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Protein

26S proteasome non-ATPase regulatory subunit 9

Gene

PSMD9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process.1 Publication

Caution

Was initially identified as a component of the 26S proteasome.Curated

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL

GO - Biological processi

  • negative regulation of insulin secretion Source: BHF-UCL
  • positive regulation of insulin secretion Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • post-translational protein modification Source: Reactome
  • proteasome regulatory particle assembly Source: UniProtKB
  • protein deubiquitination Source: Reactome
  • ubiquitin-dependent protein catabolic process Source: UniProtKB

Keywordsi

Molecular functionChaperone

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 9
Alternative name(s):
26S proteasome regulatory subunit p27
Gene namesi
Name:PSMD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000110801.13
HGNCiHGNC:9567 PSMD9
MIMi603146 gene
neXtProtiNX_O00233

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

DisGeNETi5715
OpenTargetsiENSG00000110801
PharmGKBiPA33913

Polymorphism and mutation databases

BioMutaiPSMD9

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738521 – 22326S proteasome non-ATPase regulatory subunit 9Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei129PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO00233
MaxQBiO00233
PaxDbiO00233
PeptideAtlasiO00233
PRIDEiO00233
ProteomicsDBi47799
47800 [O00233-2]
TopDownProteomicsiO00233-1 [O00233-1]

2D gel databases

OGPiO00233

PTM databases

iPTMnetiO00233
PhosphoSitePlusiO00233

Expressioni

Tissue specificityi

Expressed in all tissues tested, highly expressed in liver and kidney.

Gene expression databases

BgeeiENSG00000110801
CleanExiHS_PSMD9
ExpressionAtlasiO00233 baseline and differential
GenevisibleiO00233 HS

Organism-specific databases

HPAiHPA040512
HPA044220

Interactioni

Subunit structurei

Interacts with PSMC3. Part of a transient complex (modulator) containing PSMD9, PSMC6 and PSMC3 formed during the assembly of the 26S proteasome.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111687, 99 interactors
CORUMiO00233
IntActiO00233, 24 interactors
MINTiO00233
STRINGi9606.ENSP00000440485

Structurei

3D structure databases

ProteinModelPortaliO00233
SMRiO00233
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini108 – 195PDZAdd BLAST88

Sequence similaritiesi

Belongs to the proteasome subunit p27 family.Curated

Phylogenomic databases

eggNOGiKOG3129 Eukaryota
COG0265 LUCA
GeneTreeiENSGT00390000004147
HOGENOMiHOG000216665
HOVERGENiHBG001851
InParanoidiO00233
KOiK06693
OMAiLGCNIVP
OrthoDBiEOG091G0N53
PhylomeDBiO00233
TreeFamiTF105995

Family and domain databases

InterProiView protein in InterPro
IPR001478 PDZ
IPR036034 PDZ_sf
IPR035269 PSMD9
PANTHERiPTHR12651 PTHR12651, 1 hit
PfamiView protein in Pfam
PF13180 PDZ_2, 1 hit
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform p27-L (identifier: O00233-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDEEARQSG GSSQAGVVTV SDVQELMRRK EEIEAQIKAN YDVLESQKGI
60 70 80 90 100
GMNEPLVDCE GYPRSDVDLY QVRTARHNII CLQNDHKAVM KQVEEALHQL
110 120 130 140 150
HARDKEKQAR DMAEAHKEAM SRKLGQSESQ GPPRAFAKVN SISPGSPASI
160 170 180 190 200
AGLQVDDEIV EFGSVNTQNF QSLHNIGSVV QHSEGKPLNV TVIRRGEKHQ
210 220
LRLVPTRWAG KGLLGCNIIP LQR
Length:223
Mass (Da):24,682
Last modified:January 11, 2011 - v3
Checksum:i98B3A623323A8F37
GO
Isoform p27-S (identifier: O00233-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     186-223: KPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR → ALAPTILLSVSMNLTTPGTSSRSP

Show »
Length:209
Mass (Da):22,764
Checksum:i0DA575AA7A0C5005
GO
Isoform 3 (identifier: O00233-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-151: Missing.

Note: No experimental confirmation available.
Show »
Length:118
Mass (Da):13,053
Checksum:i69E5EA1033F547B9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00995317V → ACombined sources2 PublicationsCorresponds to variant dbSNP:rs2230681Ensembl.1
Natural variantiVAR_05704774T → I. Corresponds to variant dbSNP:rs2291116Ensembl.1
Natural variantiVAR_057048134R → W. Corresponds to variant dbSNP:rs1177573Ensembl.1
Natural variantiVAR_057049197E → G. Corresponds to variant dbSNP:rs14259Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04600447 – 151Missing in isoform 3. 1 PublicationAdd BLAST105
Alternative sequenceiVSP_005300186 – 223KPLNV…IPLQR → ALAPTILLSVSMNLTTPGTS SRSP in isoform p27-S. 1 PublicationAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003177 mRNA Translation: BAA19790.1
AK315389 mRNA Translation: BAG37782.1
CB111716 mRNA No translation available.
AC069503 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW98296.1
BC002383 mRNA Translation: AAH02383.1
BC004184 mRNA Translation: AAH04184.1
BC004213 mRNA Translation: AAH04213.1
CCDSiCCDS58284.1 [O00233-3]
CCDS9225.1 [O00233-1]
RefSeqiNP_001248329.1, NM_001261400.2 [O00233-3]
NP_002804.2, NM_002813.6 [O00233-1]
UniGeneiHs.131151

Genome annotation databases

EnsembliENST00000537407; ENSP00000445058; ENSG00000110801 [O00233-2]
ENST00000541212; ENSP00000440485; ENSG00000110801 [O00233-1]
ENST00000542602; ENSP00000443772; ENSG00000110801 [O00233-3]
GeneIDi5715
KEGGihsa:5715
UCSCiuc001ubl.5 human [O00233-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSMD9_HUMAN
AccessioniPrimary (citable) accession number: O00233
Secondary accession number(s): B2RD35, G3V1Q6, Q9BQ42
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 11, 2011
Last modified: June 20, 2018
This is version 175 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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