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UniProtKB - P28062 (PSB8_HUMAN)

Entry version 225 (17 Jun 2020)
Sequence version 3 (31 May 2011)
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Protein

Proteasome subunit beta type-8

Gene

PSMB8

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

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (PubMed:27049119). Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes.5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleavage of peptide bonds with very broad specificity. EC:3.4.25.1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei73NucleophileBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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>Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processDifferentiation, Host-virus interaction, Immunity

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-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-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815 Ubiquitin-dependent degradation of Cyclin D
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-909733 Interferon alpha/beta signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

SIGNOR Signaling Network Open Resource

More...SIGNORi		P28062

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.015

<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%5Fand%5Ftaxonomy%5Fsection">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:
Proteasome subunit beta type-8 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 7
Macropain subunit C13
Multicatalytic endopeptidase complex subunit C13
Proteasome component C13
Proteasome subunit beta-5i
Really interesting new gene 10 protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PSMB8
Synonyms:LMP7, PSMB5i, RING10, Y2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000204264.8

Human Gene Nomenclature Database

More...HGNCi		HGNC:9545 PSMB8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		177046 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P28062

<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 & Seán O’Donoghue; Source: COMPARTMENTS

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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Proteasome-associated autoinflammatory syndrome 1 (PRAAS1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive autoinflammatory disorder characterized by early childhood onset of recurrent fever, joint stiffness and severe contractures of the hands and feet, and erythematous skin lesions with subsequent development of lipodystrophy and laboratory evidence of immune dysregulation. Accompanying features may include muscle weakness and atrophy, hepatosplenomegaly, and microcytic anemia.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06529175T → M in PRAAS1; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function; some patients are heterozygotes for this mutation and also carry a mutation in PSMA3; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome. 2 PublicationsCorresponds to variant dbSNP:rs748082671Ensembl.1
Natural variantiVAR_07525694A → P in PRAAS1; unknown pathological significance. 1 Publication1
Natural variantiVAR_075257105K → Q in PRAAS1; some patients are heterozygotes for this mutation and also carry a mutation in PSMB4. 1 PublicationCorresponds to variant dbSNP:rs1554239543EnsemblClinVar.1
Natural variantiVAR_066449201G → V in PRAAS1; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. 2 PublicationsCorresponds to variant dbSNP:rs387906680EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		5696

MalaCards human disease database

More...MalaCardsi		PSMB8
MIMi256040 phenotype

NIAGADS Genomics Database

More...NIAGADSi		ENSG00000204264

Open Targets

More...OpenTargetsi		ENSG00000204264

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		325004 CANDLE syndrome
324999 JMP syndrome
2615 Nakajo-Nishimura syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33890

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P28062 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5620

Drug and drug target database

More...DrugBanki		DB08889 Carfilzomib

DrugCentral

More...DrugCentrali		P28062

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2408

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PSMB8

Domain mapping of disease mutations (DMDM)

More...DMDMi		334302881

<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%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000265971 – 72Removed in mature formBy similarityAdd BLAST72
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002659873 – 276Proteasome subunit beta type-8Add BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: P28062-2)
<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 residuei5PhosphothreonineCurated1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei72 – 73Cleavage; by autolysisBy similarity2

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P28062

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P28062

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P28062

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

More...PaxDbi		P28062

PeptideAtlas

More...PeptideAtlasi		P28062

PRoteomics IDEntifications database

More...PRIDEi		P28062

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54437 [P28062-1]
54438 [P28062-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P28062

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

More...PhosphoSitePlusi		P28062

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P28062

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Highly expressed in immature dendritic cells (at protein level).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

Up-regulated by IFNG/IFN-gamma and IRF1 (at protein level). Up-regulated by TNF (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Down-regulated by the selective inhibitor PR-957. Down-regulated in mature dendritic cells by HSV-1 infection. Up-regulated by heat shock treatment.9 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000204264 Expressed in spleen and 185 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P28062 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P28062 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000204264 Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.

Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB5.

Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP.

Interacts with TAP1.

