Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 166 (16 Oct 2019)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Transthyretin

Gene

Ttr

Organism
Rattus norvegicus (Rat)
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

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.1 Publication

Miscellaneous

This protein binds retinol-binding protein at levels similar to, and the thyroid hormones at levels much higher than, the human protein.
Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei35Thyroid hormone1
Binding sitei74Thyroid hormone1

<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

GO - Biological processi

<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 functionHormone, Thyroid hormone
Biological processTransport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2453902 The canonical retinoid cycle in rods (twilight vision)
R-RNO-3000171 Non-integrin membrane-ECM interactions
R-RNO-6798695 Neutrophil degranulation
R-RNO-975634 Retinoid metabolism and transport

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.B.35.1.1 the putative thyronine-transporting transthyretin (transthyretin) family

<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:
Transthyretin
Alternative name(s):
Prealbumin
TBPA
<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:Ttr
Synonyms:Tt
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 18

Organism-specific databases

Rat genome database

More...
RGDi
3916 Ttr

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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
CHEMBL2151

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 201 PublicationAdd BLAST20
<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_000003576421 – 147TransthyretinAdd BLAST127

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 residuei624-carboxyglutamateBy similarity1
Modified residuei72PhosphoserineCombined 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>Glycosylationi118N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Gamma-carboxyglutamic acid, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P02767

PRoteomics IDEntifications database

More...
PRIDEi
P02767

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02767

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

More...
PhosphoSitePlusi
P02767

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in the choroid plexus. Detected at lower levels in the liver.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000016275 Expressed in 9 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P02767 RN

<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

Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules.

Interacts with RBP4.

3 Publications

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P02767, 2 interactors

Molecular INTeraction database

More...
MINTi
P02767

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000022113

<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

1147
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
P02767

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
P02767

<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>Regioni135 – 139Thyroid hormone binding5

<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 transthyretin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3006 Eukaryota
COG2351 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153229

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000251776

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02767

KEGG Orthology (KO)

More...
KOi
K20731

Identification of Orthologs from Complete Genome Data

More...
OMAi
EPFATGK

Database of Orthologous Groups

More...
OrthoDBi
1453185at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02767

TreeFam database of animal gene trees

More...
TreeFami
TF300210

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023418 Thyroxine_BS
IPR030178 Transthyretin
IPR000895 Transthyretin/HIU_hydrolase
IPR023416 Transthyretin/HIU_hydrolase_d
IPR036817 Transthyretin/HIU_hydrolase_sf
IPR023419 Transthyretin_CS

The PANTHER Classification System

More...
PANTHERi
PTHR10395 PTHR10395, 1 hit
PTHR10395:SF12 PTHR10395:SF12, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00576 Transthyretin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00189 TRNSTHYRETIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00095 TR_THY, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49472 SSF49472, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00768 TRANSTHYRETIN_1, 1 hit
PS00769 TRANSTHYRETIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P02767-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASLRLFLLC LAGLIFASEA GPGGAGESKC PLMVKVLDAV RGSPAVDVAV
60 70 80 90 100
KVFKKTADGS WEPFASGKTA ESGELHGLTT DEKFTEGVYR VELDTKSYWK
110 120 130 140
ALGISPFHEY AEVVFTANDS GHRHYTIAAL LSPYSYSTTA VVSNPQN
Length:147
Mass (Da):15,720
Last modified:July 21, 1986 - 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:i67F00D09BCF195BA
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 conflicti55K → R in AAA41801 (PubMed:3922975).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
K03252 mRNA Translation: AAA41801.1
K03251 Genomic DNA Translation: AAA41802.1
X14876 mRNA Translation: CAA33017.1
AF479660 mRNA Translation: AAL78377.1
BC086946 mRNA Translation: AAH86946.1
M18685 Genomic DNA Translation: AAA40708.1
M20246 Genomic DNA Translation: AAA40709.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A92542 VBRT

