Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q2I3H2 (COX1_ELEMA)

Entry version 64 (17 Jun 2020)
Sequence version 1 (07 Mar 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Cytochrome c oxidase subunit 1

Gene

MT-CO1

Organism
Elephas maximus (Indian elephant)
Status
Reviewed-Annotation score:

Annotation score:4 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>-Protein inferred from homologyi <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

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.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

Protein has several cofactor binding sites:

<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: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

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 bindingi40Sodium or calciumBy similarity1
Metal bindingi45Sodium or calcium; via carbonyl oxygenBy similarity1
Metal bindingi61Iron 1 (low-spin heme A axial ligand); via tele nitrogenBy similarity1
Metal bindingi240Copper B; via pros nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei244OxygenBy similarity1
Metal bindingi290Copper B; via tele nitrogenBy similarity1
Metal bindingi291Copper B; via tele nitrogenBy similarity1
Metal bindingi368Magnesium; shared with MT-CO2By similarity1
Metal bindingi369Magnesium; shared with MT-CO2By similarity1
Metal bindingi376Iron 2 (high-spin heme A3 axial ligand); via tele nitrogenBy similarity1
Metal bindingi378Iron 1 (low-spin heme A axial ligand); via tele nitrogenBy similarity1
Metal bindingi441Sodium or calcium; via carbonyl oxygenBy 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 functionTranslocase
Biological processElectron transport, Respiratory chain, Transport
LigandCalcium, Copper, Heme, Iron, Magnesium, Metal-binding, Sodium

Enzyme and pathway databases

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

More...UniPathwayi		UPA00705

<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:
Cytochrome c oxidase subunit 1 (EC:7.1.1.9)
Alternative name(s):
Cytochrome c oxidase polypeptide I
<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:MT-CO1
Synonyms:COI, COXI, MTCO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniMitochondrion
<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>OrganismiElephas maximus (Indian elephant)
<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 identifieri9783 [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 › Afrotheria › Proboscidea › Elephantidae › Elephas

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 11Mitochondrial matrixBy similarityAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei12 – 40Helical; Name=IBy similarityAdd BLAST29
Topological domaini41 – 50Mitochondrial intermembraneBy similarity10
Transmembranei51 – 86Helical; Name=IIBy similarityAdd BLAST36
Topological domaini87 – 94Mitochondrial matrixBy similarity8
Transmembranei95 – 117Helical; Name=IIIBy similarityAdd BLAST23
Topological domaini118 – 140Mitochondrial intermembraneBy similarityAdd BLAST23
Transmembranei141 – 170Helical; Name=IVBy similarityAdd BLAST30
Topological domaini171 – 182Mitochondrial matrixBy similarityAdd BLAST12
Transmembranei183 – 212Helical; Name=VBy similarityAdd BLAST30
Topological domaini213 – 227Mitochondrial intermembraneBy similarityAdd BLAST15
Transmembranei228 – 261Helical; Name=VIBy similarityAdd BLAST34
Topological domaini262 – 269Mitochondrial matrixBy similarity8
Transmembranei270 – 286Helical; Name=VIIBy similarityAdd BLAST17
Topological domaini287 – 298Mitochondrial intermembraneBy similarityAdd BLAST12
Transmembranei299 – 327Helical; Name=VIIIBy similarityAdd BLAST29
Topological domaini328 – 335Mitochondrial matrixBy similarity8
Transmembranei336 – 357Helical; Name=IXBy similarityAdd BLAST22
Topological domaini358 – 370Mitochondrial intermembraneBy similarityAdd BLAST13
Transmembranei371 – 400Helical; Name=XBy similarityAdd BLAST30
Topological domaini401 – 406Mitochondrial matrixBy similarity6
Transmembranei407 – 433Helical; Name=XIBy similarityAdd BLAST27
Topological domaini434 – 446Mitochondrial intermembraneBy similarityAdd BLAST13
Transmembranei447 – 478Helical; Name=XIIBy similarityAdd BLAST32
Topological domaini479 – 515Mitochondrial matrixBy similarityAdd BLAST37

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002328401 – 515Cytochrome c oxidase subunit 1Add BLAST515

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <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-linki240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr)By similarity

<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

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of 14 subunits. The complex is composed of a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A, COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which are encoded in the nuclear genome. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), resulting in different assemblies (supercomplex SCI1III2IV1 and megacomplex MCI2III2IV2) (By similarity). As a newly synthesized protein, rapidly incorporates into a multi-subunit assembly intermediate in the inner membrane, called MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly synthesized MT-CO1 and prevents its premature turnover.

