LOCUS       NP_031970                907 aa            linear   ROD 30-APR-2024
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform a [Mus
            musculus].
ACCESSION   NP_031970
VERSION     NP_031970.2
DBSOURCE    REFSEQ: accession NM_007944.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Milesi,C., Alberici,P., Pozzi,B., Oldani,A., Beznoussenko,G.V.,
            Raimondi,A., Soppo,B.E., Amodio,S., Caldieri,G., Malabarba,M.G.,
            Bertalot,G., Confalonieri,S., Parazzoli,D., Mironov,A.A.,
            Tacchetti,C., Di Fiore,P.P., Sigismund,S. and Offenhauser,N.
  TITLE     Redundant and nonredundant organismal functions of EPS15 and
            EPS15L1
  JOURNAL   Life Sci Alliance 2 (1), e201800273 (2019)
   PUBMED   30692166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Evergren,E., Cobbe,N. and McMahon,H.T.
  TITLE     Eps15R and clathrin regulate EphB2-mediated cell repulsion
  JOURNAL   Traffic 19 (1), 44-57 (2018)
   PUBMED   28972287
  REMARK    GeneRIF: A novel interaction motif in Eps15R, DPFxxLDPF, is shown
            to bind directly to the clathrin terminal domain in vitro.
            Interaction between Eps15R and clathrin is required for
            EphB2-mediated cell repulsion.
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Teckchandani,A., Mulkearns,E.E., Randolph,T.W., Toida,N. and
            Cooper,J.A.
  TITLE     The clathrin adaptor Dab2 recruits EH domain scaffold proteins to
            regulate integrin beta1 endocytosis
  JOURNAL   Mol Biol Cell 23 (15), 2905-2916 (2012)
   PUBMED   22648170
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Polo,S., Sigismund,S., Faretta,M., Guidi,M., Capua,M.R., Bossi,G.,
            Chen,H., De Camilli,P. and Di Fiore,P.P.
  TITLE     A single motif responsible for ubiquitin recognition and
            monoubiquitination in endocytic proteins
  JOURNAL   Nature 416 (6879), 451-455 (2002)
   PUBMED   11919637
  REMARK    GeneRIF: a short amino-acid stretch at the carboxy-termini of the
            monoubiquitinated endocytic proteins Eps15 and eps15R is
            indispensable for their monoubiquitination
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Offenhauser,N., Santolini,E., Simeone,A. and Di Fiore,P.P.
  TITLE     Differential patterns of expression of Eps15 and Eps15R during
            mouse embryogenesis
  JOURNAL   Mech Dev 95 (1-2), 309-312 (2000)
   PUBMED   10906484
REFERENCE   8  (residues 1 to 907)
  AUTHORS   Coda,L., Salcini,A.E., Confalonieri,S., Pelicci,G., Sorkina,T.,
            Sorkin,A., Pelicci,P.G. and Di Fiore,P.P.
  TITLE     Eps15R is a tyrosine kinase substrate with characteristics of a
            docking protein possibly involved in coated pits-mediated
            internalization
  JOURNAL   J Biol Chem 273 (5), 3003-3012 (1998)
   PUBMED   9446614
REFERENCE   9  (residues 1 to 907)
  AUTHORS   Wong,W.T., Schumacher,C., Salcini,A.E., Romano,A., Castagnino,P.,
            Pelicci,P.G. and Di Fiore,P.P.
  TITLE     A protein-binding domain, EH, identified in the receptor tyrosine
            kinase substrate Eps15 and conserved in evolution
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9530-9534 (1995)
   PUBMED   7568168
REFERENCE   10 (residues 1 to 907)
  AUTHORS   Schumacher,C., Knudsen,B.S., Ohuchi,T., Di Fiore,P.P.,
            Glassman,R.H. and Hanafusa,H.
  TITLE     The SH3 domain of Crk binds specifically to a conserved
            proline-rich motif in Eps15 and Eps15R
  JOURNAL   J Biol Chem 270 (25), 15341-15347 (1995)
   PUBMED   7797522
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY270130.1, AK146781.1 and CD774936.1.
            
            On Mar 26, 2008 this sequence version replaced NP_031970.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK146781.1, U29156.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 35.02 cM"
     Protein         1..907
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform a"
                     /note="eps15-related protein; epidermal growth factor
                     receptor pathway substrate 15-related sequence"
                     /calculated_mol_wt=99178
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Region          13..103
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          15..368
                     /region_name="Interaction with DAB2.
                     /evidence=ECO:0000269|PubMed:22648170"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60902.3)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Region          121..200
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          229..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60902.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Region          266..362
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Region          363..>594
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Region          611..860
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60902.3)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC2; propagated from
                     UniProtKB/Swiss-Prot (Q60902.3)"
     CDS             1..907
                     /gene="Eps15l1"
                     /gene_synonym="9830147J04Rik; Eps15-rs; Eps15R"
                     /coded_by="NM_007944.3:38..2761"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS52597.1"
                     /db_xref="GeneID:13859"
                     /db_xref="MGI:MGI:104582"
ORIGIN      
        1 maaplvplsq qipggnplye syykqvdpay tgrvgaseaa lflkksglsd iilgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsslsltmpp pkfhdtsspl matqssaeth
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psilppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqppvawvvp vadkmrfdei flktdldldg yvsgqevkei
      301 fmhsgltqnl lahiwaladt rqtgklskeq falamyfiqq kvskgidppq vlspdmvpps
      361 ergtpipdss stlasgeftg vkelddisqe iaqlqrekys leqdirekee airqktsevq
      421 elqndldret sslqeleaqk qdaqdrldem dqqkaklrdm lsdvrqkcqd etqtisslkt
      481 qiqsqesdlk sqeddlnrak selnrlqqee tqleqsiqag raqletilrs lkctqddinq
      541 arsklsqlqe shleahrsle qydqvpdgvs gtslpdlatl negillaerg gfgamddpfk
      601 nkallfsnns qelhpdpfqa edpfksdpfk gadpfkgdpf qsdpfseqqt aatdpfggdp
      661 fkesdpfhss ssddffkkqt kndpftsdpf tknpslpskl dpfessdpfs sssisskgsd
      721 pfgtldpfgs ssfssaegfa dfsqmskppp sgpfssslgg tgfsddpfks kqdtpalppk
      781 kpapprpkpp sgqstpvsql gssdfpespd pfqplgadsg dpfqnkkgfg dpfsgkdpfa
      841 psssakppkt sssgfadfts fgneeqqlaw akresekaeq erlarlrrqe qedlelaial
      901 skadmpa
//
