Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback. Take me to UniProt BETA

UniProtKB - P17289 (TY3H_BOVIN)

Entry version 144 (25 May 2022)
Sequence version 5 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Tyrosine 3-monooxygenase

Gene

TH

Organism
Bos taurus (Bovine)
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

Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity).

In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity).

Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity).

By similarity

<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

Fe2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited in feedback fashion by the catecholamine neurotransmitters, especially by dopamine in competition with tetrahydrobiopterin. Phosphorylation of several Ser/Thr residues in the N-terminus regulates the catalytic activity. Ser-31 and Ser-40 are readily phosphorylated to activate the catalytic activity. A Cysteine modification induced by N-ethylmaleimide (NEM), inhibits tyrosine 3-monooxygenase activity through the modification of the Cys-170.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dopamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dopamine from L-tyrosine.By similarity This subpathway is part of the pathway dopamine biosynthesis, which is itself part of Catecholamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dopamine from L-tyrosine, the pathway dopamine biosynthesis and in Catecholamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi324Iron; via tele nitrogenBy similarity1
Metal bindingi329Iron; via tele nitrogenBy similarity1
Metal bindingi369IronBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei418Important for substrate specificityBy similarity1

<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 functionMonooxygenase, Oxidoreductase
Biological processCatecholamine biosynthesis, Neurotransmitter biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P17289

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00747;UER00733

<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:
Tyrosine 3-monooxygenase (EC:1.14.16.2By similarity)
Alternative name(s):
Tyrosine 3-hydroxylase
Short name:
TH
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:TH
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

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

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Nucleus, Synapse

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3713

<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 indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002055602 – 491Tyrosine 3-monooxygenaseAdd BLAST490

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 residuei19Phosphoserine; by CaMK21 Publication1
Modified residuei31Phosphoserine1 Publication1
Modified residuei40Phosphoserine; by CaMK2 and PKA1 Publication1
Modified residuei465PhosphoserineBy similarity1

<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

Phosphorylated on Ser-19, Ser-31 and Ser-40 by several protein kinases with different site specificities. Phosphorylation at Ser-31 and Ser-40 leads to an increase of TH activity. Phosphorylation at Ser-40 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (By similarity). Phosphorylation of Ser-19 and Ser-31 triggers the proteasomal degradation of TH through the ubiquitin-proteasome pathway (By similarity). Phosphorylation at Ser-31 facilitates transport of TH from the soma to the nerve terminals via the microtubule network (By similarity). Phosphorylation at Ser-19 induces the high-affinity binding to the 14-3-3 protein YWHAG; this interaction may influence the phosphorylation and dephosphorylation of other sites (By similarity). Ser-19 increases the phosphorylation at Ser-40 in a hierarchical manner, leading to increased activity (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...PaxDbi		P17289

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17289

<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

Homotetramer (By similarity).

Interacts (when phosphorylated at Ser-19) with YWHAG; one YWHAG dimer bounds to one TH tetramer this interaction may influence the phosphorylation and dephosphorylation of other sites (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000038050

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P17289

<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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P17289

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

More...SMRi		P17289

Database of comparative protein structure models

More...ModBasei		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 biopterin-dependent aromatic amino acid hydroxylase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3820, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17289

Database of Orthologous Groups

More...OrthoDBi		614557at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd03345, eu_TyrOH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.800.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR045865, ACT-like_dom_sf
IPR001273, ArAA_hydroxylase
IPR036951, ArAA_hydroxylase_sf
IPR036329, Aro-AA_hydroxylase_C_sf
IPR019774, Aromatic-AA_hydroxylase_C
IPR041903, Eu_TyrOH_cat
IPR005962, Tyr_3_mOase
IPR019773, Tyrosine_3-monooxygenase-like
IPR021164, Tyrosine_hydroxylase_CS

The PANTHER Classification System

More...PANTHERi		PTHR11473, PTHR11473, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00351, Biopterin_H, 1 hit
PF12549, TOH_N, 2 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000336, TH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00372, FYWHYDRXLASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55021, SSF55021, 1 hit
SSF56534, SSF56534, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01269, Tyr_3_monoox, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51410, BH4_AAA_HYDROXYL_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.

