ESRP2_MOUSE
ID ESRP2_MOUSE Reviewed; 717 AA.
AC Q8K0G8; Q8CEK2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-717.
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=14681479; DOI=10.1093/nar/gkh029;
RA Visel A., Thaller C., Eichele G.;
RT "GenePaint.org: an atlas of gene expression patterns in the mouse embryo.";
RL Nucleic Acids Res. 32:D552-D556(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Epithelial cell-specific.
CC {ECO:0000269|PubMed:14681479}.
CC -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
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DR EMBL; BC031444; AAH31444.1; -; mRNA.
DR EMBL; AK020578; BAC25635.1; -; mRNA.
DR CCDS; CCDS22629.1; -.
DR RefSeq; NP_789808.1; NM_176838.2.
DR AlphaFoldDB; Q8K0G8; -.
DR SMR; Q8K0G8; -.
DR IntAct; Q8K0G8; 1.
DR STRING; 10090.ENSMUSP00000111639; -.
DR iPTMnet; Q8K0G8; -.
DR PhosphoSitePlus; Q8K0G8; -.
DR MaxQB; Q8K0G8; -.
DR PaxDb; Q8K0G8; -.
DR PRIDE; Q8K0G8; -.
DR ProteomicsDB; 275689; -.
DR Antibodypedia; 29741; 209 antibodies from 30 providers.
DR DNASU; 77411; -.
DR Ensembl; ENSMUST00000115979; ENSMUSP00000111639; ENSMUSG00000084128.
DR GeneID; 77411; -.
DR KEGG; mmu:77411; -.
DR UCSC; uc009nff.1; mouse.
DR CTD; 80004; -.
DR MGI; MGI:1924661; Esrp2.
DR VEuPathDB; HostDB:ENSMUSG00000084128; -.
DR eggNOG; KOG1365; Eukaryota.
DR GeneTree; ENSGT00940000157187; -.
DR InParanoid; Q8K0G8; -.
DR OMA; VQHPSAC; -.
DR OrthoDB; 376996at2759; -.
DR PhylomeDB; Q8K0G8; -.
DR TreeFam; TF316157; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR BioGRID-ORCS; 77411; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Esrp2; mouse.
DR PRO; PR:Q8K0G8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K0G8; protein.
DR Bgee; ENSMUSG00000084128; Expressed in lip and 174 other tissues.
DR ExpressionAtlas; Q8K0G8; baseline and differential.
DR Genevisible; Q8K0G8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IGI:MGI.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IGI:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IGI:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS: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 mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..717
FT /note="Epithelial splicing regulatory protein 2"
FT /id="PRO_0000273051"
FT DOMAIN 247..343
FT /note="RRM 1"
FT DOMAIN 348..428
FT /note="RRM 2"
FT DOMAIN 465..545
FT /note="RRM 3"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T0"
SQ SEQUENCE 717 AA; 77361 MW; 121C06A0B8457340 CRC64;
MTPPPPPPPP PGPDPAVDSA TDPCPEPQSL VVLFGATAGA LGPDLGSDET DLILLVWQVV
EPRSRQVGTL HKSLVRAEAA ALSPQCREAS GLSADSLARA ESLDKVLQQF SQLVSGDVAL
LGGGPYVLCT DGQQLLRQVL HPEASRKNLV LPDTFFSFYD LRREFHMQHP STCSARDLTV
GTMAQDLGLE TDATEDDFGV WEVKTMVAVI LHLLEGSNGQ LFSKPEVVKQ KYETGPCSKA
DVVDNETVVR ARGLPWQSSD QDVARFFKGL NIARGGVALC LNAQGRRNGE ALIRFVDSEQ
RDLALQRHKH HMGVRYIEVY KATGEEFVKI AGGTSLEVAR FLSREDQVIL RLRGLPFSAG
PTDVLGFLGP ECPVTGGADG LLFVRHPDGR PTGDAFALFA CEELAQAALR RHKGMLGKRY
IELFRSTAAE VQQVLNRYAA SPLLPTLTAP LLPIPFPLAG GTGRDCVRLR GLPYTATIED
ILSFLGEAAA DIRPHGVHMV LNQQGRPSGD AFIQMMSVER ALAAAQRCHK KMMKERYVEV
VPCSTEEMSR VLMGGSLSRS GLSPPPCKLP CLSPPTYATF QATPALIPTE TTALYPSSAL
LPAARVPAAA TPLAYYPGPA TQLYMNYTAY YPSPPVSPTT VGYLTTPPTA LASTPTTMLS
QPGALVRMQG VPYTAGMKDL LSVFQAYQLA PDDYTTLMPV GDPPRTVLQA PKEWVCL
