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O88339

- EPN1_RAT

UniProt

O88339 - EPN1_RAT

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Protein
Epsin-1
Gene
Epn1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Phosphatidylinositol lipid headgroup
Binding sitei11 – 111Phosphatidylinositol lipid headgroup
Binding sitei25 – 251Phosphatidylinositol lipid headgroup
Binding sitei30 – 301Phosphatidylinositol lipid headgroup
Binding sitei63 – 631Phosphatidylinositol lipid headgroup
Binding sitei73 – 731Phosphatidylinositol lipid headgroup

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. transcription factor binding Source: RGD

GO - Biological processi

  1. Notch signaling pathway Source: Ensembl
  2. embryonic organ development Source: Ensembl
  3. endocytosis Source: RGD
  4. female pregnancy Source: Ensembl
  5. in utero embryonic development Source: Ensembl
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
ProteomesiUP000002494: Chromosome 1

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/ZNF145.4 Publications

GO - Cellular componenti

  1. coated pit Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: RGD
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61L → E, H or Q: Reduces lipid binding. 1 Publication
Mutagenesisi8 – 81R → A: Strongly reduces lipid binding. 1 Publication
Mutagenesisi63 – 631R → L: Strongly reduces lipid binding. Abolishes lipid binding; when associated with L-73. 2 Publications
Mutagenesisi72 – 721R → A: Abolishes ZNF145 binding. 1 Publication
Mutagenesisi73 – 731H → L: Abolishes lipid binding; when associated with L-63. 1 Publication
Mutagenesisi76 – 761K → A: Strongly reduces lipid binding. 1 Publication
Mutagenesisi190 – 1901L → A: Abolishes mono-ubiquitination. 1 Publication
Mutagenesisi257 – 2593LMD → AAA: Strongly reduces clathrin binding. 1 Publication
Mutagenesisi260 – 2634LADV → AAAA: Strongly reduces clathrin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Epsin-1
PRO_0000074515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei382 – 3821Phosphoserine By similarity
Modified residuei418 – 4181Phosphoserine By similarity
Modified residuei419 – 4191Phosphoserine By similarity
Modified residuei434 – 4341Phosphoserine By similarity
Modified residuei453 – 4531Phosphoserine By similarity
Modified residuei459 – 4591Phosphothreonine By similarity
Modified residuei469 – 4691Phosphothreonine By similarity
Modified residuei493 – 4931Phosphothreonine By similarity

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

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO88339.
PRIDEiO88339.

PTM databases

PhosphoSiteiO88339.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevestigatoriO88339.

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 AP2B1.8 Publications

Protein-protein interaction databases

BioGridi250724. 16 interactions.
IntActiO88339. 2 interactions.
MINTiMINT-101104.
STRINGi10116.ENSRNOP00000021286.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1514
Helixi19 – 279
Beta strandi30 – 334
Helixi37 – 4610
Helixi50 – 6415
Helixi68 – 703
Helixi71 – 8717
Helixi90 – 989
Helixi100 – 1045
Helixi105 – 1084
Helixi120 – 13516
Helixi137 – 15519

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDUX-ray1.80A12-160[»]
1EYHX-ray1.56A15-158[»]
1H0AX-ray1.70A1-158[»]
1KY6X-ray2.00P375-381[»]
DisProtiDP00251.
ProteinModelPortaliO88339.
SMRiO88339. Positions 1-158.

Miscellaneous databases

EvolutionaryTraceiO88339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 144133ENTH
Add
BLAST
Repeati183 – 20220UIM 1
Add
BLAST
Repeati208 – 22720UIM 2
Add
BLAST
Repeati233 – 25220UIM 3
Add
BLAST
Repeati274 – 27631
Repeati294 – 29632
Repeati306 – 30833
Repeati319 – 32134
Repeati332 – 33435
Repeati349 – 35136
Repeati367 – 36937
Repeati377 – 37938
Repeati501 – 50331
Repeati517 – 51932
Repeati571 – 57333

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 3791068 X 3 AA repeats of D-P-W
Add
BLAST
Regioni501 – 573733 X 3 AA repeats of N-P-F
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi401 – 41010[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 572306Ala/Gly/Pro-rich
Add
BLAST

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG263730.
GeneTreeiENSGT00550000074611.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiO88339.
KOiK12471.
OMAiDPWGGTQ.
OrthoDBiEOG7F511Z.
PhylomeDBiO88339.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[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

MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV    50
VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM 100
YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT 150
KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD 200
QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG 250
GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGAPA 300
VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTSDP 350
WGSADGGAPV SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP 400
DEFSDFDRLR TALPTSGSST GELELLAGEV PARSPGAFDM SGVGGSLAES 450
VGSPPPAATP TPTPPTRKTP ESFLGPNAAL VDLDSLVSRP GPTPPGAKAS 500
NPFLPSGAPA TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV PGAPPTYISP 550
LGGGPGLPPM MPPGPPAPNT NPFLL 575
Length:575
Mass (Da):60,158
Last modified:November 1, 1998 - v1
Checksum:iD0B770F3B7AB5DDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF018261 mRNA. Translation: AAC33823.1.
RefSeqiNP_476477.1. NM_057136.1.
UniGeneiRn.30007.

Genome annotation databases

EnsembliENSRNOT00000021286; ENSRNOP00000021286; ENSRNOG00000015753.
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:
EMBL
GenBank
DDBJ
Links Updated
AF018261 mRNA. Translation: AAC33823.1 .
RefSeqi NP_476477.1. NM_057136.1.
UniGenei Rn.30007.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EDU X-ray 1.80 A 12-160 [» ]
1EYH X-ray 1.56 A 15-158 [» ]
1H0A X-ray 1.70 A 1-158 [» ]
1KY6 X-ray 2.00 P 375-381 [» ]
DisProti DP00251.
ProteinModelPortali O88339.
SMRi O88339. Positions 1-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250724. 16 interactions.
IntActi O88339. 2 interactions.
MINTi MINT-101104.
STRINGi 10116.ENSRNOP00000021286.

PTM databases

PhosphoSitei O88339.

Proteomic databases

PaxDbi O88339.
PRIDEi O88339.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021286 ; ENSRNOP00000021286 ; ENSRNOG00000015753 .
GeneIDi 117277.
KEGGi rno:117277.
UCSCi RGD:619772. rat.

Organism-specific databases

CTDi 29924.
RGDi 619772. Epn1.

Phylogenomic databases

eggNOGi NOG263730.
GeneTreei ENSGT00550000074611.
HOGENOMi HOG000008298.
HOVERGENi HBG006690.
InParanoidi O88339.
KOi K12471.
OMAi DPWGGTQ.
OrthoDBi EOG7F511Z.
PhylomeDBi O88339.

Miscellaneous databases

EvolutionaryTracei O88339.
NextBioi 620217.
PROi O88339.

Gene expression databases

Genevestigatori O88339.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
InterProi IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
Pfami PF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view ]
SMARTi SM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
PROSITEi PS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis."
    Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H., Di Fiore P.P., De Camilli P.
    Nature 394:793-797(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPS15; AP2A1 AND AP2A2.
    Strain: Wistar.
    Tissue: Brain.
  2. "A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain."
    Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T.
    Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2A2.
  3. "The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is inhibited by mitotic phosphorylation and enhanced by stimulation-dependent dephosphorylation in nerve terminals."
    Chen H., Slepnev V.I., Di Fiore P.P., De Camilli P.
    J. Biol. Chem. 274:3257-3260(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH AP-2.
  4. "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."
    Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.
    Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2A2.
  5. "The structure and function of the beta 2-adaptin appendage domain."
    Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.
    EMBO J. 19:4216-4227(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.
  6. "Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites."
    Drake M.T., Downs M.A., Traub L.M.
    J. Biol. Chem. 275:6479-6489(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 257-LEU--ASP-259 AND 260-LEU--VAL-263, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN HEAVY CHAIN AND AP-2.
  7. "Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis."
    Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., Takenawa T.
    Science 291:1047-1051(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZBTB16, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-8; ARG-63; ARG-72 AND LYS-76.
  8. "A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins."
    Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H., De Camilli P., Di Fiore P.P.
    Nature 416:451-455(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-190, UBIQUITINATION.
  9. "Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and Heat repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)."
    Hyman J., Chen H., Di Fiore P.P., De Camilli P., Brunger A.T.
    J. Cell Biol. 149:537-546(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-160, SUBCELLULAR LOCATION, INTERACTION WITH ZNF145.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-158 IN COMPLEX WITH INOSITOL-1,4,5-TRIPHOSPHATE, FUNCTION, MUTAGENESIS OF LEU-6; ARG-63 AND HIS-73.
  11. "Accessory protein recruitment motifs in clathrin-mediated endocytosis."
    Brett T.J., Traub L.M., Fremont D.H.
    Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 375-381 IN COMPLEX WITH AP2A2.

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: April 16, 2014
This is version 120 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

External Data

Dasty 3

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