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P42566 (EPS15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor substrate 15

Short name=Protein Eps15
Alternative name(s):
Protein AF-1p
Gene names
Name:EPS15
Synonyms:AF1P
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length896 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.20 Ref.27 Ref.35

Subunit structure

Interacts with SGIP1 By similarity. 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 with FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2. Interacts (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472'). Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.23 Ref.25 Ref.27 Ref.29 Ref.31

Subcellular location

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. Ref.15 Ref.35 Ref.36

Isoform 2: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Colocalizes with HGS on bilayered clathrin coats on endosomes. Ref.15 Ref.35 Ref.36

Tissue specificity

Ubiquitously expressed.

Domain

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. Ref.34

The UIM (ubiquitin-interacting motif) repeats specifically bind 'Lys-33'-linked ubiquitin (Ref.31). Ref.34

Post-translational modification

Phosphorylation on Tyr-849 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 similarity. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.

Involvement in disease

A chromosomal aberration involving EPS15 is found in acute leukemias. Translocation t(1;11)(p32;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Sequence similarities

Contains 2 EF-hand domains.

Contains 3 EH domains.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Caution

Studies in clathrin-mediated endocytosis of ITGB1 and TFR used a siRNA mixture of EPS15 and EPS15L1, and a Dab2 mutant with impaired binding to EH domain-containing proteins EPS15 and ITSN1 suggesting a partially overlapping role of the EH domain-containing proteins (Ref.27).

Ontologies

Keywords
   Biological processEndocytosis
Protein transport
Transport
   Cellular componentCell membrane
Coated pit
Cytoplasm
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
SH3-binding
   LigandCalcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Traceable author statement Ref.1. Source: ProtInc

clathrin coat assembly

Inferred from direct assay PubMed 12807910. Source: BHF-UCL

endocytic recycling

Inferred by curator PubMed 12807910. Source: BHF-UCL

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle organization

Traceable author statement PubMed 9762922. Source: UniProtKB

   Cellular_componentAP-2 adaptor complex

Inferred from electronic annotation. Source: Ensembl

ciliary membrane

Inferred from electronic annotation. Source: Ensembl

coated pit

Traceable author statement PubMed 9762922. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay PubMed 15465819. Source: HGNC

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 17082820PubMed 17474147Ref.36PubMed 19380743Ref.23Ref.25. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42566-1)

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.
Isoform 2 (identifier: P42566-2)

Also known as: Eps15b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-314: Missing.
     315-346: SLQKNIIGSSPVADFSAIKELDTLNNEIVDLQ → MYLKSDSGLGGWITIPAVADVLKYSCIVCWSS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 896895Epidermal growth factor receptor substrate 15
PRO_0000146116

Regions

Domain15 – 10490EH 1
Domain128 – 21689EH 2
Domain160 – 19536EF-hand 1
Domain223 – 25836EF-hand 2
Domain224 – 31491EH 3
Repeat599 – 60131
Repeat623 – 62532
Repeat629 – 63133
Repeat634 – 63634
Repeat640 – 64235
Repeat645 – 64736
Repeat651 – 65337
Repeat664 – 66638
Repeat672 – 67439
Repeat692 – 694310
Repeat709 – 711311
Repeat737 – 739312
Repeat798 – 800313
Repeat804 – 806314
Repeat825 – 827315
Repeat851 – 87020UIM 1
Repeat877 – 89620UIM 2
Calcium binding173 – 184121
Calcium binding236 – 247122
Region2 – 330329Interaction with DAB2 By similarity
Region599 – 82722915 X 3 AA repeats of D-P-F
Motif768 – 7747SH3-binding
Compositional bias768 – 85083Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.28 Ref.30
Modified residue1081Phosphoserine Ref.21
Modified residue1401Phosphoserine Ref.18
Modified residue3231Phosphoserine Ref.13 Ref.18 Ref.21
Modified residue3241Phosphoserine Ref.21 Ref.22 Ref.26
Modified residue4671Phosphoserine Ref.22
Modified residue4701Phosphoserine Ref.22
Modified residue4851Phosphoserine Ref.14 Ref.18 Ref.26
Modified residue7771Phosphothreonine By similarity
Modified residue7901Phosphoserine Ref.22 Ref.26
Modified residue7961Phosphoserine Ref.16 Ref.22 Ref.26
Modified residue8141Phosphoserine Ref.16 Ref.18 Ref.21 Ref.22 Ref.26
Modified residue8491Phosphotyrosine; by EGFR Ref.21

