ESRP2_HUMAN
ID ESRP2_HUMAN Reviewed; 727 AA.
AC Q9H6T0; Q8N6H8; Q8WZ15; Q9H6I4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Epithelial splicing regulatory protein 2;
DE AltName: Full=RNA-binding motif protein 35B;
DE AltName: Full=RNA-binding protein 35B;
GN Name=ESRP2; Synonyms=RBM35B; ORFNames=PP7059;
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 1).
RC TISSUE=Hepatoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-727.
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 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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION BY
RP 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).
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.
CC {ECO:0000269|PubMed:19285943}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19285943}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H6T0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6T0-2; Sequence=VSP_022474;
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 -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55761.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15275.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK025571; BAB15173.1; -; mRNA.
DR EMBL; AK025901; BAB15275.1; ALT_INIT; mRNA.
DR EMBL; BC030146; AAH30146.1; -; mRNA.
DR EMBL; AF289577; AAL55761.1; ALT_FRAME; mRNA.
DR CCDS; CCDS10863.1; -. [Q9H6T0-2]
DR RefSeq; NP_079215.2; NM_024939.2. [Q9H6T0-2]
DR AlphaFoldDB; Q9H6T0; -.
DR SMR; Q9H6T0; -.
DR BioGRID; 123061; 84.
DR IntAct; Q9H6T0; 9.
DR MINT; Q9H6T0; -.
DR STRING; 9606.ENSP00000418748; -.
DR iPTMnet; Q9H6T0; -.
DR PhosphoSitePlus; Q9H6T0; -.
DR BioMuta; ESRP2; -.
DR DMDM; 74761482; -.
DR EPD; Q9H6T0; -.
DR jPOST; Q9H6T0; -.
DR MassIVE; Q9H6T0; -.
DR MaxQB; Q9H6T0; -.
DR PaxDb; Q9H6T0; -.
DR PeptideAtlas; Q9H6T0; -.
DR PRIDE; Q9H6T0; -.
DR ProteomicsDB; 81030; -. [Q9H6T0-1]
DR ProteomicsDB; 81031; -. [Q9H6T0-2]
DR Antibodypedia; 29741; 209 antibodies from 30 providers.
DR DNASU; 80004; -.
DR Ensembl; ENST00000473183.7; ENSP00000418748.2; ENSG00000103067.14. [Q9H6T0-2]
DR Ensembl; ENST00000565858.5; ENSP00000454554.1; ENSG00000103067.14. [Q9H6T0-1]
DR GeneID; 80004; -.
DR KEGG; hsa:80004; -.
DR MANE-Select; ENST00000473183.7; ENSP00000418748.2; NM_024939.3; NP_079215.2. [Q9H6T0-2]
DR UCSC; uc002evq.2; human. [Q9H6T0-1]
DR CTD; 80004; -.
DR DisGeNET; 80004; -.
DR GeneCards; ESRP2; -.
DR HGNC; HGNC:26152; ESRP2.
DR HPA; ENSG00000103067; Tissue enhanced (esophagus).
DR MIM; 612960; gene.
DR neXtProt; NX_Q9H6T0; -.
DR OpenTargets; ENSG00000103067; -.
DR PharmGKB; PA164719361; -.
DR VEuPathDB; HostDB:ENSG00000103067; -.
DR eggNOG; KOG1365; Eukaryota.
DR GeneTree; ENSGT00940000157187; -.
DR HOGENOM; CLU_008009_2_1_1; -.
DR InParanoid; Q9H6T0; -.
DR OMA; VQHPSAC; -.
DR OrthoDB; 376996at2759; -.
DR PhylomeDB; Q9H6T0; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; Q9H6T0; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR SignaLink; Q9H6T0; -.
DR BioGRID-ORCS; 80004; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; ESRP2; human.
DR GenomeRNAi; 80004; -.
DR Pharos; Q9H6T0; Tbio.
DR PRO; PR:Q9H6T0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H6T0; protein.
DR Bgee; ENSG00000103067; Expressed in lower esophagus mucosa and 101 other tissues.
DR ExpressionAtlas; Q9H6T0; baseline and differential.
DR Genevisible; Q9H6T0; HS.
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; HDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034431; ESRP2.
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 PANTHER; PTHR13976:SF30; PTHR13976:SF30; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54928; SSF54928; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..727
FT /note="Epithelial splicing regulatory protein 2"
FT /id="PRO_0000273050"
FT DOMAIN 257..353
FT /note="RRM 1"
FT DOMAIN 358..438
FT /note="RRM 2"
FT DOMAIN 475..555
FT /note="RRM 3"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0G8"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 238..247
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022474"
FT VARIANT 111
FT /note="S -> L (in dbSNP:rs12597504)"
FT /id="VAR_030074"
FT VARIANT 528
FT /note="A -> V (in dbSNP:rs3743738)"
FT /id="VAR_030075"
FT VARIANT 627
FT /note="P -> S (in dbSNP:rs36054935)"
FT /id="VAR_057245"
FT CONFLICT 586
FT /note="T -> I (in Ref. 1; BAB15275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 78401 MW; 8831BA8284D6BD60 CRC64;
MTPPPPPPPP PGPDPAADPA ADPCPWPGSL VVLFGATAGA LGRDLGSDET DLILLVWQVV
EPRSRQVGTL HKSLVRAEAA ALSTQCREAS GLSADSLARA EPLDKVLQQF SQLVNGDVAL
LGGGPYMLCT DGQQLLRQVL HPEASRKNLV LPDMFFSFYD LRREFHMQHP STCPARDLTV
ATMAQGLGLE TDATEDDFGV WEVKTMVAVI LHLLKEPSSQ LFSKPEVIKQ KYETGPCSDS
TVPCPYSSKA DVVDSETVVR ARGLPWQSSD QDVARFFKGL NVARGGVALC LNAQGRRNGE
ALIRFVDSEQ RDLALQRHKH HMGVRYIEVY KATGEEFVKI AGGTSLEVAR FLSREDQVIL
RLRGLPFSAG PTDVLGFLGP ECPVTGGTEG LLFVRHPDGR PTGDAFALFA CEELAQAALR
RHKGMLGKRY IELFRSTAAE VQQVLNRYAS GPLLPTLTAP LLPIPFPLAP GTGRDCVRLR
GLPYTATIED ILSFLGEAAA DIRPHGVHMV LNQQGRPSGD AFIQMTSAER ALAAAQRCHK
KVMKERYVEV VPCSTEEMSR VLMGGTLGRS GMSPPPCKLP CLSPPTYTTF QATPTLIPTE
TAALYPSSAL LPAARVPAAP TPVAYYPGPA TQLYLNYTAY YPSPPVSPTT VGYLTTPTAA
LASAPTSVLS QSGALVRMQG VPYTAGMKDL LSVFQAYQLP ADDYTSLMPV GDPPRTVLQA
PKEWVCL
