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Database: UniProt
Entry: WBP4_MOUSE
LinkDB: WBP4_MOUSE
Original site: 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   24-JAN-2024, entry version 154.
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). Interacts
CC       with SNRNP200 (By similarity). {ECO:0000250|UniProtKB:O75554,
CC       ECO:0000269|PubMed:10748127, 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; 10090-ENSMUSP00000022601; -.
DR   ProteomicsDB; 297634; -.
DR   Pumba; Q61048; -.
DR   Antibodypedia; 42181; 59 antibodies from 13 providers.
DR   DNASU; 22380; -.
DR   Ensembl; ENSMUST00000022601.7; ENSMUSP00000022601.6; ENSMUSG00000022023.7.
DR   GeneID; 22380; -.
DR   KEGG; mmu:22380; -.
DR   UCSC; uc007uta.1; mouse.
DR   AGR; MGI:109568; -.
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; 38440at2759; -.
DR   PhylomeDB; Q61048; -.
DR   TreeFam; TF316671; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 22380; 12 hits in 81 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 272 other cell types or 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   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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; WW DOMAIN BINDING PROTEIN 4; 1.
DR   PANTHER; PTHR13173:SF10; WW DOMAIN-BINDING PROTEIN 4; 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; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
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   REGION          357..375
FT                   /note="Interaction with SNRNP200"
FT                   /evidence="ECO:0000250|UniProtKB:O75554"
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
//
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