Q6P9I7 · SMC6_XENLA

Function

function

Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components (By similarity).

Features

Showing features for binding site.

111281002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site115-122ATP (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 Componentchromosome, telomeric region
Cellular ComponentPML body
Cellular ComponentSmc5-Smc6 complex
Molecular FunctionATP binding
Biological Processcellular senescence
Biological ProcessDNA repair
Biological Processtelomere maintenance via recombination

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Structural maintenance of chromosomes protein 6
  • Short names
    SMC protein 6; SMC-6; xSMC6

Gene names

    • Name
      smc6
    • Synonyms
      smc6l1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q6P9I7
  • Secondary accessions
    • Q805A0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002709591-1128Structural maintenance of chromosomes protein 6

Expression

Developmental stage

Loaded onto chromatin during DNA replication in a manner dependent on the initiation of DNA synthesis, and it dissociated from chromatin during mitosis. Chromatin loading is not induced by DNA double-strand breaks.

Gene expression databases

    • 398986Expressed in testis and 19 other cell types or tissues

Interaction

Subunit

Forms a heterodimer with smc5. Component of the SMC5-SMC6 complex which consists at least of smc5, smc6, nsmce2, nsmce1 and nsmce4a (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region1-80Disordered
Compositional bias44-59Basic and acidic residues
Compositional bias60-80Polar residues
Coiled coil275-519
Region520-692Flexible hinge
Coiled coil693-955

Domain

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC5, forming a V-shaped heterodimer.

Sequence similarities

Belongs to the SMC family. SMC6 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,128
  • Mass (Da)
    130,513
  • Last updated
    2004-07-05 v1
  • Checksum
    126806396112F088
MGKRKDGSPIAPSSQRKKQRQEVDDPYDEEDYGQAGPSVSNDYGQRKKQRKEADNSHTDSDYENSVSCASSQRVSASQSGTGDVGIIESIFLRNFMCHSMLGPFRFGPNVNFVIGNNGSGKSAVLTALIVGLGGKAAITNRGSSIKGFVKEGQTFAEISITLRNRGQDAYKPDVFGNSITVQQRLTTDGSRTYKLKSATGAVVSNKKEELTAILDHFNIQVDNPVSVLTQEMSKHFLQSKNESDKYKFFMKATQLEQMKEDYSYIMETKSRTHDQVENGGERLRDLRQECIQKEERFKSIASLGEMKEKLEDLKNKMAWALVTESEKQIKPFIEQISTEEGRTVKYEQKIEECQGKVINAEEKFRAKQEELDKITQEAVALKPQGIGLKEDVQKKRKSYNESEVLYNRHRMELKRLERDAEQLHKRIEELKKSADNDSESEKMARQKEINQIRERMKALHDKDITTNQQIHQFQQAIEKYKEERARIGNEERNIKQRLEQHKRQLKELHESKTDRLKRFGQNMPALLAAIDEADKLGRFRKKPVGPLGACIHLKDQELALAVESCLKGLMFAFCCDNHQDERMLQNIMSREYPRGRRPQIIVNEFIDHVYDVRQRATFHPDHPTVLTALEIDHPVVTNCLIDMRGIETILIIKGKDEAREIMQKRAPPRNCREAFTGEGDQVYTNRYYSSDSRRATLLSRDVEAEISHLEKELRNFGSQMATFQQRAQSVDKDIKENEGILRQYHNSKKQIQIDLRPLLERISELENVEEQPSIDIATLEGEAEENLNKIELVKQEVELAKEKMGNLKSFLTTAEINYEEIKKKISSVAEVAEPVKEDLHRVDQEVENCKRHRKHYEEKLKEHLDRIQKRKEEVAAKEQELEVKISQAKCICPERIEVSRTARSLDTEINRLREKINSEEVLHGNREEIIKQYHEAKERYQDVEGKVKHLKRFIKLLDEIMAQRYKSYQQFRRCLTFRCKIYFDSLLSQRAYSGKINFDHKNETLSITVQPGEGNKAALSDMKCLSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRISMDMMLSMADSQRFRQFILLTPQNMSSLPSTSLVRILRMKDPERGQTTLPFQPLNQEAEDEE

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias44-59Basic and acidic residues
Sequence conflict58in Ref. 1; BAC56937
Compositional bias60-80Polar residues
Sequence conflict62in Ref. 1; BAC56937
Sequence conflict68in Ref. 1; BAC56937
Sequence conflict755in Ref. 1; BAC56937
Sequence conflict1023-1024in Ref. 1; BAC56937

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB103031
EMBL· GenBank· DDBJ
BAC56937.1
EMBL· GenBank· DDBJ
mRNA
BC060747
EMBL· GenBank· DDBJ
AAH60747.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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