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UniProtKB - P20618 (PSB1_HUMAN)

Protein

Proteasome subunit beta type-1

Gene

PSMB1

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 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<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

  • endopeptidase activity Source: GO_Central
  • threonine-type endopeptidase activity Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 processHost-virus interaction

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

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.986

<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:
Proteasome subunit beta type-1 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain
<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:PSMB1
Synonyms:PSC5
<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 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_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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000008018.8

Human Gene Nomenclature Database

More...HGNCi		HGNC:9537 PSMB1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602017 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P20618

<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

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

Organism-specific databases

DisGeNET

More...DisGeNETi		5689

Open Targets

More...OpenTargetsi		ENSG00000008018

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33882

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4208

Drug and drug target database

More...DrugBanki		DB00188 Bortezomib
DB08889 Carfilzomib

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2404

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PSMB1

Domain mapping of disease mutations (DMDM)

More...DMDMi		130853

<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 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_00002596231 – 281 PublicationAdd BLAST28
<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_000014803029 – 241Proteasome subunit beta type-1Add BLAST213

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 residuei1N-acetylmethionineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi58O-linked (GlcNAc) serineBy similarity1
Modified residuei62PhosphoserineCombined sources1
Modified residuei68PhosphoserineCombined sources1
Modified residuei150PhosphotyrosineBy similarity1
Modified residuei162PhosphoserineCombined sources1
Modified residuei204N6-acetyllysineCombined sources1
Glycosylationi209O-linked (GlcNAc) serineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P20618

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P20618

MaxQB - The MaxQuant DataBase

More...MaxQBi		P20618

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

More...PaxDbi		P20618

PeptideAtlas

More...PeptideAtlasi		P20618

PRoteomics IDEntifications database

More...PRIDEi		P20618

ProteomicsDB human proteome resource

More...ProteomicsDBi		53768

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P20618

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00025019

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P20618

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P20618

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

More...PhosphoSitePlusi		P20618

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P20618

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000008018 Expressed in 234 organ(s), highest expression level in endometrium

CleanEx database of gene expression profiles

More...CleanExi		HS_PSMB1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P20618 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P20618 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB033911
HPA029635
HPA029637

<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

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Interacts with SERPINB2. Interacts with RFPL4A (By similarity).By similarity6 Publications
(Microbial infection) Interacts with HIV-1 protein Tat.1 Publication

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111662, 136 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P20618

Database of interacting proteins

More...DIPi		DIP-31193N

Protein interaction database and analysis system

More...IntActi		P20618, 118 interactors

Molecular INTeraction database

More...MINTi		P20618

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000262193

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P20618

<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

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
4R3OX-ray2.601/M29-241[»]
4R67X-ray2.891/M/a/o29-241[»]
5A0Qelectron microscopy3.50M/a29-241[»]
5GJQelectron microscopy4.50f/t1-241[»]
5GJRelectron microscopy3.50f/t1-241[»]
5L4Gelectron microscopy4.021/U1-241[»]
5L5BX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5DX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5EX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5FX-ray2.50L/Z124-138[»]
L/Z145-160[»]
5L5HX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5IX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5JX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5OX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5PX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5QX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5RX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5SX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5TX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5UX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5VX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5WX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5XX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5YX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5ZX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L60X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L61X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L62X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L63X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L64X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5LE5X-ray1.80L/Z29-241[»]
5LEXX-ray2.20L/Z29-241[»]
5LEYX-ray1.90L/Z29-241[»]
5LEZX-ray2.19L/Z29-241[»]
5LF0X-ray2.41L/Z29-241[»]
5LF1X-ray2.00L/Z29-241[»]
5LF3X-ray2.10L/Z29-241[»]
5LF4X-ray1.99L/Z29-241[»]
5LF6X-ray2.07L/Z29-241[»]
5LF7X-ray2.00L/Z29-241[»]
5LN3electron microscopy6.8061-241[»]
5M2BX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5M32electron microscopy3.80L/Z1-241[»]
5T0Celectron microscopy3.80AS/BS2-241[»]
5T0Gelectron microscopy4.40S2-241[»]
5T0Helectron microscopy6.80S2-241[»]
5T0Ielectron microscopy8.00S2-241[»]
5T0Jelectron microscopy8.00S2-241[»]
5VFOelectron microscopy3.50S/s29-241[»]
5VFPelectron microscopy4.20S/s29-241[»]
5VFQelectron microscopy4.20S/s29-241[»]
5VFRelectron microscopy4.90S/s29-241[»]
5VFSelectron microscopy3.60S/s29-241[»]
5VFTelectron microscopy7.00S/s29-241[»]
5VFUelectron microscopy5.80S/s29-241[»]
6AVOelectron microscopy3.80S/X29-241[»]
6MSEelectron microscopy3.30A151-231[»]
6MSGelectron microscopy3.50S/s2-241[»]
6MSHelectron microscopy3.60S/s2-241[»]
6MSJelectron microscopy3.30S/s2-241[»]
6MSKelectron microscopy3.20S/s2-241[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P20618

