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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5UQ3

Crystal structure of human Cdk2-Spy1-P27 ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000086biological_processG2/M transition of mitotic cell cycle
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000781cellular_componentchromosome, telomeric region
A0000793cellular_componentcondensed chromosome
A0000805cellular_componentX chromosome
A0000806cellular_componentY chromosome
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0007099biological_processcentriole replication
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0007346biological_processregulation of mitotic cell cycle
A0008284biological_processpositive regulation of cell population proliferation
A0015030cellular_componentCajal body
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0019904molecular_functionprotein domain specific binding
A0030332molecular_functioncyclin binding
A0031453biological_processpositive regulation of heterochromatin formation
A0031571biological_processmitotic G1 DNA damage checkpoint signaling
A0035173molecular_functionhistone kinase activity
A0043247biological_processtelomere maintenance in response to DNA damage
A0043687biological_processpost-translational protein modification
A0045740biological_processpositive regulation of DNA replication
A0046872molecular_functionmetal ion binding
A0051298biological_processcentrosome duplication
A0051301biological_processcell division
A0051321biological_processmeiotic cell cycle
A0071732biological_processcellular response to nitric oxide
A0090398biological_processcellular senescence
A0097123cellular_componentcyclin A1-CDK2 complex
A0097124cellular_componentcyclin A2-CDK2 complex
A0097134cellular_componentcyclin E1-CDK2 complex
A0097135cellular_componentcyclin E2-CDK2 complex
A0097472molecular_functioncyclin-dependent protein kinase activity
A0106310molecular_functionprotein serine kinase activity
A0120186biological_processnegative regulation of protein localization to chromatin
A0120261biological_processregulation of heterochromatin organization
A1905784biological_processregulation of anaphase-promoting complex-dependent catabolic process
B0019901molecular_functionprotein kinase binding
B0045737biological_processpositive regulation of cyclin-dependent protein serine/threonine kinase activity
C0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
C0000082biological_processG1/S transition of mitotic cell cycle
C0004860molecular_functionprotein kinase inhibitor activity
C0004861molecular_functioncyclin-dependent protein serine/threonine kinase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005768cellular_componentendosome
C0005829cellular_componentcytosol
C0007165biological_processsignal transduction
C0007507biological_processheart development
C0008285biological_processnegative regulation of cell population proliferation
C0012501biological_processprogrammed cell death
C0019901molecular_functionprotein kinase binding
C0019903molecular_functionprotein phosphatase binding
C0019914molecular_functioncyclin-dependent protein kinase regulator activity
C0030308biological_processnegative regulation of cell growth
C0030330biological_processDNA damage response, signal transduction by p53 class mediator
C0030332molecular_functioncyclin binding
C0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
C0031625molecular_functionubiquitin protein ligase binding
C0044877molecular_functionprotein-containing complex binding
C0045732biological_processpositive regulation of protein catabolic process
C0045740biological_processpositive regulation of DNA replication
C0045926biological_processnegative regulation of growth
C0045930biological_processnegative regulation of mitotic cell cycle
C0048102biological_processautophagic cell death
C0050680biological_processnegative regulation of epithelial cell proliferation
C0051087molecular_functionprotein-folding chaperone binding
C0051168biological_processnuclear export
C0051726biological_processregulation of cell cycle
C0060090molecular_functionmolecular adaptor activity
C0071285biological_processcellular response to lithium ion
C0090398biological_processcellular senescence
C0140678molecular_functionmolecular function inhibitor activity
C1901990biological_processregulation of mitotic cell cycle phase transition
C1902806biological_processregulation of cell cycle G1/S phase transition
C1904706biological_processnegative regulation of vascular associated smooth muscle cell proliferation
C1905179biological_processnegative regulation of cardiac muscle tissue regeneration
C1990757molecular_functionubiquitin ligase activator activity
C2000045biological_processregulation of G1/S transition of mitotic cell cycle
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK
ChainResidueDetails
AILE10-LYS33
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
ChainResidueDetails
AVAL123-ILE135
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"CDK7 binding","evidences":[{"source":"PubMed","id":"17373709","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CAK and CCRK","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14597612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17570665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues132
DetailsRegion: {"description":"Speedy/Ringo box; Required for CDK-binding","evidences":[{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsRegion: {"description":"Interaction with CDK2","evidences":[{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"17254967","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL, LYN, SRC and JAK2","evidences":[{"source":"PubMed","id":"16195327","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17254966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17254967","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21423214","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16195327","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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