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Epidermal growth factor receptor kinase substrate 8-like protein 2 (EPS8-like protein 2) (Epidermal growth factor receptor pathway substrate 8-related protein 2) (EPS8-related protein 2)

 ES8L2_HUMAN             Reviewed;         715 AA.
Q9H6S3; B3KSX1; B7ZKL3; Q53GM8; Q8WYW7; Q96K06; Q9H6K9;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 2.
05-DEC-2018, entry version 148.
RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 2;
Short=EPS8-like protein 2;
AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 2;
Short=EPS8-related protein 2;
Name=EPS8L2; Synonyms=EPS8R2; ORFNames=PP13181;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12620401; DOI=10.1016/S0888-7543(03)00002-8;
Tocchetti A., Confalonieri S., Scita G., Di Fiore P.P., Betsholtz C.;
"In silico analysis of the EPS8 gene family: genomic organization,
expression profile, and protein structure.";
Genomics 81:234-244(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain cortex, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, INTERACTION
WITH ABI1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=14565974; DOI=10.1091/mbc.E03-06-0427;
Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I.,
Iannolo G., Di Fiore P.P., Scita G.;
"The eps8 family of proteins links growth factor stimulation to actin
reorganization generating functional redundancy in the Ras/Rac
pathway.";
Mol. Biol. Cell 15:91-98(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-469 AND SER-570, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-570, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
STRUCTURE BY NMR OF 495-549.
RIKEN structural genomics initiative (RSGI);
"solution structure of the SH3 domain from human epidermal growth
factor receptor pathway substrate 8-like protein.";
Submitted (JUL-2005) to the PDB data bank.
[16]
INVOLVEMENT IN DFNB106.
PubMed=26282398; DOI=10.1186/s13023-015-0316-8;
Dahmani M., Ammar-Khodja F., Bonnet C., Lefevre G.M., Hardelin J.P.,
Ibrahim H., Mallek Z., Petit C.;
"EPS8L2 is a new causal gene for childhood onset autosomal recessive
progressive hearing loss.";
Orphanet J. Rare Dis. 10:96-96(2015).
[17]
INVOLVEMENT IN DFNB106.
PubMed=28281779; DOI=10.1089/gtmb.2016.0328;
Wang R., Han S., Khan A., Zhang X.;
"Molecular Analysis of Twelve Pakistani Families with Nonsyndromic or
Syndromic Hearing Loss.";
Genet. Test. Mol. Biomarkers 21:316-321(2017).
-!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a
role in membrane ruffling and remodeling of the actin
cytoskeleton. In the cochlea, is required for stereocilia
maintenance in adult hair cells (By similarity).
{ECO:0000250|UniProtKB:Q99K30, ECO:0000269|PubMed:14565974}.
-!- SUBUNIT: Interacts with ABI1. Part of a complex that contains
SOS1, ABI1 and EPS8L2. Associates with F-actin.
{ECO:0000269|PubMed:14565974}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565974}.
Cell projection, stereocilium {ECO:0000250|UniProtKB:Q99K30}.
Note=Localizes at the tips of the stereocilia of the inner and
outer hair cells. {ECO:0000250|UniProtKB:Q99K30}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H6S3-1; Sequence=Displayed;
Name=2;
IsoId=Q9H6S3-2; Sequence=VSP_019092;
Name=3;
IsoId=Q9H6S3-3; Sequence=VSP_054144;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in fibroblasts and placenta.
{ECO:0000269|PubMed:14565974}.
-!- DISEASE: Deafness, autosomal recessive, 106 (DFNB106)
[MIM:617637]: A form of non-syndromic sensorineural hearing loss.
Sensorineural deafness results from damage to the neural receptors
of the inner ear, the nerve pathways to the brain, or the area of
the brain that receives sound information.
{ECO:0000269|PubMed:26282398, ECO:0000269|PubMed:28281779}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL55838.1; Type=Frameshift; Positions=593; Evidence={ECO:0000305};
Sequence=BAB15180.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY074929; AAL76118.1; -; mRNA.
