Full text data of WBP4
WBP4
(FBP21, FNBP21)
[Confidence: low (only semi-automatic identification from reviews)]
WW domain-binding protein 4; WBP-4 (Formin-binding protein 21; WW domain-containing-binding protein 4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WW domain-binding protein 4; WBP-4 (Formin-binding protein 21; WW domain-containing-binding protein 4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75554
ID WBP4_HUMAN Reviewed; 376 AA.
AC O75554; Q32P29;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 109.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION 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
RT protein that binds a third class of proline-rich motif: the proline
RT glycine and methionine-rich motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-262 AND
RP SER-277, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP STRUCTURE BY NMR OF 124-164.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WW domain in WW domain binding protein 4 (WBP-
RT 4).";
RL Submitted (OCT-2006) to the PDB data bank.
RN [7]
RP STRUCTURE BY NMR OF 122-196, FUNCTION, MUTAGENESIS OF TRP-150 AND
RP TRP-191, SUBCELLULAR LOCATION, AND INTERACTION WITH WBP11.
RX PubMed=19592703; DOI=10.1074/jbc.M109.024828;
RA Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B.,
RA Hu Q., Wu J., Bollen M., Shi Y.;
RT "Structure and function of the two tandem WW domains of the pre-mRNA
RT splicing factor FBP21 (formin-binding protein 21).";
RL J. Biol. Chem. 284:25375-25387(2009).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-113.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Promotes pre-mRNA splicing. A spliceosome-associated
CC protein; may play a role in cross-intron bridging of U1 and U2
CC snRNPs in the mammalian A complex.
CC -!- SUBUNIT: Associated with U2 snRNPs. Binds splicing factors SNRPB,
CC SNRPC and SF1. Interacts via the WW domains with the Pro-rich
CC domains of KHDRBS1/SAM68 (By similarity). Interacts via the WW
CC domains with the Pro-rich domains of WBP11.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC -!- DOMAIN: The WW domain recognizes the proline, glycine and
CC methionine-rich (PGM) motif present in the splicing factors, as
CC well as the Arg/Gly-rich-flanked Pro-rich domains found in several
CC WW domain-binding proteins (By similarity).
CC -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC -!- SIMILARITY: Contains 2 WW domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF071185; AAC34811.1; -; mRNA.
DR EMBL; AL157877; CAI13223.1; -; Genomic_DNA.
DR EMBL; BC104879; AAI04880.1; -; mRNA.
DR EMBL; BC108310; AAI08311.1; -; mRNA.
DR RefSeq; NP_009118.1; NM_007187.3.
DR UniGene; Hs.411300; -.
DR PDB; 2DK1; NMR; -; A=127-163.
DR PDB; 2JXW; NMR; -; A=122-196.
DR PDBsum; 2DK1; -.
DR PDBsum; 2JXW; -.
DR ProteinModelPortal; O75554; -.
DR SMR; O75554; 122-196.
DR MINT; MINT-127038; -.
DR STRING; 9606.ENSP00000368801; -.
DR PhosphoSite; O75554; -.
DR PaxDb; O75554; -.
DR PRIDE; O75554; -.
DR Ensembl; ENST00000379487; ENSP00000368801; ENSG00000120688.
DR GeneID; 11193; -.
DR KEGG; hsa:11193; -.
DR UCSC; uc001uxt.3; human.
DR CTD; 11193; -.
DR GeneCards; GC13P041635; -.
DR HGNC; HGNC:12739; WBP4.
DR HPA; HPA038965; -.
DR MIM; 604981; gene.
DR neXtProt; NX_O75554; -.
DR PharmGKB; PA37350; -.
DR eggNOG; COG5104; -.
DR HOGENOM; HOG000067962; -.
DR HOVERGEN; HBG053152; -.
DR InParanoid; O75554; -.
DR KO; K13220; -.
DR OMA; ESHEEVD; -.
DR OrthoDB; EOG7H7930; -.
DR PhylomeDB; O75554; -.
DR SignaLink; O75554; -.
DR EvolutionaryTrace; O75554; -.
DR GeneWiki; WBP4; -.
DR GenomeRNAi; 11193; -.
DR NextBio; 42605; -.
DR PRO; PR:O75554; -.
DR ArrayExpress; O75554; -.
DR Bgee; O75554; -.
DR CleanEx; HS_WBP4; -.
DR Genevestigator; O75554; -.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR000690; Znf_C2H2_matrin.
DR InterPro; IPR003604; Znf_U1.
DR InterPro; IPR013085; Znf_U1-C.
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 PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1 376 WW domain-binding protein 4.
