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UniProtKB - P25788 (PSA3_HUMAN)

Protein

Proteasome subunit alpha type-3

Gene

PSMA3

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). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.5 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

  • 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
  • ubiquitin protein ligase binding Source: ARUK-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-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

More...SIGNORi		P25788

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.977

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P25788 Predicted

<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-3 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
<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:PSMA3
Synonyms:HC8, PSC8
<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 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000100567.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:9532 PSMA3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		176843 gene
176845 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P25788

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		5684

Open Targets

More...OpenTargetsi		ENSG00000100567

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33877

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3831201

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PSMA3

Domain mapping of disease mutations (DMDM)

More...DMDMi		130859

<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 indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00001240912 – 255Proteasome subunit alpha type-3Add BLAST254

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 residuei2N-acetylserineCombined sources1 Publication1
Modified residuei57N6-acetyllysineCombined sources1
Modified residuei206N6-acetyllysineCombined sources1
Modified residuei230N6-acetyllysineCombined sources1
Modified residuei243PhosphoserineCombined sources1
Modified residuei250PhosphoserineCombined sources1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P25788

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P25788

MaxQB - The MaxQuant DataBase

More...MaxQBi		P25788

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

More...PaxDbi		P25788

PeptideAtlas

More...PeptideAtlasi		P25788

PRoteomics IDEntifications database

More...PRIDEi		P25788

ProteomicsDB human proteome resource

More...ProteomicsDBi		54290
54291 [P25788-2]

2D gel databases

USC-OGP 2-DE database

More...OGPi		P25788

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00171199

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P25788

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

More...PhosphoSitePlusi		P25788

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P25788

<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 antioxidants BO-653 and probucol. Up-regulated by bacterial lipopolysaccharides (LPS) and TNF.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000100567 Expressed in 232 organ(s), highest expression level in adenohypophysis

CleanEx database of gene expression profiles

More...CleanExi		HS_PSMA3

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P25788 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P25788 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA000905

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Interacts with AURKB. Interacts with CDKN1A (PubMed:11350925). Interacts with MDM2 and RB1 (PubMed:16337594). Interacts with the C-terminus of TBXA2R isoform 2 (PubMed:17499743). Interacts with DNAJB2 (PubMed:15936278).11 Publications
(Microbial infection) Interacts with HIV-1 Tat protein.1 Publication
(Microbial infection) Interacts with hepatitis C virus (HCV) F protein.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus EBNA3 proteins.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

