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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9HJT

Structure of Zincore (SEPHS1:QRICH1) binding to ZFP91 on DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000981molecular_functionDNA-binding transcription factor activity, RNA polymerase II-specific
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0006357biological_processregulation of transcription by RNA polymerase II
A0007250biological_processactivation of NF-kappaB-inducing kinase activity
A0016567biological_processprotein ubiquitination
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0061630molecular_functionubiquitin protein ligase activity
A0070534biological_processprotein K63-linked ubiquitination
F0004756molecular_functionselenide, water dikinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005525molecular_functionGTP binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0005737cellular_componentcytoplasm
F0005886cellular_componentplasma membrane
F0016260biological_processL-selenocysteine biosynthetic process
F0031965cellular_componentnuclear membrane
F0036211biological_processprotein modification process
F0042802molecular_functionidentical protein binding
F0045454biological_processcell redox homeostasis
G0004756molecular_functionselenide, water dikinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005525molecular_functionGTP binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0005737cellular_componentcytoplasm
G0005886cellular_componentplasma membrane
G0016260biological_processL-selenocysteine biosynthetic process
G0031965cellular_componentnuclear membrane
G0036211biological_processprotein modification process
G0042802molecular_functionidentical protein binding
G0045454biological_processcell redox homeostasis
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0005737cellular_componentcytoplasm
H0005886cellular_componentplasma membrane
H0030968biological_processendoplasmic reticulum unfolded protein response
H0034976biological_processresponse to endoplasmic reticulum stress
H0036499biological_processPERK-mediated unfolded protein response
H0043065biological_processpositive regulation of apoptotic process
H0045893biological_processpositive regulation of DNA-templated transcription
H0070059biological_processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
H0140467biological_processintegrated stress response signaling
I0003677molecular_functionDNA binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005694cellular_componentchromosome
I0005737cellular_componentcytoplasm
I0005886cellular_componentplasma membrane
I0030968biological_processendoplasmic reticulum unfolded protein response
I0034976biological_processresponse to endoplasmic reticulum stress
I0036499biological_processPERK-mediated unfolded protein response
I0043065biological_processpositive regulation of apoptotic process
I0045893biological_processpositive regulation of DNA-templated transcription
I0070059biological_processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
I0140467biological_processintegrated stress response signaling
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues24
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. CemegCgtvLahprylqhHikyq.H
ChainResidueDetails
ACYS23-HIS46
ACYS54-HIS76
ACYS84-HIS104
ACYS112-HIS132
ACYS142-HIS163
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues25
DetailsZinc finger: {"description":"C2H2-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues24
DetailsZinc finger: {"description":"C2H2-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues23
DetailsZinc finger: {"description":"C2H2-type 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues30
DetailsRegion: {"description":"Interaction with MAP3K14/NIK","evidences":[{"source":"PubMed","id":"20682767","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40608935","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9HJT","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"9HJU","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19477186","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FD5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FD6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P16456","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsSite: {"description":"Arginine clamp","evidences":[{"source":"PubMed","id":"40608935","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

253389

PDB entries from 2026-05-13

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