Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 186 (13 Nov 2019)
Sequence version 2 (03 May 2011)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Epsin-1

Gene

EPN1

Organism
Homo sapiens (Human)
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 (By similarity). Regulates receptor-mediated endocytosis.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei8Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei11Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei25Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei30Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei63Phosphatidylinositol lipid headgroupBy similarity1
Binding sitei73Phosphatidylinositol lipid headgroupBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

Biological processEndocytosis
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-182971 EGFR downregulation
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9Y6I3

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9Y6I3

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q9Y6I3 Curated

<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):
EH domain-binding mitotic phosphoprotein
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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 19

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:21604 EPN1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
607262 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9Y6I3

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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>Mutagenesisi382S → A: Abolishes phosphorylation by CDK1. 1 Publication1
Mutagenesisi382S → D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding. 1 Publication1
Mutagenesisi404F → A: Reduces interaction with AP2B1. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
29924

Open Targets

More...
OpenTargetsi
ENSG00000063245

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134860916

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9Y6I3

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3259465

Drug and drug target database

More...
DrugBanki
DB03316 1,4-Diethylene Dioxide
DB03401 1D-myo-inositol 1,4,5-trisphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EPN1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
332278179

<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_00000745131 – 576Epsin-1Add BLAST576

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 residuei382Phosphoserine; by CDK11 Publication1
Modified residuei419PhosphoserineCombined sources1
Modified residuei420PhosphoserineCombined sources1
Modified residuei435PhosphoserineCombined sources1
Modified residuei447PhosphoserineCombined sources1
Modified residuei454PhosphoserineCombined sources1
Modified residuei460PhosphothreonineCombined sources1
Modified residuei464PhosphothreonineCombined sources1
Modified residuei470PhosphothreonineCombined sources1
Modified residuei473PhosphoserineBy similarity1
Modified residuei494PhosphothreonineCombined sources1
Modified residuei534Omega-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

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
Ubiquitinated.By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9Y6I3

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9Y6I3

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9Y6I3

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9Y6I3

PeptideAtlas

More...
PeptideAtlasi
Q9Y6I3

PRoteomics IDEntifications database

More...
PRIDEi
Q9Y6I3

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
86689 [Q9Y6I3-2]
86690 [Q9Y6I3-1]
86691 [Q9Y6I3-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Y6I3

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

More...
PhosphoSitePlusi
Q9Y6I3

<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
ENSG00000063245 Expressed in 206 organ(s), highest expression level in body of stomach

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9Y6I3 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Y6I3 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB009729
HPA061136

<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 clathrin, ZBTB16/ZNF145 and ITSN1 (By similarity). Binds ubiquitinated proteins (By similarity). Binds REPS2, EPS15, AP2A1 and AP2A2.

Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis.

Interacts with AP2B1.

Interacts with UBQLN2.

By similarity5 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
118965, 71 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9Y6I3

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q9Y6I3

Protein interaction database and analysis system

More...
IntActi
Q9Y6I3, 38 interactors

Molecular INTeraction database

More...
MINTi
Q9Y6I3

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000406209

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q9Y6I3

<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

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q9Y6I3

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Y6I3

<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
Repeati502 – 50413
Repeati518 – 52023
Repeati572 – 57433

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 [ED]-P-WAdd BLAST106
Regioni502 – 5743 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>Motifi402 – 411[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 – 573Ala/Gly/Pro-richAdd BLAST307

<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 with 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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160411

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000008298

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Y6I3

KEGG Orthology (KO)

More...
KOi
K12471

Identification of Orthologs from Complete Genome Data

More...
OMAi
NPWGQPQ

Database of Orthologous Groups

More...
OrthoDBi
1263849at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313361

Family and domain databases

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
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>. 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>Sequences (3+)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 describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Y6I3-2) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 AQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG
260 270 280 290 300
GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP
310 320 330 340 350
VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP
360 370 380 390 400
WGSSDGGVPV SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE
410 420 430 440 450
PDEFSDFDRL RTALPTSGSS AGELELLAGE VPARSPGAFD MSGVRGSLAE
460 470 480 490 500
AVGSPPPAAT PTPTPPTRKT PESFLGPNAA LVDLDSLVSR PGPTPPGAKA
510 520 530 540 550
SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP VPGAPPTYIS
560 570
PLGGGPGLPP MMPPGPPAPN TNPFLL
Length:576
Mass (Da):60,293
Last modified:May 3, 2011 - v2
<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:i68DD433F3168E975
GO
Isoform 2 (identifier: Q9Y6I3-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGDQSWLWNQ...CPLLLQPGTM
     202-226: Missing.

Show »
Length:662
Mass (Da):69,040
Checksum:iBE8DD37499E2DB6A
GO
Isoform 3 (identifier: Q9Y6I3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-226: Missing.
     393-393: Missing.

