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6KIV

Cryo-EM structure of human MLL1-ubNCP complex (4.0 angstrom)

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
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
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
N0000976molecular_functiontranscription cis-regulatory region binding
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005730cellular_componentnucleolus
N0006325biological_processchromatin organization
N0006974biological_processDNA damage response
N0035097cellular_componenthistone methyltransferase complex
N0042393molecular_functionhistone binding
N0043627biological_processresponse to estrogen
N0044665cellular_componentMLL1/2 complex
N0044666cellular_componentMLL3/4 complex
N0045815biological_processtranscription initiation-coupled chromatin remodeling
N0048188cellular_componentSet1C/COMPASS complex
N0071339cellular_componentMLL1 complex
R0000122biological_processnegative regulation of transcription by RNA polymerase II
R0000123cellular_componenthistone acetyltransferase complex
R0001501biological_processskeletal system development
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0006094biological_processgluconeogenesis
R0006325biological_processchromatin organization
R0006355biological_processregulation of DNA-templated transcription
R0006357biological_processregulation of transcription by RNA polymerase II
R0035064molecular_functionmethylated histone binding
R0035097cellular_componenthistone methyltransferase complex
R0042393molecular_functionhistone binding
R0042800molecular_functionhistone H3K4 methyltransferase activity
R0044545cellular_componentNSL complex
R0044665cellular_componentMLL1/2 complex
R0044666cellular_componentMLL3/4 complex
R0045722biological_processpositive regulation of gluconeogenesis
R0045815biological_processtranscription initiation-coupled chromatin remodeling
R0045893biological_processpositive regulation of DNA-templated transcription
R0045995biological_processregulation of embryonic development
R0048188cellular_componentSet1C/COMPASS complex
R0051302biological_processregulation of cell division
R0051726biological_processregulation of cell cycle
R0071339cellular_componentMLL1 complex
R0072686cellular_componentmitotic spindle
R0090043biological_processregulation of tubulin deacetylation
R0140672cellular_componentATAC complex
T0048188cellular_componentSet1C/COMPASS complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue SAH K 4001
ChainResidue
KHIS3839
KARG3841
KTYR3883
KPHE3904
KASN3906
KHIS3907
KASN3958
KCYS3959
KLEU3968

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN K 4002
ChainResidue
KCYS3957
KCYS3959
KCYS3964

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

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

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
OLYS27-ASP52

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. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsdDkTLKIWDV
ChainResidueDetails
RLEU102-VAL116
RILE144-VAL158
RILE186-THR200
RILE274-LEU288

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250
ChainResidueDetails
CSER1
GSER1
EARG2
EARG17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
CLYS5
GLYS5

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS9
CLYS95
GLYS9
GLYS95

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS36
GLYS36
RLYS27
RLYS46

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS74
CLYS75
GLYS74
GLYS75
FLYS8
FLYS16
FLYS44
FLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N5-methylglutamine => ECO:0000250
ChainResidueDetails
CGLN104
GGLN104
FLYS12
FLYS20

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS118
GLYS118
FLYS31
FLYS91

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
ChainResidueDetails
CLYS13
ESER10
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119

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

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

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
ALYS37
ELYS37
FLYS91

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

229183

PDB entries from 2024-12-18

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