Skip Header

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

Epsin-1

Gene

Epn1

Organism
Rattus norvegicus (Rat)
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

Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei8Phosphatidylinositol lipid headgroup1
Binding sitei11Phosphatidylinositol lipid headgroup1
Binding sitei25Phosphatidylinositol lipid headgroup1
Binding sitei30Phosphatidylinositol lipid headgroup1
Binding sitei63Phosphatidylinositol lipid headgroup1
Binding sitei73Phosphatidylinositol lipid headgroup1

<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

  • clathrin adaptor activity Source: CAFA
  • ion channel binding Source: RGD
  • lipid binding Source: UniProtKB-KW
  • transcription factor binding Source: RGD

GO - Biological processi

  • endocytosis Source: RGD
  • positive regulation of clathrin coat assembly Source: CAFA

<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

Biological processEndocytosis
LigandLipid-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Epsin-1
Alternative name(s):
EPS-15-interacting protein 1
<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:Epn1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
619772 Epn1

<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

Cell membrane, Coated pit, Cytoplasm, Membrane, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi6L → E, H or Q: Reduces lipid binding. 1 Publication1
Mutagenesisi8R → A: Strongly reduces lipid binding. 1 Publication1
Mutagenesisi63R → L: Strongly reduces lipid binding. Abolishes lipid binding; when associated with L-73. 2 Publications1
Mutagenesisi72R → A: Abolishes ZNF145 binding. 1 Publication1
Mutagenesisi73H → L: Abolishes lipid binding; when associated with L-63. 1 Publication1
Mutagenesisi76K → A: Strongly reduces lipid binding. 1 Publication1
Mutagenesisi190L → A: Abolishes mono-ubiquitination. 1 Publication1
Mutagenesisi257 – 259LMD → AAA: Strongly reduces clathrin binding. 1 Publication3
Mutagenesisi260 – 263LADV → AAAA: Strongly reduces clathrin binding. 1 Publication4

<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_00000745151 – 575Epsin-1Add BLAST575

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei382PhosphoserineBy similarity1
Modified residuei418PhosphoserineBy similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei420PhosphothreonineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei446PhosphoserineBy similarity1
Modified residuei453PhosphoserineCombined sources1
Modified residuei459PhosphothreonineBy similarity1
Modified residuei463PhosphothreonineBy similarity1
Modified residuei469PhosphothreonineCombined sources1
Modified residuei472PhosphoserineBy similarity1
Modified residuei493PhosphothreonineBy similarity1
Modified residuei533Omega-N-methylarginineBy similarity1

<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

Ubiquitinated.1 Publication
Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
O88339

PeptideAtlas

More...
PeptideAtlasi
O88339

PRoteomics IDEntifications database

More...
PRIDEi
O88339

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88339

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O88339

<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

Ubiquitous.1 Publication

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O88339 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Binds REPS2 and ITSN1 (By similarity). Binds EPS15, clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. Interacts with UBQLN2 (By similarity).By similarity10 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
250724, 15 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O88339

Database of interacting proteins

More...
DIPi
DIP-40738N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
O88339

Protein interaction database and analysis system

More...
IntActi
O88339, 4 interactors

Molecular INTeraction database

More...
MINTi
O88339

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000021286

<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

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00251

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O88339

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

More...
SMRi
O88339

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O88339

<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>Domaini12 – 144ENTHPROSITE-ProRule annotationAdd BLAST133
Domaini183 – 202UIM 1PROSITE-ProRule annotationAdd BLAST20
Domaini208 – 227UIM 2PROSITE-ProRule annotationAdd BLAST20
Domaini233 – 252UIM 3PROSITE-ProRule annotationAdd BLAST20
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati274 – 27613
Repeati294 – 29623
Repeati306 – 30833
Repeati319 – 32143
Repeati332 – 33453
Repeati349 – 35163
Repeati367 – 36973
Repeati377 – 37983
Repeati501 – 50313
Repeati517 – 51923
Repeati571 – 57333

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni274 – 3798 X 3 AA repeats of D-P-WAdd BLAST106
Regioni501 – 5733 X 3 AA repeats of N-P-FAdd BLAST73