Natural variations

Alternative sequence1 – 314314Missing in isoform 2.
VSP_036168
Alternative sequence315 – 34632SLQKN…IVDLQ → MYLKSDSGLGGWITIPAVAD VLKYSCIVCWSS in isoform 2.
VSP_036169
Natural variant8221I → M. Ref.1
Corresponds to variant rs17567 [ dbSNP | Ensembl ].
VAR_016142

Experimental info

Mutagenesis1541V → E: Loss of interaction with STON2 NPF motifs. Ref.36
Mutagenesis1691W → A: Loss of interaction with STON2 NPF motifs. Ref.36
Sequence conflict4461Missing in BX647676. Ref.5

Secondary structure

................................... 896
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: A1B9FE15B47ABAFF

FASTA89698,656
        10         20         30         40         50         60 
MAAAAQLSLT QLSSGNPVYE KYYRQVDTGN TGRVLASDAA AFLKKSGLPD LILGKIWDLA 

        70         80         90        100        110        120 
DTDGKGILNK QEFFVALRLV ACAQNGLEVS LSSLNLAVPP PRFHDTSSPL LISGTSAAEL 

       130        140        150        160        170        180 
PWAVKPEDKA KYDAIFDSLS PVNGFLSGDK VKPVLLNSKL PVDILGRVWE LSDIDHDGML 

       190        200        210        220        230        240 
DRDEFAVAMF LVYCALEKEP VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD 

       250        260        270        280        290        300 
GFVSGLEVRE IFLKTGLPST LLAHIWSLCD TKDCGKLSKD QFALAFHLIS QKLIKGIDPP 

       310        320        330        340        350        360 
HVLTPEMIPP SDRASLQKNI IGSSPVADFS AIKELDTLNN EIVDLQREKN NVEQDLKEKE 

       370        380        390        400        410        420 
DTIKQRTSEV QDLQDEVQRE NTNLQKLQAQ KQQVQELLDE LDEQKAQLEE QLKEVRKKCA 

       430        440        450        460        470        480 
EEAQLISSLK AELTSQESQI STYEEELAKA REELSRLQQE TAELEESVES GKAQLEPLQQ 

       490        500        510        520        530        540 
HLQDSQQEIS SMQMKLMEMK DLENHNSQLN WCSSPHSILV NGATDYCSLS TSSSETANLN 

       550        560        570        580        590        600 
EHVEGQSNLE SEPIHQESPA RSSPELLPSG VTDENEVTTA VTEKVCSELD NNRHSKEEDP 

       610        620        630        640        650        660 
FNVDSSSLTG PVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS DPFASDCFFR 

       670        680        690        700        710        720 
QSTDPFATSS TDPFSAANNS SITSVETLKH NDPFAPGGTV VAASDSATDP FASVFGNESF 

       730        740        750        760        770        780 
GGGFADFSTL SKVNNEDPFR SATSSSVSNV VITKNVFEET SVKSEDEPPA LPPKIGTPTR 

       790        800        810        820        830        840 
PCPLPPGKRS INKLDSPDPF KLNDPFQPFP GNDSPKEKDP EIFCDPFTSA TTTTNKEADP 

       850        860        870        880        890 
SNFANFSAYP SEEDMIEWAK RESEREEEQR LARLNQQEQE DLELAIALSK SEISEA 

« Hide

Isoform 2 (Eps15b) [UniParc].

Checksum: 2A7BACA24604E8CA
Show »

