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7X3X

Cryo-EM structure of N1 nucleosome-RA

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
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
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
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
V0000182molecular_functionrDNA binding
V0000976molecular_functiontranscription cis-regulatory region binding
V0001178biological_processregulation of transcriptional start site selection at RNA polymerase II promoter
V0003677molecular_functionDNA binding
V0003730molecular_functionmRNA 3'-UTR binding
V0004386molecular_functionhelicase activity
V0005515molecular_functionprotein binding
V0005524molecular_functionATP binding
V0005634cellular_componentnucleus
V0006325biological_processchromatin organization
V0006338biological_processchromatin remodeling
V0006354biological_processDNA-templated transcription elongation
V0006355biological_processregulation of DNA-templated transcription
V0006363biological_processtermination of RNA polymerase I transcription
V0006369biological_processtermination of RNA polymerase II transcription
V0007062biological_processsister chromatid cohesion
V0008094molecular_functionATP-dependent activity, acting on DNA
V0009408biological_processresponse to heat
V0016587cellular_componentIsw1 complex
V0016787molecular_functionhydrolase activity
V0016887molecular_functionATP hydrolysis activity
V0030874cellular_componentnucleolar chromatin
V0031491molecular_functionnucleosome binding
V0036436cellular_componentIsw1a complex
V0036437cellular_componentIsw1b complex
V0045944biological_processpositive regulation of transcription by RNA polymerase II
V0046832biological_processnegative regulation of RNA export from nucleus
V0140658molecular_functionATP-dependent chromatin remodeler activity
V1902275biological_processregulation of chromatin organization
V1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
HLYS2
HLYS9
HLYS12
HLYS17
AARG2
AARG17
EARG2
EARG17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR3
ETHR3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181
ChainResidueDetails
GLYS9
GLYS95
ALYS4
ELYS4

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
HLYS117
AGLN5
EGLN5

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
FLYS8
FLYS16
FLYS44
FLYS79
ATHR6
ATHR11
ETHR6
ETHR11

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250
ChainResidueDetails
FLYS12
FLYS20
AARG8
EARG8

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181
ChainResidueDetails
FLYS31
FLYS91
ALYS9
ELYS9

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119
ASER10
ESER10

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
FTYR51
FTYR88
ALYS14
ELYS14

site_idSWS_FT_FI10
Number of Residues10
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ELYS64
ALYS27
ALYS36
ALYS64
ELYS18
ELYS23
ELYS27
ELYS36
ALYS18
ALYS23

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AARG26
EARG26

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER28
ESER28

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
FLYS91
ALYS37
ELYS37

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATYR41
ETYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR80
ATHR107
ETHR80
ETHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ACYS110
ECYS110

219869

PDB entries from 2024-05-15

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