P17289-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPTPNAASPQ AKGFRRAVSE LDAKQAEAIM SPRFVGRRQS LIQDARKERE 
        60         70         80         90        100
KAEAAASSSE SAEAAAWLER DGEAVLTLLF ALPPTRPPAL TRAIKVFETF 
       110        120        130        140        150
EAHLHHLETR PAQPLRAGSP PLECFVRCEV PGPVVPALLS ALRRVAEDVR 
       160        170        180        190        200
AAGESKVLWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI 
       210        220        230        240        250
AEIAFQYKQG DPIPHVEYTA EETATWKEVY STLRGLYPTH ACREHLEAFE 
       260        270        280        290        300
LLERFCGYRE DRIPQLEDVS RFLKERTGFQ LRPAAGLLSA RDFLASLAFR 
       310        320        330        340        350
VFQCTQYIRH ASSPMHSPEP ECCHELLGHV PMLADRTFAQ FSQDIGLASL 
       360        370        380        390        400
GVSDEEIEKL STLYWFTVEF GLCKQNGEVK AYGAGLLSSY GELLHSLSEE 
       410        420        430        440        450
PEIRAFDPDA AAVQPYQDQT YQPVYFVSES FSDAKDKLRS YASRIQRPFS 
       460        470        480        490 
VKFDPYTLAI DVLDSPHAIR HALDGVQDEM QALAHALNAI S
Length:491
Mass (Da):55,123
Last modified:January 23, 2007 - v5
<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:i86707712238F12F2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti65 – 68AAWL → GSLV in AAA30798 (PubMed:2899135).Curated4
Sequence conflicti73E → K in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti83P → R in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti86R → K in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti284A → V in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti321E → D in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti328 – 330GHV → AHG in AAA30798 (PubMed:2899135).Curated3
Sequence conflicti380K → N in AAA30798 (PubMed:2899135).Curated1
Sequence conflicti471H → R in AAA30798 (PubMed:2899135).Curated1

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
M36794 mRNA Translation: AAA30779.1
M36705 mRNA Translation: AAA30798.1

Protein sequence database of the Protein Information Resource

More...PIRi		I45983
JL0039

NCBI Reference Sequences

More...RefSeqi		NP_776309.1, NM_173884.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		280707

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:280707

<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
M36794 mRNA Translation: AAA30779.1
M36705 mRNA Translation: AAA30798.1
PIRiI45983
JL0039
RefSeqiNP_776309.1, NM_173884.2

3D structure databases

AlphaFoldDBiP17289
SMRiP17289
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000038050

Chemistry databases

BindingDBiP17289
ChEMBLiCHEMBL3713

PTM databases

iPTMnetiP17289

Proteomic databases

PaxDbiP17289

Genome annotation databases

GeneIDi280707
KEGGibta:280707

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7054

Phylogenomic databases

eggNOGiKOG3820, Eukaryota
InParanoidiP17289
OrthoDBi614557at2759

Enzyme and pathway databases

UniPathwayiUPA00747;UER00733
SABIO-RKiP17289

Miscellaneous databases

Protein Ontology

More...PROi		PR:P17289

Family and domain databases

CDDicd03345, eu_TyrOH, 1 hit
Gene3Di1.10.800.10, 1 hit
InterProiView protein in InterPro
IPR045865, ACT-like_dom_sf
IPR001273, ArAA_hydroxylase
IPR036951, ArAA_hydroxylase_sf
IPR036329, Aro-AA_hydroxylase_C_sf
IPR019774, Aromatic-AA_hydroxylase_C
IPR041903, Eu_TyrOH_cat
IPR005962, Tyr_3_mOase
IPR019773, Tyrosine_3-monooxygenase-like
IPR021164, Tyrosine_hydroxylase_CS
PANTHERiPTHR11473, PTHR11473, 1 hit
PfamiView protein in Pfam
PF00351, Biopterin_H, 1 hit
PF12549, TOH_N, 2 hits
PIRSFiPIRSF000336, TH, 1 hit
PRINTSiPR00372, FYWHYDRXLASE
SUPFAMiSSF55021, SSF55021, 1 hit
SSF56534, SSF56534, 1 hit
TIGRFAMsiTIGR01269, Tyr_3_monoox, 1 hit
PROSITEiView protein in PROSITE
PS51410, BH4_AAA_HYDROXYL_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTY3H_BOVIN
<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: P17289
<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: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 144 of the entry and version 5 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again