FASTA58264,376

References

« Hide 'large scale' references
[1]"The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32."
Wong W.T., Kraus M.H., Carlomagno F., Zelano A., Druck T., Croce C.M., Huebner K., di Fiore P.P.
Oncogene 9:1591-1597(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-822.
Tissue: Melanoma.
[2]"A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL."
Bernard O.A., Mauchauffe M., Mecucci C., van den Berghe H., Berger R.
Oncogene 9:1039-1045(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Trachea.
[4]"Eps15 in human umbilical vein endothelial cells."
Kronstein R., Grossklaus S., Schnittler H.-J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins."
Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T.
J. Biol. Chem. 271:14468-14472(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRK.
[9]"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: INTERACTION WITH EPN1.
[10]"STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes."
Bache K.G., Raiborg C., Mehlum A., Stenmark H.
J. Biol. Chem. 278:12513-12521(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HGS AND STAM2.
[11]"TTP specifically regulates the internalization of the transferrin receptor."
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3BP4.
[12]"Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB2.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor."
Roxrud I., Raiborg C., Pedersen N.M., Stang E., Stenmark H.
J. Cell Biol. 180:1205-1218(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH HSG AND AP2A2.
[16]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-323; SER-485 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits."
Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G., Schmid S.L.
Mol. Biol. Cell 20:3251-3260(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324; SER-814 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-467; SER-470; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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.
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-485; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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: FUNCTION, INTERACTION WITH DAB2.
[28]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCHO1.
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
Mol. Cell 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CORO7.
[32]"Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain."
de Beer T., Carter R.E., Lobel-Rice K.E., Sorkin A., Overduin M.
Science 281:1357-1360(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH CALCIUM IONS.
[33]"Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites."
Enmon J.L., de Beer T., Overduin M.
Biochemistry 39:4309-4319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 217-311 IN COMPLEX WITH CALCIUM IONS.
[34]"Molecular mechanism of NPF recognition by EH domains."
de Beer T., Hoofnagle A.N., Enmon J.L., Bowers R.C., Yamabhai M., Kay B.K., Overduin M.
Nat. Struct. Biol. 7:1018-1022(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH PEPTIDE LIGAND AND CALCIUM IONS, DOMAIN.
[35]"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 719-730 IN COMPLEX WITH AP2B1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
[36]"Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity."
Rumpf J., Simon B., Jung N., Maritzen T., Haucke V., Sattler M., Groemping Y.
EMBO J. 27:558-569(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH STON2 AND CALCIUM IONS, MUTAGENESIS OF VAL-154 AND TRP-169, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07707 mRNA. Translation: AAA52101.1.
Z29064 mRNA. Translation: CAA82305.1.
AK313396 mRNA. Translation: BAG36194.1.
DQ367924 mRNA. Translation: ABD34786.1.
BX647676 mRNA. No translation available.
AL671986, AC104170 Genomic DNA. Translation: CAI13030.1.
CH471059 Genomic DNA. Translation: EAX06823.1.
CCDSCCDS557.1. [P42566-1]
PIRS43074.
RefSeqNP_001153441.1. NM_001159969.1. [P42566-2]
NP_001972.1. NM_001981.2. [P42566-1]
UniGeneHs.83722.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C07NMR-A217-311[»]
1EH2NMR-A121-218[»]
1F8HNMR-A121-215[»]
1FF1NMR-A121-215[»]
2IV9X-ray1.90P723-730[»]
2JXCNMR-A121-215[»]
ProteinModelPortalP42566.
SMRP42566. Positions 7-105, 121-215, 217-311, 371-420, 448-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108374. 111 interactions.
DIPDIP-33064N.
IntActP42566. 39 interactions.
MINTMINT-107223.
STRING9606.ENSP00000360798.

PTM databases

PhosphoSiteP42566.

Polymorphism databases

DMDM67476728.

2D gel databases

OGPP42566.

Proteomic databases

MaxQBP42566.
PaxDbP42566.
PeptideAtlasP42566.
PRIDEP42566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371733; ENSP00000360798; ENSG00000085832. [P42566-1]
GeneID2060.
KEGGhsa:2060.
UCSCuc001csp.3. human. [P42566-2]
uc001csq.1. human. [P42566-1]

Organism-specific databases

CTD2060.
GeneCardsGC01M051819.
HGNCHGNC:3419. EPS15.
HPACAB010164.
HPA008451.
MIM600051. gene.
neXtProtNX_P42566.
PharmGKBPA27838.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301764.
HOGENOMHOG000004804.
HOVERGENHBG005591.
InParanoidP42566.
KOK12472.
OMAPPPRFHD.
PhylomeDBP42566.
TreeFamTF324293.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP42566.

Gene expression databases

ArrayExpressP42566.
BgeeP42566.
CleanExHS_EPS15.
GenevestigatorP42566.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPS15. human.
EvolutionaryTraceP42566.
GeneWikiEPS15.
GenomeRNAi2060.
NextBio8377.
PROP42566.
SOURCESearch...

Entry information

Entry nameEPS15_HUMAN
AccessionPrimary (citable) accession number: P42566
Secondary accession number(s): B2R8J7, D3DPJ2, Q5SRH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM