ES8L2_HUMAN
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 03-AUG-2022, entry version 170.
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};
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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. [Q9H6S3-1]
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; 46.
DR CORUM; Q9H6S3; -.
DR IntAct; Q9H6S3; 22.
DR MINT; Q9H6S3; -.
DR STRING; 9606.ENSP00000435585; -.
DR GlyGen; Q9H6S3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H6S3; -.
DR MetOSite; Q9H6S3; -.
DR PhosphoSitePlus; Q9H6S3; -.
DR BioMuta; EPS8L2; -.
DR DMDM; 108864726; -.
DR EPD; Q9H6S3; -.
DR jPOST; Q9H6S3; -.
DR MassIVE; Q9H6S3; -.
DR MaxQB; Q9H6S3; -.
DR PaxDb; Q9H6S3; -.
DR PeptideAtlas; Q9H6S3; -.
DR PRIDE; Q9H6S3; -.
DR ProteomicsDB; 7181; -.
DR ProteomicsDB; 81028; -. [Q9H6S3-1]
DR ProteomicsDB; 81029; -. [Q9H6S3-2]
DR Antibodypedia; 22613; 264 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 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; 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; YEPTPAM; -.
DR OrthoDB; 218804at2759; -.
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; 27 hits in 1077 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 145 other tissues.
DR ExpressionAtlas; Q9H6S3; baseline and differential.
DR Genevisible; Q9H6S3; HS.
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:0050790; P:regulation of catalytic activity; IEA:GOC.
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; 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; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
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
