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UniProtKB - P25786 (PSA1_HUMAN)

Entry version 219 (13 Feb 2019)
Sequence version 1 (01 May 1992)
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Protein

Proteasome subunit alpha type-1

Gene

PSMA1

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
  • lipopolysaccharide binding Source: Ensembl
  • RNA binding Source: ProtInc
  • threonine-type endopeptidase activity Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionHydrolase, Protease, Threonine protease
Biological processImmunity

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

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.976

<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-1 (EC:3.4.25.11 Publication)
Alternative name(s):
30 kDa prosomal protein
Short name:
PROS-30
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu 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:PSMA1
Synonyms:HC2, NU, PROS30, PSC2
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000129084.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:9530 PSMA1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602854 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P25786

<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		5682

Open Targets

More...OpenTargetsi		ENSG00000129084

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33875

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		PSMA1

Domain mapping of disease mutations (DMDM)

More...DMDMi		130848

<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_00001240601 – 263Proteasome subunit alpha type-1Add BLAST263

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 residuei110Phosphoserine; alternateCombined 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>Glycosylationi110O-linked (GlcNAc) serine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei177PhosphoserineCombined sources1
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P25786

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P25786

MaxQB - The MaxQuant DataBase

More...MaxQBi		P25786

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

More...PaxDbi		P25786

PeptideAtlas

More...PeptideAtlasi		P25786

PRoteomics IDEntifications database

More...PRIDEi		P25786

ProteomicsDB human proteome resource

More...ProteomicsDBi		54287
54288 [P25786-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P25786-1 [P25786-1]

2D gel databases

USC-OGP 2-DE database

More...OGPi		P25786

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00016832

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P25786

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

More...PhosphoSitePlusi		P25786

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P25786

<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

Induced in breast cancer tissue (at protein level). Up-regulated in liver tumor tissues.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000129084 Expressed in 108 organ(s), highest expression level in left adrenal gland

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P25786 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P25786 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB033765
HPA037646
HPA043891

<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 NOTCH3. Interacts with ZFAND1 (PubMed:29804830).7 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

WithEntry#Exp.IntActNotes
ABI3Q9P2A43EBI-359352,EBI-742038
APIPQ96GX93EBI-359352,EBI-359248
BANF2Q9H503-24EBI-359352,EBI-11977289
BLZF1Q9H2G93EBI-359352,EBI-2548012
CALCOCO2Q131373EBI-359352,EBI-739580
CBSP355203EBI-359352,EBI-740135
CCDC102BQ68D865EBI-359352,EBI-10171570
CCNHP519468EBI-359352,EBI-741406
CDAP323203EBI-359352,EBI-9250559
CEP70Q8NHQ15EBI-359352,EBI-739624
CEP72Q9P2095EBI-359352,EBI-739498
EHMT2A2ABF93EBI-359352,EBI-10174566
GNPTABQ3T9063EBI-359352,EBI-1104907
GOLGA2Q083795EBI-359352,EBI-618309
HEL-S-70V9HW803EBI-359352,EBI-10175326
HOMER3Q9NSC57EBI-359352,EBI-748420
IFT20Q8IY313EBI-359352,EBI-744203
IKZF1Q134223EBI-359352,EBI-745305
IKZF3Q9UKT93EBI-359352,EBI-747204
INO80EQ8NBZ03EBI-359352,EBI-769401
KAZNQ674X7-24EBI-359352,EBI-12024294
KCTD1Q719H93EBI-359352,EBI-9027502
KCTD6Q8NC694EBI-359352,EBI-2511344
KCTD9Q7L2735EBI-359352,EBI-4397613
KRT15P190124EBI-359352,EBI-739566
KRT31Q153233EBI-359352,EBI-948001
KRT38O760155EBI-359352,EBI-1047263
KRT40Q6A1623EBI-359352,EBI-10171697
KRTAP5-9P263715EBI-359352,EBI-3958099
LDOC1O957517EBI-359352,EBI-740738
LZTS2Q9BRK43EBI-359352,EBI-741037
MAD1L1Q9Y6D93EBI-359352,EBI-742610
MAPRE1Q156915EBI-359352,EBI-1004115
MAPRE3Q9UPY84EBI-359352,EBI-726739
MID2Q9UJV3-25EBI-359352,EBI-10172526
MKRN3Q130645EBI-359352,EBI-2340269
MLH1P406923EBI-359352,EBI-744248
MRFAP1L1Q96HT84EBI-359352,EBI-748896
MTUS2Q5JR596EBI-359352,EBI-742948
NOTCH2NLAQ7Z3S95EBI-359352,EBI-945833
PNMA1Q8ND905EBI-359352,EBI-302345
PNMA2Q9UL423EBI-359352,EBI-302355
PNMA5Q96PV43EBI-359352,EBI-10171633
PRDM14Q9GZV83EBI-359352,EBI-3957793
PSMA2P257878EBI-359352,EBI-603262
PSMA3P2578813EBI-359352,EBI-348380
PSMA4P257897EBI-359352,EBI-359310
PSMA7O1481814EBI-359352,EBI-603272
PSMB2P497217EBI-359352,EBI-359335
RELQ048643EBI-359352,EBI-307352
ROPN1Q9HAT05EBI-359352,EBI-1378139
SH3GLB1Q9Y3713EBI-359352,EBI-2623095
SSX2IPQ9Y2D83EBI-359352,EBI-2212028
TCF12Q990813EBI-359352,EBI-722877
TCF4P158843EBI-359352,EBI-533224
TNFAIP1Q138293EBI-359352,EBI-2505861
TNRA1L3063EBI-359352,EBI-10182881
TRAF1Q130773EBI-359352,EBI-359224
TRIM10Q9UDY63EBI-359352,EBI-6427325
TRIM23P364065EBI-359352,EBI-740098
TRIM27P143735EBI-359352,EBI-719493
TRIM42Q8IWZ53EBI-359352,EBI-5235829
UBXN11Q5T1243EBI-359352,EBI-746004

