BIR1_SCHPO
ID BIR1_SCHPO Reviewed; 997 AA.
AC O14064; Q9USG4; Q9UTZ0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein bir1;
DE AltName: Full=Chromosome segregation protein cut17;
GN Name=bir1; Synonyms=cut17, pbh1; ORFNames=SPCC962.02c, SPCP31B10.10c;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11554922; DOI=10.1046/j.1365-2443.2001.00459.x;
RA Morishita J., Matsusaka T., Goshima G., Nakamura T., Tatebe H.,
RA Yanagida M.;
RT "Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is
RT required for condensation, spindle elongation and repair.";
RL Genes Cells 6:743-763(2001).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 577-810, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION.
RX PubMed=10571085; DOI=10.1016/s0014-5793(99)01329-0;
RA Rajagopalan S., Balasubramanian M.K.;
RT "S. pombe Pbh1p: an inhibitor of apoptosis domain containing protein is
RT essential for chromosome segregation.";
RL FEBS Lett. 460:187-190(1999).
RN [5]
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 [6]
RP CHARACTERIZATION.
RX PubMed=11861551; DOI=10.1093/genetics/160.2.445;
RA Rajagopalan S., Balasubramanian M.K.;
RT "Schizosaccharomyces pombe Bir1p, a nuclear protein that localizes to
RT kinetochores and the spindle midzone, is essential for chromosome
RT condensation and spindle elongation during mitosis.";
RL Genetics 160:445-456(2002).
RN [7]
RP PHOSPHORYLATION BY ARK1.
RX PubMed=11950927; DOI=10.1091/mbc.01-07-0330;
RA Leverson J.D., Huang H.-K., Forsburg S.L., Hunter T.;
RT "The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with
RT the inner centromere protein Pic1 and mediates chromosome segregation and
RT cytokinesis.";
RL Mol. Biol. Cell 13:1132-1143(2002).
RN [8]
RP INTERACTION WITH ARK1 AND MAD3.
RX PubMed=12676091; DOI=10.1016/s0960-9822(03)00205-7;
RA Petersen J., Hagan I.M.;
RT "S. pombe aurora kinase/survivin is required for chromosome condensation
RT and the spindle checkpoint attachment response.";
RL Curr. Biol. 13:590-597(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-976 AND ALA-990.
RX PubMed=16199877; DOI=10.1128/mcb.25.20.9000-9015.2005;
RA Huang H.-K., Bailis J.M., Leverson J.D., Gomez E.B., Forsburg S.L.,
RA Hunter T.;
RT "Suppressors of Bir1p (Survivin) identify roles for the chromosomal
RT passenger protein Pic1p (INCENP) and the replication initiation factor
RT Psf2p in chromosome segregation.";
RL Mol. Cell. Biol. 25:9000-9015(2005).
RN [10]
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).
CC -!- FUNCTION: Seems to act in the pleiotropic control of cell division. Has
CC a role in chromosome segregation by recruiting condensin and ark1
CC kinase to appropriate sites as the cell progresses through mitosis.
CC Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with
CC bir1 function is required for full-scale association with kinetochores
CC and formation of a complex with mad3. {ECO:0000269|PubMed:10571085,
CC ECO:0000269|PubMed:11554922, ECO:0000269|PubMed:16199877}.
CC -!- SUBUNIT: Interacts with ark1 and mad3 to form part of the mad2 complex
CC involved in checkpoint activation. {ECO:0000269|PubMed:12676091}.
CC -!- INTERACTION:
CC O14064; O13734: sgo2; NbExp=3; IntAct=EBI-15872259, EBI-15872428;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, centromere. Note=Interacts with the outer centromeric
CC regions of the chromosomes during interphase. After chromatid
CC separation moves to the middle of the spindle.
CC -!- PTM: Phosphorylated by ark1. {ECO:0000269|PubMed:11950927}.
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DR EMBL; AB031034; BAA83415.1; -; mRNA.
DR EMBL; CU329672; CAA20434.1; -; Genomic_DNA.
DR EMBL; AB027919; BAA87223.1; -; Genomic_DNA.
DR PIR; T43523; T43523.
DR RefSeq; NP_587866.3; NM_001022859.3.
DR AlphaFoldDB; O14064; -.
