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UniProtKB - O14818 (PSA7_HUMAN)

Entry version 223 (29 Sep 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Proteasome subunit alpha type-7

Gene

PSMA7

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). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.

8 Publications

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Biological processHost-virus interaction

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O14818

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 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-8932339, ROS sensing by NFE2L2
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		O14818

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.974

<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-7
Alternative name(s):
Proteasome subunit RC6-1
Proteasome subunit XAPC7
<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:PSMA7
Synonyms:HSPC
<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 20

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9536, PSMA7

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606607, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O14818

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000101182

<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

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>Mutagenesisi153Y → F: Displays impaired G1/S transition and S/G2 progression. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5688

Open Targets

More...OpenTargetsi		ENSG00000101182

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33881

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O14818, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2364701
CHEMBL3831201

Drug and drug target database

More...DrugBanki		DB08515, (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE
DB07558, acetylleucyl-leucyl-norleucinal

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PSMA7

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001241421 – 248Proteasome subunit alpha type-7Add BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi130O-linked (GlcNAc) serineBy similarity1
<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 residuei153Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei227N6-acetyllysineCombined sources1

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

Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O14818

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O14818

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O14818

MaxQB - The MaxQuant DataBase

More...MaxQBi		O14818

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

More...PaxDbi		O14818

PeptideAtlas

More...PeptideAtlasi		O14818

PRoteomics IDEntifications database

More...PRIDEi		O14818

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		48256 [O14818-1]
48257 [O14818-2]
63458

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00024175

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		O14818

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O14818, 2 sites, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O14818

MetOSite database of methionine sulfoxide sites

More...MetOSitei		O14818

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

More...PhosphoSitePlusi		O14818

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O14818

<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 the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000101182, Expressed in gastrocnemius and 236 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O14818, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O14818, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000101182, Low tissue specificity

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_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. PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (PubMed:16251969).

Interacts with HIF1A.

Interacts with RAB7A (PubMed:14998988).

Interacts with PRKN (PubMed:15987638).

Interacts with ABL1 and ABL2 (PubMed:16678104).

Interacts with EMAP2 (PubMed:19362550).

Interacts with MAVS (PubMed:19734229).

12 Publications

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

1 Publication

(Microbial infection) Interacts with hepatitis B virus X protein (HBX).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111661, 175 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5993, 26S Proteasome complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O14818

Database of interacting proteins

More...DIPi		DIP-29363N

Protein interaction database and analysis system

More...IntActi		O14818, 68 interactors

Molecular INTeraction database

More...MINTi		O14818

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000359910

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O14818

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O14818, protein

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

Secondary structure

1248
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		O14818

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

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

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0183, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159695

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_035750_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O14818

Identification of Orthologs from Complete Genome Data

More...OMAi		CMLDHHV

Database for complete collections of gene phylogenies

More...PhylomeDBi		O14818

TreeFam database of animal gene trees

More...TreeFami		TF106212

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
IPR023332, Proteasome_alpha-type
IPR035190, Proteasome_alpha7
IPR000426, Proteasome_asu_N
IPR001353, Proteasome_sua/b

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF40, PTHR11599:SF40, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00948, Proteasome_A_N, 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
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>. 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.

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
Note: Experimental confirmation may be lacking for some isoforms.

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O14818-1) [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
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV 
        60         70         80         90        100
AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED 
       110        120        130        140        150
PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS 
       160        170        180        190        200
GTYHAWKANA IGRGAKSVRE FLEKNYTDEA IETDDLTIKL VIKALLEVVQ 
       210        220        230        240 
SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
Length:248
Mass (Da):27,887
Last modified:January 1, 1998 - v1
<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:i5DD0276A1C2DEF91
GO
Isoform 2 (identifier: O14818-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Show »
Length:178
Mass (Da):20,193
Checksum:iA4A7D8924670D890
GO
Isoform 3 (identifier: O14818-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-149: RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP → VGACPLACSPLAAGQSRLRHGGSCHVTSGESEN
     150-248: Missing.