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111655, 217 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P25786

Database of interacting proteins

More...DIPi		DIP-29369N

Protein interaction database and analysis system

More...IntActi		P25786, 220 interactors

Molecular INTeraction database

More...MINTi		P25786

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000414359

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P25786

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

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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-ray2.60F/T4-241[»]
4R67X-ray2.89F/T/h/v4-241[»]
5A0Qelectron microscopy3.50F/T1-263[»]
5GJQelectron microscopy4.50G/m1-263[»]
5GJRelectron microscopy3.50G/m1-263[»]
5L4Gelectron microscopy4.02F/S1-263[»]
5LE5X-ray1.80E/S1-263[»]
5LEXX-ray2.20E/S1-263[»]
5LEYX-ray1.90E/S1-263[»]
5LEZX-ray2.19E/S1-263[»]
5LF0X-ray2.41E/S1-263[»]
5LF1X-ray2.00E/S1-263[»]
5LF3X-ray2.10E/S1-263[»]
5LF4X-ray1.99E/S1-263[»]
5LF6X-ray2.07E/S1-263[»]
5LF7X-ray2.00E/S1-263[»]
5LN3electron microscopy6.80F1-263[»]
5M32electron microscopy3.80E/S2-239[»]
5T0Celectron microscopy3.80AL/BL2-263[»]
5T0Gelectron microscopy4.40L2-263[»]
5T0Helectron microscopy6.80L2-263[»]
5T0Ielectron microscopy8.00L2-263[»]
5T0Jelectron microscopy8.00L2-263[»]
5VFOelectron microscopy3.50L/l4-241[»]
5VFPelectron microscopy4.20L/l4-241[»]
5VFQelectron microscopy4.20L/l4-241[»]
5VFRelectron microscopy4.90L/l4-241[»]
5VFSelectron microscopy3.60L/l4-241[»]
5VFTelectron microscopy7.00L/l4-241[»]
5VFUelectron microscopy5.80L/l4-241[»]
6AVOelectron microscopy3.80G/L1-263[»]
6MSBelectron microscopy3.00L/l2-263[»]
6MSDelectron microscopy3.20L/l2-263[»]
6MSEelectron microscopy3.30Z56-234[»]
6MSGelectron microscopy3.50L/l2-263[»]
6MSHelectron microscopy3.60L/l2-263[»]
6MSJelectron microscopy3.30L/l2-263[»]
6MSKelectron microscopy3.20L/l2-263[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P25786

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

More...SMRi		P25786

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		KOG0863 Eukaryota
COG0638 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074855

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000091080

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG105373

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P25786

KEGG Orthology (KO)

More...KOi		K02725

Identification of Orthologs from Complete Genome Data

More...OMAi		CPSANYY

Database of Orthologous Groups

More...OrthoDBi		1222564at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P25786

TreeFam database of animal gene trees

More...TreeFami		TF106206

Family and domain databases

Conserved Domains Database

More...CDDi		cd03749 proteasome_alpha_type_1, 1 hit

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
IPR035144 Proteasome_alpha1
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF12 PTHR11599:SF12, 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.

