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Entry version 180 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • structural molecule activity Source: GO_Central

GO - Biological processi

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-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-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-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PSMD11
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000108671.9

Human Gene Nomenclature Database

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HGNCi
HGNC:9556 PSMD11

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604449 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O00231

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
5717

Open Targets

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OpenTargetsi
ENSG00000108671

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33902

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2364701

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PSMD11

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001738572 – 42226S proteasome non-ATPase regulatory subunit 11Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by AMPK.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O00231

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O00231

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O00231

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O00231

PeptideAtlas

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PeptideAtlasi
O00231

PRoteomics IDEntifications database

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PRIDEi
O00231

ProteomicsDB human proteome resource

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ProteomicsDBi
47796

2D gel databases

USC-OGP 2-DE database

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OGPi
O00231

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O00231

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O00231

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O00231

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000108671 Expressed in 232 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O00231 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O00231 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA042275
HPA067433

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT6Q96LA82EBI-357816,EBI-912440

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111689, 168 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O00231

Protein interaction database and analysis system

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IntActi
O00231, 70 interactors

Molecular INTeraction database

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MINTi
O00231

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000261712

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50Q1-422[»]
5GJRelectron microscopy3.504/Q1-422[»]
5L4Kelectron microscopy4.50Q1-422[»]
5LN3electron microscopy6.80Q1-422[»]
5M32electron microscopy3.80l1-422[»]
5T0Celectron microscopy3.80AX/BX1-422[»]
5T0Gelectron microscopy4.40X1-422[»]
5T0Helectron microscopy6.80X1-422[»]
5T0Ielectron microscopy8.00X1-422[»]
5T0Jelectron microscopy8.00X1-422[»]
5VFPelectron microscopy4.20X43-422[»]
5VFQelectron microscopy4.20X43-422[»]
5VFRelectron microscopy4.90X43-422[»]
5VFSelectron microscopy3.60X43-422[»]
5VFTelectron microscopy7.00X43-422[»]
5VFUelectron microscopy5.80X43-422[»]
5VGZelectron microscopy3.70X38-422[»]
5VHFelectron microscopy5.70X38-422[»]
5VHHelectron microscopy6.10X38-422[»]
5VHIelectron microscopy6.80X38-422[»]
5VHSelectron microscopy8.80X38-422[»]
6MSBelectron microscopy3.00X1-422[»]
6MSDelectron microscopy3.20X1-422[»]
6MSEelectron microscopy3.30F266-399[»]
6MSGelectron microscopy3.50X1-422[»]
6MSHelectron microscopy3.60X1-422[»]
6MSJelectron microscopy3.30X1-422[»]
6MSKelectron microscopy3.20X1-422[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O00231

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O00231

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini224 – 392PCIPROSITE-ProRule annotationAdd BLAST169

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the proteasome subunit S9 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1463 Eukaryota
COG5159 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063301

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000210093

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053738

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O00231

KEGG Orthology (KO)

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KOi
K03036

Identification of Orthologs from Complete Genome Data

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OMAi
DKVFYGV

Database of Orthologous Groups

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OrthoDBi
1052430at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O00231

TreeFam database of animal gene trees

More...
TreeFami
TF106230

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000717 PCI_dom
IPR035295 PSMD11
IPR040780 Rpn6_C_helix
IPR040773 Rpn6_N
IPR011990 TPR-like_helical_dom_sf
IPR036390 WH_DNA-bd_sf

The PANTHER Classification System

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PANTHERi
PTHR10678:SF6 PTHR10678:SF6, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01399 PCI, 1 hit
PF18503 RPN6_C_helix, 1 hit
PF18055 RPN6_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00088 PINT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF48452 SSF48452, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50250 PCI, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KSW3J3KSW3_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
45Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QS13J3QS13_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
90Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QRY4J3QRY4_HUMAN
26S proteasome non-ATPase regulator...
PSMD11
187Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti113C → S in AAB58732 (PubMed:9119060).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044400375H → HA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11272.1 [O00231-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC6524

NCBI Reference Sequences

More...
RefSeqi
NP_001257411.1, NM_001270482.1 [O00231-1]
NP_002806.2, NM_002815.3 [O00231-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.443379