Show »
Length:149
Mass (Da):16,135
Checksum:i90D6129907EDE5C7
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y586H0Y586_HUMAN
Proteasome subunit alpha type-7
PSMA7
187Annotation score:

Annotation score:2 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti160A → S in AAC99402 (PubMed:11042152).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_078692112A → D Found in patient with severe intellectual disability; unknown pathological significance. 1 Publication1

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_0052811 – 70Missing in isoform 2. CuratedAdd BLAST70
Alternative sequenceiVSP_046556117 – 149RYTQS…YQTDP → VGACPLACSPLAAGQSRLRH GGSCHVTSGESEN in isoform 3. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_046557150 – 248Missing in isoform 3. 1 PublicationAdd BLAST99

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
AF022815 mRNA Translation: AAB81515.1
AF054185 mRNA Translation: AAC99402.1
BT007165 mRNA Translation: AAP35829.1
AK312025 mRNA Translation: BAG34962.1
AL078633 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75398.1
BC004427 mRNA Translation: AAH04427.1
BI906714 mRNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13489.1 [O14818-1]

Protein sequence database of the Protein Information Resource

More...PIRi		PC2326

NCBI Reference Sequences

More...RefSeqi		NP_002783.1, NM_002792.3 [O14818-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000370858; ENSP00000359895; ENSG00000101182 [O14818-4]
ENST00000370861; ENSP00000359898; ENSG00000101182 [O14818-2]
ENST00000370873; ENSP00000359910; ENSG00000101182 [O14818-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5688

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5688

UCSC genome browser

More...UCSCi		uc002ybx.3, human [O14818-1]

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
AF022815 mRNA Translation: AAB81515.1
AF054185 mRNA Translation: AAC99402.1
BT007165 mRNA Translation: AAP35829.1
AK312025 mRNA Translation: BAG34962.1
AL078633 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75398.1
BC004427 mRNA Translation: AAH04427.1
BI906714 mRNA No translation available.
CCDSiCCDS13489.1 [O14818-1]
PIRiPC2326
RefSeqiNP_002783.1, NM_002792.3 [O14818-1]

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-ray2.60D/R2-244[»]
4R67X-ray2.89D/R/f/t2-244[»]
5A0Qelectron microscopy3.50D/R1-248[»]
5GJQelectron microscopy4.50E/k1-248[»]
5GJRelectron microscopy3.50E/k1-248[»]
5L4Gelectron microscopy4.02D/Q1-248[»]
5LE5X-ray1.80C/Q1-248[»]
5LEXX-ray2.20C/Q1-248[»]
5LEYX-ray1.90C/Q1-248[»]
5LEZX-ray2.19C/Q1-248[»]
5LF0X-ray2.41C/Q1-248[»]
5LF1X-ray2.00C/Q1-248[»]
5LF3X-ray2.10C/Q1-248[»]
5LF4X-ray1.99C/Q1-248[»]
5LF6X-ray2.07C/Q1-248[»]
5LF7X-ray2.00C/Q1-248[»]
5LN3electron microscopy6.80D1-248[»]
5M32electron microscopy3.80C2-235[»]
Q2-236[»]
5T0Celectron microscopy3.80AJ/BJ2-248[»]
5T0Gelectron microscopy4.40J2-248[»]
5T0Helectron microscopy6.80J2-248[»]
5T0Ielectron microscopy8.00J2-248[»]
5T0Jelectron microscopy8.00J2-248[»]
5VFOelectron microscopy3.50J/j2-244[»]
5VFPelectron microscopy4.20J/j2-244[»]
5VFQelectron microscopy4.20J/j2-244[»]
5VFRelectron microscopy4.90J/j2-244[»]
5VFSelectron microscopy3.60J/j2-244[»]
5VFTelectron microscopy7.00J/j2-244[»]
5VFUelectron microscopy5.80J/j2-244[»]
6AVOelectron microscopy3.80I/N1-248[»]
6E5BX-ray2.77C/Q1-248[»]
6KWYelectron microscopy2.72C/Q1-248[»]
6MSBelectron microscopy3.00J/j2-248[»]
6MSDelectron microscopy3.20J/j2-248[»]
6MSEelectron microscopy3.30J/j2-248[»]
6MSGelectron microscopy3.50J/j2-248[»]
6MSHelectron microscopy3.60J/j2-248[»]
6MSJelectron microscopy3.30J/j2-248[»]
6MSKelectron microscopy3.20J/j2-248[»]
6R70electron microscopy3.50C/Q2-238[»]
6REYelectron microscopy3.00D/R1-248[»]
6RGQelectron microscopy2.60D/R1-248[»]
6WJDelectron microscopy4.80J/j2-248[»]
6WJNelectron microscopy5.70J/j2-244[»]
6XMJelectron microscopy3.00D2-244[»]
7AWEX-ray2.29D/R2-238[»]
SMRiO14818
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111661, 175 interactors
ComplexPortaliCPX-5993, 26S Proteasome complex
CORUMiO14818
DIPiDIP-29363N
IntActiO14818, 68 interactors
MINTiO14818
STRINGi9606.ENSP00000359910