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi401 – 410[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi267 – 572Ala/Gly/Pro-richAdd BLAST306

<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 NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP2A2 and clathrin binding.
The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1.By similarity

<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 epsin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2056 Eukaryota
ENOG410XSM0 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000008298

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG006690

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O88339

KEGG Orthology (KO)

More...
KOi
K12471

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0L45

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O88339

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03571 ENTH_epsin, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013809 ENTH
IPR008942 ENTH_VHS
IPR039416 Epsin_ENTH
IPR003903 UIM_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01417 ENTH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00273 ENTH, 1 hit
SM00726 UIM, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48464 SSF48464, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50942 ENTH, 1 hit
PS50330 UIM, 3 hits

<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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O88339-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV
60 70 80 90 100
VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM
110 120 130 140 150
YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT
160 170 180 190 200
KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD
210 220 230 240 250
QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG
260 270 280 290 300
GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGAPA
310 320 330 340 350
VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTSDP
360 370 380 390 400
WGSADGGAPV SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP
410 420 430 440 450
DEFSDFDRLR TALPTSGSST GELELLAGEV PARSPGAFDM SGVGGSLAES
460 470 480 490 500
VGSPPPAATP TPTPPTRKTP ESFLGPNAAL VDLDSLVSRP GPTPPGAKAS
510 520 530 540 550
NPFLPSGAPA TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV PGAPPTYISP
560 570
LGGGPGLPPM MPPGPPAPNT NPFLL
Length:575
Mass (Da):60,158
Last modified:November 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:iD0B770F3B7AB5DDA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A140TAC3A0A140TAC3_RAT
Epsin-1
Epn1
576Annotation score:

Annotation score:1 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>

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
AF018261 mRNA Translation: AAC33823.1

NCBI Reference Sequences

More...
RefSeqi
NP_476477.1, NM_057136.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.30007

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
117277

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:117277

UCSC genome browser

More...
UCSCi
RGD:619772 rat

<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

The bubble's bend - Issue 42 of January 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018261 mRNA Translation: AAC33823.1
RefSeqiNP_476477.1, NM_057136.1
UniGeneiRn.30007

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
1EDUX-ray1.80A12-160[»]
1EYHX-ray1.56A15-158[»]
1H0AX-ray1.70A1-158[»]
1KY6X-ray2.00P375-381[»]
DisProtiDP00251
ProteinModelPortaliO88339
SMRiO88339
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250724, 15 interactors
CORUMiO88339
DIPiDIP-40738N
ELMiO88339
IntActiO88339, 4 interactors
MINTiO88339
STRINGi10116.ENSRNOP00000021286

PTM databases

iPTMnetiO88339
PhosphoSitePlusiO88339

Proteomic databases

PaxDbiO88339
PeptideAtlasiO88339
PRIDEiO88339

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117277
KEGGirno:117277
UCSCiRGD:619772 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
29924
RGDi619772 Epn1

Phylogenomic databases

eggNOGiKOG2056 Eukaryota
ENOG410XSM0 LUCA
HOGENOMiHOG000008298
HOVERGENiHBG006690
InParanoidiO88339
KOiK12471
OrthoDBiEOG091G0L45
PhylomeDBiO88339

Miscellaneous databases

EvolutionaryTraceiO88339

Protein Ontology

More...
PROi
PR:O88339

Gene expression databases

GenevisibleiO88339 RN

Family and domain databases

CDDicd03571 ENTH_epsin, 1 hit
Gene3Di1.25.40.90, 1 hit
InterProiView protein in InterPro
IPR013809 ENTH
IPR008942 ENTH_VHS
IPR039416 Epsin_ENTH
IPR003903 UIM_dom
PfamiView protein in Pfam
PF01417 ENTH, 1 hit
SMARTiView protein in SMART
SM00273 ENTH, 1 hit
SM00726 UIM, 3 hits
SUPFAMiSSF48464 SSF48464, 1 hit
PROSITEiView protein in PROSITE
PS50942 ENTH, 1 hit
PS50330 UIM, 3 hits

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 nameiEPN1_RAT
<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: O88339
<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 16, 2004
Last sequence update: November 1, 1998
Last modified: December 5, 2018
This is version 158 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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