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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9RSX

Structure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
N20000077biological_processDNA damage checkpoint signaling
N20000165biological_processMAPK cascade
N20000287molecular_functionmagnesium ion binding
N20003723molecular_functionRNA binding
N20004674molecular_functionprotein serine/threonine kinase activity
N20004706molecular_functionJUN kinase kinase kinase activity
N20004709molecular_functionMAP kinase kinase kinase activity
N20005515molecular_functionprotein binding
N20005524molecular_functionATP binding
N20005634cellular_componentnucleus
N20005737cellular_componentcytoplasm
N20005829cellular_componentcytosol
N20006468biological_processprotein phosphorylation
N20006954biological_processinflammatory response
N20007059biological_processchromosome segregation
N20007254biological_processJNK cascade
N20008219biological_processcell death
N20030071biological_processregulation of mitotic metaphase/anaphase transition
N20030154biological_processcell differentiation
N20030295molecular_functionprotein kinase activator activity
N20031098biological_processstress-activated protein kinase signaling cascade
N20035556biological_processintracellular signal transduction
N20038066biological_processp38MAPK cascade
N20042733biological_processembryonic digit morphogenesis
N20043022molecular_functionribosome binding
N20043065biological_processpositive regulation of apoptotic process
N20043068biological_processpositive regulation of programmed cell death
N20046777biological_processprotein autophosphorylation
N20051403biological_processstress-activated MAPK cascade
N20060173biological_processlimb development
N20070181molecular_functionsmall ribosomal subunit rRNA binding
N20070269biological_processpyroptotic inflammatory response
N20071480biological_processcellular response to gamma radiation
N20071493biological_processcellular response to UV-B
N20106310molecular_functionprotein serine kinase activity
N20140469biological_processGCN2-mediated signaling
N21904291biological_processpositive regulation of mitotic DNA damage checkpoint
N30003723molecular_functionRNA binding
N30003730molecular_functionmRNA 3'-UTR binding
N30005515molecular_functionprotein binding
N30005634cellular_componentnucleus
N30005737cellular_componentcytoplasm
N30005829cellular_componentcytosol
N30016020cellular_componentmembrane
N30017148biological_processnegative regulation of translation
N30030371molecular_functiontranslation repressor activity
N30030578biological_processPML body organization
N30032183molecular_functionSUMO binding
N30043022molecular_functionribosome binding
N30043488biological_processregulation of mRNA stability
N30045296molecular_functioncadherin binding
N30048471cellular_componentperinuclear region of cytoplasm
N30061770molecular_functiontranslation elongation factor binding
N30070062cellular_componentextracellular exosome
N30141014biological_processribosome hibernation
RD0001228molecular_functionDNA-binding transcription activator activity, RNA polymerase II-specific
RD0002181biological_processcytoplasmic translation
RD0002183biological_processcytoplasmic translational initiation
RD0003677molecular_functionDNA binding
RD0003684molecular_functiondamaged DNA binding
RD0003723molecular_functionRNA binding
RD0003729molecular_functionmRNA binding
RD0003735molecular_functionstructural constituent of ribosome
RD0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
RD0004520molecular_functionDNA endonuclease activity
RD0005515molecular_functionprotein binding
RD0005634cellular_componentnucleus
RD0005654cellular_componentnucleoplasm
RD0005730cellular_componentnucleolus
RD0005737cellular_componentcytoplasm
RD0005743cellular_componentmitochondrial inner membrane
RD0005759cellular_componentmitochondrial matrix
RD0005783cellular_componentendoplasmic reticulum
RD0005819cellular_componentspindle
RD0005829cellular_componentcytosol
RD0005840cellular_componentribosome
RD0005886cellular_componentplasma membrane
RD0005925cellular_componentfocal adhesion
RD0006281biological_processDNA repair
RD0006284biological_processbase-excision repair
RD0006974biological_processDNA damage response
RD0007059biological_processchromosome segregation
RD0008017molecular_functionmicrotubule binding
RD0010628biological_processpositive regulation of gene expression
RD0014069cellular_componentpostsynaptic density
RD0015631molecular_functiontubulin binding
RD0016020cellular_componentmembrane
RD0017148biological_processnegative regulation of translation
RD0019104molecular_functionDNA N-glycosylase activity
RD0019899molecular_functionenzyme binding
RD0019900molecular_functionkinase binding
RD0019901molecular_functionprotein kinase binding
RD0022626cellular_componentcytosolic ribosome
RD0022627cellular_componentcytosolic small ribosomal subunit
RD0030544molecular_functionHsp70 protein binding
RD0031116biological_processpositive regulation of microtubule polymerization
RD0031397biological_processnegative regulation of protein ubiquitination
RD0032357molecular_functionoxidized purine DNA binding
RD0032358molecular_functionoxidized pyrimidine DNA binding
RD0032587cellular_componentruffle membrane
RD0034614biological_processcellular response to reactive oxygen species
RD0042981biological_processregulation of apoptotic process
RD0044390molecular_functionubiquitin-like protein conjugating enzyme binding
RD0045202cellular_componentsynapse
RD0045738biological_processnegative regulation of DNA repair
RD0045739biological_processpositive regulation of DNA repair
RD0045944biological_processpositive regulation of transcription by RNA polymerase II
RD0051018molecular_functionprotein kinase A binding
RD0051225biological_processspindle assembly
RD0051536molecular_functioniron-sulfur cluster binding
RD0051879molecular_functionHsp90 protein binding
RD0061481biological_processresponse to TNF agonist
