVVAPFVVEKLQLDVPARLFEISQQDPSSSSASQIPEIFNLSKIGYQSSVRSAKPLIEELEAMSTYPEPRAPEVGGFRFNRTAFVAKNPHTEESEDEGVMRSRVLPKPINGTAQPLQNGNSIPQNAPNRPQTSCIRSKTVVNTVPLTISTDRSGFHFNMANVGRGVVRLDDSARMSPPLKRQKLTGTATNWSDYVPRHVVEKMEESRKNQLEIVRRRFEMIRAPIIPLEMVALVREEIIAEFPRLAVEEDEVVQERLLEYCELLVQRFGMYVEPVLTDAWQCRPSSSGLPSYIRNNLSNIELNSRSLLLNTSTNFDTRMSISRALQFPELRLIEYDCGKLQTLAVLLRQLYLYKHRCLIFTQMSKMLDVLQTFLSHHGYQYFRLDGTTGVEQRQAMMERFNADPKVFCFILSTRSGGVGVNLTGADTVIFYDSDWNPTMDAQAQDRCHRIGQTRNVSIYRLISERTIEENILRKATQKRRLGELAIDEAGFTPEFFKQSDSIRDLFDGENVEVTAVADVATTMSEKEMEVAMAKCEDEADVNAAKIAVAEANVDNAEFDEKSLPPMSNLQGDEEADEKYMELIQQLKPIERYAINFLETQYKPEFEEECKEAEALIDQKREEWDKNLNDTAVIDLDDSDSLLLNDPSTSADFYQSSSLLDEIKFYDELDDIMPIWLPPSPPDSDADFDLRMEDDCLDLMYEIEQMNEARLPQVCHEMRRPLAEKQQKQNTLNAFNDILSAKEKESVYDAVNKCLQMPQSEAITAESAASPAYTEHSSFSMDDTSQDAKIEPSLTENQQPTTTATTTTTVPQQQQQQQQQKSSKKKRNDNRTAQNRTAENGVKRATTPPPSWREEPDYDGAEWNIVEDYALLQAVQVEFANAHLVEKSANEGMVLNWEFVSNAVNKQTRFFRSARQCSIRYQMFVRPKELGQLVASDPISKKTMKVDLSHTELSHLRKGRMTTESQYAHDYGILTDKKHVNRFKSVRVAATRRPVQFWRGPKALESRNLQSLNGGMPPRHESRLAEFDVKTNIRLDAEDIVTMSDESIVAYEASKKKLLASRQTKPSPRQDVRFHTLVLRPYTVPVTTEYSAAPSRREMRIAVPPLQPSALSTISSVAAAATSGPLPSIQHLQSSSTGLGSQQNLQNSHNSEQRNNVQNMHQNQYNSSQNPPIPIRQIGAASSHQHDQGSQGPGGKPQAYHLVQQGSQQQQQQQQQATLQRRNAAAAAGSNVQFIQQQQQQQQSGKNCGQGQSFVVMGSQSSSNDGQGGASTVGGGGGGSQQPHQQQQQQPQQRIQYIPQVTGSGNNGGGGGRGGYGSTLVMPRGGRVVRPAGTLPGGGRLYVDHNRHPYPMSSNVVPVRVLPATQQGQQRMMTGQRRPAPAPGTVAAMVLPNRGAGGIPQMRSLQRGSYTGGGGQQRINVMVQPQQMRSNNGGGVGGQGGLQGGPGGPQGIRRPLVGRPLQRGVDNQAPTVAQVVVAPPQGMQQASQGPPVLHMQRAVSMQMPTSHHHQGQQQAPPQSSQQASQQAPTSDSGTSAPPRQAPPPQN

Q9NEL2-2

  • Name
    b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1512-1920: IKFYDELDDIMPIWLPPSPPDSDADFDLRMEDDCLDLMYEIEQMNEARLPQVCHEMRRPLAEKQQKQNTLNAFNDILSAKEKESVYDAVNKCLQMPQSEAITAESAASPAYTEHSSFSMDDTSQDAKIEPSLTENQQPTTTATTTTTVPQQQQQQQQQKSSKKKRNDNRTAQNRTAENGVKRATTPPPSWREEPDYDGAEWNIVEDYALLQAVQVEFANAHLVEKSANEGMVLNWEFVSNAVNKQTRFFRSARQCSIRYQMFVRPKELGQLVASDPISKKTMKVDLSHTELSHLRKGRMTTESQYAHDYGILTDKKHVNRFKSVRVAATRRPVQFWRGPKALESRNLQSLNGGMPPRHESRLAEFDVKTNIRLDAEDIVTMSDESIVAYEASKKKLLASRQTKPSPRQD → VRDRRRRSSSLLQKAAQKPAKKPQNFQIRARSPSKRKSQAPSFDPYVSYAPHALASPPDSPRKRRSRGARSLGSGGGGGGGSRSVGRPARRSVKKEESDDDDEDYCQEEEVKRNPAEKVPPKRKRVVFVEPPEVKPPEPKKRVVVPAPSSSSSALTTLPQQGPLISLPKAVPVVPRPQQQAPPQLIKKHQQTLMPVKVLKISGGGGGTPGPSSVSPGPSILRRTVVPGIGAGGVGRLPLVRMPVRPPFPGSQAPAPPLRSGVAPTAPAAAPRQFVVPSSRVRVITTRTPVATTMVQQQQSPSPLMFPVRVVQRPGPSGPPPPGPPDRPGFGIYEKPRFSLGSRRSRGDSGPEDPAPPQPPPPTTSRPPPQA
    • 1921-2395: Missing

Q9NEL2-3

  • Name
    c
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9NEL2-4

  • Name
    d
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for compositional bias, alternative sequence.

Type
IDPosition(s)Description
Compositional bias1-31Polar residues
Alternative sequenceVSP_0436861-146in isoform d
Alternative sequenceVSP_0436851-1521in isoform c
Compositional bias48-62Basic and acidic residues
Compositional bias363-404Basic and acidic residues
Compositional bias444-469Basic and acidic residues
Compositional bias470-491Polar residues
Alternative sequenceVSP_0436871512-1920in isoform b
Compositional bias1615-1670Polar residues
Alternative sequenceVSP_0436881921-2395in isoform b
Compositional bias1977-2041Polar residues
Compositional bias2050-2073Polar residues
Compositional bias2350-2385Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY551965
EMBL· GenBank· DDBJ
AAS65429.1
EMBL· GenBank· DDBJ
mRNA
AL132904
EMBL· GenBank· DDBJ
CAC35851.3
EMBL· GenBank· DDBJ
Genomic DNA
AL132904
EMBL· GenBank· DDBJ
CBW48563.1
EMBL· GenBank· DDBJ
Genomic DNA
AL132904
EMBL· GenBank· DDBJ
CBW48564.1
EMBL· GenBank· DDBJ
Genomic DNA
AL132904
EMBL· GenBank· DDBJ
CBW48565.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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