EMBL; AF318331; AAL55838.1; ALT_FRAME; mRNA.
EMBL; AK025588; BAB15180.1; ALT_INIT; mRNA.
EMBL; AK025824; BAB15248.1; -; mRNA.
EMBL; AK027765; BAB55354.1; -; mRNA.
EMBL; AK094539; BAG52883.1; -; mRNA.
EMBL; AK222903; BAD96623.1; -; mRNA.
EMBL; BC080636; AAH80636.1; -; mRNA.
EMBL; BC093878; AAH93878.1; -; mRNA.
EMBL; BC101481; AAI01482.1; -; mRNA.
EMBL; BC143242; AAI43243.1; -; mRNA.
EMBL; AC131934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS31328.1; -. [Q9H6S3-1]
RefSeq; NP_073609.2; NM_022772.3. [Q9H6S3-1]
RefSeq; XP_016873619.1; XM_017018130.1.
RefSeq; XP_016873620.1; XM_017018131.1. [Q9H6S3-1]
RefSeq; XP_016873621.1; XM_017018132.1. [Q9H6S3-1]
UniGene; Hs.55016; -.
PDB; 1WWU; NMR; -; A=612-697.
PDB; 1WXB; NMR; -; A=495-549.
PDBsum; 1WWU; -.
PDBsum; 1WXB; -.
ProteinModelPortal; Q9H6S3; -.
SMR; Q9H6S3; -.
BioGrid; 122297; 14.
CORUM; Q9H6S3; -.
IntAct; Q9H6S3; 10.
MINT; Q9H6S3; -.
STRING; 9606.ENSP00000320828; -.
iPTMnet; Q9H6S3; -.
PhosphoSitePlus; Q9H6S3; -.
BioMuta; EPS8L2; -.
DMDM; 108864726; -.
EPD; Q9H6S3; -.
MaxQB; Q9H6S3; -.
PaxDb; Q9H6S3; -.
PeptideAtlas; Q9H6S3; -.
PRIDE; Q9H6S3; -.
ProteomicsDB; 81028; -.
ProteomicsDB; 81029; -. [Q9H6S3-2]
Ensembl; ENST00000318562; ENSP00000320828; ENSG00000177106. [Q9H6S3-1]
Ensembl; ENST00000526198; ENSP00000436230; ENSG00000177106. [Q9H6S3-3]
Ensembl; ENST00000530636; ENSP00000436035; ENSG00000177106. [Q9H6S3-1]
Ensembl; ENST00000533256; ENSP00000435585; ENSG00000177106. [Q9H6S3-1]
Ensembl; ENST00000614442; ENSP00000480201; ENSG00000177106. [Q9H6S3-3]
GeneID; 64787; -.
KEGG; hsa:64787; -.
UCSC; uc001lqt.4; human. [Q9H6S3-1]
CTD; 64787; -.
EuPathDB; HostDB:ENSG00000177106.14; -.
GeneCards; EPS8L2; -.
HGNC; HGNC:21296; EPS8L2.
HPA; HPA041143; -.
MalaCards; EPS8L2; -.
MIM; 614988; gene.
MIM; 617637; phenotype.
neXtProt; NX_Q9H6S3; -.
OpenTargets; ENSG00000177106; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKB; PA134981048; -.
eggNOG; KOG3557; Eukaryota.
eggNOG; ENOG410XT9R; LUCA.
GeneTree; ENSGT00940000160990; -.
HOGENOM; HOG000060324; -.
HOVERGEN; HBG003090; -.
InParanoid; Q9H6S3; -.
KO; K17277; -.
OMA; NKQWWKL; -.
OrthoDB; EOG091G023T; -.
PhylomeDB; Q9H6S3; -.
TreeFam; TF313069; -.
ChiTaRS; EPS8L2; human.
EvolutionaryTrace; Q9H6S3; -.
GeneWiki; EPS8L2; -.
GenomeRNAi; 64787; -.
PRO; PR:Q9H6S3; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000177106; Expressed in 164 organ(s), highest expression level in lower esophagus mucosa.
CleanEx; HS_EPS8L2; -.
ExpressionAtlas; Q9H6S3; baseline and differential.
Genevisible; Q9H6S3; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0032421; C:stereocilium bundle; ISS:UniProtKB.
GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:1900029; P:positive regulation of ruffle assembly; IGI:UniProtKB.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
CDD; cd01210; PTB_EPS8; 1.
CDD; cd11764; SH3_Eps8; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR039801; EPS8-like.
InterPro; IPR033928; EPS8_PTB.
InterPro; IPR035462; Eps8_SH3.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR013625; PTB.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR12287; PTHR12287; 1.
Pfam; PF08416; PTB; 1.
Pfam; PF00018; SH3_1; 1.
SMART; SM00462; PTB; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS01179; PID; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection;
Complete proteome; Cytoplasm; Deafness; Non-syndromic deafness;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 715 Epidermal growth factor receptor kinase
substrate 8-like protein 2.
/FTId=PRO_0000239084.
DOMAIN 46 202 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 492 551 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 303 303 Phosphothreonine.
{ECO:0000250|UniProtKB:Q99K30}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 469 469 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 388 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15498874}.
/FTId=VSP_019092.
VAR_SEQ 108 108 S -> SQSAQTPGASRVRAMYP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054144.
CONFLICT 146 146 S -> N (in Ref. 4; BAD96623).
{ECO:0000305}.
CONFLICT 198 198 I -> F (in Ref. 3; BAB15180).
{ECO:0000305}.
CONFLICT 589 589 H -> R (in Ref. 3; BAB15180).
{ECO:0000305}.
CONFLICT 620 620 V -> A (in Ref. 3; BAB15180).
{ECO:0000305}.
STRAND 506 510 {ECO:0000244|PDB:1WXB}.
STRAND 518 523 {ECO:0000244|PDB:1WXB}.
STRAND 525 532 {ECO:0000244|PDB:1WXB}.
STRAND 538 542 {ECO:0000244|PDB:1WXB}.
TURN 543 545 {ECO:0000244|PDB:1WXB}.
HELIX 630 640 {ECO:0000244|PDB:1WWU}.
HELIX 646 649 {ECO:0000244|PDB:1WWU}.
HELIX 655 659 {ECO:0000244|PDB:1WWU}.
HELIX 663 670 {ECO:0000244|PDB:1WWU}.
TURN 671 673 {ECO:0000244|PDB:1WWU}.
HELIX 674 689 {ECO:0000244|PDB:1WWU}.
SEQUENCE 715 AA; 80621 MW; DAB07744B04CFEE2 CRC64;
MSQSGAVSCC PGATNGSLGR SDGVAKMSPK DLFEQRKKYS NSNVIMHETS QYHVQHLATF
IMDKSEAITS VDDAIRKLVQ LSSKEKIWTQ EMLLQVNDQS LRLLDIESQE ELEDFPLPTV
QRSQTVLNQL RYPSVLLLVC QDSEQSKPDV HFFHCDEVEA ELVHEDIESA LADCRLGKKM
RPQTLKGHQE KIRQRQSILP PPQGPAPIPF QHRGGDSPEA KNRVGPQVPL SEPGFRRRES
QEEPRAVLAQ KIEKETQILN CALDDIEWFV ARLQKAAEAF KQLNQRKKGK KKGKKAPAEG
VLTLRARPPS EGEFIDCFQK IKLAINLLAK LQKHIQNPSA AELVHFLFGP LDLIVNTCSG
PDIARSVSCP LLSRDAVDFL RGHLVPKEMS LWESLGESWM RPRSEWPREP QVPLYVPKFH
SGWEPPVDVL QEAPWEVEGL ASAPIEEVSP VSRQSIRNSQ KHSPTSEPTP PGDALPPVSS
PHTHRGYQPT PAMAKYVKIL YDFTARNANE LSVLKDEVLE VLEDGRQWWK LRSRSGQAGY
VPCNILGEAR PEDAGAPFEQ AGQKYWGPAS PTHKLPPSFP GNKDELMQHM DEVNDELIRK
ISNIRAQPQR HFRVERSQPV SQPLTYESGP DEVRAWLEAK AFSPRIVENL GILTGPQLFS
LNKEELKKVC GEEGVRVYSQ LTMQKAFLEK QQSGSELEEL MNKFHSMNQR RGEDS


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EIAAB13302 Epidermal growth factor receptor kinase substrate 8-like protein 3,Epidermal growth factor receptor pathway substrate 8-related protein 3,EPS8L3,EPS8-like protein 3,EPS8R3,EPS8-related protein 3,Homo
EIAAB13299 Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,Eps8l1,EPS8-like protein 1,Eps8r1,EPS8-related protein 1,Mouse
EIAAB13298 DRC3,Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,EPS8L1,EPS8-like protein 1,EPS8R1,EPS8-related protein 1,
18-003-43740 Epidermal growth factor receptor kinase substrate 8-like protein 1 - Epidermal growth factor receptor pathway substrate 8-related protein 1; EPS8-like protein 1 Polyclonal 0.1 mg Protein A
29-763 EPS8L1 a protein that is related to epidermal growth factor receptor pathway substrate 8 (EPS8), a substrate for the epidermal growth factor receptor. The function of this protein is unknown.This gene 0.1 mg
EIAAB13048 Epidermal growth factor receptor pathway substrate 15-related sequence,Epidermal growth factor receptor substrate 15-like 1,Eps15l1,Eps15R,Eps15R,Eps15-related protein,Eps15-rs,Eps15-rs,Mouse,Mus musc
EPS8 EPS15 Gene epidermal growth factor receptor pathway substrate 15
EPS8L2 EPS8 Gene epidermal growth factor receptor pathway substrate 8
CSB-EL007751MO Mouse Epidermal growth factor receptor kinase substrate 8(EPS8) ELISA kit 96T
EIAAB13144 Epidermal growth factor receptor kinase substrate 8,Eps8,Mouse,Mus musculus
CSB-EL007751HU Human Epidermal growth factor receptor kinase substrate 8(EPS8) ELISA kit 96T
CSB-EL007751MO Mouse Epidermal growth factor receptor kinase substrate 8(EPS8) ELISA kit SpeciesMouse 96T
EIAAB13143 Epidermal growth factor receptor kinase substrate 8,EPS8,Homo sapiens,Human
CSB-EL007751HU Human Epidermal growth factor receptor kinase substrate 8(EPS8) ELISA kit SpeciesHuman 96T
EPS8_MOUSE ELISA Kit FOR Epidermal growth factor receptor kinase substrate 8; organism: Mouse; gene name: Eps8 96T
CSB-EL007751MO Mouse epidermal growth factor receptor pathway substrate 8 (EPS8) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007751HU Human epidermal growth factor receptor pathway substrate 8 (EPS8) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB13047 Epidermal growth factor receptor substrate 15-like 1,EPS15L1,Eps15R,EPS15R,Eps15-related protein,Homo sapiens,Human
CSB-EL007754MO Mouse Epidermal growth factor receptor kinase substrate 8-like protein 3(EPS8L3) ELISA kit 96T
CSB-EL007752MO Mouse Epidermal growth factor receptor kinase substrate 8-like protein 1(EPS8L1) ELISA kit 96T
CSB-EL007752HU Human Epidermal growth factor receptor kinase substrate 8-like protein 1(EPS8L1) ELISA kit 96T
CSB-EL007753MO Mouse Epidermal growth factor receptor kinase substrate 8-like protein 2(EPS8L2) ELISA kit 96T


 

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