RD0070062cellular_componentextracellular exosome
RD0070181molecular_functionsmall ribosomal subunit rRNA binding
RD0070301biological_processcellular response to hydrogen peroxide
RD0071159cellular_componentNF-kappaB complex
RD0072686cellular_componentmitotic spindle
RD0097100molecular_functionsupercoiled DNA binding
RD0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
RD0140297molecular_functionDNA-binding transcription factor binding
RD1901224biological_processpositive regulation of non-canonical NF-kappaB signal transduction
RD1902231biological_processpositive regulation of intrinsic apoptotic signaling pathway in response to DNA damage
RD1905053biological_processpositive regulation of base-excision repair
RD1990904cellular_componentribonucleoprotein complex
RD2000144biological_processpositive regulation of DNA-templated transcription initiation
RD2001235biological_processpositive regulation of apoptotic signaling pathway
Rg0001891cellular_componentphagocytic cup
Rg0001934biological_processpositive regulation of protein phosphorylation
Rg0002181biological_processcytoplasmic translation
Rg0003723molecular_functionRNA binding
Rg0005080molecular_functionprotein kinase C binding
Rg0005102molecular_functionsignaling receptor binding
Rg0005515molecular_functionprotein binding
Rg0005634cellular_componentnucleus
Rg0005654cellular_componentnucleoplasm
Rg0005737cellular_componentcytoplasm
Rg0005739cellular_componentmitochondrion
Rg0005829cellular_componentcytosol
Rg0005886cellular_componentplasma membrane
Rg0008047molecular_functionenzyme activator activity
Rg0008200molecular_functionion channel inhibitor activity
Rg0010629biological_processnegative regulation of gene expression
Rg0015935cellular_componentsmall ribosomal subunit
Rg0016567biological_processprotein ubiquitination
Rg0017148biological_processnegative regulation of translation
Rg0019899molecular_functionenzyme binding
Rg0019903molecular_functionprotein phosphatase binding
Rg0022627cellular_componentcytosolic small ribosomal subunit
Rg0030178biological_processnegative regulation of Wnt signaling pathway
Rg0030291molecular_functionprotein serine/threonine kinase inhibitor activity
Rg0030292molecular_functionprotein tyrosine kinase inhibitor activity
Rg0030308biological_processnegative regulation of cell growth
Rg0030332molecular_functioncyclin binding
Rg0030335biological_processpositive regulation of cell migration
Rg0030425cellular_componentdendrite
Rg0030496cellular_componentmidbody
Rg0030971molecular_functionreceptor tyrosine kinase binding
Rg0031334biological_processpositive regulation of protein-containing complex assembly
Rg0032091biological_processnegative regulation of protein binding
Rg0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Rg0032880biological_processregulation of protein localization
Rg0035591molecular_functionsignaling adaptor activity
Rg0042169molecular_functionSH2 domain binding
Rg0042802molecular_functionidentical protein binding
Rg0042803molecular_functionprotein homodimerization activity
Rg0042998biological_processpositive regulation of Golgi to plasma membrane protein transport
Rg0043005cellular_componentneuron projection
Rg0043022molecular_functionribosome binding
Rg0043025cellular_componentneuronal cell body
Rg0043065biological_processpositive regulation of apoptotic process
Rg0043204cellular_componentperikaryon
Rg0043547biological_processpositive regulation of GTPase activity
Rg0044297cellular_componentcell body
Rg0045296molecular_functioncadherin binding
Rg0045879biological_processnegative regulation of smoothened signaling pathway
Rg0048471cellular_componentperinuclear region of cytoplasm
Rg0050765biological_processnegative regulation of phagocytosis
Rg0051302biological_processregulation of cell division
Rg0051434molecular_functionBH3 domain binding
Rg0051726biological_processregulation of cell cycle
Rg0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Rg0060090molecular_functionmolecular adaptor activity
Rg0070062cellular_componentextracellular exosome
Rg0071333biological_processcellular response to glucose stimulus
Rg0071363biological_processcellular response to growth factor stimulus
Rg0072344biological_processrescue of stalled cytosolic ribosome
Rg0106070biological_processregulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
Rg1900102biological_processnegative regulation of endoplasmic reticulum unfolded protein response
Rg1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
Rg1990630cellular_componentIRE1-RACK1-PP2A complex
Rg2000114biological_processregulation of establishment of cell polarity
Rg2000543biological_processpositive regulation of gastrulation
Rg2001125biological_processnegative regulation of translational frameshifting
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKsrNVVI
ChainResidueDetails
N2VAL129-ILE141
site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKsmkfvdGlMihSgdpVnyyVDtavrhvlLrqGvlG
ChainResidueDetails
RDALA147-GLY183
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ALSGswDgTLRLWDL
ChainResidueDetails
RgALA78-LEU92
RgILE120-THR134
RgILE165-LEU179
RgCYS207-LEU221
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21871177","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16807684","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues31
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues30
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues32
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues30
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues29
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues30
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Kanor S.","Tissot J.-D.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"19423701","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"11279199","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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