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UniProtKB - P02692 (FABPL_RAT)

Protein

Fatty acid-binding protein, liver

Gene

Fabp1

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

Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (By similarity). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity).By similarity1 Publication

Miscellaneous

There are three fractions of Z-protein: DE-I, DE-II and DE-III. DE-I is virtually lipid free, DE-II binds palmitic, stearic, oleic, linoleic and arachidonic acids and DE-III binds mainly arachidonic acid.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei31Fatty acid 11 Publication1
Binding sitei39Fatty acid 21 Publication1
Binding sitei122Fatty acid 21 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

  • antioxidant activity Source: Ensembl
  • bile acid binding Source: RGD
  • chromatin binding Source: Ensembl
  • drug binding Source: RGD
  • fatty acid binding Source: RGD
  • long-chain fatty acid transporter activity Source: RGD
  • lysophospholipid transporter activity Source: RGD
  • phospholipid binding Source: RGD
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

Biological processTransport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-163560 Triglyceride catabolism
R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001517

<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:
Fatty acid-binding protein, liver
Alternative name(s):
Fatty acid-binding protein 1
Liver-type fatty acid-binding protein
Short name:
L-FABP
Squalene- and sterol-carrier protein
Short name:
SCP
Z-protein
p14
<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:Fabp1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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 4

Organism-specific databases

Rat genome database

More...RGDi		2590 Fabp1

<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

<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		CHEMBL5738

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2531

<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_00000673371 – 127Fatty acid-binding protein, liverAdd 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 residuei1N-acetylmethionine2 Publications1
Modified residuei11PhosphoserineCombined sources1
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei36N6-succinyllysineBy similarity1
Modified residuei39PhosphoserineCombined sources1
Modified residuei46N6-succinyllysineBy similarity1
Modified residuei51PhosphothreonineBy similarity1
Modified residuei56PhosphoserineCombined sources1
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei78N6-succinyllysineBy similarity1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei90N6-succinyllysineBy similarity1
Modified residuei100PhosphoserineBy 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-linki105 ↔ 106Isoaspartyl glycine isopeptide (Asn-Gly); alternate
Modified residuei105Deamidated asparagine; alternate1 Publication1
Modified residuei121N6-succinyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Deamidation and transpeptidation at the beta carboxyl of Asn-105 forms an isoaspartyl residue found in an isoform of the DE-III fraction. This rearrangement gives rise to an extra negative charge carried by the acid form.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P02692

PRoteomics IDEntifications database

More...PRIDEi		P02692

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P02692

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02692

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

More...PhosphoSitePlusi		P02692

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000006675 Expressed in 8 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02692 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%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
Hnf4aP224493EBI-1209448,EBI-5261592

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P02692, 2 interactors

Molecular INTeraction database

More...MINTi		P02692

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000008841

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P02692

<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

1127
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
1LFOX-ray2.30A1-127[»]
2JU3NMR-A1-127[»]
2JU7NMR-A1-127[»]
2JU8NMR-A1-127[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02692

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

More...SMRi		P02692

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02692

<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>Regioni54 – 56Fatty acid 1 binding3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

<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 calycin superfamily. Fatty-acid binding protein (FABP) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4015 Eukaryota
ENOG4111US8 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155135

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000004830

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005633

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02692

KEGG Orthology (KO)

More...KOi		K08750

Identification of Orthologs from Complete Genome Data

More...OMAi		FTLGEEC

Database of Orthologous Groups

More...OrthoDBi		1440574at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02692

TreeFam database of animal gene trees

More...TreeFami		TF330348

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.128.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012674 Calycin
IPR000463 Fatty_acid-bd
IPR031259 ILBP
IPR031276 Lb-FABP

The PANTHER Classification System

More...PANTHERi		PTHR11955 PTHR11955, 1 hit
PTHR11955:SF96 PTHR11955:SF96, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00178 FATTYACIDBP

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50814 SSF50814, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00214 FABP, 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>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.

