BIR1_YEAST
ID BIR1_YEAST Reviewed; 954 AA.
AC P47134; D6VWQ7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein BIR1;
GN Name=BIR1; OrderedLocusNames=YJR089W; ORFNames=J1880;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10468581; DOI=10.1073/pnas.96.18.10170;
RA Uren A.G., Beilharz T., O'Connell M.J., Bugg S.J., van Driel R., Vaux D.L.,
RA Lithgow T.;
RT "Role for yeast inhibitor of apoptosis (IAP)-like proteins in cell
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10170-10175(1999).
RN [5]
RP CHARACTERIZATION, AND INTERACTION WITH NDC10 AND SKP1.
RX PubMed=10557299; DOI=10.1073/pnas.96.23.13208;
RA Yoon H.J., Carbon J.;
RT "Participation of Bir1p, a member of the inhibitor of apoptosis family, in
RT yeast chromosome segregation events.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13208-13213(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10702224; DOI=10.1074/jbc.275.10.6707;
RA Li F., Flanary P.L., Altieri D.C., Dohlman H.G.;
RT "Cell division regulation by BIR1, a member of the inhibitor of apoptosis
RT family in yeast.";
RL J. Biol. Chem. 275:6707-6711(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Seems to act in the pleiotropic control of cell division. May
CC participate in chromosome segregation events.
CC -!- SUBUNIT: Strongly interacts with CBF2/NDC10. Also interacts with
CC CBF3D/SKP1. {ECO:0000269|PubMed:10557299}.
CC -!- INTERACTION:
CC P47134; P38991: IPL1; NbExp=4; IntAct=EBI-3648, EBI-9319;
CC P47134; Q3E7Y6: NBL1; NbExp=5; IntAct=EBI-3648, EBI-9513736;
CC P47134; P38283: SLI15; NbExp=8; IntAct=EBI-3648, EBI-20842;
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DR EMBL; Z49589; CAA89616.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39312.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08873.1; -; Genomic_DNA.
DR PIR; S57108; S57108.
DR RefSeq; NP_012622.3; NM_001181746.3.
DR AlphaFoldDB; P47134; -.
DR BioGRID; 33843; 977.
DR ComplexPortal; CPX-1900; Chromosomal passenger complex.
DR DIP; DIP-5259N; -.
DR IntAct; P47134; 10.
DR MINT; P47134; -.
DR STRING; 4932.YJR089W; -.
DR CarbonylDB; P47134; -.
DR iPTMnet; P47134; -.
DR MaxQB; P47134; -.
DR PaxDb; P47134; -.
DR PRIDE; P47134; -.
DR EnsemblFungi; YJR089W_mRNA; YJR089W; YJR089W.
DR GeneID; 853551; -.
DR KEGG; sce:YJR089W; -.
DR SGD; S000003849; BIR1.
DR VEuPathDB; FungiDB:YJR089W; -.
DR eggNOG; KOG1101; Eukaryota.
DR HOGENOM; CLU_341677_0_0_1; -.
DR InParanoid; P47134; -.
DR OMA; QINMENG; -.
DR BioCyc; YEAST:G3O-31716-MON; -.
DR PRO; PR:P47134; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47134; protein.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IGI:SGD.
DR GO; GO:0005874; C:microtubule; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005819; C:spindle; IDA:SGD.
DR GO; GO:0051233; C:spindle midzone; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR CDD; cd00022; BIR; 1.
DR InterPro; IPR001370; BIR_rpt.
DR Pfam; PF00653; BIR; 2.
DR SMART; SM00238; BIR; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..954
FT /note="Protein BIR1"
FT /id="PRO_0000122388"
FT REPEAT 20..117
FT /note="BIR 1"
FT REPEAT 153..241
FT /note="BIR 2"
FT REGION 375..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 954 AA; 108667 MW; 6B20DC16065B4C39 CRC64;
MDGQIDKMEK RYSMTKLENR LRTFQDGVAL EKKKLKWSFK VIPYQAMAKL GFYFDPVIDP
KTSKLKKDSV RCCYCHRQTY NVRDCRSKRK DVLETLSNIM RQHLTVTDNK QVCLLIYLRN
KLLTDYSFHM GVSDWKNDKY FSNPDDENVI NLRKFTFQDN WPHSGSQNEH PLGIEKMVNA
GLMRYDSSIE GLGDPSMDKT LMNDTCYCIY CKQLLQGWSI NDDPMSRHYK VSQNGNCYFF
QTRNRFERIK NDNDSITKNC EVSPTLGENG KREVINTKTA SQRQCPLFES PPSSTGPQLD
DYNEKTDISV IQHNISVLDG AQGENVKRNS VEEKEQINME NGSTTLEEGN INRDVLADKK
EVISTPTAKE IKRPNVQLTQ SSSPIKKKRK FKRISPRKIF DEEDSEHSLN NNSANGDNKD
KDLVIDFTSH IIKNRDVGRK NAILDDSTDE FSFSNQGHNT FDIPIPTSSH LLKGIDSDND
NVIREDDTGI NTDTKGASSK HEKFSVNSEE DLNFSEVKLT GRDSSTNILI RTQIVDQNLG
DIDRDKVPNG GSPEVPKTHE LIRDNSEKRE AQNGEFRHQK DSTVRQSPDI LHSNKSGDNS
SNITAIPKEE QRRGNSKTSS IPADIHPKPR KNLQEPRSLS ISGKVVPTER KLDNINIDLN
FSASDFSPSS QSEQSSKSSS VISTPVASPK INLTRSLHAV KELSGLKKET DDGKYFTNKQ
ETIKILEDVS VKNETPNNEM LLFETGTPIA SQENKSRKLF DEEFSGKELD IPIDSSTVEI
KKVIKPEFEP VPSVARNLVS GTSSYPRNSR LEEQRKETST SLADNSKKGS SFNEGNNEKE
PNAAEWFKID ENRHLVKNYF HDLLKYINNN DATLANDKDG DLAFLIKQMP AEELDMTFNN
WVNLKVQSIK REFIDDCDKK LDILRRDYYT ATNFIETLED DNQLIDIAKK MGIL
