WBP4_MOUSE
ID WBP4_MOUSE Reviewed; 376 AA.
AC Q61048; Q3TUU8; Q8K1Z9; Q9CS45;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=WW domain-binding protein 4;
DE Short=WBP-4;
DE AltName: Full=Formin-binding protein 21;
DE AltName: Full=WW domain-containing-binding protein 4;
GN Name=Wbp4; Synonyms=Fbp21, Fnbp21;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SNRPB; SNRPC; SF1 AND U2.
RX PubMed=9724750; DOI=10.1073/pnas.95.18.10602;
RA Bedford M.T., Reed R., Leder P.;
RT "WW domain-mediated interactions reveal a spliceosome-associated protein
RT that binds a third class of proline-rich motif: the proline glycine and
RT methionine-rich motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Wolffian duct;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [5]
RP INTERACTION WITH KHDRBS1.
RX PubMed=10748127; DOI=10.1074/jbc.m909368199;
RA Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.;
RT "Arginine methylation inhibits the binding of proline-rich ligands to Src
RT homology 3, but not WW, domains.";
RL J. Biol. Chem. 275:16030-16036(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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: Involved in pre-mRNA splicing as a component of the
CC spliceosome. May play a role in cross-intron bridging of U1 and U2
CC snRNPs in the mammalian A complex. {ECO:0000269|PubMed:9724750}.
CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:9724750).
CC Associated with U2 snRNPs. Binds splicing factors SNRPB, SNRPC and SF1
CC (PubMed:9724750). Interacts via the WW domains with the Pro-rich
CC domains of KHDRBS1/SAM68 (PubMed:10748127). Interacts via the WW
CC domains with the Pro-rich domains of WBP11 (By similarity).
CC {ECO:0000250|UniProtKB:O75554, ECO:0000269|PubMed:10748127,
CC ECO:0000269|PubMed:9724750}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75554}. Nucleus
CC speckle {ECO:0000255|PROSITE-ProRule:PRU00130,
CC ECO:0000269|PubMed:9724750}.
CC -!- DOMAIN: The WW domain recognizes the proline, glycine and methionine-
CC rich (PGM) motif present in the splicing factors, as well as the
CC Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-
CC binding proteins.
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DR EMBL; AF071184; AAC34810.1; -; mRNA.
DR EMBL; AK019160; BAB31575.3; -; mRNA.
DR EMBL; AK135215; BAE22462.1; -; mRNA.
DR EMBL; AK160559; BAE35873.1; -; mRNA.
DR EMBL; AK162009; BAE36679.1; -; mRNA.
DR EMBL; CH466535; EDL35764.1; -; Genomic_DNA.
DR EMBL; BC034851; AAH34851.1; -; mRNA.
DR CCDS; CCDS27300.1; -.
DR PIR; S64714; S64714.
DR RefSeq; NP_061235.2; NM_018765.3.
DR AlphaFoldDB; Q61048; -.
DR SMR; Q61048; -.
DR BioGRID; 204548; 4.
DR ELM; Q61048; -.
DR IntAct; Q61048; 1.
DR MINT; Q61048; -.
DR STRING; 10090.ENSMUSP00000022601; -.
DR iPTMnet; Q61048; -.
DR PhosphoSitePlus; Q61048; -.
DR EPD; Q61048; -.
DR MaxQB; Q61048; -.
DR PaxDb; Q61048; -.
DR PRIDE; Q61048; -.
DR ProteomicsDB; 297634; -.
DR Antibodypedia; 42181; 53 antibodies from 12 providers.
DR DNASU; 22380; -.
DR Ensembl; ENSMUST00000022601; ENSMUSP00000022601; ENSMUSG00000022023.
DR GeneID; 22380; -.
DR KEGG; mmu:22380; -.
DR UCSC; uc007uta.1; mouse.
DR CTD; 11193; -.
DR MGI; MGI:109568; Wbp4.
DR VEuPathDB; HostDB:ENSMUSG00000022023; -.
DR eggNOG; KOG0150; Eukaryota.
DR GeneTree; ENSGT00390000013956; -.
DR HOGENOM; CLU_050927_1_0_1; -.
DR InParanoid; Q61048; -.
DR OMA; MERESQG; -.
DR OrthoDB; 1585242at2759; -.
DR PhylomeDB; Q61048; -.
DR TreeFam; TF316671; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 22380; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Wbp4; mouse.
DR PRO; PR:Q61048; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q61048; protein.
DR Bgee; ENSMUSG00000022023; Expressed in spermatocyte and 269 other tissues.
DR ExpressionAtlas; Q61048; baseline and differential.
DR Genevisible; Q61048; MM.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR040023; WBP4.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13173; PTHR13173; 1.
DR Pfam; PF00397; WW; 2.
DR Pfam; PF06220; zf-U1; 1.
DR SMART; SM00456; WW; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="WW domain-binding protein 4"
FT /id="PRO_0000076066"
FT DOMAIN 123..156
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 164..197
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 11..42
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 94..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75554"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75554"
FT CONFLICT 80..83
FT /note="LKRL -> SEKA (in Ref. 1; AAC34810)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> K (in Ref. 3; AAH34851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42137 MW; ECA7288FC94F3F83 CRC64;
MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV ARRISEIKQK SLDKAKEEEK
ASKEFAAMEA AALKAYQEDL KRLGLPLPSD ISEPTVSPVI STVQPTPTSN QQKEKKKKKK
KKEASKGGWV EGVTADGHCY YYDLITGASQ WEKPEGFQGN LKKTAAKAVW VEGLSEDGYT
YYYNTETGES KWEKPEDFIP HGGDVLSSKD SGKLPDTLED AKSSDSHSDS EGEQKKAGEA
STETKKLIIK FKEKNKSTEK RIGPEIQKEK STPKQNPSNT NEEKPKTLKK STNPYGEWQE
IKQEAESQEE VDLELPSTEG ECLSTSEAGV GEIKVVFKEK TVSSLGVAAD GVAPVFKKRR
LENGKSRNLR QRGDDE