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000261712; ENSP00000261712; ENSG00000108671 [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671 [O00231-1]
ENST00000649012; ENSP00000497128; ENSG00000108671 [O00231-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5717

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5717

UCSC genome browser

More...
UCSCi
uc002hhm.5 human [O00231-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

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[»]
5M32electron microscopy3.80l1-422[»]
5T0Celectron microscopy3.80AX/BX1-422[»]
5T0Gelectron microscopy4.40X1-422[»]
5T0Helectron microscopy6.80X1-422[»]
5T0Ielectron microscopy8.00X1-422[»]
5T0Jelectron microscopy8.00X1-422[»]
5VFPelectron microscopy4.20X43-422[»]
5VFQelectron microscopy4.20X43-422[»]
5VFRelectron microscopy4.90X43-422[»]
5VFSelectron microscopy3.60X43-422[»]
5VFTelectron microscopy7.00X43-422[»]
5VFUelectron microscopy5.80X43-422[»]
5VGZelectron microscopy3.70X38-422[»]
5VHFelectron microscopy5.70X38-422[»]
5VHHelectron microscopy6.10X38-422[»]
5VHIelectron microscopy6.80X38-422[»]
5VHSelectron microscopy8.80X38-422[»]
6MSBelectron microscopy3.00X1-422[»]
6MSDelectron microscopy3.20X1-422[»]
6MSEelectron microscopy3.30F266-399[»]
6MSGelectron microscopy3.50X1-422[»]
6MSHelectron microscopy3.60X1-422[»]
6MSJelectron microscopy3.30X1-422[»]
6MSKelectron microscopy3.20X1-422[»]
ProteinModelPortaliO00231
SMRiO00231
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111689, 168 interactors
CORUMiO00231
IntActiO00231, 70 interactors
MINTiO00231
STRINGi9606.ENSP00000261712

Chemistry databases

ChEMBLiCHEMBL2364701

PTM databases

iPTMnetiO00231
PhosphoSitePlusiO00231
SwissPalmiO00231

Polymorphism and mutation databases

BioMutaiPSMD11

2D gel databases

OGPiO00231

Proteomic databases

EPDiO00231
jPOSTiO00231
MaxQBiO00231
PaxDbiO00231
PeptideAtlasiO00231
PRIDEiO00231
ProteomicsDBi47796

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261712; ENSP00000261712; ENSG00000108671 [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671 [O00231-1]
ENST00000649012; ENSP00000497128; ENSG00000108671 [O00231-1]
GeneIDi5717
KEGGihsa:5717
UCSCiuc002hhm.5 human [O00231-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5717
DisGeNETi5717
EuPathDBiHostDB:ENSG00000108671.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PSMD11
HGNCiHGNC:9556 PSMD11
HPAiHPA042275
HPA067433
MIMi604449 gene
neXtProtiNX_O00231
OpenTargetsiENSG00000108671
PharmGKBiPA33902

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1463 Eukaryota
COG5159 LUCA
GeneTreeiENSGT00530000063301
HOGENOMiHOG000210093
HOVERGENiHBG053738
InParanoidiO00231
KOiK03036
OMAiDKVFYGV
OrthoDBi1052430at2759
PhylomeDBiO00231
TreeFamiTF106230

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-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-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-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PSMD11 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PSMD11

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5717

Protein Ontology

More...
PROi
PR:O00231

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000108671 Expressed in 232 organ(s), highest expression level in testis
ExpressionAtlasiO00231 baseline and differential
GenevisibleiO00231 HS

Family and domain databases

InterProiView protein in InterPro
IPR000717 PCI_dom
IPR035295 PSMD11
IPR040780 Rpn6_C_helix
IPR040773 Rpn6_N
IPR011990 TPR-like_helical_dom_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR10678:SF6 PTHR10678:SF6, 1 hit
PfamiView protein in Pfam
PF01399 PCI, 1 hit
PF18503 RPN6_C_helix, 1 hit
PF18055 RPN6_N, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPSD11_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O00231
Secondary accession number(s): A8K3I7
, E1P663, O00495, Q53FT5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 180 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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