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Protein

Epsin-2

Gene

Epn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the formation of clathrin-coated invaginations and endocytosis.By similarity

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

  • embryonic organ development Source: MGI
  • endocytosis Source: UniProtKB-KW
  • in utero embryonic development Source: MGI
  • Notch signaling pathway Source: MGI
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
Intersectin-EH-binding protein 2
Short name:
Ibp2
Gene namesi
Name:Epn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1333766. 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Epsin-2PRO_0000074517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei526 – 5261PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8CHU3.
PaxDbiQ8CHU3.
PRIDEiQ8CHU3.

PTM databases

PhosphoSiteiQ8CHU3.

Expressioni

Gene expression databases

BgeeiQ8CHU3.
CleanExiMM_EPN2.
ExpressionAtlasiQ8CHU3. baseline and differential.
GenevisibleiQ8CHU3. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi199486. 4 interactions.
IntActiQ8CHU3. 3 interactions.
MINTiMINT-93098.

Structurei

3D structure databases

ProteinModelPortaliQ8CHU3.
SMRiQ8CHU3. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 144133ENTHPROSITE-ProRule annotationAdd
BLAST
Domaini218 – 23720UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini255 – 27420UIM 2PROSITE-ProRule annotationAdd
BLAST
Repeati313 – 31531
Repeati325 – 32732
Repeati338 – 34033
Repeati352 – 35434
Repeati370 – 37235
Repeati387 – 38936
Repeati494 – 49631
Repeati508 – 51032
Repeati591 – 59333

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni313 – 389776 X 3 AA repeats of [DE]-P-WAdd
BLAST
Regioni494 – 5931003 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

eggNOGiNOG263730.
GeneTreeiENSGT00550000074611.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ8CHU3.
KOiK12471.
PhylomeDBiQ8CHU3.
TreeFamiTF313361.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CHU3-1) [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
MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV
60 70 80 90 100
VAFSEIMSMV WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI
110 120 130 140 150
FAIQTLKDFQ YIDRDGKDQG INVREKSKQL VALLKDEERL KVERVQALKT
160 170 180 190 200
KERMAQVATG VGSNQITFGR GSSQPNLSTS YSEQEYGKAG GSPASYHGST
210 220 230 240 250
SPRVSSELEQ ARPQTSGEEE LQLQLALAMS REVAEQSSES VQTARGSKEE
260 270 280 290 300
RLRRGDDLRL QMALEESRRD TVKVPKKKEA KACCKPGSHS QQTTLLDLMD
310 320 330 340 350
ALPSSGPVTQ KTEPWSAGAS ANQTNPWGGT VAPSNITDPW PSFGTKPAAS
360 370 380 390 400
VDPWGVPTTA STQSVPKNSD PWAASQQPAS NAGKTTDAWG AAKPSSASGS
410 420 430 440 450
FELFSNFNGT VKDDFSEFDN LRTSKKPAES GASVPPQDSR TTSPDLFESQ
460 470 480 490 500
SLTSASSKPS SARKTPESFL GPNAALVNLD SLVTKPAPPA QSLNPFLAPG
510 520 530 540 550
AAAPAPVNPF QVNQPQPLTL NQLRGSPVLG SSASFGSGPG VETVAPMTSV
560 570 580 590
APHSSVGASG SSLTPLGPTA MNMVGSVGIP PSAAQSTGTT NPFLL
Length:595
Mass (Da):63,472
Last modified:March 1, 2003 - v1
Checksum:i255DC7BC7E1B2D13
GO
Isoform 2 (identifier: Q8CHU3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     237-248: Missing.

Note: No experimental confirmation available.
Show »
Length:583
Mass (Da):62,253
Checksum:iEFC06A1371A85980
GO

Sequence cautioni

The sequence AAC97476.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751Y → S in AAC97476 (PubMed:9813051).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei237 – 24812Missing in isoform 2. 2 PublicationsVSP_009157Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036331 mRNA. Translation: BAC29387.1.
AL604029 Genomic DNA. Translation: CAI24192.1.
BC039138 mRNA. Translation: AAH39138.1.
AF057286 mRNA. Translation: AAC97476.1. Different initiation.
CCDSiCCDS24816.1. [Q8CHU3-1]
CCDS56779.1. [Q8CHU3-2]
RefSeqiNP_001239118.1. NM_001252189.1. [Q8CHU3-2]
NP_034278.1. NM_010148.3. [Q8CHU3-1]
UniGeneiMm.139695.
Mm.489800.

Genome annotation databases

EnsembliENSMUST00000001063; ENSMUSP00000001063; ENSMUSG00000001036. [Q8CHU3-1]
ENSMUST00000108713; ENSMUSP00000104353; ENSMUSG00000001036. [Q8CHU3-2]
ENSMUST00000178202; ENSMUSP00000136553; ENSMUSG00000001036. [Q8CHU3-1]
GeneIDi13855.
KEGGimmu:13855.
UCSCiuc007jhv.2. mouse. [Q8CHU3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK036331 mRNA. Translation: BAC29387.1.
AL604029 Genomic DNA. Translation: CAI24192.1.
BC039138 mRNA. Translation: AAH39138.1.
AF057286 mRNA. Translation: AAC97476.1. Different initiation.
CCDSiCCDS24816.1. [Q8CHU3-1]
CCDS56779.1. [Q8CHU3-2]
RefSeqiNP_001239118.1. NM_001252189.1. [Q8CHU3-2]
NP_034278.1. NM_010148.3. [Q8CHU3-1]
UniGeneiMm.139695.
Mm.489800.

3D structure databases

ProteinModelPortaliQ8CHU3.
SMRiQ8CHU3. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199486. 4 interactions.
IntActiQ8CHU3. 3 interactions.
MINTiMINT-93098.

PTM databases

PhosphoSiteiQ8CHU3.

Proteomic databases

MaxQBiQ8CHU3.
PaxDbiQ8CHU3.
PRIDEiQ8CHU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001063; ENSMUSP00000001063; ENSMUSG00000001036. [Q8CHU3-1]
ENSMUST00000108713; ENSMUSP00000104353; ENSMUSG00000001036. [Q8CHU3-2]
ENSMUST00000178202; ENSMUSP00000136553; ENSMUSG00000001036. [Q8CHU3-1]
GeneIDi13855.
KEGGimmu:13855.
UCSCiuc007jhv.2. mouse. [Q8CHU3-1]

Organism-specific databases

CTDi22905.
MGIiMGI:1333766. Epn2.

Phylogenomic databases

eggNOGiNOG263730.
GeneTreeiENSGT00550000074611.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
InParanoidiQ8CHU3.
KOiK12471.
PhylomeDBiQ8CHU3.
TreeFamiTF313361.

Miscellaneous databases

ChiTaRSiEpn2. mouse.
NextBioi284722.
PROiQ8CHU3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHU3.
CleanExiMM_EPN2.
ExpressionAtlasiQ8CHU3. baseline and differential.
GenevisibleiQ8CHU3. MM.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Intersectin, a novel adaptor protein with two eps15 homology and five src homology 3 domains."
    Yamabhai M., Hoffman N.G., Hardison N.L., McPherson P.S., Castagnoli L., Cesareni G., Kay B.K.
    J. Biol. Chem. 273:31401-31407(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-595 (ISOFORM 2), INTERACTION WITH ITSN1.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-86, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.

Entry informationi

Entry nameiEPN2_MOUSE
AccessioniPrimary (citable) accession number: Q8CHU3
Secondary accession number(s): O70447, Q5NCM4, Q8BZ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 118 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.