Interacts with TMEM177 in a COX20-dependent manner (By similarity).

By similarity

<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		Q2I3H2

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 heme-copper respiratory oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...CDDi		cd01663, Cyt_c_Oxidase_I, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023616, Cyt_c_oxase-like_su1_dom
IPR036927, Cyt_c_oxase-like_su1_sf
IPR000883, Cyt_C_Oxase_1
IPR023615, Cyt_c_Oxase_su1_BS
IPR033944, Cyt_c_oxase_su1_dom

The PANTHER Classification System

More...PANTHERi		PTHR10422, PTHR10422, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00115, COX1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01165, CYCOXIDASEI

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF81442, SSF81442, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50855, COX1, 1 hit
PS00077, COX1_CUB, 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.

Q2I3H2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFANRWLYST NHKDIGTLYL LFGAWAGMVG TAFSILIRAE LGQPGSLLGD 
        60         70         80         90        100
DQIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLIPLMIGAP DMAFPRMNNM 
       110        120        130        140        150
SFWLLPPSFL LLLASSMVEA GTGTGWTVYP PLAGNLAHAG ASVDLTIFSL 
       160        170        180        190        200
HLAGVSSILS AINFITTIIN MKPPAMSQYH MPLFVWSILV TAVLLLLSLP 
       210        220        230        240        250
VLAAGITMLL TDRNLNTTFF DPAGGGDPVL YQHLFWFFGH PEVYILILPG 
       260        270        280        290        300
FGMVSHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 
       310        320        330        340        350
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTI 
       360        370        380        390        400
GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF 
       410        420        430        440        450
SGYTLNYTWA KIQFLVMFIG VNLTFFPQHF LGLSGMPRRY SDYPDAYTAW 
       460        470        480        490        500
NTASSMGSFI SLVAVILMVF MIWEAFASKR EVSMMELMTT NVEWLNGCPP 
       510 
PHHTFEEPAY VKSNS
Length:515
Mass (Da):57,165
Last modified:March 7, 2006 - 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:iDF28109BCDC07449
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
DQ316068 Genomic DNA Translation: ABC17893.1

NCBI Reference Sequences

More...RefSeqi		YP_626369.1, NC_005129.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2610363

<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
DQ316068 Genomic DNA Translation: ABC17893.1
RefSeqiYP_626369.1, NC_005129.2

3D structure databases

SMRiQ2I3H2
ModBaseiSearch...

Genome annotation databases

GeneIDi2610363

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4512

Enzyme and pathway databases

UniPathwayiUPA00705

Family and domain databases

CDDicd01663, Cyt_c_Oxidase_I, 1 hit
Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616, Cyt_c_oxase-like_su1_dom
IPR036927, Cyt_c_oxase-like_su1_sf
IPR000883, Cyt_C_Oxase_1
IPR023615, Cyt_c_Oxase_su1_BS
IPR033944, Cyt_c_oxase_su1_dom
PANTHERiPTHR10422, PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115, COX1, 1 hit
PRINTSiPR01165, CYCOXIDASEI
SUPFAMiSSF81442, SSF81442, 1 hit
PROSITEiView protein in PROSITE
PS50855, COX1, 1 hit
PS00077, COX1_CUB, 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 nameiCOX1_ELEMA
<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: Q2I3H2
<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: April 18, 2006
Last sequence update: March 7, 2006
Last modified: June 17, 2020
This is version 64 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

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