ID ES8L1_HUMAN Reviewed; 723 AA. AC Q8TE68; Q71RE2; Q8NC10; Q96BB7; Q9BSQ2; Q9GZQ2; Q9NXH0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 164. 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=DRC3, EPS8R1; ORFNames=PP10566; 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 [GENOMIC DNA / MRNA] (ISOFORM 4). RX PubMed=10514543; RA Wu K., Xu Z., Wang M., Xu X., Han Y., Cao Y., Wang R., Sun Y., Wu M.; RT "Cloning and expression analyses of down-regulated cDNA C6-2A in human RT esophageal cancer."; RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 16:325-327(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-4; GLU-457 AND RP ARG-669. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-4; RP GLU-457 AND ARG-669. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP ARG-669. RC TISSUE=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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Muscle, and Skin; 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 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, 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). CC -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role CC in membrane ruffling and remodeling of the actin cytoskeleton. 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 Q8TE68; Q9H013: ADAM19; NbExp=2; IntAct=EBI-7487998, EBI-8567699; CC Q8TE68; P07766: CD3E; NbExp=6; IntAct=EBI-7487998, EBI-1211297; CC Q8TE68; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-7487998, EBI-750109; CC Q8TE68-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12003490, EBI-11096309; CC Q8TE68-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12003490, EBI-3867333; CC Q8TE68-3; P28799: GRN; NbExp=3; IntAct=EBI-21574901, EBI-747754; CC Q8TE68-3; P42858: HTT; NbExp=3; IntAct=EBI-21574901, EBI-466029; CC Q8TE68-3; O43933: PEX1; NbExp=3; IntAct=EBI-21574901, EBI-988601; CC Q8TE68-3; O76024: WFS1; NbExp=3; IntAct=EBI-21574901, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565974}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=A; CC IsoId=Q8TE68-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q8TE68-2; Sequence=VSP_019083, VSP_019085; CC Name=3; Synonyms=C; CC IsoId=Q8TE68-3; Sequence=VSP_019084, VSP_019088, VSP_019089; CC Name=4; CC IsoId=Q8TE68-4; Sequence=VSP_019082, VSP_019086, VSP_019087, CC VSP_019088; CC -!- TISSUE SPECIFICITY: Detected in placenta. CC {ECO:0000269|PubMed:14565974}. CC -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG03038.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG03039.1; Type=Erroneous gene model prediction; 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; AF282168; AAG03039.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF282167; AAG03038.1; ALT_FRAME; mRNA. DR EMBL; AY074928; AAL76117.1; -; mRNA. DR EMBL; AF370395; AAQ15231.1; -; mRNA. DR EMBL; AK000265; BAA91041.1; -; mRNA. DR EMBL; AK075098; BAC11399.1; -; mRNA. DR EMBL; AC005782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004907; AAH04907.2; -; mRNA. DR EMBL; BC015763; AAH15763.1; -; mRNA. DR CCDS; CCDS12914.1; -. [Q8TE68-1] DR CCDS; CCDS12915.1; -. [Q8TE68-2] DR RefSeq; NP_060199.3; NM_017729.3. [Q8TE68-2] DR RefSeq; NP_573441.2; NM_133180.2. [Q8TE68-1] DR PDB; 2K2M; NMR; -; A=481-536. DR PDB; 2ROL; NMR; -; A=478-537. DR PDBsum; 2K2M; -. DR PDBsum; 2ROL; -. DR AlphaFoldDB; Q8TE68; -. DR BMRB; Q8TE68; -. DR SMR; Q8TE68; -. DR BioGRID; 120218; 60. DR CORUM; Q8TE68; -. DR IntAct; Q8TE68; 13. DR MINT; Q8TE68; -. DR STRING; 9606.ENSP00000201647; -. DR iPTMnet; Q8TE68; -. DR PhosphoSitePlus; Q8TE68; -. DR BioMuta; EPS8L1; -. DR EPD; Q8TE68; -. DR jPOST; Q8TE68; -. DR MassIVE; Q8TE68; -. DR MaxQB; Q8TE68; -. DR PaxDb; 9606-ENSP00000201647; -. DR PeptideAtlas; Q8TE68; -. DR ProteomicsDB; 74407; -. [Q8TE68-1] DR ProteomicsDB; 74408; -. [Q8TE68-2] DR ProteomicsDB; 74409; -. [Q8TE68-3] DR ProteomicsDB; 74410; -. [Q8TE68-4] DR Antibodypedia; 19481; 180 antibodies from 24 providers. DR DNASU; 54869; -. DR Ensembl; ENST00000201647.11; ENSP00000201647.5; ENSG00000131037.15. [Q8TE68-1] DR Ensembl; ENST00000245618.5; ENSP00000245618.4; ENSG00000131037.15. [Q8TE68-2] DR GeneID; 54869; -. DR KEGG; hsa:54869; -. DR MANE-Select; ENST00000201647.11; ENSP00000201647.5; NM_133180.3; NP_573441.2. DR UCSC; uc002qis.5; human. [Q8TE68-1] DR AGR; HGNC:21295; -. DR CTD; 54869; -. DR DisGeNET; 54869; -. DR GeneCards; EPS8L1; -. DR HGNC; HGNC:21295; EPS8L1. DR HPA; ENSG00000131037; Tissue enhanced (esophagus, skin). DR MIM; 614987; gene. DR neXtProt; NX_Q8TE68; -. DR OpenTargets; ENSG00000131037; -. DR PharmGKB; PA134990326; -. DR VEuPathDB; HostDB:ENSG00000131037; -. DR eggNOG; KOG3557; Eukaryota. DR GeneTree; ENSGT00940000158125; -. DR HOGENOM; CLU_014510_0_0_1; -. DR InParanoid; Q8TE68; -. DR OMA; SEVRRPH; -. DR OrthoDB; 2997036at2759; -. DR PhylomeDB; Q8TE68; -. DR TreeFam; TF313069; -. DR PathwayCommons; Q8TE68; -. DR SignaLink; Q8TE68; -. DR BioGRID-ORCS; 54869; 20 hits in 1157 CRISPR screens. DR ChiTaRS; EPS8L1; human. DR EvolutionaryTrace; Q8TE68; -. DR GeneWiki; EPS8L1; -. DR GenomeRNAi; 54869; -. DR Pharos; Q8TE68; Tbio. DR PRO; PR:Q8TE68; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8TE68; Protein. DR Bgee; ENSG00000131037; Expressed in lower esophagus mucosa and 165 other cell types or tissues. DR ExpressionAtlas; Q8TE68; baseline and differential. 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:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042608; F:T cell receptor binding; IPI:UniProtKB. 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 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:SF19; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE 8-LIKE PROTEIN 1; 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; PS50002; SH3; 1. DR Genevisible; Q8TE68; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein; KW Reference proteome; SH3 domain. FT CHAIN 1..723 FT /note="Epidermal growth factor receptor kinase substrate 8- FT like protein 1" FT /id="PRO_0000239082" FT DOMAIN 35..164 FT /note="PTB" FT /evidence="ECO:0000255" FT DOMAIN 478..537 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 162..247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 442..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 537..589 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 609..636 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 689..719 FT /evidence="ECO:0000255" FT COMPBIAS 162..182 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 550..571 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 572..589 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 187 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8R5F8" FT VAR_SEQ 1..177 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10514543" FT /id="VSP_019082" FT VAR_SEQ 1..127 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019083" FT VAR_SEQ 1..39 FT /note="MSTATGPEAAPKPSAKSIYEQRKRYSTVVMADVSQYPVN -> MGRKAIVLA FT IANTSLAFPLCQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019084" FT VAR_SEQ 128..143 FT /note="ERAQPDVHFFQGLRLG -> MNRTWPRRIWGSSQDE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019085" FT VAR_SEQ 178..187 FT /note="QRDRSPAAET -> MSPLSPGSPL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10514543" FT /id="VSP_019086" FT VAR_SEQ 191..300 FT /note="QRRPSVRAVISTVERGAGRGRPQAKPIPEAEEAQRPEPVGTSSNADSASPDL FT GPRGPDLAVLQAEREVDILNHVFDDVESFVSRLQKSAEAARVLEHRERGRRSRRRAAG FT -> ARADLTAILTGCPPLSACLVLAPRPHRRARLLPS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10514543" FT /id="VSP_019087" FT VAR_SEQ 451 FT /note="R -> RQVTQATQQGRGWEVRGRGRSAWPRLTRLSYFL (in isoform 3 FT and isoform 4)" FT /evidence="ECO:0000303|PubMed:10514543, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019088" FT VAR_SEQ 509..696 FT /note="DDSRKWWKVRDPAGQEGYVPYNILTPYPGPRLHHSQSPARSLNSTPPPPPAP FT APAPPPALARPRWDRPRWDSCDSLNGLDPSEKEKFSQMLIVNEELQARLAQGRSGPSRA FT VPGPRAPEPQLSPGSDASEVRAWLQAKGFSSGTVDALGVLTGAQLFSLQKEELRAVSPE FT EGARVYSQVTVQRSLLED -> ED (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019089" FT VARIANT 4 FT /note="A -> T (in dbSNP:rs12609976)" FT /evidence="ECO:0000269|PubMed:12620401, FT ECO:0000269|PubMed:15498874" FT /id="VAR_060375" FT VARIANT 288 FT /note="R -> G (in dbSNP:rs1620074)" FT /id="VAR_060376" FT VARIANT 457 FT /note="Q -> E (in dbSNP:rs1628576)" FT /evidence="ECO:0000269|PubMed:12620401, FT ECO:0000269|PubMed:15498874" FT /id="VAR_056870" FT VARIANT 669 FT /note="K -> R (in dbSNP:rs1054940)" FT /evidence="ECO:0000269|PubMed:12620401, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15498874" FT /id="VAR_060377" FT VARIANT 703 FT /note="L -> P (in dbSNP:rs60073068)" FT /id="VAR_061647" FT CONFLICT 30 FT /note="M -> T (in Ref. 4; BAC11399)" FT /evidence="ECO:0000305" FT CONFLICT 555 FT /note="P -> S (in Ref. 2; AAL76117)" FT /evidence="ECO:0000305" FT CONFLICT 688 FT /note="T -> I (in Ref. 4; BAA91041)" FT /evidence="ECO:0000305" FT CONFLICT 695 FT /note="E -> G (in Ref. 4; BAC11399)" FT /evidence="ECO:0000305" FT STRAND 482..487 FT /evidence="ECO:0007829|PDB:2K2M" FT STRAND 493..496 FT /evidence="ECO:0007829|PDB:2K2M" FT STRAND 504..509 FT /evidence="ECO:0007829|PDB:2K2M" FT STRAND 511..518 FT /evidence="ECO:0007829|PDB:2K2M" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:2K2M" FT HELIX 529..531 FT /evidence="ECO:0007829|PDB:2K2M" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:2K2M" SQ SEQUENCE 723 AA; 80251 MW; E55F71B6E128151E CRC64; MSTATGPEAA PKPSAKSIYE QRKRYSTVVM ADVSQYPVNH LVTFCLGEDD GVHTVEDASR KLAVMDSQGR VWAQEMLLRV SPDHVTLLDP ASKEELESYP LGAIVRCDAV MPPGRSRSLL LLVCQEPERA QPDVHFFQGL RLGAELIRED IQGALHNYRS GRGERRAAAL RATQEELQRD RSPAAETPPL QRRPSVRAVI STVERGAGRG RPQAKPIPEA EEAQRPEPVG TSSNADSASP DLGPRGPDLA VLQAEREVDI LNHVFDDVES FVSRLQKSAE AARVLEHRER GRRSRRRAAG EGLLTLRAKP PSEAEYTDVL QKIKYAFSLL ARLRGNIADP SSPELLHFLF GPLQMIVNTS GGPEFASSVR RPHLTSDAVA LLRDNVTPRE NELWTSLGDS WTRPGLELSP EEGPPYRPEF FSGWEPPVTD PQSRAWEDPV EKQLQHERRR RQQSAPQVAV NGHRDLEPES EPQLESETAG KWVLCNYDFQ ARNSSELSVK QRDVLEVLDD SRKWWKVRDP AGQEGYVPYN ILTPYPGPRL HHSQSPARSL NSTPPPPPAP APAPPPALAR PRWDRPRWDS CDSLNGLDPS EKEKFSQMLI VNEELQARLA QGRSGPSRAV PGPRAPEPQL SPGSDASEVR AWLQAKGFSS GTVDALGVLT GAQLFSLQKE ELRAVSPEEG ARVYSQVTVQ RSLLEDKEKV SELEAVMEKQ KKKVEGEVEM EVI //