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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9NB9

Viral protein DP71L in complex with phosphorylated eIF2alpha (NTD) and protein phosphatase 1A (D64A), stabilized by G-actin/DNAseI

Functional Information from GO Data
ChainGOidnamespacecontents
B0004865molecular_functionprotein serine/threonine phosphatase inhibitor activity
B0019888molecular_functionprotein phosphatase regulator activity
B0034976biological_processresponse to endoplasmic reticulum stress
B0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
B0039606biological_processsymbiont-mediated suppression of host translation initiation
B0052031biological_processsymbiont-mediated perturbation of host defense response
B0052170biological_processsymbiont-mediated suppression of host innate immune response
B0060255biological_processregulation of macromolecule metabolic process
B0080090biological_processregulation of primary metabolic process
C0000164cellular_componentprotein phosphatase type 1 complex
C0000781cellular_componentchromosome, telomeric region
C0001111biological_processRNA polymerase II promoter clearance
C0004721molecular_functionphosphoprotein phosphatase activity
C0004722molecular_functionprotein serine/threonine phosphatase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005829cellular_componentcytosol
C0005912cellular_componentadherens junction
C0005977biological_processglycogen metabolic process
C0005979biological_processregulation of glycogen biosynthetic process
C0005981biological_processregulation of glycogen catabolic process
C0006470biological_processprotein dephosphorylation
C0008157molecular_functionprotein phosphatase 1 binding
C0010288biological_processresponse to lead ion
C0016787molecular_functionhydrolase activity
C0016791molecular_functionphosphatase activity
C0032922biological_processcircadian regulation of gene expression
C0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
C0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
C0042587cellular_componentglycogen granule
C0042752biological_processregulation of circadian rhythm
C0043021molecular_functionribonucleoprotein complex binding
C0043025cellular_componentneuronal cell body
C0043153biological_processentrainment of circadian clock by photoperiod
C0043197cellular_componentdendritic spine
C0043204cellular_componentperikaryon
C0043247biological_processtelomere maintenance in response to DNA damage
C0043558biological_processregulation of translational initiation in response to stress
C0044877molecular_functionprotein-containing complex binding
C0045725biological_processpositive regulation of glycogen biosynthetic process
C0046579biological_processpositive regulation of Ras protein signal transduction
C0046872molecular_functionmetal ion binding
C0046914molecular_functiontransition metal ion binding
C0050821biological_processprotein stabilization
C0051301biological_processcell division
C0060828biological_processregulation of canonical Wnt signaling pathway
C0070062cellular_componentextracellular exosome
C0072357cellular_componentPTW/PP1 phosphatase complex
C0098609biological_processcell-cell adhesion
C0098641molecular_functioncadherin binding involved in cell-cell adhesion
C0098793cellular_componentpresynapse
C0098794cellular_componentpostsynapse
C0098978cellular_componentglutamatergic synapse
C0180007molecular_functionRNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
C2000806biological_processpositive regulation of termination of RNA polymerase II transcription, poly(A)-coupled
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016787molecular_functionhydrolase activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
CLEU121-GLU126
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
DTYR55-GLY65
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
DTRP358-GLU366
site_idPS00918
Number of Residues8
DetailsDNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS
ChainResidueDetails
EGLY189-SER196
site_idPS00919
Number of Residues21
DetailsDNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
ChainResidueDetails
EILE152-VAL172
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
DLEU106-ARG118
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsRegion: {"description":"Important for host CHOP inhibition","evidences":[{"source":"UniProtKB","id":"Q65212","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30100357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35830882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35831509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36175670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39446389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SW5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues25
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylcysteine; in intermediate form","evidences":[{"source":"UniProtKB","id":"P62737","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4976790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Involved in actin-binding","evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsSite: {"description":"Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1748997","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3560229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by HRI","evidences":[{"source":"UniProtKB","id":"P83268","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"38340717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails
DGLN61metal ligand
DVAL98electrostatic stabiliser
DPRO100electrostatic stabiliser, increase acidity, increase basicity
DASP156proton acceptor, proton donor
DTYR190metal ligand
DSER234electrostatic stabiliser, increase acidity, increase basicity
DALA274proton acceptor, proton donor

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PDB entries from 2026-01-07

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