ID   INCE_YEAST              Reviewed;         698 AA.
AC   P38283; D6VQF1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=Inner centromere protein SLI15;
DE            Short=INCENP-related protein SLI15;
GN   Name=SLI15; OrderedLocusNames=YBR156C; ORFNames=YBR1206;
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=8488729; DOI=10.1002/yea.320090308;
RA   Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M.,
RA   Zimmermann F.K.;
RT   "Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II
RT   including three essential open reading frames.";
RL   Yeast 9:289-293(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7483850; DOI=10.1002/yea.320110908;
RA   Rose M., Kiesau P., Proft M., Entian K.-D.;
RT   "Sequence and functional analysis of a 7.2 kb DNA fragment containing four
RT   open reading frames located between RPB5 and CDC28 on the right arm of
RT   chromosome II.";
RL   Yeast 11:865-871(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10385519; DOI=10.1083/jcb.145.7.1381;
RA   Kim J.-H., Kang J.-S., Chan C.S.M.;
RT   "Sli15 associates with the ipl1 protein kinase to promote proper chromosome
RT   segregation in Saccharomyces cerevisiae.";
RL   J. Cell Biol. 145:1381-1394(1999).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=11724818; DOI=10.1083/jcb.200105029;
RA   Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G.,
RA   Chan C.S.M.;
RT   "Functional cooperation of Dam1, Ipl1, and the inner centromere protein
RT   (INCENP)-related protein Sli15 during chromosome segregation.";
RL   J. Cell Biol. 155:763-774(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=11853667; DOI=10.1016/s0092-8674(02)00633-5;
RA   Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E.,
RA   Stark M.J.R., Nasmyth K.;
RT   "Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes
RT   chromosome bi-orientation by altering kinetochore-spindle pole
RT   connections.";
RL   Cell 108:317-329(2002).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP   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: Component of the chromosomal passenger complex (CPC), a
CC       complex that acts as a key regulator of mitosis (By similarity).
CC       Stimulates IPL1 kinase activity and facilitates its association with
CC       the mitotic spindle. Has a role in attaching the kinetochores to the
CC       microtubules and ensuring that sister kinetochores connect to opposite
CC       poles (PubMed:10385519, PubMed:11724818, PubMed:11853667).
CC       {ECO:0000250|UniProtKB:Q1MTN3, ECO:0000269|PubMed:10385519,
CC       ECO:0000269|PubMed:11724818, ECO:0000269|PubMed:11853667}.
CC   -!- SUBUNIT: Component of the CPC complex at least composed of IPL1, BIR1
CC       and SLI15. {ECO:0000250|UniProtKB:Q1MTN3}.
CC   -!- INTERACTION:
CC       P38283; P47134: BIR1; NbExp=7; IntAct=EBI-20842, EBI-3648;
CC       P38283; Q00684: CDC14; NbExp=2; IntAct=EBI-20842, EBI-4192;
CC       P38283; P24869: CLB2; NbExp=2; IntAct=EBI-20842, EBI-4515;
CC       P38283; P53267: DAM1; NbExp=2; IntAct=EBI-20842, EBI-23268;
CC       P38283; P38991: IPL1; NbExp=11; IntAct=EBI-20842, EBI-9319;
CC       P38283; Q3E7Y6: NBL1; NbExp=5; IntAct=EBI-20842, EBI-9513736;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10385519}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:10385519,
CC       ECO:0000269|PubMed:11724818}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:11724818}. Note=Associates with the mitotic spindle
CC       and the kinetochore (PubMed:11724818). {ECO:0000269|PubMed:11724818}.
CC   -!- PTM: Phosphorylated by serine/threonine protein kinase IPL1.
CC       {ECO:0000269|PubMed:11724818}.
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
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DR   EMBL; X71329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S59774; AAC60557.1; -; Genomic_DNA.
DR   EMBL; Z36025; CAA85115.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07271.1; -; Genomic_DNA.
DR   PIR; S46027; S46027.
DR   RefSeq; NP_009714.3; NM_001178504.3.
DR   AlphaFoldDB; P38283; -.
DR   SMR; P38283; -.
DR   BioGRID; 32855; 358.
