BYR4_SCHPO
ID BYR4_SCHPO Reviewed; 665 AA.
AC Q10951;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein byr4;
GN Name=byr4; ORFNames=SPAC222.10c;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=8682866; DOI=10.1083/jcb.133.6.1307;
RA Song K., Mach K.E., Chen C.-Y., Reynolds T., Albright C.F.;
RT "A novel suppressor of ras1 in fission yeast, byr4, is a dosage-dependent
RT inhibitor of cytokinesis.";
RL J. Cell Biol. 133:1307-1319(1996).
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 INTERACTION WITH CDC11.
RX PubMed=12546793; DOI=10.1016/s0960-9822(02)01417-3;
RA Krapp A., Cano E., Simanis V.;
RT "Mitotic hyperphosphorylation of the fission yeast SIN scaffold protein
RT cdc11p is regulated by the protein kinase cdc7p.";
RL Curr. Biol. 13:168-172(2003).
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-326, AND IDENTIFICATION BY
RP 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: Has an essential role in ensuring cytokinesis and septation
CC occur only once during mitosis. It does so by interacting with the ras1
CC signaling pathways, thereby suppressing them.
CC -!- SUBUNIT: Interacts with hyperphosphorylated cdc11.
CC {ECO:0000269|PubMed:12546793}.
CC -!- INTERACTION:
CC Q10951; P36618: cdc16; NbExp=6; IntAct=EBI-1997311, EBI-1997321;
CC Q10951; P87027: spg1; NbExp=7; IntAct=EBI-1997311, EBI-1999803;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16823372};
CC Peripheral membrane protein {ECO:0000269|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: To yeast BFA1. {ECO:0000305}.
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DR EMBL; U59224; AAC49372.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB60702.1; -; Genomic_DNA.
DR PIR; T46570; T46570.
DR RefSeq; NP_593149.1; NM_001018546.2.
DR AlphaFoldDB; Q10951; -.
DR BioGRID; 278423; 15.
DR IntAct; Q10951; 3.
DR MINT; Q10951; -.
DR STRING; 4896.SPAC222.10c.1; -.
DR iPTMnet; Q10951; -.
DR MaxQB; Q10951; -.
DR PaxDb; Q10951; -.
DR PRIDE; Q10951; -.
DR EnsemblFungi; SPAC222.10c.1; SPAC222.10c.1:pep; SPAC222.10c.
DR GeneID; 2541936; -.
DR KEGG; spo:SPAC222.10c; -.
DR PomBase; SPAC222.10c; byr4.
DR VEuPathDB; FungiDB:SPAC222.10c; -.
DR eggNOG; ENOG502QX1K; Eukaryota.
DR HOGENOM; CLU_421008_0_0_1; -.
DR InParanoid; Q10951; -.
DR OMA; LWELYNI; -.
DR PRO; PR:Q10951; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990334; C:Bfa1-Bub2 complex; IPI:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0035591; F:signaling adaptor activity; EXP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IEA:InterPro.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IGI:PomBase.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IGI:PomBase.
DR InterPro; IPR034586; Bfa1/Byr4.
DR PANTHER; PTHR35140; PTHR35140; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cytoplasm; Membrane; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..665
FT /note="Protein byr4"
FT /id="PRO_0000065032"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 665 AA; 75693 MW; EF576A8C535B782D CRC64;
MTEVECWDDD PDFASDVDNA SLFTQSIATT SASTSVDDGF SFDDSISRLN SLSISDVPSA
HSRVEQWNQQ VHNLNHELSS NKNRISSNVE GYEDDFSFDE EGEEGNNEFN TLRPNKYQDA
DVDEFNTIRA SETASQRPPI PFSSDTLKKT YLSSENDARY PSVSDSPYCE SEGFSSFEDD
FEIDPDTDLN SILHRKQNRM DPKASFSSVE QSSLRTPSSA HNDDGFWDDF DIDFNNETES
IFRKKIRSPN TINQKHPYIS STISYQPNVH QDAKYYPLCK DIFPSLANEN PHSDNPNLKY
SSKTLSKRDT SSHYPETLKA SSKHSSPVKG NSSISSTWTP SNLKIYHSKN SMGLMDLDAL
KTVASNSKYR TKPKNCKTYG DGTELDTLDE LPVDYEFELK LRKKQTTKVS GTPKSKHAGS
TQEWHSHTTP RSTSKHENNL NNITNSAKNE HIRSQRQHKT HAAPSKELTK ESLSNDQLSV
KEKRRHHKKA PTLIQNLNSP RTPKIVGKMR YNPTKHCWEG NDYAIRDFDT PISPSRPALI
SNISTKKGIQ VVGNMVYDPT RLRWIDNSIS GQEAEDPFSG FDDLEDTDST SQYLNENSGS
FNGSINSIIN FPDMSEIYDV GPEFEKKQFS EDIQWRKRID GWFFSFKNDD RSRLWELYNI
LNAEQ
