ES8L1_MOUSE
ID ES8L1_MOUSE Reviewed; 716 AA.
AC Q8R5F8; Q8R0D6; Q9D2M6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 1;
DE Short=EPS8-like protein 1;
DE AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 1;
DE Short=EPS8-related protein 1;
GN Name=Eps8l1; Synonyms=Eps8r1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12620401; DOI=10.1016/s0888-7543(03)00002-8;
RA Tocchetti A., Confalonieri S., Scita G., Di Fiore P.P., Betsholtz C.;
RT "In silico analysis of the EPS8 gene family: genomic organization,
RT expression profile, and protein structure.";
RL Genomics 81:234-244(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14565974; DOI=10.1091/mbc.e03-06-0427;
RA Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I.,
RA Iannolo G., Di Fiore P.P., Scita G.;
RT "The eps8 family of proteins links growth factor stimulation to actin
RT reorganization generating functional redundancy in the Ras/Rac pathway.";
RL Mol. Biol. Cell 15:91-98(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role
CC in membrane ruffling and remodeling of the actin cytoskeleton (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1,
CC ABI1 and EPS8L2. Associates with F-actin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in placenta, skin, mammary gland, bone
CC marrow and stomach. {ECO:0000269|PubMed:14565974}.
CC -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC027043; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY074931; AAL76120.1; -; mRNA.
DR EMBL; AK019490; BAB31756.2; -; mRNA.
DR EMBL; BC027043; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS20736.1; -.
DR RefSeq; NP_001277345.1; NM_001290416.1.
DR RefSeq; NP_080422.1; NM_026146.4.
DR RefSeq; XP_006540387.1; XM_006540324.3.
DR RefSeq; XP_006540388.1; XM_006540325.3.
DR RefSeq; XP_006540389.1; XM_006540326.1.
DR RefSeq; XP_017167747.1; XM_017312258.1.
DR PDB; 2CY4; X-ray; 1.94 A; A=26-165.
DR PDB; 2CY5; X-ray; 1.90 A; A=26-165.
DR PDBsum; 2CY4; -.
DR PDBsum; 2CY5; -.
DR AlphaFoldDB; Q8R5F8; -.
DR SMR; Q8R5F8; -.
DR BioGRID; 212177; 1.
DR STRING; 10090.ENSMUSP00000083559; -.
DR iPTMnet; Q8R5F8; -.
DR PhosphoSitePlus; Q8R5F8; -.
DR MaxQB; Q8R5F8; -.
DR PaxDb; Q8R5F8; -.
DR PRIDE; Q8R5F8; -.
DR ProteomicsDB; 275947; -.
DR Antibodypedia; 19481; 159 antibodies from 24 providers.
DR DNASU; 67425; -.
DR Ensembl; ENSMUST00000086372; ENSMUSP00000083559; ENSMUSG00000006154.
DR Ensembl; ENSMUST00000163893; ENSMUSP00000125840; ENSMUSG00000006154.
DR GeneID; 67425; -.
DR KEGG; mmu:67425; -.
DR UCSC; uc009exo.2; mouse.
DR CTD; 54869; -.
DR MGI; MGI:1914675; Eps8l1.
DR VEuPathDB; HostDB:ENSMUSG00000006154; -.
DR eggNOG; KOG3557; Eukaryota.
DR GeneTree; ENSGT00940000158125; -.
DR HOGENOM; CLU_014510_0_0_1; -.
DR InParanoid; Q8R5F8; -.
DR OMA; SEVRRPH; -.
DR PhylomeDB; Q8R5F8; -.
DR TreeFam; TF313069; -.
DR BioGRID-ORCS; 67425; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q8R5F8; -.
DR PRO; PR:Q8R5F8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R5F8; protein.
DR Bgee; ENSMUSG00000006154; Expressed in esophagus and 110 other tissues.
DR ExpressionAtlas; Q8R5F8; baseline and differential.
DR Genevisible; Q8R5F8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISA:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR CDD; cd01210; PTB_EPS8; 1.
DR CDD; cd11764; SH3_Eps8; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039801; EPS8-like.
DR InterPro; IPR033928; EPS8_PTB.
DR InterPro; IPR035462; Eps8_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12287; PTHR12287; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF18016; SAM_3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..716
FT /note="Epidermal growth factor receptor kinase substrate 8-
FT like protein 1"
FT /id="PRO_0000239083"
FT DOMAIN 477..536
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 682..713
FT /evidence="ECO:0000255"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 464
FT /note="Missing (in Ref. 3; BC027043)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="R -> S (in Ref. 3; BC027043)"
FT /evidence="ECO:0000305"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2CY4"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2CY5"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2CY5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2CY5"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2CY5"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2CY4"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:2CY5"
SQ SEQUENCE 716 AA; 80028 MW; E996E664722E885D CRC64;
MSTTTGPEAA PKPSAKSIYE QRKRYSTVVM ADVSQYHVNH LVTFCLGEED GVHTVEDASR
KLAVMDSQGR VWAQEMLLRV SPSQVTLLDP VSKEELESYP LDAIVRCDAV MPRGRSRSLL
LLVCQEPERA QPDVHFFQGL LLGAELIRED IQGALQNYRS GRGERRAAAL RATQEELRRG
ASPAAETPPL QRRPSVRLVI NTVEPSAVRG RPQVESIPET EEARKPDQAR TTSSADPTSP
DLGPRGPELA GLQAERDVDI LNHVFDDVES FVSRLQKSAE ATRVLEHRER GRRTRRRAAG
EGLLTLRAKP PTEAEYTDVL QKIKYAFSLL ARLRGNIANP SSPELLHFLF GPLQMIVNTS
GGPEFAKSVR RPHLTLEAVT LLRDNVTPGE NELWTSLGDS WTCPGVELPP EEGSPYSPEF
YNGWEPPATD PQGRPWEDPV EKQLQHEKRR RQQSAPQVAV NGQQDPELET ESQLEEKARK
WVLCNYDFQA RNGSELSVKH RDVLEVLDDR RKWWKVRDHQ GQEGYVPYNI LTPHPGPQVH
RSQSPARHLE TSTPPPPPAP APAPTQVRPQ WDSCDSLNSL DPSEKEKFSQ MLCVNEELQS
RLAQGRSGPS RVTPGPRAQE PQLSPRSEAS VVRAWLQTKG FSSGTVEALG VLTGAQLFSL
QKEELRAVCP EEGARVYSQV TVQRALLEDR EKVSELEAVM EKQKKKVEGE TKTEVI
