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UniProtKB - P46881 (PAOX_ARTGO)

Entry version 113 (11 Dec 2019)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
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Protein

Phenylethylamine oxidase

Gene
N/A
Organism
Arthrobacter globiformis
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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei298Proton acceptorBy similarity1
Active sitei382Schiff-base intermediate with substrate; via topaquinoneBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi431Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi433Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi592Copper; via pros nitrogenCombined sources1 Publication1

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.4.3.21 444

<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%5Fand%5Ftaxonomy%5Fsection">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:
Phenylethylamine oxidase (EC:1.4.3.21By similarity)
Alternative name(s):
Primary amine oxidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiArthrobacter globiformis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1665 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Actinobacteria › Micrococcales › Micrococcaceae › Arthrobacter

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi382Y → F: Loss of activity. 1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02511 2-Hydroxy-5-({1-[(2-Naphthyloxy)Methyl]-3-Oxoprop-1-Enyl}Amino)Tyrosine
DB02537 2-Hydroxy-5-({1-[(4-Methylphenoxy)Methyl]-3-Oxoprop-1-Enyl}Amino)-L-Tyrosine
DB06988 2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE
DB04334 6-hydroxydopa quinone

<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%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000356811 – 22
<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_00000356823 – 638Phenylethylamine oxidaseAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi317 ↔ 343Combined sources1 Publication
<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 residuei3822',4',5'-topaquinone1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication

Keywords - PTMi

Disulfide bond, TPQ

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P46881

<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

By phenethylamine.

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<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

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P46881

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P46881

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni296 – 307Substrate bindingBy similarityAdd BLAST12
Regioni379 – 384Substrate bindingBy similarity6

<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 copper/topaquinone oxidase family.Curated

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K00276

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.70.98.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015802 Cu_amine_oxidase_N3

The PANTHER Classification System

More...PANTHERi		PTHR10638 PTHR10638, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P46881-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPSTIQTAS PFRLASAGEI SEVQGILRTA GLLGPEKRIA YLGVLDPARG 
        60         70         80         90        100
AGSEAEDRRF RVFIHDVSGA RPQEVTVSVT NGTVISAVEL DTAATGELPV 
       110        120        130        140        150
LEEEFEVVEQ LLATDERWLK ALAARNLDVS KVRVAPLSAG VFEYAEERGR 
       160        170        180        190        200
RILRGLAFVQ DFPEDSAWAH PVDGLVAYVD VVSKEVTRVI DTGVFPVPAE 
       210        220        230        240        250
HGNYTDPELT GPLRTTQKPI SITQPEGPSF TVTGGNHIEW EKWSLDVGFD 
       260        270        280        290        300
VREGVVLHNI AFRDGDRLRP IINRASIAEM VVPYGDPSPI RSWQNYFDTG 
       310        320        330        340        350
EYLVGQYANS LELGCDCLGD ITYLSPVISD AFGNPREIRN GICMHEEDWG 
       360        370        380        390        400
ILAKHSDLWS GINYTRRNRR MVISFFTTIG NYDYGFYWYL YLDGTIEFEA 
       410        420        430        440        450
KATGVVFTSA FPEGGSDNIS QLAPGLGAPF HQHIFSARLD MAIDGFTNRV 
       460        470        480        490        500
EEEDVVRQTM GPGNERGNAF SRKRTVLTRE SEAVREADAR TGRTWIISNP 
       510        520        530        540        550
ESKNRLNEPV GYKLHAHNQP TLLADPGSSI ARRAAFATKD LWVTRYADDE 
       560        570        580        590        600
RYPTGDFVNQ HSGGAGLPSY IAQDRDIDGQ DIVVWHTFGL THFPRVEDWP 
       610        620        630 
IMPVDTVGFK LRPEGFFDRS PVLDVPANPS QSGSHCHG
Length:638
Mass (Da):70,646
Last modified:November 1, 1995 - 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:i1800396BA7A983F2
GO

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
U03517 Unassigned DNA Translation: AAA18114.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC2139

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:AAA18114

<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
U03517 Unassigned DNA Translation: AAA18114.1
PIRiJC2139

