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Protein

Epsin-2

Gene

Epn2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the formation of clathrin-coated invaginations and endocytosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Phosphatidylinositol lipid headgroupBy similarity
Binding sitei11 – 111Phosphatidylinositol lipid headgroupBy similarity
Binding sitei25 – 251Phosphatidylinositol lipid headgroupBy similarity
Binding sitei30 – 301Phosphatidylinositol lipid headgroupBy similarity
Binding sitei63 – 631Phosphatidylinositol lipid headgroupBy similarity
Binding sitei73 – 731Phosphatidylinositol lipid headgroupBy similarity

GO - Molecular functioni

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • regulation of endocytosis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-2
Alternative name(s):
EPS-15-interacting protein 2
Gene namesi
Name:Epn2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619773. Epn2.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: In punctate structures throughout the cell and particularly concentrated in the region of the Golgi complex.By similarity

GO - Cellular componenti

  • clathrin coat of endocytic vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583Epsin-2PRO_0000074518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731PhosphoserineBy similarity
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei195 – 1951PhosphoserineCombined sources
Modified residuei431 – 4311PhosphoserineCombined sources
Modified residuei453 – 4531PhosphothreonineCombined sources
Modified residuei514 – 5141PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9Z1Z3.

Expressioni

Tissue specificityi

Highly expressed in brain. Detected at lower levels in lung, liver, muscle and testis.1 Publication

Interactioni

Subunit structurei

Binds AP-2 and clathrin (By similarity). Interacts with ITSN1 (By similarity). Interacts with UBQLN2 (By similarity). Binds EPS15.By similarity1 Publication

Protein-protein interaction databases

BioGridi248836. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1Z3.
SMRiQ9Z1Z3. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 144133ENTHPROSITE-ProRule annotationAdd
BLAST
Domaini218 – 23720UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini243 – 26220UIM 2PROSITE-ProRule annotationAdd
BLAST
Repeati301 – 30331
Repeati313 – 31532
Repeati326 – 32833
Repeati340 – 34234
Repeati358 – 36035
Repeati375 – 37736
Repeati482 – 48431
Repeati496 – 49832
Repeati579 – 58133

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni301 – 377776 X 3 AA repeats of [DE]-P-WAdd
BLAST
Regioni482 – 5811003 X 3 AA repeats of N-P-FAdd
BLAST

Domaini

The NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP-2 and clathrin binding.

Sequence similaritiesi

Belongs to the epsin family.Curated
Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ9Z1Z3.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR027319. Epsin-2_metazoa.
IPR003903. UIM_dom.
[Graphical view]
PANTHERiPTHR12276:SF50. PTHR12276:SF50. 1 hit.
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSSIRRQM KNIVNSYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV
60 70 80 90 100
VRFSEIMSMV WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI
110 120 130 140 150
FAIQTLKDFQ YIDRDGKDQG INVREKSKQL VALLKDEERL KVERVQALKT
160 170 180 190 200
KERMAQVATG VGSNQITFGR GSSQPNLSIS HSEQEYGKAG GSPASYHGST
210 220 230 240 250
SPRVSSELEQ ARPQTSGEEE LQLQLALAMS REVAEQEERL RRGDDLRLQM
260 270 280 290 300
ALEESRRDTV KVPKKKEVKA CCKPGSHSQQ TTLLDLMDAL PSSGPVAQKT
310 320 330 340 350
EPWSTGTPAN QTNPWGGTVA PANISDPWPS FGTKPAASVD PWGVPTTASI
360 370 380 390 400
QSVPKNSDPW AASQQPASDA GKTADAWGAA KPSPASGSFE LFSNFNGTVK
410 420 430 440 450
DDFSEFDNLR TSKKPAESGA SVPPQDSRTT SPDLFESQSL TSASSKPSSA
460 470 480 490 500
RKTPESFLGP NAALVNLDSL VTKPAPPAQS LNPFLAPGAA APAPVNPFQV
510 520 530 540 550
NQPQPLTLNQ LRGSPVLGSS ASFGSGPGVE TVAPMPSVAP HSALGATGSS
560 570 580
LTPLGPTAMN MVGSMGIPPS AAQPAGTTNP FLL
Length:583
Mass (Da):62,349
Last modified:May 1, 1999 - v1
Checksum:i2C2982B72C8FDC79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF096269 mRNA. Translation: AAC79495.1.
UniGeneiRn.44273.

Genome annotation databases

UCSCiRGD:619773. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF096269 mRNA. Translation: AAC79495.1.
UniGeneiRn.44273.

3D structure databases

ProteinModelPortaliQ9Z1Z3.
SMRiQ9Z1Z3. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248836. 2 interactions.

Proteomic databases

PRIDEiQ9Z1Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:619773. rat.

Organism-specific databases

RGDi619773. Epn2.

Phylogenomic databases

HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ9Z1Z3.

Miscellaneous databases

NextBioi612174.
PROiQ9Z1Z3.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR027319. Epsin-2_metazoa.
IPR003903. UIM_dom.
[Graphical view]
PANTHERiPTHR12276:SF50. PTHR12276:SF50. 1 hit.
PfamiPF01417. ENTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module."
    Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E., Di Fiore P.P., De Camilli P.
    J. Biol. Chem. 274:33959-33965(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EPS15, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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: UBIQUITINATION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-195; SER-431 AND THR-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEPN2_RAT
AccessioniPrimary (citable) accession number: Q9Z1Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1999
Last modified: November 11, 2015
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. 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.