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Entry version 89 (18 Sep 2019)
Sequence version 2 (02 Oct 2007)
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Protein

Acyl-coenzyme A synthetase ACSM1, mitochondrial

Gene

ACSM1

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 activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (PubMed:11382754, PubMed:10561077). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (PubMed:10561077, PubMed:11382754). Also catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate (PubMed:11382754). Activates lipoate with GTP at a 1000-fold higher rate than with ATP and activates both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate (PubMed:11382754).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Mg2+1 Publication, Mn2+By similarity

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.0047 mM for (R)-lipoate with ATP as phosphate donor1 Publication
  2. KM=0.041 mM for (R)-lipoate with GTP as phosphate donor1 Publication
  3. KM=0.039 mM for (R)-lipoate with CTP as phosphate donor1 Publication
  4. KM=0.18 mM for (R)-lipoate with UTP as phosphate donor1 Publication
  5. KM=1.3 mM for ATP (with (R)-lipoate as substrate)1 Publication
  6. KM=0.37 mM for GTP (with (R)-lipoate as substrate)1 Publication
  7. KM=1.2 mM for CTP (with (R)-lipoate as substrate)1 Publication
  8. KM=8.8 mM for UTP (with (R)-lipoate as substrate)1 Publication
  9. KM=3.9 µM for hexanoate1 Publication
  10. KM=0.32 µM for ATP (with hexanoate as substrate)1 Publication
  1. Vmax=14.3 nmol/h/mg enzyme for (R)-lipoate with ATP as phosphate donor1 Publication
  2. Vmax=15300 nmol/h/mg enzyme for (R)-lipoate with GTP as phosphate donor1 Publication
  3. Vmax=12700 nmol/h/mg enzyme for (R)-lipoate with CTP as phosphate donor1 Publication
  4. Vmax=13000 nmol/h/mg enzyme for (R)-lipoate with UTP as phosphate donor1 Publication
  5. Vmax=14.4 nmol/h/mg enzyme for ATP (with (R)-lipoate as substrate)1 Publication
  6. Vmax=13800 nmol/h/mg enzyme for GTP (with (R)-lipoate as substrate)1 Publication
  7. Vmax=13500 nmol/h/mg enzyme for CTP (with (R)-lipoate as substrate)1 Publication
  8. Vmax=14100 nmol/h/mg enzyme for UTP (with (R)-lipoate as substrate)1 Publication

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 sitei452ATPBy similarity1
Binding sitei467ATPBy similarity1
Binding sitei563ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi226 – 234ATPBy similarity9

<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 functionLigase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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:
Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC:6.2.1.21 Publication)
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 1
Benzoate--CoA ligase (EC:6.2.1.251 Publication)
Butyrate--CoA ligase 1
Butyryl-coenzyme A synthetase 1
Lipoate-activating enzyme1 Publication
Middle-chain acyl-CoA synthetase 1
XL-III
Xenobiotic/medium-chain fatty acid:CoA ligase XL-3
Short name:
XM-ligase 3
<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:ACSM1
Synonyms:BUCS1, LAE1 Publication, MACS1
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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: 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

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

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 31Mitochondrion1 PublicationAdd BLAST31
<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_500004963032 – 577Acyl-coenzyme A synthetase ACSM1, mitochondrialAdd BLAST546

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 residuei85N6-succinyllysineBy similarity1
Modified residuei146N6-acetyllysine; alternateBy similarity1
Modified residuei146N6-succinyllysine; alternateBy similarity1
Modified residuei183N6-succinyllysineBy similarity1
Modified residuei204N6-acetyllysine; alternateBy similarity1
Modified residuei204N6-succinyllysine; alternateBy similarity1
Modified residuei214N6-acetyllysineBy similarity1
Modified residuei237N6-succinyllysineBy similarity1
Modified residuei356N6-acetyllysine; alternateBy similarity1
Modified residuei356N6-succinyllysine; alternateBy similarity1
Modified residuei391N6-acetyllysine; alternateBy similarity1
Modified residuei391N6-succinyllysine; alternateBy similarity1
Modified residuei531N6-acetyllysineBy similarity1
Modified residuei538N6-acetyllysine; alternateBy similarity1
Modified residuei538N6-succinyllysine; alternateBy similarity1
Modified residuei549N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
Q9BEA2

PeptideAtlas

More...
PeptideAtlasi
Q9BEA2

PRoteomics IDEntifications database

More...
PRIDEi
Q9BEA2

<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 liver.1 Publication

<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

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000001859

<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

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

More...
SMRi
Q9BEA2

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1175 Eukaryota
COG0365 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000229982

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9BEA2

KEGG Orthology (KO)

More...
KOi
K01896

Database of Orthologous Groups

More...
OrthoDBi
683933at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.12780, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 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.

Q9BEA2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRLMKFRVL WGIHMSCPGF HHAPQHLRCR SLSGAGTLRW NDYDRPEEFN
60 70 80 90 100
FASDVLDHWT QMEKEGKRSP NPALWWVNDQ GDEVKWSFRE MTDLTCRTAN
110 120 130 140 150
VLTQTCGLQT GDRLALILPR VPEWWLVCVG CIRTGIIFMP GTTQMKAKDI
160 170 180 190 200
LYRLQVSGAK AIVTTDTLAP EVESVAPECP SLKTKLLVSD HSREGWLDFR
210 220 230 240 250
SLVKSASPDH ICIKSKTLDP MAIFFTSGTT GFPKMAKHSH GFALRSYFPA
260 270 280 290 300
CRKLLQLKMS DVFWCLSDTG WILAALGSLL EPWTAGSTVF AHHLPQFDPK
310 320 330 340 350
VIIETFFKYP ITQCLAAPSV YRMILQQNYT SLRFPTLEHC CTGGEALLPE
360 370 380 390 400
EQEQWKRQTG VLLYQAYGQS ETGISCGTLR GMKIKPGSMG KAIPPFDIQI
410 420 430 440 450
IDDKGNIQPP NTEGNIGIRI KPTRPIGLFM YYENNPEKTA EVECGDFYNT
460 470 480 490 500
GDRATIDEEG YFWFLGRSDD VINASGYRVG PAEVENALAE HPAVAESAVV
510 520 530 540 550
SSPDPVRGEV VKAFIVLNPE FSSRDPGELT KELQQHVKSV TAPYKYPRKV
560 570
EFVSELPKTI TGKIKRSELR KKEFGQK
Length:577
Mass (Da):64,923
Last modified:October 2, 2007 - v2
<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:i33C3DA651E461BE4
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 conflicti186L → H in AAI09603 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti372T → A2 Publications1

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
AF126145 mRNA Translation: AAD39140.1
AJ132751 mRNA Translation: CAB44431.1
AB048289 mRNA Translation: BAB40420.1
BC109602 mRNA Translation: AAI09603.1

NCBI Reference Sequences

More...
RefSeqi
NP_777107.1, NM_174682.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
282576

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:282576

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126145 mRNA Translation: AAD39140.1
AJ132751 mRNA Translation: CAB44431.1
AB048289 mRNA Translation: BAB40420.1
BC109602 mRNA Translation: AAI09603.1
RefSeqiNP_777107.1, NM_174682.2

3D structure databases

SMRiQ9BEA2
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001859

Proteomic databases

PaxDbiQ9BEA2
PeptideAtlasiQ9BEA2
PRIDEiQ9BEA2

Genome annotation databases

GeneIDi282576
KEGGibta:282576

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
116285

Phylogenomic databases

eggNOGiKOG1175 Eukaryota
COG0365 LUCA
HOGENOMiHOG000229982
InParanoidiQ9BEA2
KOiK01896
OrthoDBi683933at2759

Family and domain databases

Gene3Di3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 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 nameiACSM1_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: Q9BEA2
Secondary accession number(s): Q32LF8, Q9TVB5, Q9XT43
<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: October 2, 2007
Last sequence update: October 2, 2007
Last modified: September 18, 2019
This is version 89 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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