NCBI Reference Sequences

More...
RefSeqi
NP_036813.2, NM_012681.2
XP_006254519.1, XM_006254457.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000022113; ENSRNOP00000022113; ENSRNOG00000016275

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24856

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24856

<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
K03252 mRNA Translation: AAA41801.1
K03251 Genomic DNA Translation: AAA41802.1
X14876 mRNA Translation: CAA33017.1
AF479660 mRNA Translation: AAL78377.1
BC086946 mRNA Translation: AAH86946.1
M18685 Genomic DNA Translation: AAA40708.1
M20246 Genomic DNA Translation: AAA40709.1
PIRiA92542 VBRT
RefSeqiNP_036813.2, NM_012681.2
XP_006254519.1, XM_006254457.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GKEX-ray2.50A/B/C/D28-147[»]
1IE4X-ray2.50A/B/C/D21-147[»]
1KGIX-ray1.80A/B/C/D21-147[»]
1KGJX-ray2.30A/B/C/D21-147[»]
1RVSNMR-A125-135[»]
2M5Kelectron microscopy12.70A/B/C/D/E/F/G/H125-135[»]
2M5Melectron microscopy12.20A/B/C/D/E/F/G/H/I/J/K/L125-135[»]
3ZPKNMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P125-135[»]
SMRiP02767
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP02767, 2 interactors
MINTiP02767
STRINGi10116.ENSRNOP00000022113

Chemistry databases

ChEMBLiCHEMBL2151

Protein family/group databases

TCDBi9.B.35.1.1 the putative thyronine-transporting transthyretin (transthyretin) family

PTM databases

iPTMnetiP02767
PhosphoSitePlusiP02767

Proteomic databases

PaxDbiP02767
PRIDEiP02767

Genome annotation databases

EnsembliENSRNOT00000022113; ENSRNOP00000022113; ENSRNOG00000016275
GeneIDi24856
KEGGirno:24856

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7276
RGDi3916 Ttr

Phylogenomic databases

eggNOGiKOG3006 Eukaryota
COG2351 LUCA
GeneTreeiENSGT00940000153229
HOGENOMiHOG000251776
InParanoidiP02767
KOiK20731
OMAiEPFATGK
OrthoDBi1453185at2759
PhylomeDBiP02767
TreeFamiTF300210

Enzyme and pathway databases

ReactomeiR-RNO-2453902 The canonical retinoid cycle in rods (twilight vision)
R-RNO-3000171 Non-integrin membrane-ECM interactions
R-RNO-6798695 Neutrophil degranulation
R-RNO-975634 Retinoid metabolism and transport

Miscellaneous databases

EvolutionaryTraceiP02767

Protein Ontology

More...
PROi
PR:P02767

Gene expression databases

BgeeiENSRNOG00000016275 Expressed in 9 organ(s), highest expression level in liver
GenevisibleiP02767 RN

Family and domain databases

Gene3Di2.60.40.180, 1 hit
InterProiView protein in InterPro
IPR023418 Thyroxine_BS
IPR030178 Transthyretin
IPR000895 Transthyretin/HIU_hydrolase
IPR023416 Transthyretin/HIU_hydrolase_d
IPR036817 Transthyretin/HIU_hydrolase_sf
IPR023419 Transthyretin_CS
PANTHERiPTHR10395 PTHR10395, 1 hit
PTHR10395:SF12 PTHR10395:SF12, 1 hit
PfamiView protein in Pfam
PF00576 Transthyretin, 1 hit
PRINTSiPR00189 TRNSTHYRETIN
SMARTiView protein in SMART
SM00095 TR_THY, 1 hit
SUPFAMiSSF49472 SSF49472, 1 hit
PROSITEiView protein in PROSITE
PS00768 TRANSTHYRETIN_1, 1 hit
PS00769 TRANSTHYRETIN_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 nameiTTHY_RAT
<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: P02767
Secondary accession number(s): Q547K9
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2019
This is version 166 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

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