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7M3X

Crystal Structure of the Apo Form of Human RBBP7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006355biological_processregulation of DNA-templated transcription
A0007420biological_processbrain development
A0016581cellular_componentNuRD complex
A0016589cellular_componentNURF complex
A0030308biological_processnegative regulation of cell growth
A0030336biological_processnegative regulation of cell migration
A0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
A0035098cellular_componentESC/E(Z) complex
A0042393molecular_functionhistone binding
A0042659biological_processregulation of cell fate specification
A0045892biological_processnegative regulation of DNA-templated transcription
A0045893biological_processpositive regulation of DNA-templated transcription
A0048545biological_processresponse to steroid hormone
A0070370biological_processcellular heat acclimation
A0070822cellular_componentSin3-type complex
A1902455biological_processnegative regulation of stem cell population maintenance
A1902459biological_processpositive regulation of stem cell population maintenance
A1904949cellular_componentATPase complex
A2000736biological_processregulation of stem cell differentiation
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTVCLWDI
ChainResidueDetails
ALEU192-ILE206
ALEU288-LEU302
ALEU332-LEU346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR10

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER95

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q60973
ChainResidueDetails
ALYS119

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60973
ChainResidueDetails
ALYS159

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER354

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS101
ALYS155

site_idSWS_FT_FI7
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
ALYS159

226707

PDB entries from 2024-10-30

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