FT /FTId=PRO_0000076065.
FT DOMAIN 122 155 WW 1.
FT DOMAIN 163 196 WW 2.
FT ZN_FING 11 42 Matrin-type.
FT COMPBIAS 111 125 Lys-rich.
FT MOD_RES 220 220 Phosphoserine.
FT MOD_RES 262 262 Phosphoserine.
FT MOD_RES 277 277 Phosphoserine.
FT VARIANT 113 113 K -> R (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036352.
FT MUTAGEN 150 150 W->A: Nearly abolishes activation of pre-
FT mRNA splicing. Abolishes interaction with
FT WBP11.
FT MUTAGEN 191 191 W->A: Nearly abolishes activation of pre-
FT mRNA splicing. Abolishes interaction with
FT WBP11.
FT STRAND 128 130
FT TURN 134 136
FT STRAND 140 145
FT STRAND 148 151
FT STRAND 161 164
FT STRAND 168 174
FT TURN 175 177
FT STRAND 178 183
FT TURN 184 187
FT STRAND 188 192
SQ SEQUENCE 376 AA; 42507 MW; 7A122A29D4325D11 CRC64;
MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK SLDKAKEEEK
ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST IPPTSTSNQQ KEKKEKKKRK
KDPSKGRWVE GITSEGYHYY YDLISGASQW EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY
YYNTETGESR WEKPDDFIPH TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV
STETEKPKIK FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI
KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD GVAPVFKKRR
TENGKSRNLR QRGDDQ
//
ID WBP4_HUMAN Reviewed; 376 AA.
AC O75554; Q32P29;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 109.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION 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
RT protein that binds a third class of proline-rich motif: the proline
RT glycine and methionine-rich motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-262 AND
RP SER-277, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP STRUCTURE BY NMR OF 124-164.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WW domain in WW domain binding protein 4 (WBP-
RT 4).";
RL Submitted (OCT-2006) to the PDB data bank.
RN [7]
RP STRUCTURE BY NMR OF 122-196, FUNCTION, MUTAGENESIS OF TRP-150 AND
RP TRP-191, SUBCELLULAR LOCATION, AND INTERACTION WITH WBP11.
RX PubMed=19592703; DOI=10.1074/jbc.M109.024828;
RA Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B.,
RA Hu Q., Wu J., Bollen M., Shi Y.;
RT "Structure and function of the two tandem WW domains of the pre-mRNA
RT splicing factor FBP21 (formin-binding protein 21).";
RL J. Biol. Chem. 284:25375-25387(2009).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-113.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Promotes pre-mRNA splicing. A spliceosome-associated
CC protein; may play a role in cross-intron bridging of U1 and U2
CC snRNPs in the mammalian A complex.
CC -!- SUBUNIT: Associated with U2 snRNPs. Binds splicing factors SNRPB,
CC SNRPC and SF1. Interacts via the WW domains with the Pro-rich
CC domains of KHDRBS1/SAM68 (By similarity). Interacts via the WW
CC domains with the Pro-rich domains of WBP11.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC -!- DOMAIN: The WW domain recognizes the proline, glycine and
CC methionine-rich (PGM) motif present in the splicing factors, as
CC well as the Arg/Gly-rich-flanked Pro-rich domains found in several
CC WW domain-binding proteins (By similarity).
CC -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC -!- SIMILARITY: Contains 2 WW domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF071185; AAC34811.1; -; mRNA.
DR EMBL; AL157877; CAI13223.1; -; Genomic_DNA.
DR EMBL; BC104879; AAI04880.1; -; mRNA.
DR EMBL; BC108310; AAI08311.1; -; mRNA.
DR RefSeq; NP_009118.1; NM_007187.3.
DR UniGene; Hs.411300; -.
DR PDB; 2DK1; NMR; -; A=127-163.
DR PDB; 2JXW; NMR; -; A=122-196.
DR PDBsum; 2DK1; -.
DR PDBsum; 2JXW; -.
DR ProteinModelPortal; O75554; -.
DR SMR; O75554; 122-196.
DR MINT; MINT-127038; -.
DR STRING; 9606.ENSP00000368801; -.
DR PhosphoSite; O75554; -.
DR PaxDb; O75554; -.
DR PRIDE; O75554; -.
DR Ensembl; ENST00000379487; ENSP00000368801; ENSG00000120688.
DR GeneID; 11193; -.
DR KEGG; hsa:11193; -.
DR UCSC; uc001uxt.3; human.
DR CTD; 11193; -.
DR GeneCards; GC13P041635; -.
DR HGNC; HGNC:12739; WBP4.
