Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7YXY

Cryo-EM structure of USP9X, local refinement of monomer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001764biological_processneuron migration
A0004197molecular_functioncysteine-type endopeptidase activity
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005929cellular_componentcilium
A0006307biological_processDNA alkylation repair
A0006508biological_processproteolysis
A0007059biological_processchromosome segregation
A0007179biological_processtransforming growth factor beta receptor signaling pathway
A0007292biological_processfemale gamete generation
A0008104biological_processprotein localization
A0008234molecular_functioncysteine-type peptidase activity
A0016020cellular_componentmembrane
A0016477biological_processcell migration
A0016562biological_processprotein import into peroxisome matrix, receptor recycling
A0016567biological_processprotein ubiquitination
A0016579biological_processprotein deubiquitination
A0030426cellular_componentgrowth cone
A0030509biological_processBMP signaling pathway
A0032092biological_processpositive regulation of protein binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0035520biological_processmonoubiquitinated protein deubiquitination
A0042752biological_processregulation of circadian rhythm
A0042995cellular_componentcell projection
A0048511biological_processrhythmic process
A0048675biological_processaxon extension
A0050821biological_processprotein stabilization
A0051301biological_processcell division
A0060271biological_processcilium assembly
A0061578molecular_functionK63-linked deubiquitinase activity
A0061824biological_processcytosolic ciliogenesis
A0070410molecular_functionco-SMAD binding
A0070536biological_processprotein K63-linked deubiquitination
A0071947biological_processprotein deubiquitination involved in ubiquitin-dependent protein catabolic process
A0101005molecular_functiondeubiquitinase activity
A0140313molecular_functionmolecular sequestering activity
A0180017molecular_functionK11-linked deubiquitinase activity
A1904515biological_processpositive regulation of TORC2 signaling
A1990000biological_processamyloid fibril formation
A1990380molecular_functionK48-linked deubiquitinase activity
Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLknaGAtCYMNSvIQ
ChainResidueDetails
AGLY1558-GLN1573

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YrLvGVlvHsGqasg..GHY
ChainResidueDetails
ATYR1863-TYR1880

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
ACYS1566

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AHIS1879

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER588

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR590

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1600

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2443

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR2540

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2547

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR2551

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon