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Protein

Proteasome subunit alpha type-5

Gene

PSMA5

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

  • Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation1 Publication EC:3.4.25.1

<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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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

SIGNOR Signaling Network Open Resource

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SIGNORi
P28066

Protein family/group databases

MEROPS protease database

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MEROPSi
T01.975

<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 alpha type-5 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain zeta chain
Multicatalytic endopeptidase complex zeta chain
Proteasome zeta 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:PSMA5
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000143106.12

Human Gene Nomenclature Database

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HGNCi
HGNC:9534 PSMA5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176844 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P28066

<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

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DisGeNETi
5686

Open Targets

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OpenTargetsi
ENSG00000143106

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33879

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3831201

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PSMA5

Domain mapping of disease mutations (DMDM)

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DMDMi
38258905

<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 ‘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_00001241171 – 241Proteasome subunit alpha type-5Add BLAST241

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-acetylmethionineBy similarity1
Modified residuei16PhosphoserineCombined sources1
Modified residuei55PhosphothreonineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei63PhosphoserineCombined 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>Glycosylationi198O-linked (GlcNAc) serineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P28066

MaxQB - The MaxQuant DataBase

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MaxQBi
P28066

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

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PaxDbi
P28066

PeptideAtlas

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PeptideAtlasi
P28066

PRoteomics IDEntifications database

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PRIDEi
P28066

ProteomicsDB human proteome resource

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ProteomicsDBi
54441

Consortium for Top Down Proteomics

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TopDownProteomicsi
P28066-1 [P28066-1]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P28066

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00291922

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P28066

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P28066

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

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PhosphoSitePlusi
P28066

SwissPalm database of S-palmitoylation events

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SwissPalmi
P28066

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

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

Expressed in fetal brain (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 in colon cancer cell lines. Up-regulated in fetal Down syndrome (DS) brain (at protein level). May be the target of the transcriptional activator NFE2L2.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000143106 Expressed in 225 organ(s), highest expression level in oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_PSMA5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P28066 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28066 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA028392
HPA028398
HPA028441

<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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.6 Publications

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111659, 151 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P28066

Database of interacting proteins

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DIPi
DIP-29368N

Protein interaction database and analysis system

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IntActi
P28066, 34 interactors

Molecular INTeraction database

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MINTi
P28066

STRING: functional protein association networks

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STRINGi
9606.ENSP00000271308

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P28066

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P28066

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

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SMRi
P28066

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<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 T1A family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0176 Eukaryota
COG0638 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074958

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000091085

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003005

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P28066

KEGG Orthology (KO)

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KOi
K02729

Identification of Orthologs from Complete Genome Data

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OMAi
FQVEYAR

Database of Orthologous Groups

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OrthoDBi
EOG091G0GX6

Database for complete collections of gene phylogenies

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PhylomeDBi
P28066

TreeFam database of animal gene trees

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TreeFami
TF106211

Family and domain databases

Conserved Domains Database

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CDDi
cd03753 proteasome_alpha_type_5, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR033812 Proteasome_alpha_type_5
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b

Pfam protein domain database

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Pfami
View protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00948 Proteasome_A_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56235 SSF56235, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_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>Sequences (2)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P28066-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV
60 70 80 90 100
EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW
110 120 130 140 150
FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG
160 170 180 190 200
PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI
210 220 230 240
ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I
Length:241
Mass (Da):26,411
Last modified:October 31, 2003 - 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:i5610CDA00469120A
GO
Isoform 2 (identifier: P28066-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: No experimental confirmation available.
Show »
Length:183
Mass (Da):20,035
Checksum:i24D3C1197D3AD8A5
GO

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 conflicti27A → D in CAA43962 (PubMed:1888762).Curated1
Sequence conflicti184V → L in CAA43962 (PubMed:1888762).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0462411 – 58Missing in isoform 2. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X61970 mRNA Translation: CAA43962.1
CR456847 mRNA Translation: CAG33128.1
AK304448 mRNA Translation: BAG65266.1
AK313351 mRNA Translation: BAG36153.1
AL356735 Genomic DNA No translation available.
AL390252 Genomic DNA No translation available.
CH471122 Genomic DNA Translation: EAW56381.1
CH471122 Genomic DNA Translation: EAW56383.1
BC102018 mRNA Translation: AAI02019.1
BC102019 mRNA Translation: AAI02020.1
BC102020 mRNA Translation: AAI02021.1
BC103751 mRNA Translation: AAI03752.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS55619.1 [P28066-2]
CCDS799.1 [P28066-1]

Protein sequence database of the Protein Information Resource

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PIRi
S17521

NCBI Reference Sequences

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RefSeqi
NP_001186701.1, NM_001199772.1 [P28066-2]
NP_001186702.1, NM_001199773.1 [P28066-2]
NP_001186703.1, NM_001199774.1 [P28066-2]
NP_002781.2, NM_002790.3 [P28066-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.485246

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000271308; ENSP00000271308; ENSG00000143106 [P28066-1]
ENST00000538610; ENSP00000440618; ENSG00000143106 [P28066-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5686

