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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7NJ0

CryoEM structure of the human Separase-Cdk1-cyclin B1-Cks1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000212biological_processmeiotic spindle organization
A0000278biological_processmitotic cell cycle
A0000280biological_processnuclear division
A0000281biological_processmitotic cytokinesis
A0003824molecular_functioncatalytic activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0007059biological_processchromosome segregation
A0007127biological_processmeiosis I
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0040001biological_processestablishment of mitotic spindle localization
A0045143biological_processhomologous chromosome segregation
A0045842biological_processpositive regulation of mitotic metaphase/anaphase transition
A0045875biological_processnegative regulation of sister chromatid cohesion
A0051306biological_processmitotic sister chromatid separation
A0051307biological_processmeiotic chromosome separation
A0072686cellular_componentmitotic spindle
A0098813biological_processnuclear chromosome segregation
B0000082biological_processG1/S transition of mitotic cell cycle
B0000086biological_processG2/M transition of mitotic cell cycle
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
B0000781cellular_componentchromosome, telomeric region
B0001618molecular_functionvirus receptor activity
B0003682molecular_functionchromatin binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005789cellular_componentendoplasmic reticulum membrane
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005876cellular_componentspindle microtubule
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006338biological_processchromatin remodeling
B0006357biological_processregulation of transcription by RNA polymerase II
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0006974biological_processDNA damage response
B0007077biological_processmitotic nuclear membrane disassembly
B0007095biological_processmitotic G2 DNA damage checkpoint signaling
B0007098biological_processcentrosome cycle
B0007344biological_processpronuclear fusion
B0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
B0009636biological_processresponse to toxic substance
B0010628biological_processpositive regulation of gene expression
B0010629biological_processnegative regulation of gene expression
B0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
B0014038biological_processregulation of Schwann cell differentiation
B0014075biological_processresponse to amine
B0014823biological_processresponse to activity
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016477biological_processcell migration
B0016579biological_processprotein deubiquitination
B0016740molecular_functiontransferase activity
B0018107biological_processpeptidyl-threonine phosphorylation
B0030261biological_processchromosome condensation
B0030332molecular_functioncyclin binding
B0030496cellular_componentmidbody
B0030544molecular_functionHsp70 protein binding
B0030855biological_processepithelial cell differentiation
B0031397biological_processnegative regulation of protein ubiquitination
B0034501biological_processprotein localization to kinetochore
B0035173molecular_functionhistone kinase activity
B0042307biological_processpositive regulation of protein import into nucleus
B0042542biological_processresponse to hydrogen peroxide
B0042752biological_processregulation of circadian rhythm
B0043066biological_processnegative regulation of apoptotic process
B0044772biological_processmitotic cell cycle phase transition
B0045471biological_processresponse to ethanol
B0045740biological_processpositive regulation of DNA replication
B0045995biological_processregulation of embryonic development
B0046686biological_processresponse to cadmium ion
B0046688biological_processresponse to copper ion
B0046718biological_processsymbiont entry into host cell
B0048144biological_processfibroblast proliferation
B0048511biological_processrhythmic process
B0048678biological_processresponse to axon injury
B0051301biological_processcell division
B0055015biological_processventricular cardiac muscle cell development
B0060045biological_processpositive regulation of cardiac muscle cell proliferation
B0062033biological_processpositive regulation of mitotic sister chromatid segregation
B0065003biological_processprotein-containing complex assembly
B0070062cellular_componentextracellular exosome
B0070301biological_processcellular response to hydrogen peroxide
B0070371biological_processERK1 and ERK2 cascade
B0072686cellular_componentmitotic spindle
B0090166biological_processGolgi disassembly
B0097121cellular_componentcyclin A1-CDK1 complex
B0097122cellular_componentcyclin A2-CDK1 complex
B0097125cellular_componentcyclin B1-CDK1 complex
B0097472molecular_functioncyclin-dependent protein kinase activity
B0106310molecular_functionprotein serine kinase activity
