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Protein

26S proteasome non-ATPase regulatory subunit 11

Gene

PSMD11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.2 Publications

GO - Molecular functioni

GO - Biological processi

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-446652. Interleukin-1 family signaling.
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-6798695. Neutrophil degranulation.
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-8941858. Regulation of RUNX3 expression and activity.
R-HSA-8948751. Regulation of PTEN stability and activity.
R-HSA-8951664. Neddylation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 11
Alternative name(s):
26S proteasome regulatory subunit RPN6
26S proteasome regulatory subunit S9
26S proteasome regulatory subunit p44.5
Gene namesi
Name:PSMD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108671.9.
HGNCiHGNC:9556. PSMD11.

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14S → A: Does not affect phosphorylation by AMPK; when associated with A-79 and A-272. 1 Publication1
Mutagenesisi79S → A: Does not affect phosphorylation by AMPK; when associated with A-14 and A-272. 1 Publication1
Mutagenesisi272S → A: Does not affect phosphorylation by AMPK; when associated with A14- and A-79. 1 Publication1

Organism-specific databases

DisGeNETi5717.
OpenTargetsiENSG00000108671.
PharmGKBiPA33902.

Chemistry databases

ChEMBLiCHEMBL2364701.

Polymorphism and mutation databases

BioMutaiPSMD11.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001738572 – 42226S proteasome non-ATPase regulatory subunit 11Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Phosphorylated by AMPK.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO00231.
MaxQBiO00231.
PaxDbiO00231.
PeptideAtlasiO00231.
PRIDEiO00231.

2D gel databases

OGPiO00231.

PTM databases

iPTMnetiO00231.
PhosphoSitePlusiO00231.
SwissPalmiO00231.

Expressioni

Tissue specificityi

Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate.1 Publication

Inductioni

By FOXO4; expression in embryonic stem cells (ESCs) is mediated by FOXO4.1 Publication

Gene expression databases

BgeeiENSG00000108671.
CleanExiHS_PSMD11.
ExpressionAtlasiO00231. baseline and differential.
GenevisibleiO00231. HS.

Organism-specific databases

HPAiHPA042275.
HPA067433.

Interactioni

Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD11, a base containing 6 ATPases and few additional components.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111689. 150 interactors.
CORUMiO00231.
IntActiO00231. 72 interactors.
MINTiMINT-1154929.
STRINGi9606.ENSP00000261712.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50Q1-422[»]
5GJRelectron microscopy3.504/Q1-422[»]
5L4Kelectron microscopy4.50Q1-422[»]
5LN3electron microscopy6.80Q1-422[»]
5T0Celectron microscopy3.80AX/BX1-422[»]
5T0Gelectron microscopy4.40X1-422[»]
5T0Helectron microscopy6.80X1-422[»]
5T0Ielectron microscopy8.00X1-422[»]
5T0Jelectron microscopy8.00X1-422[»]
ProteinModelPortaliO00231.
SMRiO00231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini222 – 389PCIAdd BLAST168

Sequence similaritiesi

Belongs to the proteasome subunit S9 family.Curated

Phylogenomic databases

eggNOGiKOG1463. Eukaryota.
COG5159. LUCA.
GeneTreeiENSGT00530000063301.
HOGENOMiHOG000210093.
HOVERGENiHBG053738.
InParanoidiO00231.
KOiK03036.
OMAiCKIMLGQ.
OrthoDBiEOG091G0B4C.
PhylomeDBiO00231.
TreeFamiTF106230.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiView protein in InterPro
IPR000717. PCI_dom.
IPR035295. PSMD11.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
PANTHERiPTHR10678:SF8. PTHR10678:SF8. 1 hit.
PfamiView protein in Pfam
PF01399. PCI. 1 hit.
SMARTiView protein in SMART
SM00088. PINT. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48452. SSF48452. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00231-1) [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
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI
60 70 80 90 100
LELGSLLAKT GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME
110 120 130 140 150
AATGQEVELC LECIEWAKSE KRTFLRQALE ARLVSLYFDT KRYQEALHLG
160 170 180 190 200
SQLLRELKKM DDKALLVEVQ LLESKTYHAL SNLPKARAAL TSARTTANAI
210 220 230 240 250
YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD SIDSPKAITS
260 270 280 290 300
LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
310 320 330 340 350
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI
360 370 380 390 400
SSLIKLSKAD VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA
410 420
LETIQNMSKV VDSLYNKAKK LT
Length:422
Mass (Da):47,464
Last modified:January 23, 2007 - v3
Checksum:iCE113054CBEBDB05
GO
Isoform 2 (identifier: O00231-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-375: H → HA

Note: No experimental confirmation available.
Show »
Length:423
Mass (Da):47,535
Checksum:iBDE786518637385D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113C → S in AAB58732 (PubMed:9119060).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044400375H → HA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001212 mRNA. Translation: AAB58732.1.
AB003102 mRNA. Translation: BAA19748.1.
AK290602 mRNA. Translation: BAF83291.1.
AK223196 mRNA. Translation: BAD96916.1.
CH471147 Genomic DNA. Translation: EAW80229.1.
CH471147 Genomic DNA. Translation: EAW80230.1.
BC000437 mRNA. Translation: AAH00437.1.
BC004430 mRNA. Translation: AAH04430.1.
CCDSiCCDS11272.1. [O00231-1]
PIRiJC6524.
RefSeqiNP_001257411.1. NM_001270482.1. [O00231-1]
NP_002806.2. NM_002815.3. [O00231-1]
UniGeneiHs.443379.

Genome annotation databases

EnsembliENST00000261712; ENSP00000261712; ENSG00000108671. [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671. [O00231-1]
GeneIDi5717.
KEGGihsa:5717.
UCSCiuc002hhm.5. human. [O00231-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPSD11_HUMAN
AccessioniPrimary (citable) accession number: O00231
Secondary accession number(s): A8K3I7
, E1P663, O00495, Q53FT5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 166 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families