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

More...SMRi		P20618

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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

<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		KOG0179 Eukaryota
COG0638 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00550000075035

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000091081

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000961

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P20618

KEGG Orthology (KO)

More...KOi		K02732

Identification of Orthologs from Complete Genome Data

More...OMAi		FNPYSDN

Database of Orthologous Groups

More...OrthoDBi		1092660at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P20618

TreeFam database of animal gene trees

More...TreeFami		TF106218

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
IPR035202 Proteasome_beta1
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF59 PTHR11599:SF59, 1 hit

Pfam protein domain database

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

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_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>Sequencei

<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.

P20618-1 [UniParc]FASTAAdd to basket
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MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI 
        60         70         80         90        100
VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL 
       110        120        130        140        150
KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY 
       160        170        180        190        200
SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM 
       210        220        230        240 
RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D
Length:241
Mass (Da):26,489
Last modified:May 1, 1992 - v2
<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:iAE8FC42799F39157
GO

Natural variant

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_05154711P → A1 PublicationCorresponds to variant dbSNP:rs12717Ensembl.1
Natural variantiVAR_051548208I → N. Corresponds to variant dbSNP:rs10541Ensembl.1

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
D00761 mRNA Translation: BAA00658.1
BT019720 mRNA Translation: AAV38525.1
AB451312 mRNA Translation: BAG70126.1
AB451442 mRNA Translation: BAG70256.1
AL031259 Genomic DNA No translation available.
BC000508 mRNA Translation: AAH00508.1
BC020807 mRNA Translation: AAH20807.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS34577.1

Protein sequence database of the Protein Information Resource

More...PIRi		S15973 SNHUC5

NCBI Reference Sequences

More...RefSeqi		NP_002784.1, NM_002793.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.352768

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000262193; ENSP00000262193; ENSG00000008018

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5689

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5689

UCSC genome browser

More...UCSCi		uc011ehe.3 human

Keywords - Coding sequence diversityi

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
D00761 mRNA Translation: BAA00658.1
BT019720 mRNA Translation: AAV38525.1
AB451312 mRNA Translation: BAG70126.1
AB451442 mRNA Translation: BAG70256.1
AL031259 Genomic DNA No translation available.
BC000508 mRNA Translation: AAH00508.1
BC020807 mRNA Translation: AAH20807.1
CCDSiCCDS34577.1
PIRiS15973 SNHUC5
RefSeqiNP_002784.1, NM_002793.3
UniGeneiHs.352768

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.601/M29-241[»]
4R67X-ray2.891/M/a/o29-241[»]
5A0Qelectron microscopy3.50M/a29-241[»]
5GJQelectron microscopy4.50f/t1-241[»]
5GJRelectron microscopy3.50f/t1-241[»]
5L4Gelectron microscopy4.021/U1-241[»]
5L5BX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5DX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5EX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5FX-ray2.50L/Z124-138[»]
L/Z145-160[»]
5L5HX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5IX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5JX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5OX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5PX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5QX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5RX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5SX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5TX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5UX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5VX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5WX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5XX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5YX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5ZX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L60X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L61X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L62X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L63X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L64X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5LE5X-ray1.80L/Z29-241[»]
5LEXX-ray2.20L/Z29-241[»]
5LEYX-ray1.90L/Z29-241[»]
5LEZX-ray2.19L/Z29-241[»]
5LF0X-ray2.41L/Z29-241[»]
5LF1X-ray2.00L/Z29-241[»]
5LF3X-ray2.10L/Z29-241[»]
5LF4X-ray1.99L/Z29-241[»]
5LF6X-ray2.07L/Z29-241[»]
5LF7X-ray2.00L/Z29-241[»]
5LN3electron microscopy6.8061-241[»]
5M2BX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5M32electron microscopy3.80L/Z1-241[»]
5T0Celectron microscopy3.80AS/BS2-241[»]
5T0Gelectron microscopy4.40S2-241[»]
5T0Helectron microscopy6.80S2-241[»]
5T0Ielectron microscopy8.00S2-241[»]
5T0Jelectron microscopy8.00S2-241[»]
5VFOelectron microscopy3.50S/s29-241[»]
5VFPelectron microscopy4.20S/s29-241[»]
5VFQelectron microscopy4.20S/s29-241[»]
5VFRelectron microscopy4.90S/s29-241[»]
5VFSelectron microscopy3.60S/s29-241[»]
5VFTelectron microscopy7.00S/s29-241[»]
5VFUelectron microscopy5.80S/s29-241[»]
6AVOelectron microscopy3.80S/X29-241[»]
6MSEelectron microscopy3.30A151-231[»]
6MSGelectron microscopy3.50S/s2-241[»]
6MSHelectron microscopy3.60S/s2-241[»]
6MSJelectron microscopy3.30S/s2-241[»]
6MSKelectron microscopy3.20S/s2-241[»]
ProteinModelPortaliP20618
SMRiP20618
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111662, 136 interactors
CORUMiP20618
DIPiDIP-31193N
IntActiP20618, 118 interactors
MINTiP20618
STRINGi9606.ENSP00000262193

Chemistry databases

BindingDBiP20618
ChEMBLiCHEMBL4208
DrugBankiDB00188 Bortezomib
DB08889 Carfilzomib
GuidetoPHARMACOLOGYi2404

Protein family/group databases

MEROPSiT01.986

PTM databases

iPTMnetiP20618
PhosphoSitePlusiP20618
SwissPalmiP20618

Polymorphism and mutation databases

BioMutaiPSMB1
DMDMi130853

2D gel databases

REPRODUCTION-2DPAGEiIPI00025019
UCD-2DPAGEiP20618

Proteomic databases

EPDiP20618
jPOSTiP20618
MaxQBiP20618
PaxDbiP20618
PeptideAtlasiP20618
PRIDEiP20618
ProteomicsDBi53768
TopDownProteomicsiP20618

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5689
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262193; ENSP00000262193; ENSG00000008018
GeneIDi5689
KEGGihsa:5689
UCSCiuc011ehe.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5689
DisGeNETi5689
EuPathDBiHostDB:ENSG00000008018.8

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMB1
HGNCiHGNC:9537 PSMB1
HPAiCAB033911
HPA029635
HPA029637
MIMi602017 gene
neXtProtiNX_P20618
OpenTargetsiENSG00000008018
PharmGKBiPA33882

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0179 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000075035
HOGENOMiHOG000091081
HOVERGENiHBG000961
InParanoidiP20618
KOiK02732
OMAiFNPYSDN
OrthoDBi1092660at2759
PhylomeDBiP20618
TreeFamiTF106218

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		PSMB1 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PSMB1

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

More...GenomeRNAii		5689

Protein Ontology

More...PROi		PR:P20618

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000008018 Expressed in 234 organ(s), highest expression level in endometrium
CleanExiHS_PSMB1
ExpressionAtlasiP20618 baseline and differential
GenevisibleiP20618 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR035202 Proteasome_beta1
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF59 PTHR11599:SF59, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
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...

<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 nameiPSB1_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: P20618
Secondary accession number(s): B5BU76, Q9BWA8
<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: February 1, 1991
Last sequence update: May 1, 1992
Last modified: January 16, 2019
This is version 206 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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