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5T0M

A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading

Functional Information from GO Data
ChainGOidnamespacecontents
A0002039molecular_functionp53 binding
A0005634cellular_componentnucleus
A0008270molecular_functionzinc ion binding
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0042054molecular_functionhistone methyltransferase activity
B0002039molecular_functionp53 binding
B0005634cellular_componentnucleus
B0008270molecular_functionzinc ion binding
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0042054molecular_functionhistone methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1201
ChainResidue
ACYS974
ACYS987
ACYS1017
ACYS1021

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1202
ChainResidue
ACYS980
ACYS1017
ACYS1023
ACYS1027

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1203
ChainResidue
ACYS976
ACYS980
ACYS985
ACYS974

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1204
ChainResidue
ACYS1115
ACYS1168
ACYS1170
ACYS1175

site_idAC5
Number of Residues19
Detailsbinding site for residue SAM A 1205
ChainResidue
AMET1048
ATRP1050
ASER1084
ATYR1085
AARG1109
APHE1110
AILE1111
AASN1112
AHIS1113
ATYR1154
APHE1166
ATHR1167
ACYS1168
AGLN1169
ASAH1206
AHOH1404
AHOH1422
AHOH1423
AHOH1425

site_idAC6
Number of Residues19
Detailsbinding site for residue SAH A 1206
ChainResidue
AMET1048
ATRP1050
ASER1084
ATYR1085
AARG1109
APHE1110
AILE1111
AASN1112
AHIS1113
ATYR1154
APHE1166
ATHR1167
ACYS1168
AGLN1169
ASAM1205
AHOH1404
AHOH1422
AHOH1423
AHOH1425

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 1201
ChainResidue
BCYS974
BCYS987
BCYS1017
BCYS1021

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 1202
ChainResidue
BCYS980
BCYS1017
BCYS1023
BCYS1027

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 1203
ChainResidue
BCYS974
BCYS976
BCYS980
BCYS985

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 1204
ChainResidue
BCYS1115
BCYS1168
BCYS1170
BCYS1175

site_idAD2
Number of Residues18
Detailsbinding site for residue SAM B 1205
ChainResidue
BMET1048
BTRP1050
BSER1084
BTYR1085
BARG1109
BPHE1110
BILE1111
BASN1112
BHIS1113
BTYR1154
BPHE1158
BPHE1166
BTHR1167
BCYS1168
BGLN1169
BHOH1354
BHOH1402
BHOH1413

site_idAD3
Number of Residues16
Detailsbinding site for Di-peptide ARG C 8 and NLE C 9
ChainResidue
CLYS4
CTHR6
CALA7
CSER10
CHOH105
BTYR1067
BASP1074
BALA1077
BASP1078
BLEU1086
BPHE1087
BASP1088
BPHE1152
BTYR1154
BARG1157
BPHE1158

site_idAD4
Number of Residues11
Detailsbinding site for Di-peptide NLE C 9 and SER C 10
ChainResidue
BTYR1067
BLEU1086
BPHE1087
BASP1088
BASN1091
BPHE1152
BTYR1154
CARG8
CTHR11
CGLY12
CHOH105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
PARG2
AASP1082
AILE1119
ATHR1146
AGLU1149
BLYS1008
BGLU1010
BILE1014
BGLN1019
BCYS1021
BGLY1051
CARG2
BLEU1055
BTHR1057
BGLY1061
BASP1082
BILE1119
BTHR1146
BGLU1149
AILE1014
AGLN1019
ACYS1021
AGLY1051
ALEU1055
ATHR1057
AGLY1061

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
ChainResidueDetails
PTHR3
CTHR3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
PLYS4
CLYS4

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
PGLN5
CGLN5

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
PTHR6
CTHR6

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
ChainResidueDetails
PARG8
CARG8

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
PNLE9
CNLE9

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
ChainResidueDetails
PSER10
CSER10

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
ChainResidueDetails
PTHR11
CTHR11

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
PLYS14
CLYS14

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PDB entries from 2024-07-24

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