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UniProtKB - P24271 (RAG1_CHICK)

Entry version 130 (02 Dec 2020)
Sequence version 1 (01 Mar 1992)
Previous versions | rss
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Protein

V(D)J recombination-activating protein 1

Gene

RAG1

Organism
Gallus gallus (Chicken)
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

Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<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+By similarity, Mn2+By similarityNote: Binds 1 divalent metal cation per subunit. Mg2+ or Mn2+.By similarity

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 bindingi265Zinc 1By similarity1
Metal bindingi269Zinc 1By similarity1
Metal bindingi289Zinc 2By similarity1
Metal bindingi292Zinc 1By similarity1
Metal bindingi292Zinc 2By similarity1
Metal bindingi294Zinc 1By similarity1
Metal bindingi304Zinc 3By similarity1
Metal bindingi306Zinc 3By similarity1
Metal bindingi309Zinc 2By similarity1
Metal bindingi312Zinc 2By similarity1
Metal bindingi324Zinc 3By similarity1
Metal bindingi327Zinc 3By similarity1
Metal bindingi354Zinc 4By similarity1
Metal bindingi359Zinc 4By similarity1
Metal bindingi371Zinc 4By similarity1
Metal bindingi375Zinc 4By similarity1
Metal bindingi601Divalent metal cation; catalyticBy similarity1
Metal bindingi709Divalent metal cation; catalyticBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei894Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage siteBy similarity1
Metal bindingi963Divalent metal cation; catalyticBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri289 – 328RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri350 – 379RAG1-typePROSITE-ProRule annotationAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi390 – 457NBDPROSITE-ProRule annotationAdd BLAST68

<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 functionChromatin regulator, DNA-binding, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Transferase
Biological processDNA recombination, Ubl conjugation pathway
LigandMetal-binding, Zinc

<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:
V(D)J recombination-activating protein 1
Short name:
RAG-1
Including the following 2 domains:
Endonuclease RAG1 (EC:3.1.-.-)
E3 ubiquitin-protein ligase RAG1 (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase RAG1Curated
<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:RAG1
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

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

Keywords - Cellular componenti

Nucleus

<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_00000560081 – 1041V(D)J recombination-activating protein 1Add BLAST1041

Proteomic databases

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

More...PaxDbi		P24271

PRoteomics IDEntifications database

More...PRIDEi		P24271

<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

Homodimer.

Component of the RAG complex composed of core components RAG1 and RAG2 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

<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		P24271

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 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

The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity.By similarity
The NBD (nonamer binding) DNA-binding domain mediates the specific binding to the nonamer RSS motif by forming a tightly interwoven homodimer that binds and synapses 2 nonamer elements, with each NBD making contact with both DNA molecules. Each RSS is composed of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either 12 bp or 23 bp.PROSITE-ProRule annotation

<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 RAG1 family.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri289 – 328RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri350 – 379RAG1-typePROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P24271

Database of Orthologous Groups

More...OrthoDBi		85196at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P24271

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR024627, RAG1
IPR035714, RAG1_imp-bd
IPR019485, RAG1_Znf
IPR023336, RAG_nonamer-bd_dom
IPR036236, Znf_C2H2_sf
IPR018957, Znf_C3HC4_RING-type
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

