Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 219 (03 Jul 2019)
Sequence version 3 (29 Apr 2008)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Proteasome subunit beta type-5

Gene

PSMB5

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). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity.5 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei60Nucleophile2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei108Bortezomib; via amide nitrogenBy 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

GO - Biological processi

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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P28074

Protein family/group databases

MEROPS protease database

More...
MEROPSi
T01.012

<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-5 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit MB1
Proteasome subunit X
<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:PSMB5
Synonyms:LMPX, MB1, X
<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 14

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9542 PSMB5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600306 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P28074

<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

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>Mutagenesisi108A → T: Displays resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with V-109. 3 Publications1
Mutagenesisi108A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. 3 Publications1
Mutagenesisi109A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5693

Open Targets

More...
OpenTargetsi
ENSG00000100804

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33887

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4662

Drug and drug target database

More...
DrugBanki
DB00188 Bortezomib
DB08889 Carfilzomib

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2406

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PSMB5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
187608890

<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_00000265891 – 59Removed in mature form1 PublicationAdd BLAST59
<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_000002659060 – 263Proteasome subunit beta type-5Add BLAST204

Keywords - PTMi

Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P28074

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P28074

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P28074

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

More...
PaxDbi
P28074

PeptideAtlas

More...
PeptideAtlasi
P28074

PRoteomics IDEntifications database

More...
PRIDEi
P28074

ProteomicsDB human proteome resource

More...
ProteomicsDBi
54448
54449 [P28074-2]

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P28074-1 [P28074-1]

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00479306

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28074

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

More...
PhosphoSitePlusi
P28074

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P28074

<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 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

Down-regulated by IFNG/IFN-gamma (at protein level). Induced in breast cancer tissue. Up-regulated by sulforaphane in breast cancer cells.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000100804 Expressed in 231 organ(s), highest expression level in gastrocnemius

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P28074 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P28074 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA049518
HPA061796

<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. Directly interacts with POMP (PubMed:15944226).

Interacts with ABCB1 and TAP1 (PubMed:15488952).

8 Publications

(Microbial infection)

Interacts with HIV-1 TAT protein.

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
111666, 127 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P28074

Database of interacting proteins

More...
DIPi
DIP-27540N

Protein interaction database and analysis system

More...
IntActi
P28074, 42 interactors

Molecular INTeraction database

More...
MINTi
P28074

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000355325

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P28074

<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

1263
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
P28074

Database of comparative protein structure models

More...
ModBasei
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
ENSGT00940000157841

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28074

KEGG Orthology (KO)

More...
KOi
K02737

Identification of Orthologs from Complete Genome Data

More...
OMAi
WLAYLGM

Database of Orthologous Groups

More...
OrthoDBi
929961at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P28074

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
IPR037558 Proteasome_beta_5
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type

The PANTHER Classification System

More...
PANTHERi
PTHR11599:SF51 PTHR11599:SF51, 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_length">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 (3+)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 3 <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 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P28074-1) [UniParc]FASTAAdd to basket

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
MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE
60 70 80 90 100
EPGIEMLHGT TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL
110 120 130 140 150
LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK
160 170 180 190 200
GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGATFSVGSG SVYAYGVMDR
210 220 230 240 250
GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN
260
VADLHEKYSG STP
Length:263
Mass (Da):28,480
Last modified:April 29, 2008 - 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:iAED4A73DF41AA6EF
GO
Isoform 2 (identifier: P28074-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-263: GLYYVDSEGN...LHEKYSGSTP → VSEVLCLKPKSFGMYLFCGCAERIGNMARPLLRGQ

Show »
Length:203
Mass (Da):21,845
Checksum:i29788AD9561905AE
GO
Isoform 3 (identifier: P28074-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.

Note: No experimental confirmation available.
Show »
Length:160
Mass (Da):17,782
Checksum:i47A97A3A9A849846
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
G3V3K3G3V3K3_HUMAN
Proteasome subunit beta type-5
PSMB5
84Annotation 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>
H0YJM8H0YJM8_HUMAN
Proteasome subunit beta type-5
PSMB5
118Annotation 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>
G8JLC2G8JLC2_HUMAN
Proteasome subunit beta type-5
PSMB5
77Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAP35423 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA06097 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAD97956 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti3 – 6LASV → IRGR in BAA06097 (PubMed:8066462).Curated4
Sequence conflicti3 – 5LAS → HEG in BC004146 (PubMed:15489334).Curated3
Sequence conflicti85I → F AA sequence (PubMed:2306472).Curated1
Sequence conflicti109A → G in AAB33092 (PubMed:7820546).Curated1
Sequence conflicti158T → S in AAB33092 (PubMed:7820546).Curated1

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_05154924R → C. Corresponds to variant dbSNP:rs11543947Ensembl.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_0456861 – 103Missing in isoform 3. 1 PublicationAdd BLAST103
Alternative sequenceiVSP_041263169 – 263GLYYV…SGSTP → VSEVLCLKPKSFGMYLFCGC AERIGNMARPLLRGQ in isoform 2. 2 PublicationsAdd BLAST95

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
X95586 Genomic DNA Translation: CAA64838.1
AK300714 mRNA Translation: BAG62391.1
AK311895 mRNA Translation: BAG34836.1
BX538001 mRNA Translation: CAD97956.1 Different initiation.
AL132780 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW66193.1
CH471078 Genomic DNA Translation: EAW66195.1
BC004146 mRNA No translation available.
BC057840 mRNA Translation: AAH57840.1
BC107720 mRNA Translation: AAI07721.1
CD048996 mRNA No translation available.
BX248299 mRNA Translation: CAD62626.1
D29011 mRNA Translation: BAA06097.1 Different initiation.
S74378 mRNA Translation: AAB33092.1
BT006777 mRNA Translation: AAP35423.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS45083.1 [P28074-3]
CCDS45084.1 [P28074-2]
CCDS9584.1 [P28074-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A54589
I52906
PC2328
S08189

NCBI Reference Sequences

More...
RefSeqi
NP_001124197.1, NM_001130725.1 [P28074-3]
NP_001138404.1, NM_001144932.2 [P28074-2]
NP_002788.1, NM_002797.4 [P28074-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000361611; ENSP00000355325; ENSG00000100804 [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804 [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804 [P28074-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5693

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5693

UCSC genome browser

More...
UCSCi
uc001wii.3 human [P28074-1]

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
X95586 Genomic DNA Translation: CAA64838.1
AK300714 mRNA Translation: BAG62391.1
AK311895 mRNA Translation: BAG34836.1
BX538001 mRNA Translation: CAD97956.1 Different initiation.
AL132780 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW66193.1
CH471078 Genomic DNA Translation: EAW66195.1
BC004146 mRNA No translation available.
BC057840 mRNA Translation: AAH57840.1
BC107720 mRNA Translation: AAI07721.1
CD048996 mRNA No translation available.
BX248299 mRNA Translation: CAD62626.1
D29011 mRNA Translation: BAA06097.1 Different initiation.
S74378 mRNA Translation: AAB33092.1
BT006777 mRNA Translation: AAP35423.1 Different initiation.
CCDSiCCDS45083.1 [P28074-3]
CCDS45084.1 [P28074-2]
CCDS9584.1 [P28074-1]
PIRiA54589
I52906
PC2328
S08189
RefSeqiNP_001124197.1, NM_001130725.1 [P28074-3]
NP_001138404.1, NM_001144932.2 [P28074-2]
NP_002788.1, NM_002797.4 [P28074-1]