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5686

UCSC genome browser

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UCSCi
uc001dxn.4 human [P28066-1]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61970 mRNA Translation: CAA43962.1
CR456847 mRNA Translation: CAG33128.1
AK304448 mRNA Translation: BAG65266.1
AK313351 mRNA Translation: BAG36153.1
AL356735 Genomic DNA No translation available.
AL390252 Genomic DNA No translation available.
CH471122 Genomic DNA Translation: EAW56381.1
CH471122 Genomic DNA Translation: EAW56383.1
BC102018 mRNA Translation: AAI02019.1
BC102019 mRNA Translation: AAI02020.1
BC102020 mRNA Translation: AAI02021.1
BC103751 mRNA Translation: AAI03752.1
CCDSiCCDS55619.1 [P28066-2]
CCDS799.1 [P28066-1]
PIRiS17521
RefSeqiNP_001186701.1, NM_001199772.1 [P28066-2]
NP_001186702.1, NM_001199773.1 [P28066-2]
NP_001186703.1, NM_001199774.1 [P28066-2]
NP_002781.2, NM_002790.3 [P28066-1]
UniGeneiHs.485246

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60E/S8-241[»]
4R67X-ray2.89E/S/g/u8-241[»]
5A0Qelectron microscopy3.50E/S1-241[»]
5GJQelectron microscopy4.50F/l1-241[»]
5GJRelectron microscopy3.50F/l1-241[»]
5L4Gelectron microscopy4.02E/R1-241[»]
5LE5X-ray1.80D/R1-241[»]
5LEXX-ray2.20D/R1-241[»]
5LEYX-ray1.90D/R1-241[»]
5LEZX-ray2.19D/R1-241[»]
5LF0X-ray2.41D/R1-241[»]
5LF1X-ray2.00D/R1-241[»]
5LF3X-ray2.10D/R1-241[»]
5LF4X-ray1.99D/R1-241[»]
5LF6X-ray2.07D/R1-241[»]
5LF7X-ray2.00D/R1-241[»]
5LN3electron microscopy6.80E1-241[»]
5M32electron microscopy3.80D/R1-241[»]
5T0Celectron microscopy3.80AK/BK2-241[»]
5T0Gelectron microscopy4.40K2-241[»]
5T0Helectron microscopy6.80K2-241[»]
5T0Ielectron microscopy8.00K2-241[»]
5T0Jelectron microscopy8.00K2-241[»]
5VFOelectron microscopy3.50K/k8-241[»]
5VFPelectron microscopy4.20K/k8-241[»]
5VFQelectron microscopy4.20K/k8-241[»]
5VFRelectron microscopy4.90K/k8-241[»]
5VFSelectron microscopy3.60K/k8-241[»]
5VFTelectron microscopy7.00K/k8-241[»]
5VFUelectron microscopy5.80K/k8-241[»]
6AVOelectron microscopy3.80H/M1-241[»]
ProteinModelPortaliP28066
SMRiP28066
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111659, 151 interactors
CORUMiP28066
DIPiDIP-29368N
IntActiP28066, 34 interactors
MINTiP28066
STRINGi9606.ENSP00000271308

Chemistry databases

BindingDBiP28066
ChEMBLiCHEMBL3831201

Protein family/group databases

MEROPSiT01.975

PTM databases

iPTMnetiP28066
PhosphoSitePlusiP28066
SwissPalmiP28066

Polymorphism and mutation databases

BioMutaiPSMA5
DMDMi38258905

2D gel databases

DOSAC-COBS-2DPAGEiP28066
REPRODUCTION-2DPAGEiIPI00291922
SWISS-2DPAGEiP28066

Proteomic databases

EPDiP28066
MaxQBiP28066
PaxDbiP28066
PeptideAtlasiP28066
PRIDEiP28066
ProteomicsDBi54441
TopDownProteomicsiP28066-1 [P28066-1]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
5686
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271308; ENSP00000271308; ENSG00000143106 [P28066-1]
ENST00000538610; ENSP00000440618; ENSG00000143106 [P28066-2]
GeneIDi5686
KEGGihsa:5686
UCSCiuc001dxn.4 human [P28066-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5686
DisGeNETi5686
EuPathDBiHostDB:ENSG00000143106.12

GeneCards: human genes, protein and diseases

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GeneCardsi
PSMA5
HGNCiHGNC:9534 PSMA5
HPAiHPA028392
HPA028398
HPA028441
MIMi176844 gene
neXtProtiNX_P28066
OpenTargetsiENSG00000143106
PharmGKBiPA33879

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0176 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000074958
HOGENOMiHOG000091085
HOVERGENiHBG003005
InParanoidiP28066
KOiK02729
OMAiFQVEYAR
OrthoDBiEOG091G0GX6
PhylomeDBiP28066
TreeFamiTF106211

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
SIGNORiP28066

Miscellaneous databases

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

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ChiTaRSi
PSMA5 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PSMA5

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

More...
GenomeRNAii
5686

Protein Ontology

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PROi
PR:P28066

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000143106 Expressed in 225 organ(s), highest expression level in oocyte
CleanExiHS_PSMA5
ExpressionAtlasiP28066 baseline and differential
GenevisibleiP28066 HS

Family and domain databases

CDDicd03753 proteasome_alpha_type_5, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR033812 Proteasome_alpha_type_5
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_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 nameiPSA5_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: P28066
Secondary accession number(s): B2R8F6
, B4E2V4, Q3T1C1, Q6IBF7
<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: October 31, 2003
Last modified: December 5, 2018
This is version 210 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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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