The PANTHER Classification System

More...PANTHERi		PTHR11539, PTHR11539, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12940, RAG1, 1 hit
PF12560, RAG1_imp_bd, 1 hit
PF00097, zf-C3HC4, 1 hit
PF10426, zf-RAG1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57667, SSF57667, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51487, NBD, 1 hit
PS51765, ZF_RAG1, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P24271-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSITSRMDLP EEIQHPYAKF SEWKFKLFKV RPFQKEPSDK SQCINKDQEQ 
        60         70         80         90        100
EVASTDKNIT LHKDEEVPRG EKLILTQKDF MGNTQALEKD VNDMKIQDNT 
       110        120        130        140        150
AHQNNLKQLC RICGVSFKTD CYKRTHPVHG PVDDETLWLL RKKEKKATSW 
       160        170        180        190        200
PDLIAKVFKI DVRGDVDTIH PTRFCHNCWS IIHRKFSNTP CEVYFPRNST 
       210        220        230        240        250
MEWQPHSANC EVCHTPSRGV KRKSQPPNVQ HGKRVKIIAE RARVNRGIKN 
       260        270        280        290        300
QVIKNKNVMK EITNCKNRHL STKLLAVDYP ADFIKSISCQ ICEHILADPV 
       310        320        330        340        350
ETTCRHLFCR TCILSCIRVM GCYCPSCWYP CFPTDLVTPV KSFLNILDSL 
       360        370        380        390        400
SIRCPVPECD EEILHGKYGQ HFSNHKEMKD KELYNPINKG GRPRQHLLSL 
       410        420        430        440        450
TRRAQKHRLR ELKRQVKAFA EKEEGGDIKA VCMTLFLLAL RAKNEHKQAD 
       460        470        480        490        500
ELEAIMQGRG SGLHPAVCLA IRINTFLSCS QYHKMYRTVK AVTGRQIFQP 
       510        520        530        540        550
LHALRTAEKA LLPGYHPFEW KPPLKNVSTN TEVGIIDGLS GLPLSIDDYP 
       560        570        580        590        600
IDTIAKRFRY DTALVSALKD MEEEILEGMK AKNLDDYLNG PFTVVVKECC 
       610        620        630        640        650
DGMGDVSEKH GSGPAVPEKA VRFSFTVMNI AIDHENERIR IFEEVKPNSE 
       660        670        680        690        700
LCCKPLCLML ADESDHETLT AILSPLIAER EAMKNSELLL EIGGILRTFK 
       710        720        730        740        750
FIFRGTGYDE KLVREVEGLE ASGSTYICTL CDATRLEASQ NLVFHSITRS 
       760        770        780        790        800
HAENLERYEI WRSNPYHESV DELRDRVKGV SAKPFIETVP SIDALHCDIG 
       810        820        830        840        850
NATEFYRIFQ MEIGEVYKNP DATKEERKRW QLTLDKHLRK KMKLKPMMRM 
       860        870        880        890        900
SGNFARKLMS KETVEAVCEL IKCEERHEAL KELMDLYLKM KPVWRSSCPA 
       910        920        930        940        950
KECPELLCQY SYNSQRFAEL LSTKFKYRYE GKITNYFHKT LAHVPEIIER 
       960        970        980        990       1000
DGSIGAWASE GNESGNKLFR RFRKMNARQS KFYEMEDVLK HHWLYTSKYL 
      1010       1020       1030       1040 
QKFMNAHKTL RSQGFAIDPD DGLGDSLPPE ISLESNDSVE L
Length:1,041
Mass (Da):119,917
Last modified:March 1, 1992 - 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:iCB2B5D9FB141A974
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
M58530 Genomic DNA Translation: AAA49051.1

Protein sequence database of the Protein Information Resource

More...PIRi		S42509

NCBI Reference Sequences

More...RefSeqi		NP_001026359.1, NM_001031188.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		423164

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		gga:423164

<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
M58530 Genomic DNA Translation: AAA49051.1
PIRiS42509
RefSeqiNP_001026359.1, NM_001031188.1

3D structure databases

SMRiP24271
ModBaseiSearch...

Proteomic databases

PaxDbiP24271
PRIDEiP24271

Genome annotation databases

GeneIDi423164
KEGGigga:423164

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5896

Phylogenomic databases

InParanoidiP24271
OrthoDBi85196at2759
PhylomeDBiP24271

Miscellaneous databases

Protein Ontology

More...PROi		PR:P24271

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR024627, RAG1
IPR035714, RAG1_imp-bd
IPR019485, RAG1_Znf
IPR023336, RAG_nonamer-bd_dom
IPR036236, Znf_C2H2_sf
IPR018957, Znf_C3HC4_RING-type
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PANTHERiPTHR11539, PTHR11539, 1 hit
PfamiView protein in Pfam
PF12940, RAG1, 1 hit
PF12560, RAG1_imp_bd, 1 hit
PF00097, zf-C3HC4, 1 hit
PF10426, zf-RAG1, 1 hit
SUPFAMiSSF57667, SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS51487, NBD, 1 hit
PS51765, ZF_RAG1, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_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 nameiRAG1_CHICK
<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: P24271
<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: March 1, 1992
Last sequence update: March 1, 1992
Last modified: December 2, 2020
This is version 130 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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