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8EOA

Cryo-EM structure of human HSP90B-AIPL1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001890biological_processplacenta development
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006986biological_processresponse to unfolded protein
A0007004biological_processtelomere maintenance via telomerase
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0010033biological_processobsolete response to organic substance
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019062biological_processvirion attachment to host cell
A0019887molecular_functionprotein kinase regulator activity
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase binding
A0023026molecular_functionMHC class II protein complex binding
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
A0030911molecular_functionTPR domain binding
A0031072molecular_functionheat shock protein binding
A0031396biological_processregulation of protein ubiquitination
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032516biological_processpositive regulation of phosphoprotein phosphatase activity
A0032880biological_processregulation of protein localization
A0032991cellular_componentprotein-containing complex
A0034605biological_processcellular response to heat
A0034751cellular_componentaryl hydrocarbon receptor complex
A0034774cellular_componentsecretory granule lumen
A0042277molecular_functionpeptide binding
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042826molecular_functionhistone deacetylase binding
A0043008molecular_functionATP-dependent protein binding
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0044183molecular_functionprotein folding chaperone
A0044294cellular_componentdendritic growth cone
A0044295cellular_componentaxonal growth cone
A0045296molecular_functioncadherin binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0045597biological_processpositive regulation of cell differentiation
A0046983molecular_functionprotein dimerization activity
A0048156molecular_functiontau protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0051131biological_processchaperone-mediated protein complex assembly
A0051726biological_processregulation of cell cycle
A0060255biological_processregulation of macromolecule metabolic process
A0061077biological_processchaperone-mediated protein folding
A0070062cellular_componentextracellular exosome
A0070182molecular_functionDNA polymerase binding
A0071353biological_processcellular response to interleukin-4
A0097435biological_processsupramolecular fiber organization
A0097718molecular_functiondisordered domain specific binding
A0101031cellular_componentprotein folding chaperone complex
A0120293cellular_componentdynein axonemal particle
A0140662molecular_functionATP-dependent protein folding chaperone
A0141069molecular_functionreceptor ligand inhibitor activity
A1901799biological_processnegative regulation of proteasomal protein catabolic process
A1904813cellular_componentficolin-1-rich granule lumen
A1905323biological_processtelomerase holoenzyme complex assembly
A1990226molecular_functionhistone methyltransferase binding
A1990565cellular_componentHSP90-CDC37 chaperone complex
A2000010biological_processpositive regulation of protein localization to cell surface
B0001890biological_processplacenta development
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006986biological_processresponse to unfolded protein
B0007004biological_processtelomere maintenance via telomerase
B0008180cellular_componentCOP9 signalosome
B0009986cellular_componentcell surface
B0010033biological_processobsolete response to organic substance
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0019062biological_processvirion attachment to host cell
B0019887molecular_functionprotein kinase regulator activity
B0019900molecular_functionkinase binding
B0019901molecular_functionprotein kinase binding
B0023026molecular_functionMHC class II protein complex binding
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
B0030911molecular_functionTPR domain binding
B0031072molecular_functionheat shock protein binding
B0031396biological_processregulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032516biological_processpositive regulation of phosphoprotein phosphatase activity
B0032880biological_processregulation of protein localization
B0032991cellular_componentprotein-containing complex
B0034605biological_processcellular response to heat
B0034751cellular_componentaryl hydrocarbon receptor complex
B0034774cellular_componentsecretory granule lumen
B0042277molecular_functionpeptide binding
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042826molecular_functionhistone deacetylase binding
B0043008molecular_functionATP-dependent protein binding
B0043025cellular_componentneuronal cell body
B0043066biological_processnegative regulation of apoptotic process
B0044183molecular_functionprotein folding chaperone
B0044294cellular_componentdendritic growth cone
B0044295cellular_componentaxonal growth cone
B0045296molecular_functioncadherin binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0045597biological_processpositive regulation of cell differentiation
B0046983molecular_functionprotein dimerization activity
B0048156molecular_functiontau protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0051131biological_processchaperone-mediated protein complex assembly
B0051726biological_processregulation of cell cycle
B0060255biological_processregulation of macromolecule metabolic process
B0061077biological_processchaperone-mediated protein folding
B0070062cellular_componentextracellular exosome
B0070182molecular_functionDNA polymerase binding
B0071353biological_processcellular response to interleukin-4
B0097435biological_processsupramolecular fiber organization
B0097718molecular_functiondisordered domain specific binding
B0101031cellular_componentprotein folding chaperone complex
B0120293cellular_componentdynein axonemal particle
B0140662molecular_functionATP-dependent protein folding chaperone
B0141069molecular_functionreceptor ligand inhibitor activity
B1901799biological_processnegative regulation of proteasomal protein catabolic process
B1904813cellular_componentficolin-1-rich granule lumen
B1905323biological_processtelomerase holoenzyme complex assembly
B1990226molecular_functionhistone methyltransferase binding
B1990565cellular_componentHSP90-CDC37 chaperone complex
B2000010biological_processpositive regulation of protein localization to cell surface
C0001895biological_processretina homeostasis
C0001917cellular_componentphotoreceptor inner segment
C0001918molecular_functionfarnesylated protein binding
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006915biological_processapoptotic process
C0007603biological_processphototransduction, visible light
C0016607cellular_componentnuclear speck
C0022400biological_processregulation of opsin-mediated signaling pathway
C0043066biological_processnegative regulation of apoptotic process
Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR33-GLU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN46
ALYS107
APHE133
AARG392
BASN46
BLYS107
BPHE133
BARG392

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP88
BASP88

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleaved under oxidative stress => ECO:0000269|PubMed:22848402
ChainResidueDetails
AILE126
BILE126

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P11499
ChainResidueDetails
ALYS219
ALYS577
BLYS219
BLYS577

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER226
BSER226

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.12, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER255
BSER255

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11499
ChainResidueDetails
ASER261
BSER261

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR297
BTHR297

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:23585225
ChainResidueDetails
ATYR301
BTYR301

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11499
ChainResidueDetails
ATYR305
ATYR484
BTYR305
BTYR484

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER307
BSER307

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771
ChainResidueDetails
ALYS399
BLYS399

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS435
ALYS481
BLYS435
BLYS481

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER445
BSER445

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR479
BTHR479

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P11499
ChainResidueDetails
ALYS531
BLYS531

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-methylated lysine => ECO:0000269|PubMed:24880080
ChainResidueDetails
ALYS574
BLYS574

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000305|PubMed:19696785
ChainResidueDetails
ACYS590
BCYS590

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11499
ChainResidueDetails
ALYS624
BLYS624

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER669
BSER669

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PLK2 and PLK3 => ECO:0000269|PubMed:22828320
ChainResidueDetails
ASER718
BSER718

site_idSWS_FT_FI22
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250
ChainResidueDetails
ASER434
ASER452
BSER434
BSER452

222036

PDB entries from 2024-07-03

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