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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7SSA

Cryo-EM structure of pioneer factor Cbf1 bound to the nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006281biological_processDNA repair
C0006325biological_processchromatin organization
C0006974biological_processDNA damage response
C0030527molecular_functionstructural constituent of chromatin
C0031298cellular_componentreplication fork protection complex
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006301biological_processpostreplication repair
D0006325biological_processchromatin organization
D0006355biological_processregulation of DNA-templated transcription
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000122biological_processnegative regulation of transcription by RNA polymerase II
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006281biological_processDNA repair
G0006325biological_processchromatin organization
G0006974biological_processDNA damage response
G0030527molecular_functionstructural constituent of chromatin
G0031298cellular_componentreplication fork protection complex
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
H0000122biological_processnegative regulation of transcription by RNA polymerase II
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0006301biological_processpostreplication repair
H0006325biological_processchromatin organization
H0006355biological_processregulation of DNA-templated transcription
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
K0000122biological_processnegative regulation of transcription by RNA polymerase II
K0000775cellular_componentchromosome, centromeric region
K0000776cellular_componentkinetochore
K0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
K0001227molecular_functionDNA-binding transcription repressor activity, RNA polymerase II-specific
K0001228molecular_functionDNA-binding transcription activator activity, RNA polymerase II-specific
K0003677molecular_functionDNA binding
K0003700molecular_functionDNA-binding transcription factor activity
K0005634cellular_componentnucleus
K0005694cellular_componentchromosome
K0005739cellular_componentmitochondrion
K0006338biological_processchromatin remodeling
K0006357biological_processregulation of transcription by RNA polymerase II
K0007059biological_processchromosome segregation
K0019237molecular_functioncentromeric DNA binding
K0042762biological_processregulation of sulfur metabolic process
K0045944biological_processpositive regulation of transcription by RNA polymerase II
K0046983molecular_functionprotein dimerization activity
K0061431biological_processcellular response to methionine
K0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
K0089713cellular_componentCbf1-Met4-Met28 complex
K1900059biological_processpositive regulation of sulfate assimilation
K1900060biological_processnegative regulation of ceramide biosynthetic process
K1900090biological_processpositive regulation of inositol biosynthetic process
L0000122biological_processnegative regulation of transcription by RNA polymerase II
L0000775cellular_componentchromosome, centromeric region
L0000776cellular_componentkinetochore
L0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
L0001227molecular_functionDNA-binding transcription repressor activity, RNA polymerase II-specific
L0001228molecular_functionDNA-binding transcription activator activity, RNA polymerase II-specific
L0003677molecular_functionDNA binding
L0003700molecular_functionDNA-binding transcription factor activity
L0005634cellular_componentnucleus
L0005694cellular_componentchromosome
L0005739cellular_componentmitochondrion
L0006338biological_processchromatin remodeling
L0006357biological_processregulation of transcription by RNA polymerase II
L0007059biological_processchromosome segregation
L0019237molecular_functioncentromeric DNA binding
L0042762biological_processregulation of sulfur metabolic process
L0045944biological_processpositive regulation of transcription by RNA polymerase II
L0046983molecular_functionprotein dimerization activity
L0061431biological_processcellular response to methionine
L0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
L0089713cellular_componentCbf1-Met4-Met28 complex
L1900059biological_processpositive regulation of sulfate assimilation
L1900060biological_processnegative regulation of ceramide biosynthetic process
L1900090biological_processpositive regulation of inositol biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. SQEL
ChainResidueDetails
CSER128-LEU131
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLtFPV
ChainResidueDetails
CALA22-VAL28
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlILpGELaKHAVSEG
ChainResidueDetails
DARG95-GLY117
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"source":"PubMed","id":"24352239","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsSite: {"description":"Not ubiquitinated","evidences":[{"source":"PubMed","id":"10642555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2201907","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"10642555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12535538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12535539","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14660635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15280549","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16432255","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues96
DetailsDomain: {"description":"bHLH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00981","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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