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Protein

Epsin-1

Gene

EPN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000063245-MONOMER.
ReactomeiR-HSA-182971. EGFR downregulation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiQ9Y6I3.
SIGNORiQ9Y6I3.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-1
Alternative name(s):
EH domain-binding mitotic phosphoprotein
EPS-15-interacting protein 1
Gene namesi
Name:EPN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:21604. EPN1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Nucleus By similarity
  • Membraneclathrin-coated pit By similarity

  • Note: Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

OpenTargetsiENSG00000063245.
PharmGKBiPA134860916.

Chemistry databases

ChEMBLiCHEMBL3259465.

Polymorphism and mutation databases

BioMutaiEPN1.
DMDMi332278179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745131 – 576Epsin-1Add BLAST576

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiQ9Y6I3.
MaxQBiQ9Y6I3.
PeptideAtlasiQ9Y6I3.
PRIDEiQ9Y6I3.

PTM databases

iPTMnetiQ9Y6I3.
PhosphoSitePlusiQ9Y6I3.

Expressioni

Gene expression databases

BgeeiENSG00000063245.
CleanExiHS_EPN1.
ExpressionAtlasiQ9Y6I3. baseline and differential.
GenevisibleiQ9Y6I3. HS.

Organism-specific databases

HPAiCAB009729.
HPA061136.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150383EBI-713198,EBI-724310
PLEKHB2Q96CS73EBI-713198,EBI-373552

Protein-protein interaction databases

BioGridi118965. 65 interactors.
IntActiQ9Y6I3. 22 interactors.
MINTiMINT-110599.

Chemistry databases

BindingDBiQ9Y6I3.

Structurei

Secondary structure

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 27Combined sources8
Helixi39 – 47Combined sources9
Helixi51 – 62Combined sources12
Helixi63 – 65Combined sources3
Helixi72 – 86Combined sources15
Helixi90 – 98Combined sources9
Helixi100 – 108Combined sources9
Helixi121 – 134Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1INZNMR-A1-144[»]
ProteinModelPortaliQ9Y6I3.
SMRiQ9Y6I3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6I3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 144ENTHPROSITE-ProRule annotationAdd BLAST133
Domaini183 – 202UIM 1PROSITE-ProRule annotationAdd BLAST20
Domaini208 – 227UIM 2PROSITE-ProRule annotationAdd BLAST20
Domaini233 – 252UIM 3PROSITE-ProRule annotationAdd BLAST20
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
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
Motifi402 – 411[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi267 – 573Ala/Gly/Pro-richAdd BLAST307

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

Sequence similaritiesi

Belongs to the epsin family.Curated
Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
Contains 3 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074611.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ9Y6I3.
KOiK12471.
OMAiMSGVRGS.
OrthoDBiEOG091G0L45.
TreeFamiTF313361.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' 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
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

Sequence cautioni

Isoform 2 : The sequence AAD38326 differs from that shown. Reason: Frameshift at position 98.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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]
UniGeneiHs.279953.

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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

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]
UniGeneiHs.279953.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1INZNMR-A1-144[»]
ProteinModelPortaliQ9Y6I3.
SMRiQ9Y6I3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118965. 65 interactors.
IntActiQ9Y6I3. 22 interactors.
MINTiMINT-110599.

Chemistry databases

BindingDBiQ9Y6I3.
ChEMBLiCHEMBL3259465.

PTM databases

iPTMnetiQ9Y6I3.
PhosphoSitePlusiQ9Y6I3.

Polymorphism and mutation databases

BioMutaiEPN1.
DMDMi332278179.

Proteomic databases

EPDiQ9Y6I3.
MaxQBiQ9Y6I3.
PeptideAtlasiQ9Y6I3.
PRIDEiQ9Y6I3.

Protocols and materials databases

DNASUi29924.
Structural Biology KnowledgebaseSearch...

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

CTDi29924.
GeneCardsiEPN1.
H-InvDBHIX0202721.
HGNCiHGNC:21604. EPN1.
HPAiCAB009729.
HPA061136.
MIMi607262. gene.
neXtProtiNX_Q9Y6I3.
OpenTargetsiENSG00000063245.
PharmGKBiPA134860916.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00550000074611.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ9Y6I3.
KOiK12471.
OMAiMSGVRGS.
OrthoDBiEOG091G0L45.
TreeFamiTF313361.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000063245-MONOMER.
ReactomeiR-HSA-182971. EGFR downregulation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiQ9Y6I3.
SIGNORiQ9Y6I3.

Miscellaneous databases

EvolutionaryTraceiQ9Y6I3.
GeneWikiiEPN1.
GenomeRNAii29924.
PROiQ9Y6I3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000063245.
CleanExiHS_EPN1.
ExpressionAtlasiQ9Y6I3. baseline and differential.
GenevisibleiQ9Y6I3. HS.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEPN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6I3
Secondary accession number(s): Q86ST3, Q9HA18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 3, 2011
Last modified: November 30, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
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.

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.