WithEntry#Exp.IntActNotes
B2R5503EBI-348380,EBI-10175488
Q5JPT63EBI-348380,EBI-10244213
Q5W1503EBI-348380,EBI-10248148
Q7KZQ13EBI-348380,EBI-10255941
Q9H8E53EBI-348380,EBI-10309031
Q9HAA03EBI-348380,EBI-10309885
Q9NWL93EBI-348380,EBI-10315054
ATP6V0CP274493EBI-348380,EBI-721179
BTN2A2Q8WVV53EBI-348380,EBI-8648738
C1orf105O955613EBI-348380,EBI-10191951
C4orf42Q96CW73EBI-348380,EBI-752053
C9orf106A2RU003EBI-348380,EBI-10173129
CCL28Q9NRJ33EBI-348380,EBI-7783254
CRB3Q9BUF73EBI-348380,EBI-9844372
CST2P092283EBI-348380,EBI-8832659
CTAGE5O153203EBI-348380,EBI-1050253
DGLUCYQ7Z3D63EBI-348380,EBI-2807872
DMC1Q145656EBI-348380,EBI-930865
DMRT3Q9NQL93EBI-348380,EBI-9679045
FAM171A2Q8N0U13EBI-348380,EBI-10264767
FAM218AQ96MZ43EBI-348380,EBI-10291578
FBXL18Q96D163EBI-348380,EBI-744419
FBXO7Q9Y3I16EBI-348380,EBI-1161222
GATA2P237693EBI-348380,EBI-2806671
GATA3P237713EBI-348380,EBI-6664760
GORASP2Q9H8Y83EBI-348380,EBI-739467
hCG_1998195Q8N7793EBI-348380,EBI-10267476
hCG_2003792A0A024R5S03EBI-348380,EBI-10188461
IQCEQ6IPM23EBI-348380,EBI-3893098
KIRREL2Q6UWL63EBI-348380,EBI-10254473
KIRREL3-AS3Q8N7Y13EBI-348380,EBI-10267656
KRTAP19-5Q3LI723EBI-348380,EBI-1048945
KRTAP26-1Q6PEX33EBI-348380,EBI-3957672
KRTAP8-1Q8IUC23EBI-348380,EBI-10261141
LASP1Q148473EBI-348380,EBI-742828
LETM1O952023EBI-348380,EBI-1052895
MDM2Q009872EBI-348380,EBI-389668
MUM1Q9H6H23EBI-348380,EBI-10307610
NPBWR2P481463EBI-348380,EBI-10210114
NPPBP168603EBI-348380,EBI-747044
OSR2Q8N2R03EBI-348380,EBI-5660512
PATL1Q86TB93EBI-348380,EBI-2562092
PCOTHQ58A443EBI-348380,EBI-10243387
PMLP295902EBI-348380,EBI-295890
PRR10Q14CW73EBI-348380,EBI-10234793
PRR13Q9NZ813EBI-348380,EBI-740924
PRR3P795223EBI-348380,EBI-2803328
PSMA1P2578613EBI-348380,EBI-359352
PSMA4P257894EBI-348380,EBI-359310
PSMA6P609009EBI-348380,EBI-357793
PSMA7O148186EBI-348380,EBI-603272
PSMB4P280703EBI-348380,EBI-603350
PTPN23Q9H3S73EBI-348380,EBI-724478
PWWP2BQ6NUJ53EBI-348380,EBI-10251192
RAB3IL1Q8TBN03EBI-348380,EBI-743796
RAD54L2Q9Y4B43EBI-348380,EBI-948156
RAMACQ9BTL33EBI-348380,EBI-744023
RBFOX2O432513EBI-348380,EBI-746056
RBM42Q9BTD83EBI-348380,EBI-746862
RTP5Q14D333EBI-348380,EBI-10217913
RUSC1-AS1Q66K803EBI-348380,EBI-10248967
SF1Q156373EBI-348380,EBI-744603
SLAIN1Q8ND833EBI-348380,EBI-10269374
SLC22A23Q7L9D03EBI-348380,EBI-10256583
SNRPBP14678-23EBI-348380,EBI-372475
SNRPCQ5TAL43EBI-348380,EBI-10246938
SPATA8Q6RVD63EBI-348380,EBI-8635958
STX4Q128463EBI-348380,EBI-744942
STX6O437523EBI-348380,EBI-2695795
URB1-AS1Q96HZ73EBI-348380,EBI-10288943
VPS37CA5D8V63EBI-348380,EBI-2559305
ZNF366Q8N8953EBI-348380,EBI-2813661
ZNF385CQ66K414EBI-348380,EBI-8651919
ZNF688A0A0S2Z5X43EBI-348380,EBI-16429014

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111657, 294 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P25788

Database of interacting proteins

More...DIPi		DIP-29366N

Protein interaction database and analysis system

More...IntActi		P25788, 121 interactors

Molecular INTeraction database

More...MINTi		P25788

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000216455

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P25788

<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

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
5A0Qelectron microscopy3.50G/U1-255[»]
5DSVX-ray3.75A/B/C/D/E/F/G/H/I/J/K/L/M/N1-255[»]
5GJQelectron microscopy4.50X/n1-255[»]
5GJRelectron microscopy3.50X/n1-255[»]
5L4Gelectron microscopy4.02G/T1-255[»]
5LE5X-ray1.80F/T1-255[»]
5LEXX-ray2.20F/T1-255[»]
5LEYX-ray1.90F/T1-255[»]
5LEZX-ray2.19F/T1-255[»]
5LF0X-ray2.41F/T1-255[»]
5LF1X-ray2.00F/T1-255[»]
5LF3X-ray2.10F/T1-255[»]
5LF4X-ray1.99F/T1-255[»]
5LF6X-ray2.07F/T1-255[»]
5LF7X-ray2.00F/T1-255[»]
5LN3electron microscopy6.80G1-255[»]
5M32electron microscopy3.80F/T1-255[»]
5T0Celectron microscopy3.80AM/BM2-255[»]
5T0Gelectron microscopy4.40M2-255[»]
5T0Helectron microscopy6.80M2-255[»]
5T0Ielectron microscopy8.00M2-255[»]
5T0Jelectron microscopy8.00M2-255[»]
5VFOelectron microscopy3.50M/m2-246[»]
5VFPelectron microscopy4.20M/m2-246[»]
5VFQelectron microscopy4.20M/m2-246[»]
5VFRelectron microscopy4.90M/m2-246[»]
5VFSelectron microscopy3.60M/m2-246[»]
5VFTelectron microscopy7.00M/m2-246[»]
5VFUelectron microscopy5.80M/m2-246[»]
6AVOelectron microscopy3.80J/Q1-255[»]
6MSEelectron microscopy3.30a166-213[»]
6MSGelectron microscopy3.50M/m2-255[»]
6MSHelectron microscopy3.60M/m2-255[»]
6MSJelectron microscopy3.30M/m2-255[»]
6MSKelectron microscopy3.20M/m2-255[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P25788