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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Short (identifier: P25786-1) [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
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK 
        60         70         80         90        100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD 
       110        120        130        140        150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS 
       160        170        180        190        200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP 
       210        220        230        240        250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPAQPA 
       260 
DEPAEKADEP MEH
Length:263
Mass (Da):29,556
Last modified:May 1, 1992 - 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:i3F159C5BCEFE8DED
GO
Isoform Long (identifier: P25786-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQLSKVK

Show »
Length:269
Mass (Da):30,239
Checksum:iDB7435F82890F923
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GX11F5GX11_HUMAN
Proteasome endopeptidase complex
PSMA1
238Annotation score:

Annotation score:3 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>
F5H112F5H112_HUMAN
Proteasome subunit alpha type-1
PSMA1
14Annotation 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 conflicti14 – 15SP → TA in AAA92734 (PubMed:1398136).Curated2

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_06745437G → V2 PublicationsCorresponds to variant dbSNP:rs17850016Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0052791M → MQLSKVK in isoform Long. 1 Publication1

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
X61969 mRNA Translation: CAA43961.1
D00759 mRNA Translation: BAA00656.1
M64992 mRNA Translation: AAA92734.1
BT006647 mRNA Translation: AAP35293.1
AK290765 mRNA Translation: BAF83454.1
CH471064 Genomic DNA Translation: EAW68479.1
BC002577 mRNA Translation: AAH02577.1
BC005932 mRNA Translation: AAH05932.1
BC008472 mRNA Translation: AAH08472.1
BC009576 mRNA Translation: AAH09576.1
BC015105 mRNA Translation: AAH15105.1
BC015356 mRNA Translation: AAH15356.1
BC022372 mRNA Translation: AAH22372.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31431.1 [P25786-2]
CCDS7816.1 [P25786-1]

Protein sequence database of the Protein Information Resource

More...PIRi		JC1445

NCBI Reference Sequences

More...RefSeqi		NP_002777.1, NM_002786.3 [P25786-1]
NP_683877.1, NM_148976.2 [P25786-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.102798

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000396394; ENSP00000379676; ENSG00000129084 [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084 [P25786-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5682

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5682

UCSC genome browser

More...UCSCi		uc001mlk.4 human [P25786-1]

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
X61969 mRNA Translation: CAA43961.1
D00759 mRNA Translation: BAA00656.1
M64992 mRNA Translation: AAA92734.1
BT006647 mRNA Translation: AAP35293.1
AK290765 mRNA Translation: BAF83454.1
CH471064 Genomic DNA Translation: EAW68479.1
BC002577 mRNA Translation: AAH02577.1
BC005932 mRNA Translation: AAH05932.1
BC008472 mRNA Translation: AAH08472.1
BC009576 mRNA Translation: AAH09576.1
BC015105 mRNA Translation: AAH15105.1
BC015356 mRNA Translation: AAH15356.1
BC022372 mRNA Translation: AAH22372.1
CCDSiCCDS31431.1 [P25786-2]
CCDS7816.1 [P25786-1]
PIRiJC1445
RefSeqiNP_002777.1, NM_002786.3 [P25786-1]
NP_683877.1, NM_148976.2 [P25786-2]
UniGeneiHs.102798