DR   ComplexPortal; CPX-1900; Chromosomal passenger complex.
DR   DIP; DIP-5807N; -.
DR   FunCoup; P38283; 50.
DR   IntAct; P38283; 11.
DR   MINT; P38283; -.
DR   STRING; 4932.YBR156C; -.
DR   iPTMnet; P38283; -.
DR   PaxDb; 4932-YBR156C; -.
DR   PeptideAtlas; P38283; -.
DR   EnsemblFungi; YBR156C_mRNA; YBR156C; YBR156C.
DR   GeneID; 852453; -.
DR   KEGG; sce:YBR156C; -.
DR   AGR; SGD:S000000360; -.
DR   SGD; S000000360; SLI15.
DR   VEuPathDB; FungiDB:YBR156C; -.
DR   eggNOG; ENOG502S0AD; Eukaryota.
DR   HOGENOM; CLU_015675_0_0_1; -.
DR   InParanoid; P38283; -.
DR   OMA; RSNMFVP; -.
DR   OrthoDB; 6123at2759; -.
DR   BioCyc; YEAST:G3O-29106-MONOMER; -.
DR   BioGRID-ORCS; 852453; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38283; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38283; protein.
DR   GO; GO:0032133; C:chromosome passenger complex; IDA:SGD.
DR   GO; GO:0005828; C:kinetochore microtubule; IDA:SGD.
DR   GO; GO:0072686; C:mitotic spindle; IDA:CACAO.
DR   GO; GO:0005634; C:nucleus; EXP:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR   GO; GO:0051233; C:spindle midzone; IDA:SGD.
DR   GO; GO:0030295; F:protein kinase activator activity; IMP:SGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; IDA:CACAO.
DR   GO; GO:0051316; P:attachment of meiotic spindle microtubules to kinetochore; NAS:ComplexPortal.
DR   GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; NAS:ComplexPortal.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:SGD.
DR   GO; GO:0032185; P:septin cytoskeleton organization; IMP:SGD.
DR   GO; GO:0031134; P:sister chromatid biorientation; NAS:ComplexPortal.
DR   InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR   Pfam; PF03941; INCENP_ARK-bind; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Chromosome partition; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..698
FT                   /note="Inner centromere protein SLI15"
FT                   /id="PRO_0000071956"
FT   REGION          365..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   698 AA;  79186 MW;  827AC2AB884BA7D1 CRC64;
     MDWAIKAARK KTQRKPGSTR SIIETLDDLN NLTTDAHSEI NQRLYESSEW LRNNVYMNTL
     KYEDKKMEES LISPENTHNK MDVEFPKMKG EYELSNSQND AAKDVTKTPR NGLHNDKSIT
     PKSLRRKEVT EGMNRFSIHD TNKSPVEPLN SVKVDANESE KSSPWSPYKV EKVLRESSKT
     SESPINTKRF DNQTWAAKEE MENEPILQAL KKAESVKVKP PPNSGIARSQ RRSNMFVPLP
     NKDPLIIQHI PPTKSSGSIP KVRTVKESPI AFKKKSTINS PAIRAVENSD TAGSTKASSV
     FDRLSSIPTK SFENKISRGN VGHKYSSSSI DLTGSPMKKV SQKFKSINST DTDMQEALRD
     IFSVKNKITK NNSPKGKNSR KSSIPRFDKT SLKLTTHKKL AIIAEQKKKS KHSSDVHKTG
     SRPHSISPTK ISVDSSSPSK EVKNYYQSPV RGYLRPTKAS ISPNKNKNLT TSQTPHRLKI
     KEKTLRKLSP NIADISKPES RKSKNYRLTN LQLLPPAEAE RDDLKKKFDK RLSGIMRSQQ
     EHHRRKQEKQ KRMSHLEQDL KKQTSFSNDY KDIRLKESLA PFDNHVRDTI NKNTAFSTDN
     ILATINTVDH REIIGNVTPK IASVNDSLPE INTDSEDEAS VTLAAWAKSP YLQEQLIRQQ
     DINPQTIFGP IPPLHTDEIF PNPRLNRLKP RQIVPKRS
//