Note: May be due to a competing donor splice site. No experimental confirmation available.
Show »
Length:550
Mass (Da):57,504
Checksum:iDC8BA5EBEB1D5111
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
K7EMP4K7EMP4_HUMAN
Epsin-1
EPN1
60Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Isoform 2 : The sequence AAD38326 differs from that shown. Reason: Frameshift.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0410101M → MGDQSWLWNQAAPGVRSPVF ACSVEKGNVPLVLSEHLAHS RDPGSGAVRFLISPEPWASA ILGTSGLLASPVLPAALDAV TCQHLPQPSSGSRPISPRIG ALCPLLLQPGTM in isoform 2. 1 Publication1
Alternative sequenceiVSP_041011202 – 226Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST25
Alternative sequenceiVSP_041012393Missing in isoform 3. 1 Publication1

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
AF073727 mRNA Translation: AAD38326.1 Frameshift.
AK022454 mRNA Translation: BAB14041.1
AC008735 Genomic DNA No translation available.
AC010525 Genomic DNA No translation available.
BC044651 mRNA Translation: AAH44651.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS46198.1 [Q9Y6I3-1]
CCDS46199.1 [Q9Y6I3-2]
CCDS46200.1 [Q9Y6I3-3]

NCBI Reference Sequences

More...
RefSeqi
NP_001123543.1, NM_001130071.1 [Q9Y6I3-1]
NP_001123544.1, NM_001130072.1 [Q9Y6I3-2]
NP_037465.2, NM_013333.3 [Q9Y6I3-3]
XP_005258886.1, XM_005258829.2 [Q9Y6I3-2]
XP_011525183.1, XM_011526881.1
XP_016882211.1, XM_017026722.1 [Q9Y6I3-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000085079; ENSP00000085079; ENSG00000063245 [Q9Y6I3-3]
ENST00000270460; ENSP00000270460; ENSG00000063245 [Q9Y6I3-2]
ENST00000411543; ENSP00000406209; ENSG00000063245 [Q9Y6I3-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29924

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:29924

UCSC genome browser

More...
UCSCi
uc002qlv.4 human [Q9Y6I3-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF073727 mRNA Translation: AAD38326.1 Frameshift.
AK022454 mRNA Translation: BAB14041.1
AC008735 Genomic DNA No translation available.
AC010525 Genomic DNA No translation available.
BC044651 mRNA Translation: AAH44651.1
CCDSiCCDS46198.1 [Q9Y6I3-1]
CCDS46199.1 [Q9Y6I3-2]
CCDS46200.1 [Q9Y6I3-3]
RefSeqiNP_001123543.1, NM_001130071.1 [Q9Y6I3-1]
NP_001123544.1, NM_001130072.1 [Q9Y6I3-2]
NP_037465.2, NM_013333.3 [Q9Y6I3-3]
XP_005258886.1, XM_005258829.2 [Q9Y6I3-2]
XP_011525183.1, XM_011526881.1
XP_016882211.1, XM_017026722.1 [Q9Y6I3-3]

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
1INZNMR-A1-144[»]
1KYDX-ray2.00P366-370[»]
SMRiQ9Y6I3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi118965, 71 interactors
CORUMiQ9Y6I3
ELMiQ9Y6I3
IntActiQ9Y6I3, 38 interactors
MINTiQ9Y6I3
STRINGi9606.ENSP00000406209

Chemistry databases

BindingDBiQ9Y6I3
ChEMBLiCHEMBL3259465
DrugBankiDB03316 1,4-Diethylene Dioxide
DB03401 1D-myo-inositol 1,4,5-trisphosphate

Protein family/group databases

MoonDBiQ9Y6I3 Curated

PTM databases

iPTMnetiQ9Y6I3
PhosphoSitePlusiQ9Y6I3

Polymorphism and mutation databases

BioMutaiEPN1
DMDMi332278179

Proteomic databases

EPDiQ9Y6I3
jPOSTiQ9Y6I3
MassIVEiQ9Y6I3
MaxQBiQ9Y6I3
PeptideAtlasiQ9Y6I3
PRIDEiQ9Y6I3
ProteomicsDBi86689 [Q9Y6I3-2]
86690 [Q9Y6I3-1]
86691 [Q9Y6I3-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
29924

Genome annotation databases

EnsembliENST00000085079; ENSP00000085079; ENSG00000063245 [Q9Y6I3-3]
ENST00000270460; ENSP00000270460; ENSG00000063245 [Q9Y6I3-2]
ENST00000411543; ENSP00000406209; ENSG00000063245 [Q9Y6I3-1]
GeneIDi29924
KEGGihsa:29924
UCSCiuc002qlv.4 human [Q9Y6I3-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
29924
DisGeNETi29924

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EPN1
HGNCiHGNC:21604 EPN1
HPAiCAB009729
HPA061136
MIMi607262 gene
neXtProtiNX_Q9Y6I3
OpenTargetsiENSG00000063245
PharmGKBiPA134860916

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00940000160411
HOGENOMiHOG000008298
InParanoidiQ9Y6I3
KOiK12471
OMAiNPWGQPQ
OrthoDBi1263849at2759
TreeFamiTF313361

Enzyme and pathway databases

ReactomeiR-HSA-182971 EGFR downregulation
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
SignaLinkiQ9Y6I3
SIGNORiQ9Y6I3

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
EPN1 human
EvolutionaryTraceiQ9Y6I3

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
EPN1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
29924
PharosiQ9Y6I3

Protein Ontology

More...
PROi
PR:Q9Y6I3

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000063245 Expressed in 206 organ(s), highest expression level in body of stomach
ExpressionAtlasiQ9Y6I3 baseline and differential
GenevisibleiQ9Y6I3 HS

Family and domain databases

Gene3Di1.25.40.90, 1 hit
InterProiView protein in InterPro
IPR013809 ENTH
IPR008942 ENTH_VHS
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...

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 nameiEPN1_HUMAN
<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: Q9Y6I3
Secondary accession number(s): Q86ST3, Q9HA18
<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: May 3, 2011
Last modified: November 13, 2019
This is version 186 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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