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Protein

Major royal jelly protein 1

Gene

MRJP1

Organism
Apis mellifera (Honeybee)
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

Major royal jelly protein 1: induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20-hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.1 Publication
Jellein-1: has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation.1 Publication
Jellein-2: has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation.1 Publication
Jellein-4: lacks antibacterial and antifungal activity. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation.1 Publication

Miscellaneous

Exhibits a growth factor-like action on primary-cultured rat hepatocytes by stimulating DNA synthesis and protecting cells from apoptosis induced by serum deprivation. Also activates mitogen-activated protein kinase, as well as protein kinase B, a key regulator of cell survival (PubMed:16290177).1 Publication
Degraded proportionally to the period of storage, and is completely lost during storage at 40 degrees Celsius for 30 days.1 Publication

Caution

Neither His-431 nor Leu-432 is followed in the nucleotide sequence by the expected Gly residue that would be required to produce amidation.Curated

<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 - 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 functionAntibiotic, Antimicrobial, Developmental protein, Fungicide

<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:
Major royal jelly protein 11 Publication
Short name:
MRJP-1
Short name:
MRJP12 Publications
Alternative name(s):
56-kDa protein 41 Publication
Short name:
p56kP-41 Publication
Apalbumin 1Curated
Apisin subunit MRJP11 Publication
Bee-milk protein1 Publication
Royalactin1 Publication
Cleaved into the following 3 chains:
Jellein-1Curated
Alternative name(s):
Jelleine-I1 Publication
Jellein-2Curated
Alternative name(s):
Jelleine-II1 Publication
Jellein-4Curated
Alternative name(s):
Jelleine-IV1 Publication
<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:MRJP1
<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>OrganismiApis mellifera (Honeybee)
<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 identifieri7460 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaHymenopteraApocritaAculeataApoideaApidaeApis
<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
  • UP000005203 <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: Linkage group 11

<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

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
7627 Api m Apalbumin 1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 192 PublicationsAdd BLAST19
<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_000003104320 – 432Major royal jelly protein 12 PublicationsAdd BLAST413
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000224649424 – 432Jellein-21 Publication9
PeptideiPRO_0000224650424 – 431Jellein-41 Publication8
PeptideiPRO_0000224648425 – 432Jellein-11 Publication8

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi28N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi144N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi177N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei431Histidine amide; atypical1 Publication1
Modified residuei432Leucine amide; atypical1 Publication1

<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

Glycosylated.1 Publication
Jellein-2 is probably processed to yield jellein-1 and jellein-4.

Keywords - PTMi

Amidation, Glycoprotein

Proteomic databases

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

More...
PaxDbi
O18330

PRoteomics IDEntifications database

More...
PRIDEi
O18330

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2

<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

Found in the hypopharyngeal glands of the worker honeybee.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Produced in the cephalic glands of both the nurse bee and the forager bee. This bee milk protein changes to alpha-glucosidase in accordance with the age-dependent role change of the worker bee.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

Is present in royal jelly in different forms: monomer (55 kDa), oligomeric subunit (ca. 420 kDa), and water-insoluble aggregates in sediment after interaction with fatty acids (Ref. 7). Interacts with apisimin to form the heterooligomer apisin (350 kDa) (PubMed:27721892).2 Publications

<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

1432
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
5YYLX-ray2.65A/B1-432[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O18330

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

More...
SMRi
O18330

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 major royal jelly protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410KG2T Eukaryota
ENOG4110SQU LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000136640

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O18330

Identification of Orthologs from Complete Genome Data

More...
OMAi
SIMCADA

Database of Orthologous Groups

More...
OrthoDBi
940689at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O18330

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.120.10.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR017996 Royal_jelly/protein_yellow

The PANTHER Classification System

More...
PANTHERi
PTHR10009 PTHR10009, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03022 MRJP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01366 ROYALJELLY

<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.

<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.

O18330-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTRLFMLVCL GIVCQGTTGN ILRGESLNKS LPILHEWKFF DYDFGSDERR
60 70 80 90 100
QDAILSGEYD YKNNYPSDID QWHDKIFVTM LRYNGVPSSL NVISKKVGDG
110 120 130 140 150
GPLLQPYPDW SFAKYDDCSG IVSASKLAID KCDRLWVLDS GLVNNTQPMC
160 170 180 190 200
SPKLLTFDLT TSQLLKQVEI PHDVAVNATT GKGRLSSLAV QSLDCNTNSD
210 220 230 240 250
TMVYIADEKG EGLIVYHNSD DSFHRLTSNT FDYDPKFTKM TIDGESYTAQ
260 270 280 290 300
DGISGMALSP MTNNLYYSPV ASTSLYYVNT EQFRTSDYQQ NDIHYEGVQN
310 320 330 340 350
ILDTQSSAKV VSKSGVLFFG LVGDSALGCW NEHRTLERHN IRTVAQSDET
360 370 380 390 400
LQMIASMKIK EALPHVPIFD RYINREYILV LSNKMQKMVN NDFNFDDVNF
410 420 430
RIMNANVNEL ILNTRCENPD NDRTPFKISI HL
Length:432
Mass (Da):48,886
Last modified:January 1, 1998 - 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:i9F42BF08D34A1A7B
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 conflicti28N → L AA sequence (PubMed:11302159).Curated1
Sequence conflicti30S → K AA sequence (PubMed:11302159).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 953.24±0.17 Da from positions 425 - 432. Determined by ESI. Jellein-1.1 Publication
Molecular mass is 1054.30±0.18 Da from positions 424 - 432. Determined by ESI. Jellein-2.1 Publication
Molecular mass is 942.13±0.17 Da from positions 424 - 431. Determined by ESI. Jellein-4.1 Publication

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
D79207 mRNA Translation: BAA23639.1
AF000633 mRNA Translation: AAC61895.1
AF388203 Genomic DNA Translation: AAM73637.1
GQ160518 mRNA Translation: ACS66836.1

NCBI Reference Sequences

More...
RefSeqi
NP_001011579.1, NM_001011579.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Ame.208

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
GB55205-RA; GB55205-PA; GB55205

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
406090

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ame:406090

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

A queen's dinner - Issue 130 of August 2011

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D79207 mRNA Translation: BAA23639.1
AF000633 mRNA Translation: AAC61895.1
AF388203 Genomic DNA Translation: AAM73637.1
GQ160518 mRNA Translation: ACS66836.1
RefSeqiNP_001011579.1, NM_001011579.1
UniGeneiAme.208

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5YYLX-ray2.65A/B1-432[»]
ProteinModelPortaliO18330
SMRiO18330
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei7627 Api m Apalbumin 1

PTM databases

GlyConnecti2

Proteomic databases

PaxDbiO18330
PRIDEiO18330

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiGB55205-RA; GB55205-PA; GB55205
GeneIDi406090
KEGGiame:406090

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
406090

Phylogenomic databases

eggNOGiENOG410KG2T Eukaryota
ENOG4110SQU LUCA
HOGENOMiHOG000136640
InParanoidiO18330
OMAiSIMCADA
OrthoDBi940689at2759
PhylomeDBiO18330

Family and domain databases

Gene3Di2.120.10.30, 1 hit
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR017996 Royal_jelly/protein_yellow
PANTHERiPTHR10009 PTHR10009, 1 hit
PfamiView protein in Pfam
PF03022 MRJP, 1 hit
PRINTSiPR01366 ROYALJELLY

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 nameiMRJP1_APIME
<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: O18330
Secondary accession number(s): C6K481, Q548D6
<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: January 23, 2002
Last sequence update: January 1, 1998
Last modified: January 16, 2019
This is version 99 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)

<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
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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