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Protein

Epsin-1

Gene

Epn1

Organism
Rattus norvegicus (Rat)
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. Regulates receptor-mediated endocytosis.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8Phosphatidylinositol lipid headgroup1
Binding sitei11Phosphatidylinositol lipid headgroup1
Binding sitei25Phosphatidylinositol lipid headgroup1
Binding sitei30Phosphatidylinositol lipid headgroup1
Binding sitei63Phosphatidylinositol lipid headgroup1
Binding sitei73Phosphatidylinositol lipid headgroup1

GO - Molecular functioni

  • ion channel binding Source: RGD
  • lipid binding Source: UniProtKB-KW
  • transcription factor binding Source: RGD

GO - Biological processi

  • endocytosis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-1
Alternative name(s):
EPS-15-interacting protein 1
Gene namesi
Name:Epn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619772. Epn1.

Subcellular locationi

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

  • 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. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.

GO - Cellular componenti

  • clathrin-coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745151 – 575Epsin-1Add BLAST575

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

PaxDbiO88339.
PeptideAtlasiO88339.
PRIDEiO88339.

PTM databases

iPTMnetiO88339.
PhosphoSitePlusiO88339.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSRNOG00000015753.
GenevisibleiO88339. RN.

Interactioni

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

GO - Molecular functioni

  • ion channel binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi250724. 15 interactors.
DIPiDIP-40738N.
IntActiO88339. 2 interactors.
MINTiMINT-101104.
STRINGi10116.ENSRNOP00000021286.

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 15Combined sources14
Helixi19 – 27Combined sources9
Beta strandi30 – 33Combined sources4
Helixi37 – 46Combined sources10
Helixi50 – 64Combined sources15
Helixi68 – 70Combined sources3
Helixi71 – 87Combined sources17
Helixi90 – 98Combined sources9
Helixi100 – 104Combined sources5
Helixi105 – 108Combined sources4
Helixi120 – 135Combined sources16
Helixi137 – 155Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiO88339.

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
Repeati501 – 50313
Repeati517 – 51923
Repeati571 – 57333

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi401 – 410[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi267 – 572Ala/Gly/Pro-richAdd BLAST306

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

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

eggNOGiKOG2056. Eukaryota.
ENOG410XSM0. LUCA.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiO88339.
KOiK12471.
OrthoDBiEOG091G0L45.
PhylomeDBiO88339.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[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]

Sequencei

Sequence statusi: Complete.

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
Checksum:iD0B770F3B7AB5DDA
GO

Sequence databases

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

Genome annotation databases

GeneIDi117277.
KEGGirno:117277.
UCSCiRGD:619772. rat.

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
AF018261 mRNA. Translation: AAC33823.1.
RefSeqiNP_476477.1. NM_057136.1.
UniGeneiRn.30007.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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.
DIPiDIP-40738N.
IntActiO88339. 2 interactors.
MINTiMINT-101104.
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

CTDi29924.
RGDi619772. Epn1.

Phylogenomic databases

eggNOGiKOG2056. Eukaryota.
ENOG410XSM0. LUCA.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiO88339.
KOiK12471.
OrthoDBiEOG091G0L45.
PhylomeDBiO88339.

Miscellaneous databases

EvolutionaryTraceiO88339.
PROiO88339.

Gene expression databases

BgeeiENSRNOG00000015753.
GenevisibleiO88339. RN.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[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_RAT
AccessioniPrimary (citable) accession number: O88339
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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