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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7CL0

Crystal structure of human SIRT6

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003684molecular_functiondamaged DNA binding
A0003714molecular_functiontranscription corepressor activity
A0003723molecular_functionRNA binding
A0003950molecular_functionNAD+ poly-ADP-ribosyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005721cellular_componentpericentric heterochromatin
A0005730cellular_componentnucleolus
A0005783cellular_componentendoplasmic reticulum
A0006111biological_processregulation of gluconeogenesis
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006284biological_processbase-excision repair
A0006302biological_processdouble-strand break repair
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006476biological_processprotein deacetylation
A0006606biological_processprotein import into nucleus
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0008285biological_processnegative regulation of cell population proliferation
A0008340biological_processdetermination of adult lifespan
A0009411biological_processresponse to UV
A0010526biological_processtransposable element silencing
A0010569biological_processregulation of double-strand break repair via homologous recombination
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0017136molecular_functionhistone deacetylase activity, NAD-dependent
A0019216biological_processregulation of lipid metabolic process
A0031490molecular_functionchromatin DNA binding
A0031491molecular_functionnucleosome binding
A0031508biological_processpericentric heterochromatin formation
A0031509biological_processsubtelomeric heterochromatin formation
A0031648biological_processprotein destabilization
A0032024biological_processpositive regulation of insulin secretion
A0032129molecular_functionhistone H3K9 deacetylase activity, hydrolytic mechanism
A0032206biological_processpositive regulation of telomere maintenance
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032922biological_processcircadian regulation of gene expression
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
A0034979molecular_functionNAD-dependent protein lysine deacetylase activity
A0035861cellular_componentsite of double-strand break
A0042181biological_processketone biosynthetic process
A0042308biological_processnegative regulation of protein import into nucleus
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0042803molecular_functionprotein homodimerization activity
A0043687biological_processpost-translational protein modification
A0045600biological_processpositive regulation of fat cell differentiation
A0045721biological_processnegative regulation of gluconeogenesis
A0045814biological_processnegative regulation of gene expression, epigenetic
A0045820biological_processnegative regulation of glycolytic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0046325biological_processnegative regulation of D-glucose import
A0046827biological_processpositive regulation of protein export from nucleus
A0046872molecular_functionmetal ion binding
A0046969molecular_functionhistone H3K9 deacetylase activity, NAD-dependent
A0048146biological_processpositive regulation of fibroblast proliferation
A0050708biological_processregulation of protein secretion
A0050994biological_processregulation of lipid catabolic process
A0051697biological_processprotein delipidation
A0055007biological_processcardiac muscle cell differentiation
A0070403molecular_functionNAD+ binding
A0090734cellular_componentsite of DNA damage
A0097372molecular_functionhistone H3K18 deacetylase activity, NAD-dependent
A0099115cellular_componentchromosome, subtelomeric region
A0106222molecular_functionlncRNA binding
A0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0120186biological_processnegative regulation of protein localization to chromatin
A0120187biological_processpositive regulation of protein localization to chromatin
A0140612molecular_functionDNA damage sensor activity
A0140765molecular_functionhistone H3K56 deacetylase activity, NAD-dependent
A0140773molecular_functionNAD-dependent protein demyristoylase activity
A0140774molecular_functionNAD-dependent protein depalmitoylase activity
A0140804molecular_functionNAD+-protein-lysine ADP-ribosyltransferase activity
A0140861biological_processDNA repair-dependent chromatin remodeling
A1902459biological_processpositive regulation of stem cell population maintenance
A1902732biological_processpositive regulation of chondrocyte proliferation
A1903076biological_processregulation of protein localization to plasma membrane
A1904841molecular_functionTORC2 complex binding
A1905555biological_processpositive regulation of blood vessel branching
A1905564biological_processpositive regulation of vascular endothelial cell proliferation
A1990166biological_processprotein localization to site of double-strand break
A1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
A2000648biological_processpositive regulation of stem cell proliferation
A2000738biological_processpositive regulation of stem cell differentiation
A2000773biological_processnegative regulation of cellular senescence
A2000781biological_processpositive regulation of double-strand break repair
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues245
DetailsDomain: {"description":"Deacetylase sirtuin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsCompositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18337721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23892288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27322069","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28406396","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27990725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PKJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MGN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Formation of an covalent adduct with nitro-fatty acid activators","evidences":[{"source":"PubMed","id":"33122195","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"27568560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"32538779","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24043303","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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