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
1AV4X-ray2.20A1-638[»]
1AVKX-ray2.20A1-638[»]
1AVLX-ray2.80A1-638[»]
1IQXX-ray2.00A/B1-638[»]
1IQYX-ray1.80A/B1-638[»]
1IU7X-ray1.80A/B1-638[»]
1IVUX-ray1.90A/B1-638[»]
1IVVX-ray2.10A/B1-638[»]
1IVWX-ray1.80A/B1-638[»]
1IVXX-ray2.20A/B1-638[»]
1RJOX-ray1.67A3-638[»]
1SIHX-ray1.73A3-638[»]
1SIIX-ray1.70A3-638[»]
1UI7X-ray2.00A/B1-638[»]
1UI8X-ray1.80A/B1-638[»]
1W4NX-ray1.65A/B3-638[»]
1W5ZX-ray1.86A3-638[»]
1W6CX-ray2.20A3-638[»]
1W6GX-ray1.55A3-638[»]
1WMNX-ray1.80A/B1-638[»]
1WMOX-ray1.80A/B1-638[»]
1WMPX-ray2.00A/B1-638[»]
2BT3X-ray1.73A3-638[»]
2CFDX-ray1.60A/B3-638[»]
2CFGX-ray1.55A/B3-638[»]
2CFKX-ray1.80A3-638[»]
2CFLX-ray1.80A3-638[»]
2CFWX-ray1.74A3-638[»]
2CG0X-ray1.80A3-638[»]
2CG1X-ray1.67A3-638[»]
2CWTX-ray1.82A/B1-638[»]
2CWUX-ray1.85A/B1-638[»]
2CWVX-ray1.85A/B1-638[»]
2D1WX-ray1.74A/B1-638[»]
2E2TX-ray2.05A1-638[»]
2E2UX-ray1.68A/B1-628[»]
2E2VX-ray1.80A/B1-628[»]
2YX9X-ray1.68A/B1-638[»]
2ZL8X-ray1.73A/B1-638[»]
3AMOX-ray2.10A/B1-638[»]
3KIIX-ray1.90A/B3-638[»]
3KN4X-ray2.05A3-638[»]
3WA2X-ray1.08X9-629[»]
3WA3X-ray1.55A/B9-629[»]
3X3XX-ray1.57A/B9-628[»]
3X3YX-ray1.50A/B9-628[»]
3X3ZX-ray1.51A/B9-628[»]
3X40X-ray1.85A/B9-628[»]
3X41X-ray1.87A/B9-628[»]
3X42X-ray1.88A/B9-629[»]
5ZOUX-ray1.68A/B9-628[»]
5ZOWX-ray1.78A/B9-628[»]
5ZOXX-ray1.69A/B9-628[»]
5ZOYX-ray1.70A/B9-628[»]
5ZOZX-ray1.70A/B9-628[»]
5ZP0X-ray1.74A/B9-628[»]
5ZP1X-ray1.67A/B9-628[»]
5ZP2X-ray1.75A/B9-628[»]
5ZP3X-ray1.78A/B9-628[»]
5ZP4X-ray1.80A/B9-628[»]
5ZP5X-ray1.77A/B9-628[»]
5ZP6X-ray1.69A/B9-628[»]
5ZP7X-ray1.63A/B9-628[»]
5ZP8X-ray1.66A/B9-628[»]
5ZP9X-ray1.70A/B9-628[»]
5ZPAX-ray1.69A/B9-628[»]
5ZPBX-ray1.79A/B9-628[»]
5ZPCX-ray1.74A/B9-628[»]
5ZPDX-ray1.67A/B9-628[»]
5ZPEX-ray1.69A/B9-628[»]
5ZPFX-ray1.76A/B9-628[»]
5ZPGX-ray1.65A/B9-628[»]
5ZPHX-ray1.72A/B9-628[»]
5ZPIX-ray1.75A/B9-628[»]
5ZPJX-ray1.65A/B9-628[»]
5ZPKX-ray1.65A/B9-628[»]
5ZPLX-ray1.60A/B9-628[»]
5ZPMX-ray1.65A/B9-628[»]
5ZPNX-ray1.60A/B9-628[»]
5ZPOX-ray1.73A/B9-628[»]
5ZPPX-ray1.81A/B9-628[»]
5ZPQX-ray1.85A/B9-628[»]
5ZPRX-ray1.92A/B9-628[»]
5ZPSX-ray1.75A/B9-628[»]
5ZPTX-ray1.90A/B9-628[»]
SMRiP46881
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB02511 2-Hydroxy-5-({1-[(2-Naphthyloxy)Methyl]-3-Oxoprop-1-Enyl}Amino)Tyrosine
DB02537 2-Hydroxy-5-({1-[(4-Methylphenoxy)Methyl]-3-Oxoprop-1-Enyl}Amino)-L-Tyrosine
DB06988 2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE
DB04334 6-hydroxydopa quinone

Proteomic databases

PRIDEiP46881

Genome annotation databases

KEGGiag:AAA18114

Phylogenomic databases

KOiK00276

Enzyme and pathway databases

BRENDAi1.4.3.21 444

Miscellaneous databases

EvolutionaryTraceiP46881

Family and domain databases

Gene3Di2.70.98.20, 1 hit
InterProiView protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015802 Cu_amine_oxidase_N3
PANTHERiPTHR10638 PTHR10638, 1 hit
PfamiView protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit
SUPFAMiSSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
PROSITEiView protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAOX_ARTGO
<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: P46881
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 11, 2019
This is version 113 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 programProkaryotic Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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