DR HPA; HPA038965; -.
DR MIM; 604981; gene.
DR neXtProt; NX_O75554; -.
DR PharmGKB; PA37350; -.
DR eggNOG; COG5104; -.
DR HOGENOM; HOG000067962; -.
DR HOVERGEN; HBG053152; -.
DR InParanoid; O75554; -.
DR KO; K13220; -.
DR OMA; ESHEEVD; -.
DR OrthoDB; EOG7H7930; -.
DR PhylomeDB; O75554; -.
DR SignaLink; O75554; -.
DR EvolutionaryTrace; O75554; -.
DR GeneWiki; WBP4; -.
DR GenomeRNAi; 11193; -.
DR NextBio; 42605; -.
DR PRO; PR:O75554; -.
DR ArrayExpress; O75554; -.
DR Bgee; O75554; -.
DR CleanEx; HS_WBP4; -.
DR Genevestigator; O75554; -.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR000690; Znf_C2H2_matrin.
DR InterPro; IPR003604; Znf_U1.
DR InterPro; IPR013085; Znf_U1-C.
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 PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1 376 WW domain-binding protein 4.
FT /FTId=PRO_0000076065.
FT DOMAIN 122 155 WW 1.
FT DOMAIN 163 196 WW 2.
FT ZN_FING 11 42 Matrin-type.
FT COMPBIAS 111 125 Lys-rich.
FT MOD_RES 220 220 Phosphoserine.
FT MOD_RES 262 262 Phosphoserine.
FT MOD_RES 277 277 Phosphoserine.
FT VARIANT 113 113 K -> R (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036352.
FT MUTAGEN 150 150 W->A: Nearly abolishes activation of pre-
FT mRNA splicing. Abolishes interaction with
FT WBP11.
FT MUTAGEN 191 191 W->A: Nearly abolishes activation of pre-
FT mRNA splicing. Abolishes interaction with
FT WBP11.
FT STRAND 128 130
FT TURN 134 136
FT STRAND 140 145
FT STRAND 148 151
FT STRAND 161 164
FT STRAND 168 174
FT TURN 175 177
FT STRAND 178 183
FT TURN 184 187
FT STRAND 188 192
SQ SEQUENCE 376 AA; 42507 MW; 7A122A29D4325D11 CRC64;
MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK SLDKAKEEEK
ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST IPPTSTSNQQ KEKKEKKKRK
KDPSKGRWVE GITSEGYHYY YDLISGASQW EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY
YYNTETGESR WEKPDDFIPH TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV
STETEKPKIK FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI
KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD GVAPVFKKRR
TENGKSRNLR QRGDDQ
//
MIM
604981
*RECORD*
*FIELD* NO
604981
*FIELD* TI
*604981 WW DOMAIN-CONTAINING BINDING PROTEIN 4; WBP4
;;FORMIN-BINDING PROTEIN 21; FBP21
read more*FIELD* TX
CLONING
Using a proline-rich domain derived from formin (FMN1; 136535), which is
a protein product of the murine limb deformity locus, in a
protein-protein interaction assay, Chan et al. (1996) identified a
family of murine formin-binding proteins, members of which contain 1 or
more of a special class of tyrosine-rich WW domains, which are small
compact globular structures that interact with proline-rich ligands. The
WW domain is characterized by 2 highly conserved trytophan residues and
a proline residue. Two of these WW domains, in the proteins Fbp11
(PRPF40A; 612941) and Fbp21, are strikingly similar to those found in
the yeast splicing factor PRP40. Pre-mRNA splicing requires the bridging
of the 5-prime and 3-prime ends of the intron. In yeast, this bridging
involves interactions between the WW domains in the splicing factor
PRP40 and a proline-rich domain in the branchpoint-binding protein BBP.
By searching an EST database with the mouse Fbp21 sequence, Bedford et
al. (1998) identified ESTs encoding human FBP21, which has been named
WBP4. The predicted 376-amino acid FBP21 protein contains an N-terminal
zinc finger motif and 2 WW domains. Western blot analysis of in vitro
translated FBP21 protein and of HeLa cell extracts showed that FBP21
migrates as a 58-kD polypeptide. Immunofluorescence studies of HeLa
cells indicated that endogenous FBP21 is exclusively localized to the
nucleus and concentrated in a punctate pattern. In addition, FBP21
colocalized with the essential pre-mRNA splicing factor SC35 (600813).