DR BioGRID; 275454; 14.
DR DIP; DIP-59223N; -.
DR IntAct; O14064; 3.
DR STRING; 4896.SPCC962.02c.1; -.
DR iPTMnet; O14064; -.
DR MaxQB; O14064; -.
DR PaxDb; O14064; -.
DR PRIDE; O14064; -.
DR EnsemblFungi; SPCC962.02c.1; SPCC962.02c.1:pep; SPCC962.02c.
DR GeneID; 2538875; -.
DR KEGG; spo:SPCC962.02c; -.
DR PomBase; SPCC962.02c; bir1.
DR VEuPathDB; FungiDB:SPCC962.02c; -.
DR eggNOG; KOG1101; Eukaryota.
DR HOGENOM; CLU_300377_0_0_1; -.
DR InParanoid; O14064; -.
DR OMA; PSCPWAY; -.
DR Reactome; R-SPO-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-SPO-5675482; Regulation of necroptotic cell death.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-8948747; Regulation of PTEN localization.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:O14064; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:PomBase.
DR GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:PomBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR CDD; cd00022; BIR; 2.
DR InterPro; IPR001370; BIR_rpt.
DR Pfam; PF00653; BIR; 2.
DR SMART; SM00238; BIR; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Metal-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..997
FT /note="Protein bir1"
FT /id="PRO_0000122387"
FT REPEAT 25..99
FT /note="BIR 1"
FT REPEAT 120..194
FT /note="BIR 2"
FT REGION 217..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT MUTAGEN 976
FT /note="C->Y: In bir1-46; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:16199877"
FT MUTAGEN 990
FT /note="A->T: In cut17-275; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:16199877"
SQ SEQUENCE 997 AA; 112580 MW; 952A6BAFA5C489F4 CRC64;
MKPITSSSKR RWNRFRREMC NYSKRLDTFQ KKKWPRAKPT PETLATVGFY YNPISESNSE
ERLDNVTCYM CTKSFYDWED DDDPLKEHIT HSPSCPWAYI LSSKNNPNQN PQAAALTKCR
EQTFVDKVWP YTNRPDYHCE PSVMAASGFV YNPTADAKDA AHCLYCDINL HDWEPDDDPY
TEHKRRRADC VFFTWKDPNS LSPTKLSFLS TSNIDPEDLT EDNSILPVSP TRDSTKSHKT
LNFSPSRKNN LNARPLTMSL YTNTSEEKDS QPTRAPQSPT KPVLLTAPRR KNKSPKKSKP
AVFKPVKPIF SDEDEDDDDL TASQPFSKGI CNDSMQVAKK NFTEEIPLKE DEKDNELEHL
VSPATSVHTT VSDITGHQSV TDESDEQNNC MSTPPKIEIE SKIEEEISVV SKSKEISSSV
SSVGKEQNHT EKQVAIETPE QQKVEKEDEH LNLQGSFIEE STKQPISSKP STSSPDMTDA
ATGGRVSSSS FRDKILQTNF SPRSTIDSFS NISKKRNSEE ANDENDETNL KIPIPEKKRK
FQEVLQSKNI LVSSTEDSHE PVKVTEDSQT AIHVSKFEDL ENKSMESEQS LQLLSESEND
DKPLIDLIPL LAIKRKDNLV SGVLEKGKST STSKTKFDTS IVDFIEKPKT EISEVLPEEK
RKAICDESQT VRVSIDRGVT KTRDVSSPVS DEKSENVNHE EANSGHTVMN VHSSLDPQPI
VQPNELESGS YLKDLPDRNV GNSEKVTFQE DDINSPKLQS KNNQTVEAVN TETSDKLQEK
EANHELENIE KIEEKLTEVD KVSLSDAFPD QEIKNSRTSV QNGTRSVSKN TPEKETKVDK
IDNVSKKDVE TSPGSCETSS AFAKTYAEKE VTSINLPSVR KPLDESYYDH SISPFDPLCQ
SSFLAPQTPV KSKHALPLVE ANAPPWEPID FSSLLESPVP NPVEPNKLSE KELDMTVEQW
IKFMYAKCAK EFEEACEEKI EWLLEEGKRA EEYIQNL