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60F/T4-241[»]
4R67X-ray2.89F/T/h/v4-241[»]
5A0Qelectron microscopy3.50F/T1-263[»]
5GJQelectron microscopy4.50G/m1-263[»]
5GJRelectron microscopy3.50G/m1-263[»]
5L4Gelectron microscopy4.02F/S1-263[»]
5LE5X-ray1.80E/S1-263[»]
5LEXX-ray2.20E/S1-263[»]
5LEYX-ray1.90E/S1-263[»]
5LEZX-ray2.19E/S1-263[»]
5LF0X-ray2.41E/S1-263[»]
5LF1X-ray2.00E/S1-263[»]
5LF3X-ray2.10E/S1-263[»]
5LF4X-ray1.99E/S1-263[»]
5LF6X-ray2.07E/S1-263[»]
5LF7X-ray2.00E/S1-263[»]
5LN3electron microscopy6.80F1-263[»]
5M32electron microscopy3.80E/S2-239[»]
5T0Celectron microscopy3.80AL/BL2-263[»]
5T0Gelectron microscopy4.40L2-263[»]
5T0Helectron microscopy6.80L2-263[»]
5T0Ielectron microscopy8.00L2-263[»]
5T0Jelectron microscopy8.00L2-263[»]
5VFOelectron microscopy3.50L/l4-241[»]
5VFPelectron microscopy4.20L/l4-241[»]
5VFQelectron microscopy4.20L/l4-241[»]
5VFRelectron microscopy4.90L/l4-241[»]
5VFSelectron microscopy3.60L/l4-241[»]
5VFTelectron microscopy7.00L/l4-241[»]
5VFUelectron microscopy5.80L/l4-241[»]
6AVOelectron microscopy3.80G/L1-263[»]
6MSBelectron microscopy3.00L/l2-263[»]
6MSDelectron microscopy3.20L/l2-263[»]
6MSEelectron microscopy3.30Z56-234[»]
6MSGelectron microscopy3.50L/l2-263[»]
6MSHelectron microscopy3.60L/l2-263[»]
6MSJelectron microscopy3.30L/l2-263[»]
6MSKelectron microscopy3.20L/l2-263[»]
ProteinModelPortaliP25786
SMRiP25786
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111655, 217 interactors
CORUMiP25786
DIPiDIP-29369N
IntActiP25786, 220 interactors
MINTiP25786
STRINGi9606.ENSP00000414359

Chemistry databases

BindingDBiP25786
ChEMBLiCHEMBL3831201

Protein family/group databases

MEROPSiT01.976

PTM databases

iPTMnetiP25786
PhosphoSitePlusiP25786
SwissPalmiP25786

Polymorphism and mutation databases

BioMutaiPSMA1
DMDMi130848

2D gel databases

OGPiP25786
REPRODUCTION-2DPAGEiIPI00016832

Proteomic databases

EPDiP25786
jPOSTiP25786
MaxQBiP25786
PaxDbiP25786
PeptideAtlasiP25786
PRIDEiP25786
ProteomicsDBi54287
54288 [P25786-2]
TopDownProteomicsiP25786-1 [P25786-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5682
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396394; ENSP00000379676; ENSG00000129084 [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084 [P25786-2]
GeneIDi5682
KEGGihsa:5682
UCSCiuc001mlk.4 human [P25786-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5682
DisGeNETi5682
EuPathDBiHostDB:ENSG00000129084.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMA1
HGNCiHGNC:9530 PSMA1
HPAiCAB033765
HPA037646
HPA043891
MIMi602854 gene
neXtProtiNX_P25786
OpenTargetsiENSG00000129084
PharmGKBiPA33875

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0863 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000074855
HOGENOMiHOG000091080
HOVERGENiHBG105373
InParanoidiP25786
KOiK02725
OMAiCPSANYY
OrthoDBi1222564at2759
PhylomeDBiP25786
TreeFamiTF106206

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

Miscellaneous databases

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

More...ChiTaRSi		PSMA1 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Proteasome_(prosome,_macropain)_subunit,_alpha_1

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

More...GenomeRNAii		5682

Protein Ontology

More...PROi		PR:P25786

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000129084 Expressed in 108 organ(s), highest expression level in left adrenal gland
ExpressionAtlasiP25786 baseline and differential
GenevisibleiP25786 HS

Family and domain databases

CDDicd03749 proteasome_alpha_type_1, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR035144 Proteasome_alpha1
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF12 PTHR11599:SF12, 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 nameiPSA1_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: P25786
Secondary accession number(s): A8K400, Q53YE8, Q9BRV9
<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: May 1, 1992
Last modified: February 13, 2019
This is version 219 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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