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Q60902 (EP15R_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor substrate 15-like 1
Alternative name(s):
Epidermal growth factor receptor pathway substrate 15-related sequence
Short name=Eps15-rs
Eps15-related protein
Short name=Eps15R
Gene names
Name:Eps15l1
Synonyms:Eps15-rs, Eps15R
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. 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 By similarity.

Subunit structure

Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates with the clathrin-associated adapter protein complex 2 (AP-2). Interacts with FCHO1 By similarity. Interacts with FCHO2. Interacts (via EH domains) with DAB2. Ref.5 Ref.11 Ref.12

Subcellular location

Cell membrane; Peripheral membrane protein. Nucleus. Membranecoated pit. Note: Localized to plasma membrane coated pits. Ref.5

Post-translational modification

Phosphorylated on tyrosine residues by EGFR. Ref.5

Sequence similarities

Contains 1 EF-hand domain.

Contains 3 EH domains.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Coated pit
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandCalcium
Metal-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcoated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q60902-1)

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: Q60902-2)

The sequence of this isoform differs from the canonical sequence as follows:
     794-819: STPVSQLGSSDFPESPDPFQPLGADS → YASSSRGTRRWGQGGGHRAPPLSSPE
     820-907: Missing.
Isoform 3 (identifier: Q60902-3)

The sequence of this isoform differs from the canonical sequence as follows:
     596-599: DDPF → VKVE
     600-819: Missing.
Isoform 4 (identifier: Q60902-4)

The sequence of this isoform differs from the canonical sequence as follows:
     565-595: Missing.
     748-860: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 907907Epidermal growth factor receptor substrate 15-like 1
PRO_0000146119

Regions

Domain15 – 10490EH 1
Domain127 – 21589EH 2
Domain159 – 19436EF-hand
Domain273 – 36391EH 3
Repeat863 – 88220UIM 1
Repeat889 – 90719UIM 2
Calcium binding172 – 18312 Potential
Region15 – 368354Interaction with DAB2
Compositional bias748 – 848101Pro-rich

Amino acid modifications

Modified residue91Phosphoserine Ref.10
Modified residue301Phosphotyrosine Ref.10
Modified residue311Phosphothreonine Ref.10
Modified residue741Phosphotyrosine Ref.6
Modified residue2291Phosphoserine Ref.7
Modified residue2381Phosphoserine Ref.10
Modified residue2441Phosphoserine Ref.8
Modified residue2501Phosphoserine Ref.8
Modified residue2551Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue3531Phosphoserine Ref.7
Modified residue3641Phosphothreonine Ref.7
Modified residue5581Phosphoserine By similarity
Modified residue7951Phosphothreonine By similarity

Natural variations

Alternative sequence565 – 59531Missing in isoform 4.
VSP_022638
Alternative sequence596 – 5994DDPF → VKVE in isoform 3.
VSP_010681
Alternative sequence600 – 819220Missing in isoform 3.
VSP_010682
Alternative sequence748 – 860113Missing in isoform 4.
VSP_022639
Alternative sequence794 – 81926STPVS…LGADS → YASSSRGTRRWGQGGGHRAP PLSSPE in isoform 2.
VSP_010683
Alternative sequence820 – 90788Missing in isoform 2.
VSP_010684

Experimental info

Sequence conflict141G → S in AAA87202. Ref.1
Sequence conflict141G → S in AAH15259. Ref.4
Sequence conflict291A → P in AAA87202. Ref.1
Sequence conflict1701L → V in BAE31350. Ref.2
Sequence conflict4131R → K in AAA87202. Ref.1
Sequence conflict4131R → K in AAH15259. Ref.4
Sequence conflict7261D → H in BAC29523. Ref.2
Sequence conflict8211D → E in AAA87202. Ref.1
Sequence conflict8501T → A in AAA87202. Ref.1

Sequences

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

Last modified July 27, 2011. Version 3.
Checksum: B5AF1A89B445E8A7

FASTA90799,309
        10         20         30         40         50         60 
MAAPLVPLSQ QIPGGNPLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA 

        70         80         90        100        110        120 
DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSSLSLTMPP PKFHDTSSPL MATQSSAETH 

       130        140        150        160        170        180 
WAVRVEEKAK FDGIFESLLP VNGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD 

       190        200        210        220        230        240 
RDEFAVAMHL VYRALEKEPV PSILPPPLIP PSKRKKTVFA GAVPVLPASP PPKDSLRSTP 

       250        260        270        280        290        300 
SHGSVSSLNS TGSLSPKHSV KQPPVAWVVP VADKMRFDEI FLKTDLDLDG YVSGQEVKEI 

       310        320        330        340        350        360 
FMHSGLTQNL LAHIWALADT RQTGKLSKEQ FALAMYFIQQ KVSKGIDPPQ VLSPDMVPPS 

       370        380        390        400        410        420 
ERGTPIPDSS STLASGEFTG VKELDDISQE IAQLQREKYS LEQDIREKEE AIRQKTSEVQ 