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
4R3OX-ray2.60L/Z60-260[»]
4R67X-ray2.893/L/Z/n60-260[»]
5A0Qelectron microscopy3.50L/Z60-263[»]
5GJQelectron microscopy4.50e/s1-263[»]
5GJRelectron microscopy3.50e/s1-263[»]
5L4Gelectron microscopy4.025/Y1-263[»]
5L5WX-ray2.80K/Y60-197[»]
5L5XX-ray2.90K/Y60-197[»]
5L5YX-ray2.70K/Y60-197[»]
5L5ZX-ray2.70K/Y60-197[»]
5L60X-ray2.70K/Y60-197[»]
5L61X-ray2.80K/Y60-193[»]
5L62X-ray2.80K/Y60-197[»]
5L63X-ray2.70K/Y60-197[»]
5L64X-ray2.70K/Y60-197[»]
5LE5X-ray1.80K/Y60-263[»]
5LEXX-ray2.20K/Y60-263[»]
5LEYX-ray1.90K/Y60-263[»]
5LEZX-ray2.19K/Y60-263[»]
5LF0X-ray2.41K/Y60-263[»]
5LF1X-ray2.00K/Y60-263[»]
5LF3X-ray2.10K/Y60-263[»]
5LF4X-ray1.99K/Y60-263[»]
5LF6X-ray2.07K/Y60-263[»]
5LF7X-ray2.00K/Y60-263[»]
5LN3electron microscopy6.8051-263[»]
5M32electron microscopy3.80K/Y60-263[»]
5T0Celectron microscopy3.80AR/BR2-263[»]
5T0Gelectron microscopy4.40R2-263[»]
5T0Helectron microscopy6.80R2-263[»]
5T0Ielectron microscopy8.00R2-263[»]
5T0Jelectron microscopy8.00R2-263[»]
5VFOelectron microscopy3.50R/r60-260[»]
5VFPelectron microscopy4.20R/r60-260[»]
5VFQelectron microscopy4.20R/r60-260[»]
5VFRelectron microscopy4.90R/r60-260[»]
5VFSelectron microscopy3.60R/r60-260[»]
5VFTelectron microscopy7.00R/r60-260[»]
5VFUelectron microscopy5.80R/r60-260[»]
6MSBelectron microscopy3.00R/r2-263[»]
6MSDelectron microscopy3.20R/r2-263[»]
6MSEelectron microscopy3.30f146-201[»]
6MSGelectron microscopy3.50R/r2-263[»]
6MSHelectron microscopy3.60R/r2-263[»]
6MSJelectron microscopy3.30R/r2-263[»]
6MSKelectron microscopy3.20R/r2-263[»]
SMRiP28074
ModBaseiSearch...

Protein-protein interaction databases

BioGridi111666, 127 interactors
CORUMiP28074
DIPiDIP-27540N
IntActiP28074, 42 interactors
MINTiP28074
STRINGi9606.ENSP00000355325

Chemistry databases

BindingDBiP28074
ChEMBLiCHEMBL4662
DrugBankiDB00188 Bortezomib
DB08889 Carfilzomib
GuidetoPHARMACOLOGYi2406

Protein family/group databases

MEROPSiT01.012

PTM databases

iPTMnetiP28074
PhosphoSitePlusiP28074
SwissPalmiP28074

Polymorphism and mutation databases

BioMutaiPSMB5
DMDMi187608890

2D gel databases

REPRODUCTION-2DPAGEiIPI00479306

Proteomic databases

EPDiP28074
jPOSTiP28074
MaxQBiP28074
PaxDbiP28074
PeptideAtlasiP28074
PRIDEiP28074
ProteomicsDBi54448
54449 [P28074-2]
TopDownProteomicsiP28074-1 [P28074-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5693
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361611; ENSP00000355325; ENSG00000100804 [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804 [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804 [P28074-2]
GeneIDi5693
KEGGihsa:5693
UCSCiuc001wii.3 human [P28074-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5693
DisGeNETi5693

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PSMB5
HGNCiHGNC:9542 PSMB5
HPAiHPA049518
HPA061796
MIMi600306 gene
neXtProtiNX_P28074
OpenTargetsiENSG00000100804
PharmGKBiPA33887

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0175 Eukaryota
ENOG410XQRP LUCA
GeneTreeiENSGT00940000157841
InParanoidiP28074
KOiK02737
OMAiWLAYLGM
OrthoDBi929961at2759
PhylomeDBiP28074
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-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP28074

Miscellaneous databases

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

More...
ChiTaRSi
PSMB5 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PSMB5

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

More...
GenomeRNAii
5693

Protein Ontology

More...
PROi
PR:P28074

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100804 Expressed in 231 organ(s), highest expression level in gastrocnemius
ExpressionAtlasiP28074 baseline and differential
GenevisibleiP28074 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR037558 Proteasome_beta_5
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF51 PTHR11599:SF51, 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 nameiPSB5_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: P28074
Secondary accession number(s): B2R4N9
, B4DUM9, D3DS43, E9PAV2, Q16242, Q6PEW2, Q7Z3B5, Q86T01, Q9TNN9
<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: August 1, 1992
Last sequence update: April 29, 2008
Last modified: July 3, 2019
This is version 219 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
  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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again