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2RO1

NMR Solution Structures of Human KAP1 PHD finger-bromodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003714molecular_functiontranscription corepressor activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
ACYS628
ACYS631
AHIS648

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS640
AGLN642
ACYS643
APHE645

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues42
DetailsZF_PHD_1 Zinc finger PHD-type signature. CrvCqkpgdl.......................................VmCnq..Cefc.FHldChlpalqdvpgee.................................WsCslC
ChainResidueDetails
ACYS628-CYS669

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues47
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AALA625-LEU672

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER683

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER689

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER697

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER752

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62318
ChainResidueDetails
ATYR755

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER757

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS770
ALYS774

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q62318
ChainResidueDetails
ALYS779

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER784

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:18488044
ChainResidueDetails
ALYS676

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS804

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS750
ALYS779

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS770
ALYS774

222036

PDB entries from 2024-07-03

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