       430        440        450        460        470        480 
ELQNDLDRET SSLQELEAQK QDAQDRLDEM DQQKAKLRDM LSDVRQKCQD ETQTISSLKT 

       490        500        510        520        530        540 
QIQSQESDLK SQEDDLNRAK SELNRLQQEE TQLEQSIQAG RAQLETILRS LKCTQDDINQ 

       550        560        570        580        590        600 
ARSKLSQLQE SHLEAHRSLE QYDQVPDGVS GTSLPDLATL NEGILLAERG GFGAMDDPFK 

       610        620        630        640        650        660 
NKALLFSNNS QELHPDPFQA EDPFKSDPFK GADPFKGDPF QSDPFSEQQT AATDPFGGDP 

       670        680        690        700        710        720 
FKESDPFHSS SSDDFFKKQT KNDPFTSDPF TKNPSLPSKL DPFESSDPFS SSSISSKGSD 

       730        740        750        760        770        780 
PFGTLDPFGS SSFSSAEGFA DFSQMSKPPP SGPFSSSLGG TGFSDDPFKS KQDTPALPPK 

       790        800        810        820        830        840 
KPAPPRPKPP SGQSTPVSQL GSSDFPESPD PFQPLGADSG DPFQNKKGFG DPFSGKDPFA 

       850        860        870        880        890        900 
PSSSAKPPKT SSSGFADFTS FGNEEQQLAW AKRESEKAEQ ERLARLRRQE QEDLELAIAL 


SKADMPA 

« Hide

Isoform 2 [UniParc].

Checksum: D46667729E593945
Show »

FASTA81989,728
Isoform 3 [UniParc].

Checksum: F30E20D19F47A4DA
Show »

FASTA68775,877
Isoform 4 [UniParc].

Checksum: 1739157C3A8045B5
Show »

FASTA76384,752

References

« Hide 'large scale' references
[1]"A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution."
Wong W.T., Schumacher C., Salcini A.E., Romano A., Castagnino P., Pelicci P.G., Di Fiore P.
Proc. Natl. Acad. Sci. U.S.A. 92:9530-9534(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[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. expand/collapse author list , 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] (ISOFORMS 2; 3 AND 4).
Strain: C57BL/6J.
Tissue: Bone, Bone marrow and Kidney.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 3).
Tissue: Kidney.
[5]"Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization."
Coda L., Salcini A.E., Confalonieri S., Pelicci G., Sorkina T., Sorkin A., Pelicci P.G., Di Fiore P.P.
J. Biol. Chem. 273:3003-3012(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH EPS15; AP-2 COMPLEX; AGFG1 AND AGFG2.
[6]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, MASS SPECTROMETRY.
Tissue: Brain.
[7]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-353 AND THR-364, MASS SPECTROMETRY.
Tissue: Brain cortex.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-250 AND SER-255, MASS SPECTROMETRY.
Tissue: Liver.
[9]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY.
Tissue: Melanoma.
[10]"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-9; TYR-30; THR-31; SER-238 AND SER-255, MASS SPECTROMETRY.
Tissue: Macrophage.
[11]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29156 mRNA. Translation: AAA87202.1.
AK036662 mRNA. Translation: BAC29523.1.
AK036728 mRNA. Translation: BAC29554.1.
AK146781 mRNA. Translation: BAE27427.1.
AK152602 mRNA. Translation: BAE31350.1.
CH466525 Genomic DNA. Translation: EDL10796.1.
BC015259 mRNA. Translation: AAH15259.1.
IPIIPI00420185.
IPI00420186.
IPI00420187.
IPI00653328.
RefSeqNP_001116304.1. NM_001122832.1.
NP_031970.2. NM_007944.3.
UniGeneMm.288894.

3D structure databases

ProteinModelPortalQ60902.
SMRQ60902. Positions 11-105, 121-214, 267-360.
ModBaseSearch...

Protein-protein interaction databases

IntActQ60902. 4 interactions.
MINTMINT-234466.

PTM databases

PhosphoSiteQ60902.

Proteomic databases

PaxDbQ60902.
PRIDEQ60902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163643; ENSMUSP00000129739; ENSMUSG00000006276.
GeneID13859.
KEGGmmu:13859.
UCSCuc009mfs.2. mouse.

Organism-specific databases

CTD58513.
MGIMGI:104582. Eps15l1.

Phylogenomic databases

eggNOGNOG301764.
GeneTreeENSGT00700000104202.
HOGENOMHOG000004804.
HOVERGENHBG005591.
InParanoidQ3UIS9.
OMAMDDPFKN.
OrthoDBEOG4JM7P3.

Gene expression databases

BgeeQ60902.
GenevestigatorQ60902.
GermOnlineENSMUSG00000006276. Mus musculus.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. EF-hand-like_dom.
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. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPS15L1. mouse.
NextBio284738.
SOURCESearch...

Entry information

Entry nameEP15R_MOUSE
AccessionPrimary (citable) accession number: Q60902
Secondary accession number(s): Q3U7L9 expand/collapse secondary AC list , Q3UIS9, Q8CB60, Q8CB70, Q91WH8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families