ESRP1_HUMAN
ID ESRP1_HUMAN Reviewed; 681 AA.
AC Q6NXG1; A6NHA8; A8MPX1; E9PB47; Q2M2B0; Q499G3; Q6PJ86; Q9NXL8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Epithelial splicing regulatory protein 1;
DE AltName: Full=RNA-binding motif protein 35A;
DE AltName: Full=RNA-binding protein 35A;
GN Name=ESRP1; Synonyms=RBM35A;
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 [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Bone marrow;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Liver, Mammary gland, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-681 (ISOFORM 4).
RC TISSUE=Colon;
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 FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=19285943; DOI=10.1016/j.molcel.2009.01.025;
RA Warzecha C.C., Sato T.K., Nabet B., Hogenesch J.B., Carstens R.P.;
RT "ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2
RT splicing.";
RL Mol. Cell 33:591-601(2009).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-582, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP INVOLVEMENT IN DFNB109, VARIANT DFNB109 VAL-259, AND CHARACTERIZATION OF
RP VARIANT DFNB109 VAL-259.
RX PubMed=29107558; DOI=10.1016/j.devcel.2017.09.026;
RA Rohacek A.M., Bebee T.W., Tilton R.K., Radens C.M., McDermott-Roe C.,
RA Peart N., Kaur M., Zaykaner M., Cieply B., Musunuru K., Barash Y.,
RA Germiller J.A., Krantz I.D., Carstens R.P., Epstein D.J.;
RT "ESRP1 mutations cause hearing loss due to defects in alternative splicing
RT that disrupt cochlear development.";
RL Dev. Cell 43:318-331(2017).
RN [8]
RP STRUCTURE BY NMR OF 310-419.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second RNA recognition motif in hypothetical
RT protein FLJ201171.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: mRNA splicing factor that regulates the formation of
CC epithelial cell-specific isoforms. Specifically regulates the
CC expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2.
CC Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that
CC undergo changes in splicing during the epithelial-to-mesenchymal
CC transition (EMT). Acts by directly binding specific sequences in mRNAs.
CC Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element
CC regulatory region present in the mRNA of FGFR2 (PubMed:19285943).
CC Regulates splicing and expression of genes involved in inner ear
CC development, auditory hair cell differentiation, and cell fate
CC specification in the cochlear epithelium (By similarity).
CC {ECO:0000250|UniProtKB:Q3US41, ECO:0000269|PubMed:19285943}.
CC -!- INTERACTION:
CC Q6NXG1; Q03989: ARID5A; NbExp=3; IntAct=EBI-10213520, EBI-948603;
CC Q6NXG1; Q86V38: ATN1; NbExp=3; IntAct=EBI-10213520, EBI-11954292;
CC Q6NXG1; P13637: ATP1A3; NbExp=3; IntAct=EBI-10213520, EBI-948169;
CC Q6NXG1; P54253: ATXN1; NbExp=12; IntAct=EBI-10213520, EBI-930964;
CC Q6NXG1; P46379-2: BAG6; NbExp=3; IntAct=EBI-10213520, EBI-10988864;
CC Q6NXG1; P48643: CCT5; NbExp=3; IntAct=EBI-10213520, EBI-355710;
CC Q6NXG1; P28329-3: CHAT; NbExp=3; IntAct=EBI-10213520, EBI-25837549;
CC Q6NXG1; P02489: CRYAA; NbExp=3; IntAct=EBI-10213520, EBI-6875961;
CC Q6NXG1; Q15038: DAZAP2; NbExp=3; IntAct=EBI-10213520, EBI-724310;
CC Q6NXG1; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-10213520, EBI-25840379;
CC Q6NXG1; O14645: DNALI1; NbExp=3; IntAct=EBI-10213520, EBI-395638;
CC Q6NXG1; P00488: F13A1; NbExp=3; IntAct=EBI-10213520, EBI-2565863;
CC Q6NXG1; P22607: FGFR3; NbExp=3; IntAct=EBI-10213520, EBI-348399;
CC Q6NXG1; P04792: HSPB1; NbExp=3; IntAct=EBI-10213520, EBI-352682;
CC Q6NXG1; P10809: HSPD1; NbExp=3; IntAct=EBI-10213520, EBI-352528;
CC Q6NXG1; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10213520, EBI-10975473;
CC Q6NXG1; O14901: KLF11; NbExp=3; IntAct=EBI-10213520, EBI-948266;
CC Q6NXG1; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-10213520, EBI-9478422;
CC Q6NXG1; Q92876: KLK6; NbExp=3; IntAct=EBI-10213520, EBI-2432309;
CC Q6NXG1; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-10213520, EBI-1048945;
CC Q6NXG1; Q71SY5: MED25; NbExp=3; IntAct=EBI-10213520, EBI-394558;
CC Q6NXG1; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-10213520, EBI-12813389;
CC Q6NXG1; P16284: PECAM1; NbExp=3; IntAct=EBI-10213520, EBI-716404;
CC Q6NXG1; Q13393: PLD1; NbExp=3; IntAct=EBI-10213520, EBI-2827556;
CC Q6NXG1; P86480: PRR20D; NbExp=3; IntAct=EBI-10213520, EBI-12754095;
CC Q6NXG1; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-10213520, EBI-11987469;
CC Q6NXG1; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10213520, EBI-396669;
CC Q6NXG1; P34741: SDC2; NbExp=3; IntAct=EBI-10213520, EBI-1172957;
CC Q6NXG1; Q13148: TARDBP; NbExp=6; IntAct=EBI-10213520, EBI-372899;
CC Q6NXG1; P02766: TTR; NbExp=3; IntAct=EBI-10213520, EBI-711909;
CC Q6NXG1; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10213520, EBI-741480;
CC Q6NXG1; P08670: VIM; NbExp=3; IntAct=EBI-10213520, EBI-353844;
CC Q6NXG1; O76024: WFS1; NbExp=3; IntAct=EBI-10213520, EBI-720609;
CC Q6NXG1; Q9Y649; NbExp=3; IntAct=EBI-10213520, EBI-25900580;
CC Q6NXG1-3; Q92870-2: APBB2; NbExp=3; IntAct=EBI-21567429, EBI-21535880;
CC Q6NXG1-3; Q86V38: ATN1; NbExp=3; IntAct=EBI-21567429, EBI-11954292;
CC Q6NXG1-3; P54253: ATXN1; NbExp=6; IntAct=EBI-21567429, EBI-930964;
CC Q6NXG1-3; P46379-2: BAG6; NbExp=3; IntAct=EBI-21567429, EBI-10988864;
CC Q6NXG1-3; P55212: CASP6; NbExp=3; IntAct=EBI-21567429, EBI-718729;
CC Q6NXG1-3; P06307: CCK; NbExp=3; IntAct=EBI-21567429, EBI-6624398;
CC Q6NXG1-3; P02489: CRYAA; NbExp=3; IntAct=EBI-21567429, EBI-6875961;
CC Q6NXG1-3; O14645: DNALI1; NbExp=3; IntAct=EBI-21567429, EBI-395638;
CC Q6NXG1-3; P00488: F13A1; NbExp=3; IntAct=EBI-21567429, EBI-2565863;
CC Q6NXG1-3; P42858: HTT; NbExp=6; IntAct=EBI-21567429, EBI-466029;
CC Q6NXG1-3; O14901: KLF11; NbExp=3; IntAct=EBI-21567429, EBI-948266;
CC Q6NXG1-3; Q92876: KLK6; NbExp=3; IntAct=EBI-21567429, EBI-2432309;
CC Q6NXG1-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-21567429, EBI-21591415;
CC Q6NXG1-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-21567429, EBI-2811583;
CC Q6NXG1-3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-21567429, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19285943}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6NXG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXG1-2; Sequence=VSP_022465, VSP_022466;
CC Name=3;
CC IsoId=Q6NXG1-3; Sequence=VSP_022464;
CC Name=4;
CC IsoId=Q6NXG1-4; Sequence=VSP_022467;
CC Name=5;
CC IsoId=Q6NXG1-5; Sequence=VSP_022464, VSP_022467;
CC -!- TISSUE SPECIFICITY: Epithelial cell-specific.
CC {ECO:0000269|PubMed:19285943}.
CC -!- INDUCTION: Down-regulated during the epithelial-to-mesenchymal
CC transition (EMT). {ECO:0000269|PubMed:19285943}.
CC -!- DISEASE: Deafness, autosomal recessive, 109 (DFNB109) [MIM:618013]: A
CC form of non-syndromic, sensorineural deafness characterized by
CC bilateral, congenital, severe to profound 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. DFNB109 affected individuals additionally exhibit
CC vestibular dysplasia, although they do not manifest problems with
CC balance or movement. {ECO:0000269|PubMed:29107558}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA90992.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90992.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BX647570; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC108860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019932; AAH19932.1; ALT_INIT; mRNA.
DR EMBL; BC067098; AAH67098.2; -; mRNA.
DR EMBL; BC099916; AAH99916.2; -; mRNA.
DR EMBL; BC112043; AAI12044.1; -; mRNA.
DR EMBL; AK000178; BAA90992.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47895.1; -. [Q6NXG1-5]
DR CCDS; CCDS47896.1; -. [Q6NXG1-2]
DR CCDS; CCDS47897.1; -. [Q6NXG1-1]
DR CCDS; CCDS47898.1; -. [Q6NXG1-3]
DR RefSeq; NP_001030087.2; NM_001034915.2. [Q6NXG1-3]
DR RefSeq; NP_001116297.1; NM_001122825.1. [Q6NXG1-2]
DR RefSeq; NP_001116298.1; NM_001122826.1. [Q6NXG1-5]
DR RefSeq; NP_001116299.1; NM_001122827.1.
DR RefSeq; NP_060167.2; NM_017697.3. [Q6NXG1-1]
DR RefSeq; XP_005251048.1; XM_005250991.3. [Q6NXG1-4]
DR PDB; 2DHA; NMR; -; A=310-419.
DR PDB; 2RVJ; NMR; -; A=438-539.
DR PDBsum; 2DHA; -.
DR PDBsum; 2RVJ; -.
DR AlphaFoldDB; Q6NXG1; -.
DR SMR; Q6NXG1; -.
DR BioGRID; 120196; 75.
DR IntAct; Q6NXG1; 52.
DR STRING; 9606.ENSP00000405738; -.
DR ChEMBL; CHEMBL4295865; -.
DR iPTMnet; Q6NXG1; -.
DR PhosphoSitePlus; Q6NXG1; -.
DR BioMuta; ESRP1; -.
DR DMDM; 124020999; -.
DR EPD; Q6NXG1; -.
DR jPOST; Q6NXG1; -.
DR MassIVE; Q6NXG1; -.
DR MaxQB; Q6NXG1; -.
DR PaxDb; Q6NXG1; -.
DR PeptideAtlas; Q6NXG1; -.
DR PRIDE; Q6NXG1; -.
DR ProteomicsDB; 19142; -.
DR ProteomicsDB; 66753; -. [Q6NXG1-1]
DR ProteomicsDB; 66754; -. [Q6NXG1-2]
DR ProteomicsDB; 66755; -. [Q6NXG1-3]
DR ProteomicsDB; 66756; -. [Q6NXG1-4]
DR Antibodypedia; 6696; 158 antibodies from 29 providers.
DR DNASU; 54845; -.
DR Ensembl; ENST00000358397.9; ENSP00000351168.5; ENSG00000104413.18. [Q6NXG1-3]
DR Ensembl; ENST00000423620.6; ENSP00000407349.2; ENSG00000104413.18. [Q6NXG1-5]
DR Ensembl; ENST00000433389.8; ENSP00000405738.2; ENSG00000104413.18. [Q6NXG1-1]
DR Ensembl; ENST00000646773.1; ENSP00000494213.1; ENSG00000104413.18. [Q6NXG1-2]
DR GeneID; 54845; -.
DR KEGG; hsa:54845; -.
DR MANE-Select; ENST00000433389.8; ENSP00000405738.2; NM_017697.4; NP_060167.2.
DR UCSC; uc003ygq.5; human. [Q6NXG1-1]
DR CTD; 54845; -.
DR DisGeNET; 54845; -.
DR GeneCards; ESRP1; -.
DR HGNC; HGNC:25966; ESRP1.
DR HPA; ENSG00000104413; Low tissue specificity.
DR MalaCards; ESRP1; -.
DR MIM; 612959; gene.
DR MIM; 618013; phenotype.
DR neXtProt; NX_Q6NXG1; -.
DR OpenTargets; ENSG00000104413; -.
DR PharmGKB; PA164719324; -.
DR VEuPathDB; HostDB:ENSG00000104413; -.
DR eggNOG; KOG1365; Eukaryota.
DR GeneTree; ENSGT00940000159511; -.
DR HOGENOM; CLU_008009_2_1_1; -.
DR InParanoid; Q6NXG1; -.
DR OMA; PEDAFMH; -.
DR OrthoDB; 376996at2759; -.
DR PhylomeDB; Q6NXG1; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; Q6NXG1; -.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR SignaLink; Q6NXG1; -.
DR BioGRID-ORCS; 54845; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; ESRP1; human.
DR EvolutionaryTrace; Q6NXG1; -.
DR GenomeRNAi; 54845; -.
DR Pharos; Q6NXG1; Tbio.
DR PRO; PR:Q6NXG1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6NXG1; protein.
DR Bgee; ENSG00000104413; Expressed in secondary oocyte and 143 other tissues.
DR ExpressionAtlas; Q6NXG1; baseline and differential.
DR Genevisible; Q6NXG1; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0042669; P:regulation of inner ear auditory receptor cell fate specification; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12736; RRM1_ESRP1; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034427; ESRP1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Deafness; Disease variant; Methylation;
KW mRNA processing; mRNA splicing; Non-syndromic deafness; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..681
FT /note="Epithelial splicing regulatory protein 1"
FT /id="PRO_0000273046"
FT DOMAIN 225..302
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 326..406
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 445..525
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T0"
FT MOD_RES 582
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 546..549
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022464"
FT VAR_SEQ 608
FT /note="P -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022465"
FT VAR_SEQ 609..681
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022466"
FT VAR_SEQ 658..681
FT /note="YATEDGLIHTNDQARTLPKEWVCI -> CLKDVW (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022467"
FT VARIANT 196
FT /note="Y -> C (in dbSNP:rs2303454)"
FT /id="VAR_030073"
FT VARIANT 259
FT /note="L -> V (in DFNB109; hypomorphic mutation affecting
FT alternative splicing in patient-derived induced pluripotent
FT stem cells and other cell-based assays;
FT dbSNP:rs1554577402)"
FT /evidence="ECO:0000269|PubMed:29107558"
FT /id="VAR_080811"
FT CONFLICT 505
FT /note="A -> V (in Ref. 1; BX647570)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="F -> S (in Ref. 3; AAH99916)"
FT /evidence="ECO:0000305"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2DHA"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:2DHA"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:2DHA"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:2DHA"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2DHA"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:2DHA"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:2RVJ"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:2RVJ"
FT HELIX 466..470
FT /evidence="ECO:0007829|PDB:2RVJ"
FT STRAND 471..481
FT /evidence="ECO:0007829|PDB:2RVJ"
FT STRAND 485..496
FT /evidence="ECO:0007829|PDB:2RVJ"
FT HELIX 498..507
FT /evidence="ECO:0007829|PDB:2RVJ"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:2RVJ"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:2RVJ"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:2RVJ"
SQ SEQUENCE 681 AA; 75585 MW; 066379C448FBAF5C CRC64;
MTASPDYLVV LFGITAGATG AKLGSDEKEL ILLFWKVVDL ANKKVGQLHE VLVRPDQLEL
TEDCKEETKI DVESLSSASQ LDQALRQFNQ SVSNELNIGV GTSFCLCTDG QLHVRQILHP
EASKKNVLLP ECFYSFFDLR KEFKKCCPGS PDIDKLDVAT MTEYLNFEKS SSVSRYGASQ
VEDMGNIILA MISEPYNHRF SDPERVNYKF ESGTCSKMEL IDDNTVVRAR GLPWQSSDQD
IARFFKGLNI AKGGAALCLN AQGRRNGEAL VRFVSEEHRD LALQRHKHHM GTRYIEVYKA
TGEDFLKIAG GTSNEVAQFL SKENQVIVRM RGLPFTATAE EVVAFFGQHC PITGGKEGIL
FVTYPDGRPT GDAFVLFACE EYAQNALRKH KDLLGKRYIE LFRSTAAEVQ QVLNRFSSAP
LIPLPTPPII PVLPQQFVPP TNVRDCIRLR GLPYAATIED ILDFLGEFAT DIRTHGVHMV
LNHQGRPSGD AFIQMKSADR AFMAAQKCHK KNMKDRYVEV FQCSAEEMNF VLMGGTLNRN
GLSPPPCKLP CLSPPSYTFP APAAVIPTEA AIYQPSVILN PRALQPSTAY YPAGTQLFMN
YTAYYPSPPG SPNSLGYFPT AANLSGVPPQ PGTVVRMQGL AYNTGVKEIL NFFQGYQYAT
EDGLIHTNDQ ARTLPKEWVC I
