Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZMS

LSD1-CoREST in complex with INSM1 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0000118cellular_componenthistone deacetylase complex
B0003682molecular_functionchromatin binding
B0003714molecular_functiontranscription corepressor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005667cellular_componenttranscription regulator complex
B0006325biological_processchromatin organization
B0006357biological_processregulation of transcription by RNA polymerase II
B0010629biological_processnegative regulation of gene expression
B0017053cellular_componenttranscription repressor complex
B0019899molecular_functionenzyme binding
B0030218biological_processerythrocyte differentiation
B0045654biological_processpositive regulation of megakaryocyte differentiation
B0045892biological_processnegative regulation of DNA-templated transcription
B1990391cellular_componentDNA repair complex
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
C0001227molecular_functionDNA-binding transcription repressor activity, RNA polymerase II-specific
C0001933biological_processnegative regulation of protein phosphorylation
C0003309biological_processtype B pancreatic cell differentiation
C0003310biological_processpancreatic A cell differentiation
C0003323biological_processtype B pancreatic cell development
C0003358biological_processnoradrenergic neuron development
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0007049biological_processcell cycle
C0007399biological_processnervous system development
C0008283biological_processcell population proliferation
C0008284biological_processpositive regulation of cell population proliferation
C0008285biological_processnegative regulation of cell population proliferation
C0010468biological_processregulation of gene expression
C0010564biological_processregulation of cell cycle process
C0016477biological_processcell migration
C0017053cellular_componenttranscription repressor complex
C0030154biological_processcell differentiation
C0030182biological_processneuron differentiation
C0030332molecular_functioncyclin binding
C0030335biological_processpositive regulation of cell migration
C0031018biological_processendocrine pancreas development
C0031490molecular_functionchromatin DNA binding
C0035270biological_processendocrine system development
C0042421biological_processnorepinephrine biosynthetic process
C0042826molecular_functionhistone deacetylase binding
C0043254biological_processregulation of protein-containing complex assembly
C0045597biological_processpositive regulation of cell differentiation
C0046872molecular_functionmetal ion binding
C0051726biological_processregulation of cell cycle
C0060090molecular_functionmolecular adaptor activity
C0060290biological_processtransdifferentiation
C0061104biological_processadrenal chromaffin cell differentiation
C0061549biological_processsympathetic ganglion development
C2000179biological_processpositive regulation of neural precursor cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 900
ChainResidue
AGLY285
AGLY315
AARG316
ALEU329
AGLY330
AALA331
AMET332
AVAL333
ATHR588
AVAL590
ATHR624
AGLY287
ALEU625
APRO626
AVAL637
ALEU659
ATRP756
ASER760
ATYR761
AGLY800
AGLU801
AALA809
AVAL288
ATHR810
AVAL811
AALA814
CPHE4
ASER289
ALEU307
AGLU308
AALA309
AARG310
AGLY314

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues21
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cpe..CakvFscpanlasHrrw..H
ChainResidueDetails
CCYS296-HIS316
CCYS368-HIS389
CCYS442-HIS463
CCYS470-HIS491

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsZN_FING: C2H2-type 1; atypical => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
CPHE266-CYS286
AGLU308
AARG310
AARG316
AMET332
AGLU801
ATHR810

site_idSWS_FT_FI2
Number of Residues22
DetailsZN_FING: C2H2-type 2 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
CTYR294-HIS316

site_idSWS_FT_FI3
Number of Residues22
DetailsZN_FING: C2H2-type 3 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
CTYR366-HIS388

site_idSWS_FT_FI4
Number of Residues23
DetailsZN_FING: C2H2-type 4 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
CHIS440-HIS463
BLYS297
BGLU466

site_idSWS_FT_FI5
Number of Residues23
DetailsZN_FING: C2H2-type 5 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
CPHE468-HIS491

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR115

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER117

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER146

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER611

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER849

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS442
ALYS469

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:25018020
ChainResidueDetails
ALYS503

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon