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P42567

- EPS15_MOUSE

UniProt

P42567 - EPS15_MOUSE

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Protein
Epidermal growth factor receptor substrate 15
Gene
Eps15
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi173 – 184121 Reviewed prediction
Add
BLAST
Calcium bindingi236 – 247122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. identical protein binding Source: IntAct
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. clathrin coat assembly Source: Ensembl
  2. endocytosis Source: UniProtKB-KW
  3. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_203917. EGFR downregulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor substrate 15
Short name:
Protein Eps15
Alternative name(s):
Protein AF-1p
Gene namesi
Name:Eps15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:104583. Eps15.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membraneclathrin-coated pit
Note: Recruited to the plasma membrane upon EGFR activation and localizes to coated pits.
Isoform 2 : Early endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Colocalizes with HGS on bilayered clathrin coats on endosomes By similarity.

GO - Cellular componenti

  1. AP-2 adaptor complex Source: UniProtKB
  2. ciliary membrane Source: MGI
  3. clathrin coat of coated pit Source: MGI
  4. clathrin-coated vesicle Source: UniProtKB
  5. coated pit Source: MGI
  6. early endosome membrane Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi850 – 8501Y → F: Inefficient EGFR internalization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 897896Epidermal growth factor receptor substrate 15
PRO_0000146117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei108 – 1081Phosphoserine By similarity
Modified residuei140 – 1401Phosphoserine By similarity
Modified residuei323 – 3231Phosphoserine By similarity
Modified residuei324 – 3241Phosphoserine1 Publication
Modified residuei467 – 4671Phosphoserine By similarity
Modified residuei470 – 4701Phosphoserine By similarity
Modified residuei485 – 4851Phosphoserine By similarity
Modified residuei779 – 7791Phosphothreonine1 Publication
Modified residuei798 – 7981Phosphoserine By similarity
Modified residuei816 – 8161Phosphoserine By similarity
Modified residuei850 – 8501Phosphotyrosine; by EGFR1 Publication

Post-translational modificationi

Phosphorylated on serine upon DNA damage, probably by ATM or ATR By similarity. Phosphorylation on Tyr-850 is involved in the internalization of EGFR. Not required for membrane translocation after EGF treatment or for targeting to coated pits, but essential for a subsequent step in EGFR endocytosis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42567.
PaxDbiP42567.
PRIDEiP42567.

PTM databases

PhosphoSiteiP42567.

Expressioni

Gene expression databases

ArrayExpressiP42567.
BgeeiP42567.
GenevestigatoriP42567.

Interactioni

Subunit structurei

Interacts with HGS; the interaction bridges the interaction of STAM or STAM2 with EPS15. Isoform 2 interacts with HGS and AP2A2. Part of a complex at least composed of EPS15, HGS, and either STAM1 or STAM2. Binds AP2A2. Interacts with AP2B1; clathrin competes with EPS15. Binds STON2 and EPN1. Interacts (via its SH3-binding sites) with CRK. Interacts with SH3BP4/TTP. Interacts with ERBB2. Interacts (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472') By similarity. Interacts with FCHO1 By similarity. Interacts with FCHO2. Interacts with SGIP1. Interacts (via EH domains) with DAB2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-443923,EBI-443923
Dab2P980782EBI-443923,EBI-1391846
Eps15l1Q609022EBI-443923,EBI-443931
REPS2Q8NFH810EBI-443923,EBI-7067016From a different organism.

Protein-protein interaction databases

BioGridi199489. 16 interactions.
DIPiDIP-29052N.
IntActiP42567. 7 interactions.
MINTiMINT-86610.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124
Turni13 – 153
Helixi18 – 269
Helixi37 – 448
Beta strandi46 – 483
Helixi50 – 6011
Beta strandi63 – 675
Helixi71 – 8313
Turni84 – 863
Helixi91 – 933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KYFX-ray1.22P627-632[»]
1KYUX-ray1.80P627-632[»]
1QJTNMR-A7-105[»]
ProteinModelPortaliP42567.
SMRiP42567. Positions 7-105, 121-215, 217-311, 336-391, 440-478.