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

More...SMRi		P25788

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

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

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0184 Eukaryota
ENOG410XP01 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074912

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000091086

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG105566

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P25788

KEGG Orthology (KO)

More...KOi		K02727

Identification of Orthologs from Complete Genome Data

More...OMAi		IIYLVHD

Database of Orthologous Groups

More...OrthoDBi		1222564at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P25788

TreeFam database of animal gene trees

More...TreeFami		TF106208

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
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF10 PTHR11599:SF10, 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>.<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.

<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 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

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P25788-1) [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
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV 
        60         70         80         90        100
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR 
       110        120        130        140        150
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY 
       160        170        180        190        200
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI 
       210        220        230        240        250
VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES 

DDDNM
Length:255
Mass (Da):28,433
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA1854ED3C0650FB1
GO
Isoform 2 (identifier: P25788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-142: Missing.

Show »
Length:248
Mass (Da):27,647
Checksum:iE1C4F1C97EC83DAD
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V4X5G3V4X5_HUMAN
Proteasome endopeptidase complex
PSMA3
180Annotation 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>
G3V5N4G3V5N4_HUMAN
Proteasome subunit alpha type-3
PSMA3
54Annotation 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>
G3V3W4G3V3W4_HUMAN
Proteasome subunit alpha type-3
PSMA3
36Annotation 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>
H0YJ03H0YJ03_HUMAN
Proteasome subunit alpha type-3
PSMA3
83Annotation 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>

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 conflicti91I → M in AAH29402 (PubMed:15489334).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_075259233Missing Found in a patient with Nakajo syndrome who also carries a mutation in PSMB8; unknown pathological significance; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome. 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. 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_005280136 – 142Missing in isoform 2. 2 Publications7

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
D00762 mRNA Translation: BAA00659.1
BT006711 mRNA Translation: AAP35357.1
BT019715 mRNA Translation: AAV38520.1
AK315158 mRNA Translation: BAG37603.1
CH471061 Genomic DNA Translation: EAW80719.1
BC005265 mRNA Translation: AAH05265.1
BC029402 mRNA Translation: AAH29402.1
BC038990 mRNA Translation: AAH38990.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS45113.1 [P25788-2]
CCDS9731.1 [P25788-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S15971 SNHUC8

NCBI Reference Sequences

More...RefSeqi		NP_002779.1, NM_002788.3 [P25788-1]
NP_687033.1, NM_152132.2 [P25788-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.558799

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000216455; ENSP00000216455; ENSG00000100567 [P25788-1]
ENST00000412908; ENSP00000390491; ENSG00000100567 [P25788-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5684

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5684

UCSC genome browser

More...UCSCi		uc001xdj.3 human [P25788-1]

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
D00762 mRNA Translation: BAA00659.1
BT006711 mRNA Translation: AAP35357.1
BT019715 mRNA Translation: AAV38520.1
AK315158 mRNA Translation: BAG37603.1
CH471061 Genomic DNA Translation: EAW80719.1
BC005265 mRNA Translation: AAH05265.1
BC029402 mRNA Translation: AAH29402.1
BC038990 mRNA Translation: AAH38990.1
CCDSiCCDS45113.1 [P25788-2]
CCDS9731.1 [P25788-1]
PIRiS15971 SNHUC8
RefSeqiNP_002779.1, NM_002788.3 [P25788-1]
NP_687033.1, NM_152132.2 [P25788-2]
UniGeneiHs.558799

