BBP_SCHPO
ID BBP_SCHPO Reviewed; 587 AA.
AC O74555;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Branchpoint-bridging protein;
DE AltName: Full=Splicing factor 1;
DE AltName: Full=Zinc finger protein bpb1;
GN Name=bpb1; Synonyms=bbp, sf1; ORFNames=SPCC962.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Potashkin J.A., Witt I.;
RT "The fission yeast homolog of the splicing factor BBP/SF1.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH U2AF59 AND U2AF23.
RX PubMed=12374752; DOI=10.1093/emboj/cdf555;
RA Huang T., Vilardell J., Query C.C.;
RT "Pre-spliceosome formation in S.pombe requires a stable complex of SF1-
RT U2AF(59)-U2AF(23).";
RL EMBO J. 21:5516-5526(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-
CC u2af23 complex has a role in the recognition of the branch site (5'-
CC UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end
CC of introns. {ECO:0000269|PubMed:12374752}.
CC -!- SUBUNIT: U2AF large subunit (u2af59), U2AF small subunit (u2af23) and
CC bpb1 interact to form a complex required for complex A formation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}.
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DR EMBL; AF073779; AAF02214.1; -; mRNA.
DR EMBL; CU329672; CAA20438.1; -; Genomic_DNA.
DR PIR; T41653; T41653.
DR RefSeq; NP_587871.1; NM_001022863.2.
DR AlphaFoldDB; O74555; -.
DR SMR; O74555; -.
DR BioGRID; 275413; 12.
DR STRING; 4896.SPCC962.06c.1; -.
DR iPTMnet; O74555; -.
DR MaxQB; O74555; -.
DR PaxDb; O74555; -.
DR PRIDE; O74555; -.
DR EnsemblFungi; SPCC962.06c.1; SPCC962.06c.1:pep; SPCC962.06c.
DR GeneID; 2538832; -.
DR KEGG; spo:SPCC962.06c; -.
DR PomBase; SPCC962.06c; bpb1.
DR VEuPathDB; FungiDB:SPCC962.06c; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_1_1_1; -.
DR InParanoid; O74555; -.
DR OMA; HYNSNTH; -.
DR PhylomeDB; O74555; -.
DR PRO; PR:O74555; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000243; C:commitment complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR031150; BBP/SF1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032570; SF1-HH.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00322; KH; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..587
FT /note="Branchpoint-bridging protein"
FT /id="PRO_0000256150"
FT DOMAIN 191..271
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 309..326
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 334..351
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 587 AA; 63622 MW; 2680FAEDF793ACF6 CRC64;
MLNSRSVGST GSNNTPLGRR RFDEKPDSLP PLPDANGMSN GYRDSYKSNS RMDHRPDGYH
DGRGRRAYRK HYWGHPTPIE EMLPSQMELE TAVKSCMTME QLELYSLNVR LEEITQKLRT
GDVVPHHRER SPSPPPQYDN HGRRLNTREI RYKKKLEDER HRIIERAMKM VPGFRAPSDY
RRPAKTQEKV YVPVKDYPEI NFIGLLIGPR GHTLKDMEAK SGAKIAIRGK GSVKEGKGRS
DPSVRGNMEE DLHCLVTADS EDKINHAIKL IDNVIQTAAS VPEGQNDLKR NQLRQLATLN
GTLRDDENQV CQNCGNVGHR RFDCPERINH TMNIVCRHCG SIGHIARDCP VRDQQPPMAD
STADREYQSL MQELGGGSAI SNGNGEPQKS IEFSESGAAS PQAGHPPPWA AASTSVSSST
SSPAPWAKPA SSAAPSNPAP WQQPAAPQSA PALSMNPSSL PPWQQPTQQS AVQPSNLVPS
QNAPFIPGTS APLPPTTFAP PGVPLPPIPG APGMPNLNMS QPPMVPPGMA LPPGMPAPFP
GYPAVPAMPG IPGATAPPGA PGSYNTSESS NLNAPPGVSM PNGYSNR