Miscellaneous databases

EvolutionaryTraceiP42567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 10490EH 1
Add
BLAST
Domaini128 – 21689EH 2
Add
BLAST
Domaini160 – 19536EF-hand 1
Add
BLAST
Domaini223 – 25836EF-hand 2
Add
BLAST
Domaini224 – 31491EH 3
Add
BLAST
Repeati599 – 60131
Repeati623 – 62532
Repeati629 – 63133
Repeati634 – 63634
Repeati640 – 64235
Repeati645 – 64736
Repeati651 – 65337
Repeati665 – 66738
Repeati673 – 67539
Repeati693 – 695310
Repeati711 – 713311
Repeati806 – 808312
Repeati827 – 829313
Repeati852 – 87120UIM 1
Add
BLAST
Repeati878 – 89720UIM 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 330329Interaction with DAB2
Add
BLAST
Regioni599 – 82923113 X 3 AA repeats of D-P-F
Add
BLAST

Domaini

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins By similarity.
The UIM (ubiquitin-interacting motif) repeats specifically bind 'Lys-33'-linked ubiquitin By similarity.

Sequence similaritiesi

Contains 2 EF-hand domains.
Contains 3 EH domains.

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG301764.
GeneTreeiENSGT00750000117388.
HOGENOMiHOG000004804.
HOVERGENiHBG005591.
InParanoidiP42567.
KOiK12472.
OrthoDBiEOG7JHM68.
PhylomeDBiP42567.
TreeFamiTF324293.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P42567-1) [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

MAAAAQLSLT QLSSGNPVYE KYYRQVEAGN TGRVLALDAA AFLKKSGLPD    50
LILGKIWDLA DTDGKGVLSK QEFFVALRLV ACAQNGLEVS LSSLSLAVPP 100
PRFHDSSSPL LTSGPSVAEL PWAVKSEDKA KYDAIFDSLS PVDGFLSGDK 150
VKPVLLNSKL PVEILGRVWE LSDIDHDGKL DRDEFAVAMF LVYCALEKEP 200
VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD GYVSGLEVRE 250
TFLKTGLPSA LLAHIWSLCD TKGCGKLSKD QFALAFHLIN QKLIKGIDPP 300
HSLTPEMIPP SDRSSLQKNI TGSSPVADFS AIKELDTLNN EIVDLQREKN 350
NVEQDLKEKE DTVKQRTSEV QDLQDEVQRE SINLQKLQAQ KQQVQELLGE 400
LDEQKAQLEE QLQEVRKKCA EEAQLISSLK AEITSQESQI SSYEEELLKA 450
REELSRLQQE TAQLEESVES GKAQLEPLQQ HLQESQQEIS SMQMRLEMKD 500
LETDNNQSNW SSSPQSVLVN GATDYCSLST SSSETANFNE HAEGQNNLES 550
EPTHQESSVR SSPEIAPSDV TDESEAVTVA GNEKVTPRFD DDKHSKEEDP 600
FNVESSSLTD AVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS 650
DPFASDCFFK QTSTDPFTTS STDPFSASSN SSNTSVETWK HNDPFAPGGT 700
VVAAASDSAT DPFASVFGNE SFGDGFADFS TLSKVNNEDA FNPTISSSTS 750
SVTIAKPMLE ETASKSEDVP PALPPKVGTP TRPCPPPPGK RPINKLDSSD 800
PLKLNDPFQP FPGNDSPKEK DPDMFCDPFT SSTTTNKEAD PSNFANFSAY 850
PSEEDMIEWA KRESEREEEQ RLARLNQQEQ EDLELAIALS KSEISEA 897
Length:897
Mass (Da):98,471
Last modified:November 1, 1995 - v1
Checksum:i08A0C0D423F873C2
GO
Isoform 2 (identifier: P42567-2) [UniParc]FASTAAdd to Basket

Also known as: Eps15b

The sequence of this isoform differs from the canonical sequence as follows:
     2-314: Missing.
     315-346: SLQKNITGSSPVADFSAIKELDTLNNEIVDLQ → MYSDSGLGGWIAIPAVADVLRYSCIVCWSS

Show »
Length:582
Mass (Da):64,203
Checksum:iD5951681ED54F90C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 314313Missing in isoform 2.
VSP_036170Add
BLAST
Alternative sequencei315 – 34632SLQKN…IVDLQ → MYSDSGLGGWIAIPAVADVL RYSCIVCWSS in isoform 2.
VSP_036171Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L21768 mRNA. Translation: AAA02912.1.
AK083176 mRNA. Translation: BAC38796.1.
AL669905 Genomic DNA. Translation: CAM13653.1.
CCDSiCCDS18462.1. [P42567-1]
PIRiA54696.
RefSeqiNP_001153436.1. NM_001159964.1.
NP_031969.1. NM_007943.3. [P42567-1]
UniGeneiMm.318250.

