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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5VHM

Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0016887molecular_functionATP hydrolysis activity
F0005524molecular_functionATP binding
F0016887molecular_functionATP hydrolysis activity
G0000122biological_processnegative regulation of transcription by RNA polymerase II
G0000502cellular_componentproteasome complex
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005929cellular_componentcilium
G0006357biological_processregulation of transcription by RNA polymerase II
G0006915biological_processapoptotic process
G0008540cellular_componentproteasome regulatory particle, base subcomplex
G0015630cellular_componentmicrotubule cytoskeleton
G0030307biological_processpositive regulation of cell growth
G0031398biological_processpositive regulation of protein ubiquitination
G0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
G0043066biological_processnegative regulation of apoptotic process
G0043409biological_processnegative regulation of MAPK cascade
G0043518biological_processnegative regulation of DNA damage response, signal transduction by p53 class mediator
G0045737biological_processpositive regulation of cyclin-dependent protein serine/threonine kinase activity
G0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
G0070682biological_processproteasome regulatory particle assembly
G0090201biological_processnegative regulation of release of cytochrome c from mitochondria
f0000502cellular_componentproteasome complex
f0005515molecular_functionprotein binding
f0005576cellular_componentextracellular region
f0005634cellular_componentnucleus
f0005654cellular_componentnucleoplasm
f0005829cellular_componentcytosol
f0005838cellular_componentproteasome regulatory particle
f0008540cellular_componentproteasome regulatory particle, base subcomplex
f0016020cellular_componentmembrane
f0022624cellular_componentproteasome accessory complex
f0030234molecular_functionenzyme regulator activity
f0034515cellular_componentproteasome storage granule
f0034774cellular_componentsecretory granule lumen
f0042176biological_processregulation of protein catabolic process
f0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
f0070062cellular_componentextracellular exosome
f1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. IkVLmATNrpdtLDpALm.R
ChainResidueDetails
AILE315-ARG333
EVAL273-ARG291
DVAL305-ARG323
BVAL325-ARG343
FVAL326-ARG344
CILE289-ARG307
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsRepeat: {"description":"ANK 2"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues32
DetailsRepeat: {"description":"ANK 3"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsRepeat: {"description":"ANK 4"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues32
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues32
DetailsRepeat: {"description":"ANK 6"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues42
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"17370265","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues33
DetailsRepeat: {"description":"PC 1"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues36
DetailsRepeat: {"description":"PC 2"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues34
DetailsRepeat: {"description":"PC 4"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues29
DetailsRepeat: {"description":"PC 5"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues11
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues48
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17323924","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17924679","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","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_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17323924","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17323924","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"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_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDM4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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