P02692-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNFSGKYQVQ SQENFEPFMK AMGLPEDLIQ KGKDIKGVSE IVHEGKKVKL 
        60         70         80         90        100
TITYGSKVIH NEFTLGEECE LETMTGEKVK AVVKMEGDNK MVTTFKGIKS 
       110        120 
VTEFNGDTIT NTMTLGDIVY KRVSKRI
Length:127
Mass (Da):14,273
Last modified:August 13, 1987 - 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:i08C7F59A99FE0D3A
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
V01235 mRNA Translation: CAA24545.1
M13501 Genomic DNA Translation: AAA41140.1
M35991 mRNA Translation: AAA41135.1
S55929 Other DNA Translation: AAB19788.1
BC086947 mRNA Translation: AAH86947.1
M17899 mRNA Translation: AAA41134.1
M10951 mRNA Translation: AAA42119.1

Protein sequence database of the Protein Information Resource

More...PIRi		A92416 FZRTL
I52354
I52850
I55238

NCBI Reference Sequences

More...RefSeqi		NP_036688.1, NM_012556.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Rn.36412

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24360

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24360

UCSC genome browser

More...UCSCi		RGD:2590 rat

<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
V01235 mRNA Translation: CAA24545.1
M13501 Genomic DNA Translation: AAA41140.1
M35991 mRNA Translation: AAA41135.1
S55929 Other DNA Translation: AAB19788.1
BC086947 mRNA Translation: AAH86947.1
M17899 mRNA Translation: AAA41134.1
M10951 mRNA Translation: AAA42119.1
PIRiA92416 FZRTL
I52354
I52850
I55238
RefSeqiNP_036688.1, NM_012556.2
UniGeneiRn.36412

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LFOX-ray2.30A1-127[»]
2JU3NMR-A1-127[»]
2JU7NMR-A1-127[»]
2JU8NMR-A1-127[»]
ProteinModelPortaliP02692
SMRiP02692
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02692, 2 interactors
MINTiP02692
STRINGi10116.ENSRNOP00000008841

Chemistry databases

BindingDBiP02692
ChEMBLiCHEMBL5738
GuidetoPHARMACOLOGYi2531
SwissLipidsiSLP:000001517

PTM databases

CarbonylDBiP02692
iPTMnetiP02692
PhosphoSitePlusiP02692

Proteomic databases

PaxDbiP02692
PRIDEiP02692

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008840; ENSRNOP00000008841; ENSRNOG00000006675
GeneIDi24360
KEGGirno:24360
UCSCiRGD:2590 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2168
RGDi2590 Fabp1

Phylogenomic databases

eggNOGiKOG4015 Eukaryota
ENOG4111US8 LUCA
GeneTreeiENSGT00940000155135
HOGENOMiHOG000004830
HOVERGENiHBG005633
InParanoidiP02692
KOiK08750
OMAiFTLGEEC
OrthoDBi1440574at2759
PhylomeDBiP02692
TreeFamiTF330348

Enzyme and pathway databases

ReactomeiR-RNO-163560 Triglyceride catabolism
R-RNO-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)

Miscellaneous databases

EvolutionaryTraceiP02692

Protein Ontology

More...PROi		PR:P02692

Gene expression databases

BgeeiENSRNOG00000006675 Expressed in 8 organ(s), highest expression level in liver
GenevisibleiP02692 RN

Family and domain databases

Gene3Di2.40.128.20, 1 hit
InterProiView protein in InterPro
IPR012674 Calycin
IPR000463 Fatty_acid-bd
IPR031259 ILBP
IPR031276 Lb-FABP
PANTHERiPTHR11955 PTHR11955, 1 hit
PTHR11955:SF96 PTHR11955:SF96, 1 hit
PRINTSiPR00178 FATTYACIDBP
SUPFAMiSSF50814 SSF50814, 1 hit
PROSITEiView protein in PROSITE
PS00214 FABP, 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 nameiFABPL_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: P02692
<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: August 13, 1987
Last modified: January 16, 2019
This is version 175 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
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