B0120261biological_processregulation of heterochromatin organization
B1900182biological_processpositive regulation of protein localization to nucleus
B1902423biological_processregulation of attachment of mitotic spindle microtubules to kinetochore
B1902850biological_processmicrotubule cytoskeleton organization involved in mitosis
B1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
B2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
C0000082biological_processG1/S transition of mitotic cell cycle
C0000086biological_processG2/M transition of mitotic cell cycle
C0000922cellular_componentspindle pole
C0000940cellular_componentouter kinetochore
C0001556biological_processoocyte maturation
C0001701biological_processin utero embryonic development
C0005113molecular_functionpatched binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005759cellular_componentmitochondrial matrix
C0005813cellular_componentcentrosome
C0005815cellular_componentmicrotubule organizing center
C0005829cellular_componentcytosol
C0007052biological_processmitotic spindle organization
C0007080biological_processmitotic metaphase chromosome alignment
C0007283biological_processspermatogenesis
C0009410biological_processresponse to xenobiotic stimulus
C0009612biological_processresponse to mechanical stimulus
C0009636biological_processresponse to toxic substance
C0010629biological_processnegative regulation of gene expression
C0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
C0016020cellular_componentmembrane
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0019901molecular_functionprotein kinase binding
C0031442biological_processpositive regulation of mRNA 3'-end processing
C0042246biological_processtissue regeneration
C0044389molecular_functionubiquitin-like protein ligase binding
C0044772biological_processmitotic cell cycle phase transition
C0045787biological_processpositive regulation of cell cycle
C0045931biological_processpositive regulation of mitotic cell cycle
C0046680biological_processresponse to DDT
C0048146biological_processpositive regulation of fibroblast proliferation
C0048565biological_processdigestive tract development
C0051301biological_processcell division
C0051987biological_processpositive regulation of attachment of spindle microtubules to kinetochore
C0055015biological_processventricular cardiac muscle cell development
C0060045biological_processpositive regulation of cardiac muscle cell proliferation
C0060623biological_processregulation of chromosome condensation
C0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
C0065003biological_processprotein-containing complex assembly
C0071283biological_processcellular response to iron(III) ion
C0071398biological_processcellular response to fatty acid
C0071456biological_processcellular response to hypoxia
C0090266biological_processregulation of mitotic cell cycle spindle assembly checkpoint
C0097125cellular_componentcyclin B1-CDK1 complex
C1905448biological_processpositive regulation of mitochondrial ATP synthesis coupled electron transport
D0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0007346biological_processregulation of mitotic cell cycle
D0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
D0019005cellular_componentSCF ubiquitin ligase complex
D0019901molecular_functionprotein kinase binding
D0042393molecular_functionhistone binding
D0043130molecular_functionubiquitin binding
D0051301biological_processcell division
D0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkGrhkttgqv..........VAMK
ChainResidueDetails
BILE10-LYS33
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
BVAL124-ILE136
site_idPS00292
Number of Residues32
DetailsCYCLINS Cyclins signature. RaiLidWLvqvqmkfrLlqetMymTVsIIDRF
ChainResidueDetails
CARG202-PHE233
site_idPS00944
Number of Residues19
DetailsCKS_1 Cyclin-dependent kinases regulatory subunits signature 1. YSdKYdDEeFEYRHVmLPK
ChainResidueDetails
DTYR8-LYS26
site_idPS00945
Number of Residues11
DetailsCKS_2 Cyclin-dependent kinases regulatory subunits signature 2. HePEpHILLFR
ChainResidueDetails
DHIS60-ARG70
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues95
DetailsDomain: {"description":"Peptidase C50"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11747808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKR","evidences":[{"source":"PubMed","id":"20395957","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKMYT1","evidences":[{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19917613","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29606300","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7569953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CAK","evidences":[{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11440","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues11
DetailsRegion: {"description":"Interaction with CDK2"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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