Genome annotation databases

EnsembliENSMUST00000030281; ENSMUSP00000030281; ENSMUSG00000028552.
ENSMUST00000102729; ENSMUSP00000099790; ENSMUSG00000028552. [P42567-1]
GeneIDi13858.
KEGGimmu:13858.
UCSCiuc008ucf.2. mouse. [P42567-1]
uc008ucg.2. mouse. [P42567-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L21768 mRNA. Translation: AAA02912.1 .
AK083176 mRNA. Translation: BAC38796.1 .
AL669905 Genomic DNA. Translation: CAM13653.1 .
CCDSi CCDS18462.1. [P42567-1 ]
PIRi A54696.
RefSeqi NP_001153436.1. NM_001159964.1.
NP_031969.1. NM_007943.3. [P42567-1 ]
UniGenei Mm.318250.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KYF X-ray 1.22 P 627-632 [» ]
1KYU X-ray 1.80 P 627-632 [» ]
1QJT NMR - A 7-105 [» ]
ProteinModelPortali P42567.
SMRi P42567. Positions 7-105, 121-215, 217-311, 336-391, 440-478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199489. 16 interactions.
DIPi DIP-29052N.
IntActi P42567. 7 interactions.
MINTi MINT-86610.

PTM databases

PhosphoSitei P42567.

Proteomic databases

MaxQBi P42567.
PaxDbi P42567.
PRIDEi P42567.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030281 ; ENSMUSP00000030281 ; ENSMUSG00000028552 .
ENSMUST00000102729 ; ENSMUSP00000099790 ; ENSMUSG00000028552 . [P42567-1 ]
GeneIDi 13858.
KEGGi mmu:13858.
UCSCi uc008ucf.2. mouse. [P42567-1 ]
uc008ucg.2. mouse. [P42567-2 ]

Organism-specific databases

CTDi 2060.
MGIi MGI:104583. Eps15.

Phylogenomic databases

eggNOGi NOG301764.
GeneTreei ENSGT00750000117388.
HOGENOMi HOG000004804.
HOVERGENi HBG005591.
InParanoidi P42567.
KOi K12472.
OrthoDBi EOG7JHM68.
PhylomeDBi P42567.
TreeFami TF324293.

Enzyme and pathway databases

Reactomei REACT_203917. EGFR downregulation.

Miscellaneous databases

EvolutionaryTracei P42567.
NextBioi 284734.
PROi P42567.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42567.
Bgeei P42567.
Genevestigatori P42567.

Family and domain databases

Gene3Di 1.10.238.10. 3 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
SMARTi SM00054. EFh. 4 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 2 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "eps15, a novel tyrosine kinase substrate, exhibits transforming activity."
    Fazioli F., Minichiello L., Matoskova B., Wong W.T., di Fiore P.P.
    Mol. Cell. Biol. 13:5814-5828(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fibroblast.
  2. "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: Hippocampus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 838-862, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis."
    Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.
    J. Cell Biol. 150:905-912(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-850 BY EGFR, MUTAGENESIS OF TYR-850.
  6. "SGIP1alpha is an endocytic protein that directly interacts with phospholipids and Eps15."
    Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K., Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.
    J. Biol. Chem. 282:26481-26489(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGIP1.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
    Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
    Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO2.
  11. "Characterization of the EFC/F-BAR domain protein, FCHO2."
    Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.
    Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO2.
  12. "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."
    Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
    Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  13. "The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins."
    Whitehead B., Tessari M., Carotenuto A., van Bergen en Henegouwen P.M., Vuister G.W.
    Biochemistry 38:11271-11277(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 7-105.
  14. "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 (1.22 ANGSTROMS) OF 628-632 IN COMPLEX WITH AP2A2.

Entry informationi

Entry nameiEPS15_MOUSE
AccessioniPrimary (citable) accession number: P42567
Secondary accession number(s): Q8C431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 144 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, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi