ID ES8L2_HUMAN Reviewed; 715 AA. AC Q9H6S3; B3KSX1; B7ZKL3; Q53GM8; Q8WYW7; Q96K06; Q9H6K9; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 2; DE Short=EPS8-like protein 2; DE AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 2; DE Short=EPS8-related protein 2; GN Name=EPS8L2; Synonyms=EPS8R2; ORFNames=PP13181; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] (ISOFORM 2). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain cortex, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Prostate; 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 [7] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, INTERACTION WITH RP ABI1, SUBCELLULAR LOCATION, AND 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-469 AND SER-570, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-570, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP STRUCTURE BY NMR OF 495-549. RG RIKEN structural genomics initiative (RSGI); RT "solution structure of the SH3 domain from human epidermal growth factor RT receptor pathway substrate 8-like protein."; RL Submitted (JUL-2005) to the PDB data bank. RN [16] RP INVOLVEMENT IN DFNB106. RX PubMed=26282398; DOI=10.1186/s13023-015-0316-8; RA Dahmani M., Ammar-Khodja F., Bonnet C., Lefevre G.M., Hardelin J.P., RA Ibrahim H., Mallek Z., Petit C.; RT "EPS8L2 is a new causal gene for childhood onset autosomal recessive RT progressive hearing loss."; RL Orphanet J. Rare Dis. 10:96-96(2015). RN [17] RP INVOLVEMENT IN DFNB106. RX PubMed=28281779; DOI=10.1089/gtmb.2016.0328; RA Wang R., Han S., Khan A., Zhang X.; RT "Molecular Analysis of Twelve Pakistani Families with Nonsyndromic or RT Syndromic Hearing Loss."; RL Genet. Test. Mol. Biomarkers 21:316-321(2017). CC -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role CC in membrane ruffling and remodeling of the actin cytoskeleton. In the CC cochlea, is required for stereocilia maintenance in adult hair cells CC (By similarity). {ECO:0000250|UniProtKB:Q99K30, CC ECO:0000269|PubMed:14565974}. CC -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1, CC ABI1 and EPS8L2. Associates with F-actin. CC {ECO:0000269|PubMed:14565974}. CC -!- INTERACTION: CC Q9H6S3; P07339: CTSD; NbExp=3; IntAct=EBI-3940939, EBI-2115097; CC Q9H6S3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3940939, EBI-10976677; CC Q9H6S3; P28799: GRN; NbExp=3; IntAct=EBI-3940939, EBI-747754; CC Q9H6S3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-3940939, EBI-10975473; CC Q9H6S3; P07196: NEFL; NbExp=3; IntAct=EBI-3940939, EBI-475646; CC Q9H6S3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3940939, EBI-5235340; CC Q9H6S3; O76024: WFS1; NbExp=3; IntAct=EBI-3940939, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565974}. Cell CC projection, stereocilium {ECO:0000250|UniProtKB:Q99K30}. Note=Localizes CC at the tips of the stereocilia of the inner and outer hair cells. CC {ECO:0000250|UniProtKB:Q99K30}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H6S3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H6S3-2; Sequence=VSP_019092; CC Name=3; CC IsoId=Q9H6S3-3; Sequence=VSP_054144; CC -!- TISSUE SPECIFICITY: Detected in fibroblasts and placenta. CC {ECO:0000269|PubMed:14565974}. CC -!- DISEASE: Deafness, autosomal recessive, 106 (DFNB106) [MIM:617637]: A CC form of non-syndromic sensorineural hearing loss. Sensorineural CC deafness results from damage to the neural receptors of the inner ear, CC the nerve pathways to the brain, or the area of the brain that receives CC sound information. {ECO:0000269|PubMed:26282398, CC ECO:0000269|PubMed:28281779}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL55838.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB15180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY074929; AAL76118.1; -; mRNA. DR EMBL; AF318331; AAL55838.1; ALT_FRAME; mRNA. DR EMBL; AK025588; BAB15180.1; ALT_INIT; mRNA. DR EMBL; AK025824; BAB15248.1; -; mRNA. DR EMBL; AK027765; BAB55354.1; -; mRNA. DR EMBL; AK094539; BAG52883.1; -; mRNA. DR EMBL; AK222903; BAD96623.1; -; mRNA. DR EMBL; BC080636; AAH80636.1; -; mRNA. DR EMBL; BC093878; AAH93878.1; -; mRNA. DR EMBL; BC101481; AAI01482.1; -; mRNA. DR EMBL; BC143242; AAI43243.1; -; mRNA. DR EMBL; AC131934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS31328.1; -. [Q9H6S3-1] DR RefSeq; NP_073609.2; NM_022772.3. [Q9H6S3-1] DR RefSeq; XP_016873619.1; XM_017018130.1. DR RefSeq; XP_016873620.1; XM_017018131.1. DR RefSeq; XP_016873621.1; XM_017018132.1. [Q9H6S3-1] DR PDB; 1WWU; NMR; -; A=612-697. DR PDB; 1WXB; NMR; -; A=495-549. DR PDBsum; 1WWU; -. DR PDBsum; 1WXB; -. DR AlphaFoldDB; Q9H6S3; -. DR SMR; Q9H6S3; -. DR BioGRID; 122297; 61. DR CORUM; Q9H6S3; -. DR IntAct; Q9H6S3; 22. DR MINT; Q9H6S3; -. DR STRING; 9606.ENSP00000435585; -. DR GlyCosmos; Q9H6S3; 1 site, 1 glycan. DR GlyGen; Q9H6S3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H6S3; -. DR MetOSite; Q9H6S3; -. DR PhosphoSitePlus; Q9H6S3; -. DR SwissPalm; Q9H6S3; -. DR BioMuta; EPS8L2; -. DR DMDM; 108864726; -. DR EPD; Q9H6S3; -. DR jPOST; Q9H6S3; -. DR MassIVE; Q9H6S3; -. DR MaxQB; Q9H6S3; -. DR PaxDb; 9606-ENSP00000435585; -. DR PeptideAtlas; Q9H6S3; -. DR ProteomicsDB; 7181; -. DR ProteomicsDB; 81028; -. [Q9H6S3-1] DR ProteomicsDB; 81029; -. [Q9H6S3-2] DR Antibodypedia; 22613; 296 antibodies from 28 providers. DR DNASU; 64787; -. DR Ensembl; ENST00000318562.13; ENSP00000320828.8; ENSG00000177106.17. [Q9H6S3-1] DR Ensembl; ENST00000526198.5; ENSP00000436230.1; ENSG00000177106.17. [Q9H6S3-3] DR Ensembl; ENST00000530636.5; ENSP00000436035.1; ENSG00000177106.17. [Q9H6S3-1] DR Ensembl; ENST00000533256.5; ENSP00000435585.1; ENSG00000177106.17. [Q9H6S3-1] DR Ensembl; ENST00000614442.4; ENSP00000480201.1; ENSG00000177106.17. [Q9H6S3-3] DR GeneID; 64787; -. DR KEGG; hsa:64787; -. DR MANE-Select; ENST00000318562.13; ENSP00000320828.8; NM_022772.4; NP_073609.2. DR UCSC; uc001lqt.4; human. [Q9H6S3-1] DR AGR; HGNC:21296; -. DR CTD; 64787; -. DR DisGeNET; 64787; -. DR GeneCards; EPS8L2; -. DR HGNC; HGNC:21296; EPS8L2. DR HPA; ENSG00000177106; Tissue enhanced (esophagus). DR MalaCards; EPS8L2; -. DR MIM; 614988; gene. DR MIM; 617637; phenotype. DR neXtProt; NX_Q9H6S3; -. DR OpenTargets; ENSG00000177106; -. DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB. DR PharmGKB; PA134981048; -. DR VEuPathDB; HostDB:ENSG00000177106; -. DR eggNOG; KOG3557; Eukaryota. DR GeneTree; ENSGT00940000160990; -. DR HOGENOM; CLU_014510_0_0_1; -. DR InParanoid; Q9H6S3; -. DR OMA; ANQRYKG; -. DR OrthoDB; 2997036at2759; -. DR PhylomeDB; Q9H6S3; -. DR TreeFam; TF313069; -. DR PathwayCommons; Q9H6S3; -. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; Q9H6S3; -. DR BioGRID-ORCS; 64787; 28 hits in 1155 CRISPR screens. DR ChiTaRS; EPS8L2; human. DR EvolutionaryTrace; Q9H6S3; -. DR GeneWiki; EPS8L2; -. DR GenomeRNAi; 64787; -. DR Pharos; Q9H6S3; Tbio. DR PRO; PR:Q9H6S3; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9H6S3; Protein. DR Bgee; ENSG00000177106; Expressed in lower esophagus mucosa and 147 other cell types or tissues. DR ExpressionAtlas; Q9H6S3; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0032421; C:stereocilium bundle; ISS:UniProtKB. DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:1900029; P:positive regulation of ruffle assembly; IGI:UniProtKB. DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IDA:UniProtKB. DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR CDD; cd01210; PTB_EPS8; 1. DR CDD; cd09540; SAM_EPS8-like; 1. DR CDD; cd11764; SH3_Eps8; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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:SF20; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE 8-LIKE PROTEIN 2; 1. DR PANTHER; PTHR12287; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE EPS8-RELATED PROTEIN; 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; SSF50729; PH domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS01179; PID; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9H6S3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; Deafness; KW Non-syndromic deafness; Phosphoprotein; Reference proteome; SH3 domain. FT CHAIN 1..715 FT /note="Epidermal growth factor receptor kinase substrate 8- FT like protein 2" FT /id="PRO_0000239084" FT DOMAIN 46..202 FT /note="PID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148" FT DOMAIN 492..551 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 183..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..467 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 303 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99K30" FT MOD_RES 449 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336" FT MOD_RES 469 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 570 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..388 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15498874" FT /id="VSP_019092" FT VAR_SEQ 108 FT /note="S -> SQSAQTPGASRVRAMYP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054144" FT CONFLICT 146 FT /note="S -> N (in Ref. 4; BAD96623)" FT /evidence="ECO:0000305" FT CONFLICT 198 FT /note="I -> F (in Ref. 3; BAB15180)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="H -> R (in Ref. 3; BAB15180)" FT /evidence="ECO:0000305" FT CONFLICT 620 FT /note="V -> A (in Ref. 3; BAB15180)" FT /evidence="ECO:0000305" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:1WXB" FT STRAND 518..523 FT /evidence="ECO:0007829|PDB:1WXB" FT STRAND 525..532 FT /evidence="ECO:0007829|PDB:1WXB" FT STRAND 538..542 FT /evidence="ECO:0007829|PDB:1WXB" FT TURN 543..545 FT /evidence="ECO:0007829|PDB:1WXB" FT HELIX 630..640 FT /evidence="ECO:0007829|PDB:1WWU" FT HELIX 646..649 FT /evidence="ECO:0007829|PDB:1WWU" FT HELIX 655..659 FT /evidence="ECO:0007829|PDB:1WWU" FT HELIX 663..670 FT /evidence="ECO:0007829|PDB:1WWU" FT TURN 671..673 FT /evidence="ECO:0007829|PDB:1WWU" FT HELIX 674..689 FT /evidence="ECO:0007829|PDB:1WWU" SQ 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 //