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1U35

Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
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
E0006325biological_processchromatin organization
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0032991cellular_componentprotein-containing complex
F0043505cellular_componentCENP-A containing nucleosome
F0045653biological_processnegative regulation of megakaryocyte differentiation
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
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
ALYS414-LEU420

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG1289-GLY1311

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO466-ILE474

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527
ChainResidueDetails
DPRO1198
HPRO1398
GLYS1009
GLYS1011

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: ADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DGLU1199
HGLU1399

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: ADP-ribosylserine => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DSER1203
HSER1403

site_idSWS_FT_FI4
Number of Residues10
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DLYS1208
HLYS1482
DLYS1212
DLYS1213
DLYS1217
DLYS1282
HLYS1408
HLYS1412
HLYS1413
HLYS1417

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
DLYS1209
HLYS1409
BARG35
GLYS1119
FGLY207
FARG235

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583
ChainResidueDetails
DSER1211
HSER1411

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS1220
DLYS1240
HLYS1420
HLYS1440
FASP268
FVAL270

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS1221
HLYS1421

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS1231
DLYS1313
HLYS1431
HLYS1513

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:32822587
ChainResidueDetails
DGLU1232
HGLU1432
EALA615
EASP723

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:20647423, ECO:0000269|PubMed:32822587
ChainResidueDetails
DSER1233
HSER1433

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DLYS1243
DLYS1305
HLYS1443
HLYS1505

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS1254
HLYS1454

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG1276
HARG1476
BILE50
BVAL70
FARG203
FGLY211
FILE250
FVAL270

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG1283
DARG1289
HARG1483
HARG1489

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR1312
HTHR1512

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS1317
HLYS1517
ESER657
ETHR680

site_idSWS_FT_FI18
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER1309
HSER1509

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
DLYS1217
HLYS1417

site_idSWS_FT_FI20
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62808
ChainResidueDetails
ASER487
DLYS1317
HLYS1517

site_idSWS_FT_FI21
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778
ChainResidueDetails
DLYS1231
HLYS1431

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
AARG516
EARG716

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: Phosphoarginine => ECO:0000305
ChainResidueDetails
AARG529
AILE530
EARG729
EILE730

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphoarginine => ECO:0000255
ChainResidueDetails
AGLY532
EGLY732

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
AGLN419
EGLN619

227561

PDB entries from 2024-11-20

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