GENE FUNCTION
Bedford et al. (1998) demonstrated that FBP21 is present in the
spliceosomal complex A. Mouse Fbp21 interacted directly with the SF1/BBP
protein, the U1 snRNP protein U1C (603522), and the core snRNP proteins
SmB and SmB-prime (SNRPB; 182282). These interactions were mediated by
the WW domains of Fbp21, which recognized a proline-, glycine-, and
methionine-rich (PGM) motif in the splicing factors. Immunoprecipitation
assays showed that Fbp21 associates with U2 snRNPs (e.g., SNRPB2;
603520). The authors concluded that FBP21 is a general spliceosomal
protein that may play a role in cross-intron bridging of U1 and U2
snRNPs in the mammalian A complex.
*FIELD* RF
1. Bedford, M. T.; Reed, R.; Leder, P.: WW domain-mediated interactions
reveal a spliceosome-associated protein that binds a third class of
proline-rich motif: the proline glycine and methionine-rich motif. Proc.
Nat. Acad. Sci. 95: 10602-10607, 1998.
2. Chan, D. C.; Bedford, M. T.; Leder, P.: Formin binding proteins
bear WWP/WW domains that bind proline-rich peptides and functionally
resemble SH3 domains. EMBO J. 15: 1045-1054, 1996.
*FIELD* CD
Patti M. Sherman: 5/19/2000
*FIELD* ED
wwang: 04/02/2010
psherman: 6/8/2000
mcapotos: 6/6/2000
mcapotos: 6/5/2000
psherman: 5/22/2000
*RECORD*
*FIELD* NO
604981
*FIELD* TI
*604981 WW DOMAIN-CONTAINING BINDING PROTEIN 4; WBP4
;;FORMIN-BINDING PROTEIN 21; FBP21
read more*FIELD* TX
CLONING
Using a proline-rich domain derived from formin (FMN1; 136535), which is
a protein product of the murine limb deformity locus, in a
protein-protein interaction assay, Chan et al. (1996) identified a
family of murine formin-binding proteins, members of which contain 1 or
more of a special class of tyrosine-rich WW domains, which are small
compact globular structures that interact with proline-rich ligands. The
WW domain is characterized by 2 highly conserved trytophan residues and
a proline residue. Two of these WW domains, in the proteins Fbp11
(PRPF40A; 612941) and Fbp21, are strikingly similar to those found in
the yeast splicing factor PRP40. Pre-mRNA splicing requires the bridging
of the 5-prime and 3-prime ends of the intron. In yeast, this bridging
involves interactions between the WW domains in the splicing factor
PRP40 and a proline-rich domain in the branchpoint-binding protein BBP.
By searching an EST database with the mouse Fbp21 sequence, Bedford et
al. (1998) identified ESTs encoding human FBP21, which has been named
WBP4. The predicted 376-amino acid FBP21 protein contains an N-terminal
zinc finger motif and 2 WW domains. Western blot analysis of in vitro
translated FBP21 protein and of HeLa cell extracts showed that FBP21
migrates as a 58-kD polypeptide. Immunofluorescence studies of HeLa
cells indicated that endogenous FBP21 is exclusively localized to the
nucleus and concentrated in a punctate pattern. In addition, FBP21
colocalized with the essential pre-mRNA splicing factor SC35 (600813).
GENE FUNCTION
Bedford et al. (1998) demonstrated that FBP21 is present in the
spliceosomal complex A. Mouse Fbp21 interacted directly with the SF1/BBP
protein, the U1 snRNP protein U1C (603522), and the core snRNP proteins
SmB and SmB-prime (SNRPB; 182282). These interactions were mediated by
the WW domains of Fbp21, which recognized a proline-, glycine-, and
methionine-rich (PGM) motif in the splicing factors. Immunoprecipitation
assays showed that Fbp21 associates with U2 snRNPs (e.g., SNRPB2;
603520). The authors concluded that FBP21 is a general spliceosomal
protein that may play a role in cross-intron bridging of U1 and U2
snRNPs in the mammalian A complex.
*FIELD* RF
1. Bedford, M. T.; Reed, R.; Leder, P.: WW domain-mediated interactions
reveal a spliceosome-associated protein that binds a third class of
proline-rich motif: the proline glycine and methionine-rich motif. Proc.
Nat. Acad. Sci. 95: 10602-10607, 1998.
2. Chan, D. C.; Bedford, M. T.; Leder, P.: Formin binding proteins
bear WWP/WW domains that bind proline-rich peptides and functionally
resemble SH3 domains. EMBO J. 15: 1045-1054, 1996.
*FIELD* CD
Patti M. Sherman: 5/19/2000
*FIELD* ED
wwang: 04/02/2010
psherman: 6/8/2000
mcapotos: 6/6/2000
mcapotos: 6/5/2000
psherman: 5/22/2000