Chemistry databases

BindingDBiO14818
ChEMBLiCHEMBL2364701
CHEMBL3831201
DrugBankiDB08515, (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE
DB07558, acetylleucyl-leucyl-norleucinal

Protein family/group databases

MEROPSiT01.974

PTM databases

GlyGeniO14818, 2 sites, 1 O-linked glycan (1 site)
iPTMnetiO14818
MetOSiteiO14818
PhosphoSitePlusiO14818
SwissPalmiO14818

Genetic variation databases

BioMutaiPSMA7

2D gel databases

REPRODUCTION-2DPAGEiIPI00024175
UCD-2DPAGEiO14818

Proteomic databases

EPDiO14818
jPOSTiO14818
MassIVEiO14818
MaxQBiO14818
PaxDbiO14818
PeptideAtlasiO14818
PRIDEiO14818
ProteomicsDBi48256 [O14818-1]
48257 [O14818-2]
63458

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		29428, 467 antibodies

The DNASU plasmid repository

More...DNASUi		5688

Genome annotation databases

EnsembliENST00000370858; ENSP00000359895; ENSG00000101182 [O14818-4]
ENST00000370861; ENSP00000359898; ENSG00000101182 [O14818-2]
ENST00000370873; ENSP00000359910; ENSG00000101182 [O14818-1]
GeneIDi5688
KEGGihsa:5688
UCSCiuc002ybx.3, human [O14818-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5688
DisGeNETi5688

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMA7
HGNCiHGNC:9536, PSMA7
HPAiENSG00000101182, Low tissue specificity
MIMi606607, gene
neXtProtiNX_O14818
OpenTargetsiENSG00000101182
PharmGKBiPA33881
VEuPathDBiHostDB:ENSG00000101182

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0183, Eukaryota
GeneTreeiENSGT00940000159695
HOGENOMiCLU_035750_4_0_1
InParanoidiO14818
OMAiCMLDHHV
PhylomeDBiO14818
TreeFamiTF106212

Enzyme and pathway databases

PathwayCommonsiO14818
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 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-8932339, ROS sensing by NFE2L2
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
SIGNORiO14818

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5688, 813 hits in 1002 CRISPR screens

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

More...ChiTaRSi		PSMA7, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PSMA7

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

More...GenomeRNAii		5688
PharosiO14818, Tbio

Protein Ontology

More...PROi		PR:O14818
RNActiO14818, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000101182, Expressed in gastrocnemius and 236 other tissues
ExpressionAtlasiO14818, baseline and differential
GenevisibleiO14818, HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055, Ntn_hydrolases_N
IPR023332, Proteasome_alpha-type
IPR035190, Proteasome_alpha7
IPR000426, Proteasome_asu_N
IPR001353, Proteasome_sua/b
PANTHERiPTHR11599:SF40, PTHR11599:SF40, 1 hit
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

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 nameiPSA7_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: O14818
Secondary accession number(s): B2R515
, Q5JXJ2, Q9BR53, Q9H4K5, Q9UEU8
<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: December 8, 2000
Last sequence update: January 1, 1998
Last modified: September 29, 2021
This is version 223 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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. SIMILARITY comments
    Index of protein domains and families
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