Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Epidermal growth factor receptor substrate 15

Gene

Eps15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 – 184121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi236 – 247122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. clathrin coat assembly Source: MGI
  2. endocytosis Source: UniProtKB-KW
  3. Golgi to endosome transport Source: UniProtKB
  4. 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_350802. 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 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:104583. Eps15.

Subcellular locationi

  1. Cytoplasm
  2. Cell membrane; Peripheral membrane protein; Cytoplasmic side
  3. Membraneclathrin-coated pit

  4. Note: Recruited to the plasma membrane upon EGFR activation and localizes to coated pits.
Isoform 2 :
  1. Early endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  2. 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-coated vesicle Source: UniProtKB
  4. clathrin coat of coated pit Source: MGI
  5. coated pit Source: MGI
  6. cytoplasm Source: MGI
  7. early endosome membrane Source: UniProtKB-SubCell
  8. intracellular membrane-bounded organelle Source: MGI
  9. membrane Source: MGI
  10. 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 – 11RemovedBy similarity
Chaini2 – 897896Epidermal growth factor receptor substrate 15PRO_0000146117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei323 – 3231PhosphoserineBy similarity
Modified residuei324 – 3241Phosphoserine1 Publication
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei470 – 4701PhosphoserineBy similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei779 – 7791Phosphothreonine1 Publication
Modified residuei798 – 7981PhosphoserineBy similarity
Modified residuei816 – 8161PhosphoserineBy 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.By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42567.
PaxDbiP42567.
PRIDEiP42567.

PTM databases

PhosphoSiteiP42567.

Expressioni

Gene expression databases

BgeeiP42567.
ExpressionAtlasiP42567. baseline and differential.
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.By similarity5 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

1
897
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Turni13 – 153Combined sources
Helixi18 – 269Combined sources
Helixi37 – 448Combined sources
Beta strandi46 – 483Combined sources
Helixi50 – 6011Combined sources
Beta strandi63 – 675Combined sources
Helixi71 – 8313Combined sources
Turni84 – 863Combined sources
Helixi91 – 933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 10490EH 1PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 21689EH 2PROSITE-ProRule annotationAdd
BLAST
Domaini160 – 19536EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini223 – 25836EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini224 – 31491EH 3PROSITE-ProRule annotationAdd
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
Domaini852 – 87120UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 89720UIM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 330329Interaction with DAB2Add
BLAST
Regioni599 – 82923113 X 3 AA repeats of D-P-FAdd
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.PROSITE-ProRule annotation
Contains 3 EH domains.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG301764.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAAAQLSLT QLSSGNPVYE KYYRQVEAGN TGRVLALDAA AFLKKSGLPD
60 70 80 90 100
LILGKIWDLA DTDGKGVLSK QEFFVALRLV ACAQNGLEVS LSSLSLAVPP
110 120 130 140 150
PRFHDSSSPL LTSGPSVAEL PWAVKSEDKA KYDAIFDSLS PVDGFLSGDK
160 170 180 190 200
VKPVLLNSKL PVEILGRVWE LSDIDHDGKL DRDEFAVAMF LVYCALEKEP
210 220 230 240 250
VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD GYVSGLEVRE
260 270 280 290 300
TFLKTGLPSA LLAHIWSLCD TKGCGKLSKD QFALAFHLIN QKLIKGIDPP
310 320 330 340 350
HSLTPEMIPP SDRSSLQKNI TGSSPVADFS AIKELDTLNN EIVDLQREKN
360 370 380 390 400
NVEQDLKEKE DTVKQRTSEV QDLQDEVQRE SINLQKLQAQ KQQVQELLGE
410 420 430 440 450
LDEQKAQLEE QLQEVRKKCA EEAQLISSLK AEITSQESQI SSYEEELLKA
460 470 480 490 500
REELSRLQQE TAQLEESVES GKAQLEPLQQ HLQESQQEIS SMQMRLEMKD
510 520 530 540 550
LETDNNQSNW SSSPQSVLVN GATDYCSLST SSSETANFNE HAEGQNNLES
560 570 580 590 600
EPTHQESSVR SSPEIAPSDV TDESEAVTVA GNEKVTPRFD DDKHSKEEDP
610 620 630 640 650
FNVESSSLTD AVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS
660 670 680 690 700
DPFASDCFFK QTSTDPFTTS STDPFSASSN SSNTSVETWK HNDPFAPGGT
710 720 730 740 750
VVAAASDSAT DPFASVFGNE SFGDGFADFS TLSKVNNEDA FNPTISSSTS
760 770 780 790 800
SVTIAKPMLE ETASKSEDVP PALPPKVGTP TRPCPPPPGK RPINKLDSSD
810 820 830 840 850
PLKLNDPFQP FPGNDSPKEK DPDMFCDPFT SSTTTNKEAD PSNFANFSAY
860 870 880 890
PSEEDMIEWA KRESEREEEQ RLARLNQQEQ EDLELAIALS KSEISEA
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:
     1-314: Missing.
     315-346: SLQKNITGSSPVADFSAIKELDTLNNEIVDLQ → MYSDSGLGGWIAIPAVADVLRYSCIVCWSS

Show »
Length:581
Mass (Da):64,071
Checksum:i9209CDDDB4446D1C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 314314Missing in isoform 2. 1 PublicationVSP_036170Add
BLAST
Alternative sequencei315 – 34632SLQKN…IVDLQ → MYSDSGLGGWIAIPAVADVL RYSCIVCWSS in isoform 2. 1 PublicationVSP_036171Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENSMUST00000102729; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP42567.

Proteomic databases

MaxQBiP42567.
PaxDbiP42567.
PRIDEiP42567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102729; ENSMUSP00000099790; ENSMUSG00000028552. [P42567-1]
GeneIDi13858.
KEGGimmu:13858.
UCSCiuc008ucf.2. mouse. [P42567-1]
uc008ucg.2. mouse. [P42567-2]

Organism-specific databases

CTDi2060.
MGIiMGI:104583. Eps15.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_350802. EGFR downregulation.

Miscellaneous databases

EvolutionaryTraceiP42567.
NextBioi284734.
PROiP42567.
SOURCEiSearch...

Gene expression databases

BgeeiP42567.
ExpressionAtlasiP42567. baseline and differential.
GenevestigatoriP42567.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 151 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

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.