2 Publications

(Microbial infection) Interacts with HIV-1 TAT protein.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111669, 67 interactors

Protein interaction database and analysis system

More...IntActi		P28062, 26 interactors

Molecular INTeraction database

More...MINTi		P28062

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000364016

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P28062

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P28062 protein

<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

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P28062

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

<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 peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0175 Eukaryota
ENOG410XQRP LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157293

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_035750_7_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P28062

KEGG Orthology (KO)

More...KOi		K02740

Identification of Orthologs from Complete Genome Data

More...OMAi		ATIRVNK

Database for complete collections of gene phylogenies

More...PhylomeDBi		P28062

TreeFam database of animal gene trees

More...TreeFami		TF106223

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR035705 Proteasome_beta8
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF53 PTHR11599:SF53, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00227 Proteasome, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00141 PROTEASOME

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56235 SSF56235, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

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

Isoform 1 (identifier: P28062-1) [UniParc]FASTAAdd to basket
Also known as: LMP7B, LMP7-E2

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MALLDVCGAP RGQRPESALP VAGSGRRSDP GHYSFSMRSP ELALPRGMQP 
        60         70         80         90        100
TEFFQSLGGD GERNVQIEMA HGTTTLAFKF QHGVIAAVDS RASAGSYISA 
       110        120        130        140        150
LRVNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA 
       160        170        180        190        200
ASKLLSNMMC QYRGMGLSMG SMICGWDKKG PGLYYVDEHG TRLSGNMFST 
       210        220        230        240        250
GSGNTYAYGV MDSGYRPNLS PEEAYDLGRR AIAYATHRDS YSGGVVNMYH 
       260        270 
MKEDGWVKVE STDVSDLLHQ YREANQ
Length:276
Mass (Da):30,354
Last modified:May 31, 2011 - 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:i4F689501677DBD44
GO
Isoform 2 (identifier: P28062-2) [UniParc]FASTAAdd to basket
Also known as: LMP7A, LMP7-E1

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MALLDVCGAP...PELALPRGMQ → MLIGTPTPRD...PVSSGCPGLE

Show »
Length:272
Mass (Da):29,770
Checksum:iE5A903101BE5C0B7
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
X5D2R7X5D2R7_HUMAN
Proteasome subunit beta
PSMB8 PSM8
276Annotation score:

Annotation score:3 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>
Q5JNW7Q5JNW7_HUMAN
Proteasome subunit beta type-8
PSMB8
252Annotation 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>
A0A140T998A0A140T998_HUMAN
Proteasome subunit beta type-8
PSMB8
252Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0064888G → R in allele LMP7C. Corresponds to variant dbSNP:rs114772012EnsemblClinVar.1
Natural variantiVAR_00648930 – 32PGH → RPD in allele LPM7C. 3
Natural variantiVAR_06520449Q → K1 PublicationCorresponds to variant dbSNP:rs2071543EnsemblClinVar.1
Natural variantiVAR_05704674T → S. Corresponds to variant dbSNP:rs17220206EnsemblClinVar.1
Natural variantiVAR_06529175T → M in PRAAS1; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function; some patients are heterozygotes for this mutation and also carry a mutation in PSMA3; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome. 2 PublicationsCorresponds to variant dbSNP:rs748082671Ensembl.1
Natural variantiVAR_07525694A → P in PRAAS1; unknown pathological significance. 1 Publication1
Natural variantiVAR_075257105K → Q in PRAAS1; some patients are heterozygotes for this mutation and also carry a mutation in PSMB4. 1 PublicationCorresponds to variant dbSNP:rs1554239543EnsemblClinVar.1
Natural variantiVAR_066449201G → V in PRAAS1; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. 2 PublicationsCorresponds to variant dbSNP:rs387906680EnsemblClinVar.1

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_0052871 – 49MALLD…PRGMQ → MLIGTPTPRDTTPSSWLTSS LLVEAAPLDDTTLPTPVSSG CPGLE in isoform 2. 2 PublicationsAdd BLAST49

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
X66401 Genomic DNA Translation: CAA47026.1
X62598 mRNA Translation: CAA44482.1
Z14982 Genomic DNA Translation: CAA78705.1
Z14982 Genomic DNA Translation: CAA78706.1
L11045 Genomic DNA No translation available.
X87344 Genomic DNA Translation: CAA60786.1
X87344 Genomic DNA Translation: CAA60787.1
U17496 mRNA Translation: AAA56777.1
U17497 mRNA Translation: AAA56778.1
AL671681 Genomic DNA No translation available.
AL669918 Genomic DNA No translation available.
AL935043 Genomic DNA No translation available.
BX682530 Genomic DNA No translation available.
BX088556 Genomic DNA No translation available.
CT009502 Genomic DNA No translation available.
BX927138 Genomic DNA No translation available.
CR762476 Genomic DNA No translation available.
CR753889 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03644.1
CH471081 Genomic DNA Translation: EAX03645.1
BC001114 mRNA Translation: AAH01114.1
U32863 Genomic DNA Translation: AAA80235.1
U32862 Genomic DNA Translation: AAA80234.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4756.1 [P28062-2]
CCDS4757.1 [P28062-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A44324
C44324
G01564
G02018

NCBI Reference Sequences

More...RefSeqi		NP_004150.1, NM_004159.4 [P28062-2]
NP_683720.2, NM_148919.3 [P28062-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000374881; ENSP00000364015; ENSG00000204264 [P28062-2]
ENST00000374882; ENSP00000364016; ENSG00000204264 [P28062-1]
ENST00000383236; ENSP00000372723; ENSG00000206298 [P28062-1]
ENST00000383238; ENSP00000372725; ENSG00000206298 [P28062-2]
ENST00000416134; ENSP00000397057; ENSG00000235715 [P28062-2]
ENST00000416564; ENSP00000408825; ENSG00000226201 [P28062-2]
ENST00000421445; ENSP00000402406; ENSG00000236443 [P28062-1]
ENST00000429645; ENSP00000394155; ENSG00000226201 [P28062-1]
ENST00000435978; ENSP00000414731; ENSG00000231631 [P28062-2]
ENST00000436627; ENSP00000392693; ENSG00000230669 [P28062-2]
ENST00000438442; ENSP00000404585; ENSG00000231631 [P28062-1]
ENST00000441960; ENSP00000407539; ENSG00000230034 [P28062-2]
ENST00000452573; ENSP00000412618; ENSG00000236443 [P28062-2]
ENST00000455660; ENSP00000406797; ENSG00000230669 [P28062-1]
ENST00000457261; ENSP00000414770; ENSG00000235715 [P28062-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5696

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5696

UCSC genome browser

More...UCSCi		uc003ocf.4 human [P28062-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
X66401 Genomic DNA Translation: CAA47026.1
X62598 mRNA Translation: CAA44482.1
Z14982 Genomic DNA Translation: CAA78705.1
Z14982 Genomic DNA Translation: CAA78706.1
L11045 Genomic DNA No translation available.
X87344 Genomic DNA Translation: CAA60786.1
X87344 Genomic DNA Translation: CAA60787.1
U17496 mRNA Translation: AAA56777.1
U17497 mRNA Translation: AAA56778.1
AL671681 Genomic DNA No translation available.
AL669918 Genomic DNA No translation available.
AL935043 Genomic DNA No translation available.
BX682530 Genomic DNA No translation available.
BX088556 Genomic DNA No translation available.
CT009502 Genomic DNA No translation available.
BX927138 Genomic DNA No translation available.
CR762476 Genomic DNA No translation available.
CR753889 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03644.1
CH471081 Genomic DNA Translation: EAX03645.1
BC001114 mRNA Translation: AAH01114.1
U32863 Genomic DNA Translation: AAA80235.1
U32862 Genomic DNA Translation: AAA80234.1
CCDSiCCDS4756.1 [P28062-2]
CCDS4757.1 [P28062-1]
PIRiA44324
C44324
G01564
G02018
RefSeqiNP_004150.1, NM_004159.4 [P28062-2]
NP_683720.2, NM_148919.3 [P28062-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L5AX-ray2.40K/Y73-210[»]
5L5BX-ray2.80K/Y73-210[»]
5L5DX-ray2.80K/Y73-210[»]
5L5EX-ray2.90K/Y73-210[»]
5L5FX-ray2.50K/Y73-210[»]
5L5HX-ray2.60K/Y73-210[»]
5L5IX-ray2.90K/Y73-210[»]
5L5JX-ray2.90K/Y73-210[»]
5L5OX-ray2.60K/Y73-210[»]
5L5PX-ray2.80K/Y73-210[»]
5L5QX-ray2.80K/Y73-210[»]
5L5RX-ray2.90K/Y73-210[»]
5L5SX-ray2.60K/Y73-210[»]
5L5TX-ray2.90K/Y73-210[»]
5L5UX-ray2.60K/Y73-210[»]
5L5VX-ray2.70K/Y73-210[»]
5LTTX-ray2.70K/Y73-210[»]
5M2BX-ray2.70K/Y73-210[»]
6AVOelectron microscopy3.80C/D73-276[»]
6E5BX-ray2.77K/Y1-276[»]
SMRiP28062
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111669, 67 interactors
IntActiP28062, 26 interactors
MINTiP28062
STRINGi9606.ENSP00000364016

Chemistry databases

BindingDBiP28062
ChEMBLiCHEMBL5620
DrugBankiDB08889 Carfilzomib
DrugCentraliP28062
GuidetoPHARMACOLOGYi2408

Protein family/group databases

MEROPSiT01.015

PTM databases

iPTMnetiP28062
PhosphoSitePlusiP28062
SwissPalmiP28062

Polymorphism and mutation databases

BioMutaiPSMB8
DMDMi334302881

Proteomic databases

EPDiP28062
jPOSTiP28062
MassIVEiP28062
PaxDbiP28062
PeptideAtlasiP28062
PRIDEiP28062
ProteomicsDBi54437 [P28062-1]
54438 [P28062-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		28713 387 antibodies

The DNASU plasmid repository

More...DNASUi		5696

Genome annotation databases

EnsembliENST00000374881; ENSP00000364015; ENSG00000204264 [P28062-2]
ENST00000374882; ENSP00000364016; ENSG00000204264 [P28062-1]
ENST00000383236; ENSP00000372723; ENSG00000206298 [P28062-1]
ENST00000383238; ENSP00000372725; ENSG00000206298 [P28062-2]
ENST00000416134; ENSP00000397057; ENSG00000235715 [P28062-2]
ENST00000416564; ENSP00000408825; ENSG00000226201 [P28062-2]
ENST00000421445; ENSP00000402406; ENSG00000236443 [P28062-1]
ENST00000429645; ENSP00000394155; ENSG00000226201 [P28062-1]
ENST00000435978; ENSP00000414731; ENSG00000231631 [P28062-2]
ENST00000436627; ENSP00000392693; ENSG00000230669 [P28062-2]
ENST00000438442; ENSP00000404585; ENSG00000231631 [P28062-1]
ENST00000441960; ENSP00000407539; ENSG00000230034 [P28062-2]
ENST00000452573; ENSP00000412618; ENSG00000236443 [P28062-2]
ENST00000455660; ENSP00000406797; ENSG00000230669 [P28062-1]
ENST00000457261; ENSP00000414770; ENSG00000235715 [P28062-1]
GeneIDi5696
KEGGihsa:5696
UCSCiuc003ocf.4 human [P28062-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5696
DisGeNETi5696
EuPathDBiHostDB:ENSG00000204264.8

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMB8
HGNCiHGNC:9545 PSMB8
HPAiENSG00000204264 Low tissue specificity
MalaCardsiPSMB8
MIMi177046 gene
256040 phenotype
neXtProtiNX_P28062
NIAGADSiENSG00000204264
OpenTargetsiENSG00000204264
Orphaneti325004 CANDLE syndrome
324999 JMP syndrome
2615 Nakajo-Nishimura syndrome
PharmGKBiPA33890

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0175 Eukaryota
ENOG410XQRP LUCA
GeneTreeiENSGT00940000157293
HOGENOMiCLU_035750_7_1_1
InParanoidiP28062
KOiK02740
OMAiATIRVNK
PhylomeDBiP28062
TreeFamiTF106223

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-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815 Ubiquitin-dependent degradation of Cyclin D
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-909733 Interferon alpha/beta signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP28062

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5696 1 hit in 790 CRISPR screens

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

More...ChiTaRSi		PSMB8 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PSMB8

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

More...GenomeRNAii		5696
PharosiP28062 Tclin

Protein Ontology

More...PROi		PR:P28062
RNActiP28062 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000204264 Expressed in spleen and 185 other tissues
ExpressionAtlasiP28062 baseline and differential
GenevisibleiP28062 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR035705 Proteasome_beta8
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF53 PTHR11599:SF53, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PRINTSiPR00141 PROTEASOME
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiPSB8_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: P28062
Secondary accession number(s): B0UZC0
, Q29824, Q5JNW6, Q5QNR8, Q96J48
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 31, 2011
Last modified: June 17, 2020
This is version 225 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  7. Peptidase families
    Classification of peptidase families and list of entries
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