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Protein

Small ubiquitin-related modifier

Gene

smo-1

Organism
Caenorhabditis elegans
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

Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).8 Publications

<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

  • identical protein binding Source: IntAct
  • protein tag Source: GO_Central
  • ubiquitin-like protein ligase binding Source: GO_Central

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 functionDevelopmental protein
Biological processUbl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-CEL-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-CEL-3065679 SUMO is proteolytically processed
R-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-3232118 SUMOylation of transcription factors
R-CEL-3899300 SUMOylation of transcription cofactors
R-CEL-4085377 SUMOylation of SUMOylation proteins
R-CEL-4090294 SUMOylation of intracellular receptors
R-CEL-4551638 SUMOylation of chromatin organization proteins
R-CEL-4570464 SUMOylation of RNA binding proteins
R-CEL-4615885 SUMOylation of DNA replication proteins
R-CEL-4755510 SUMOylation of immune response proteins
R-CEL-5696395 Formation of Incision Complex in GG-NER
R-CEL-877312 Regulation of IFNG signaling
R-CEL-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
P55853 Predicted

<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:
Small ubiquitin-related modifier
Short name:
SUMO
Alternative name(s):
Ubiquitin-like protein SMT3
<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:smo-1
Synonyms:smt3, sumo
ORF Names:K12C11.2
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome I

Organism-specific databases

WormBase

More...
WormBasei
K12C11.2 ; CE18056 ; WBGene00004888 ; smo-1

<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

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown causes chromosome misalignment and anaphase bridges during the first embryonic mitotic division (PubMed:25475837). 23 percent of mutant animals have impaired locomotion (PubMed:24285704). Ectopic expression of egl-17 in multiple vulva precursor cells and moderate increase in phosphorylation of mpk-1 (PubMed:24349540). Adult bet-1 and smo-1 double mutants have decreased myo-3 levels in muscles and increased transcription levels of egl-15, sur-1 and let-60 (PubMed:24285704).3 Publications

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001148901 – 90Small ubiquitin-related modifierAdd BLAST90
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000027122791By similarity1

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 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-linki90Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

<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

Cleavage of precursor form by ulp-1 is necessary for function.Curated

Keywords - PTMi

Isopeptide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P55853

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

More...
PaxDbi
P55853

PeptideAtlas

More...
PeptideAtlasi
P55853

PRoteomics IDEntifications database

More...
PRIDEi
P55853

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P55853

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00004888 Expressed in 5 organ(s), highest expression level in multi-cellular organism

<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

Covalently attached to tbx-2 (PubMed:16701625). Covalently attached to lin-1 (PubMed:15689373). Covalently attached to lin-11 (PubMed:15466489). Covalently attached to sop-2 (PubMed:15107848). Covalently attached to bet-1 (PubMed:24349540, PubMed:24285704).6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
57309, 30 interactors

Database of interacting proteins

More...
DIPi
DIP-25461N

Protein interaction database and analysis system

More...
IntActi
P55853, 36 interactors

STRING: functional protein association networks

More...
STRINGi
6239.K12C11.2

<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

191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XQMNMR-A1-90[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P55853

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

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SMRi
P55853

Database of comparative protein structure models

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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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 91Ubiquitin-likePROSITE-ProRule annotationAdd BLAST79

<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 ubiquitin family. SUMO subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1769 Eukaryota
COG5227 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000207495

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P55853

KEGG Orthology (KO)

More...
KOi
K12160

Identification of Orthologs from Complete Genome Data

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OMAi
IIEVYQE

Database of Orthologous Groups

More...
OrthoDBi
1583700at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P55853

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01763 Sumo, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11976 Rad60-SLD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50053 UBIQUITIN_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_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.

P55853-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV
60 70 80 90
AVNSLRFLFD GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F
Length:91
Mass (Da):10,222
Last modified:November 1, 1997 - 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:i0894E99B6F7B37F5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X99600 mRNA Translation: CAA67914.1
U94830 Genomic DNA Translation: AAB67608.1
FO081631 Genomic DNA Translation: CCD72942.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5582

NCBI Reference Sequences

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RefSeqi
NP_490842.1, NM_058441.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Cel.18381

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
K12C11.2; K12C11.2; WBGene00004888

Database of genes from NCBI RefSeq genomes

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GeneIDi
266820

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_K12C11.2

UCSC genome browser

More...
UCSCi
K12C11.2.1 c. elegans

<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
X99600 mRNA Translation: CAA67914.1
U94830 Genomic DNA Translation: AAB67608.1
FO081631 Genomic DNA Translation: CCD72942.1
PIRiJC5582
RefSeqiNP_490842.1, NM_058441.4
UniGeneiCel.18381

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XQMNMR-A1-90[»]
ProteinModelPortaliP55853
SMRiP55853
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57309, 30 interactors
DIPiDIP-25461N
IntActiP55853, 36 interactors
STRINGi6239.K12C11.2

Protein family/group databases

MoonDBiP55853 Predicted

PTM databases

iPTMnetiP55853

Proteomic databases

EPDiP55853
PaxDbiP55853
PeptideAtlasiP55853
PRIDEiP55853

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK12C11.2; K12C11.2; WBGene00004888
GeneIDi266820
KEGGicel:CELE_K12C11.2
UCSCiK12C11.2.1 c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
266820
WormBaseiK12C11.2 ; CE18056 ; WBGene00004888 ; smo-1

Phylogenomic databases

eggNOGiKOG1769 Eukaryota
COG5227 LUCA
HOGENOMiHOG000207495
InParanoidiP55853
KOiK12160
OMAiIIEVYQE
OrthoDBi1583700at2759
PhylomeDBiP55853

Enzyme and pathway databases

ReactomeiR-CEL-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-CEL-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-CEL-3065679 SUMO is proteolytically processed
R-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-3232118 SUMOylation of transcription factors
R-CEL-3899300 SUMOylation of transcription cofactors
R-CEL-4085377 SUMOylation of SUMOylation proteins
R-CEL-4090294 SUMOylation of intracellular receptors
R-CEL-4551638 SUMOylation of chromatin organization proteins
R-CEL-4570464 SUMOylation of RNA binding proteins
R-CEL-4615885 SUMOylation of DNA replication proteins
R-CEL-4755510 SUMOylation of immune response proteins
R-CEL-5696395 Formation of Incision Complex in GG-NER
R-CEL-877312 Regulation of IFNG signaling
R-CEL-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P55853

Gene expression databases

BgeeiWBGene00004888 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Family and domain databases

CDDicd01763 Sumo, 1 hit
InterProiView protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF11976 Rad60-SLD, 1 hit
SMARTiView protein in SMART
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSUMO_CAEEL
<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: P55853
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 16, 2019
This is version 146 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 programCaenorhabditis annotation project

<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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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