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
5A0Qelectron microscopy3.50G/U1-255[»]
5DSVX-ray3.75A/B/C/D/E/F/G/H/I/J/K/L/M/N1-255[»]
5GJQelectron microscopy4.50X/n1-255[»]
5GJRelectron microscopy3.50X/n1-255[»]
5L4Gelectron microscopy4.02G/T1-255[»]
5LE5X-ray1.80F/T1-255[»]
5LEXX-ray2.20F/T1-255[»]
5LEYX-ray1.90F/T1-255[»]
5LEZX-ray2.19F/T1-255[»]
5LF0X-ray2.41F/T1-255[»]
5LF1X-ray2.00F/T1-255[»]
5LF3X-ray2.10F/T1-255[»]
5LF4X-ray1.99F/T1-255[»]
5LF6X-ray2.07F/T1-255[»]
5LF7X-ray2.00F/T1-255[»]
5LN3electron microscopy6.80G1-255[»]
5M32electron microscopy3.80F/T1-255[»]
5T0Celectron microscopy3.80AM/BM2-255[»]
5T0Gelectron microscopy4.40M2-255[»]
5T0Helectron microscopy6.80M2-255[»]
5T0Ielectron microscopy8.00M2-255[»]
5T0Jelectron microscopy8.00M2-255[»]
5VFOelectron microscopy3.50M/m2-246[»]
5VFPelectron microscopy4.20M/m2-246[»]
5VFQelectron microscopy4.20M/m2-246[»]
5VFRelectron microscopy4.90M/m2-246[»]
5VFSelectron microscopy3.60M/m2-246[»]
5VFTelectron microscopy7.00M/m2-246[»]
5VFUelectron microscopy5.80M/m2-246[»]
6AVOelectron microscopy3.80J/Q1-255[»]
6MSEelectron microscopy3.30a166-213[»]
6MSGelectron microscopy3.50M/m2-255[»]
6MSHelectron microscopy3.60M/m2-255[»]
6MSJelectron microscopy3.30M/m2-255[»]
6MSKelectron microscopy3.20M/m2-255[»]
ProteinModelPortaliP25788
SMRiP25788
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111657, 294 interactors
CORUMiP25788
DIPiDIP-29366N
IntActiP25788, 121 interactors
MINTiP25788
STRINGi9606.ENSP00000216455

Chemistry databases

BindingDBiP25788
ChEMBLiCHEMBL3831201

Protein family/group databases

MEROPSiT01.977
MoonDBiP25788 Predicted

PTM databases

iPTMnetiP25788
PhosphoSitePlusiP25788
SwissPalmiP25788

Polymorphism and mutation databases

BioMutaiPSMA3
DMDMi130859

2D gel databases

OGPiP25788
REPRODUCTION-2DPAGEiIPI00171199

Proteomic databases

EPDiP25788
jPOSTiP25788
MaxQBiP25788
PaxDbiP25788
PeptideAtlasiP25788
PRIDEiP25788
ProteomicsDBi54290
54291 [P25788-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5684
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567 [P25788-1]
ENST00000412908; ENSP00000390491; ENSG00000100567 [P25788-2]
GeneIDi5684
KEGGihsa:5684
UCSCiuc001xdj.3 human [P25788-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5684
DisGeNETi5684
EuPathDBiHostDB:ENSG00000100567.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMA3

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0155215
HGNCiHGNC:9532 PSMA3
HPAiHPA000905
MIMi176843 gene
176845 gene
neXtProtiNX_P25788
OpenTargetsiENSG00000100567
PharmGKBiPA33877

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0184 Eukaryota
ENOG410XP01 LUCA
GeneTreeiENSGT00550000074912
HOGENOMiHOG000091086
HOVERGENiHBG105566
InParanoidiP25788
KOiK02727
OMAiIIYLVHD
OrthoDBi1222564at2759
PhylomeDBiP25788
TreeFamiTF106208

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-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
SIGNORiP25788

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PSMA3

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

More...GenomeRNAii		5684

Protein Ontology

More...PROi		PR:P25788

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000100567 Expressed in 232 organ(s), highest expression level in adenohypophysis
CleanExiHS_PSMA3
ExpressionAtlasiP25788 baseline and differential
GenevisibleiP25788 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 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

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 nameiPSA3_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: P25788
Secondary accession number(s): B2RCK6
, Q86U83, Q8N1D8, Q9BS70
<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: May 1, 1992
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 218 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
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