CIN8_YEAST
ID CIN8_YEAST Reviewed; 1000 AA.
AC P27895; D3DLI9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Kinesin-like protein CIN8;
DE AltName: Full=Chromosome instability protein 8;
GN Name=CIN8; Synonyms=KSL2; OrderedLocusNames=YEL061C;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1618897; DOI=10.1083/jcb.118.1.109;
RA Hoyt M.A., He L., Loo K.K., Saunders W.S.;
RT "Two Saccharomyces cerevisiae kinesin-related gene products required for
RT mitotic spindle assembly.";
RL J. Cell Biol. 118:109-120(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 983-1000.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7867803; DOI=10.1016/0014-5793(95)00038-b;
RA Rousselet G., Simon M., Ripoche P., Buhler J.-M.;
RT "A second nitrogen permease regulator in Saccharomyces cerevisiae.";
RL FEBS Lett. 359:215-219(1995).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1643659; DOI=10.1016/0092-8674(92)90169-d;
RA Saunders W.S., Hoyt M.A.;
RT "Kinesin-related proteins required for structural integrity of the mitotic
RT spindle.";
RL Cell 70:451-458(1992).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-972, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for assembly of the mitotic spindle. Interacts with
CC spindle microtubules to produce an outwardly directed force acting upon
CC the poles. Following spindle assembly, CIN8 and KIP1 apparently act to
CC oppose a force that draws separated poles back together. This force
CC seems to be mediated by KAR3. {ECO:0000269|PubMed:1618897,
CC ECO:0000269|PubMed:1643659}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Mitochondrion.
CC Note=Spindle microtubules that lie between the poles.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB65026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA77885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M90522; AAA34496.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z11859; CAA77885.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18795; AAB65026.1; ALT_INIT; Genomic_DNA.
DR EMBL; X79105; CAA55722.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07593.1; -; Genomic_DNA.
DR PIR; S50528; B42641.
DR RefSeq; NP_010853.2; NM_001178876.1.
DR AlphaFoldDB; P27895; -.
DR SMR; P27895; -.
DR BioGRID; 36668; 334.
DR DIP; DIP-3004N; -.
DR ELM; P27895; -.
DR IntAct; P27895; 10.
DR MINT; P27895; -.
DR STRING; 4932.YEL061C; -.
DR CarbonylDB; P27895; -.
DR iPTMnet; P27895; -.
DR MaxQB; P27895; -.
DR PaxDb; P27895; -.
DR PRIDE; P27895; -.
DR EnsemblFungi; YEL061C_mRNA; YEL061C; YEL061C.
DR GeneID; 856648; -.
DR KEGG; sce:YEL061C; -.
DR SGD; S000000787; CIN8.
DR VEuPathDB; FungiDB:YEL061C; -.
DR eggNOG; KOG0243; Eukaryota.
DR GeneTree; ENSGT00940000155921; -.
DR HOGENOM; CLU_001485_33_3_1; -.
DR InParanoid; P27895; -.
DR OMA; QMNSKTY; -.
DR BioCyc; YEAST:G3O-30176-MON; -.
DR Reactome; R-SCE-983189; Kinesins.
DR PRO; PR:P27895; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P27895; protein.
DR GO; GO:0000235; C:astral microtubule; IMP:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IGI:SGD.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:SGD.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IMP:SGD.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:SGD.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:SGD.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:SGD.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR GO; GO:0033047; P:regulation of mitotic sister chromatid segregation; IDA:SGD.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 2.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitochondrion; Mitosis; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1000
FT /note="Kinesin-like protein CIN8"
FT /id="PRO_0000125367"
FT DOMAIN 36..477
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 518..615
FT /evidence="ECO:0000255"
FT COILED 860..904
FT /evidence="ECO:0000255"
FT COMPBIAS 220..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 216
FT /note="D -> A (in Ref. 1; AAA34496/CAA77885)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="Q -> H (in Ref. 1; AAA34496/CAA77885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1000 AA; 113311 MW; B33141C45748CE67 CRC64;
MPAENQNTGQ DRSSNSISKN GNSQVGCHTV PNEELNITVA VRCRGRNERE ISMKSSVVVN
VPDITGSKEI SINTTGDTGI TAQMNAKRYT VDKVFGPGAS QDLIFDEVAG PLFQDFIKGY
NCTVLVYGMT STGKTYTMTG DEKLYNGELS DAAGIIPRVL LKLFDTLELQ QNDYVVKCSF
IELYNEELKD LLDSNSNGSS NTGFDGQFMK KLRIFDSSTA NNTTSNSASS SRSNSRNSSP
RSLNDLTPKA ALLRKRLRTK SLPNTIKQQY QQQQAVNSRN NSSSNSGSTT NNASSNTNTN
NGQRSSMAPN DQTNGIYIQN LQEFHITNAM EGLNLLQKGL KHRQVASTKM NDFSSRSHTI
FTITLYKKHQ DELFRISKMN LVDLAGSENI NRSGALNQRA KEAGSINQSL LTLGRVINAL
VDKSGHIPFR ESKLTRLLQD SLGGNTKTAL IATISPAKVT SEETCSTLEY ASKAKNIKNK
PQLGSFIMKD ILVKNITMEL AKIKSDLLST KSKEGIYMSQ DHYKNLNSDL ESYKNEVQEC
KREIESLTSK NALLVKDKLK SKETIQSQNC QIESLKTTID HLRAQLDKQH KTEIEISDFN
NKLQKLTEVM QMALHDYKKR ELDLNQKFEM HITKEIKKLK STLFLQLNTM QQESILQETN
IQPNLDMIKN EVLTLMRTMQ EKAELMYKDC VKKILNESPK FFNVVIEKID IIRVDFQKFY
KNIAENLSDI SEENNNMKQY LKNHFFKNNH QELLNRHVDS TYENIEKRTN EFVENFKKVL
NDHLDENKKL IMQNLTTATS AVIDQEMDLF EPKRVKWENS FDLINDCDSM NNEFYNSMAA
TLSQIKSTVD TSSNSMNESI SVMKGQVEES ENAISLLKNN TKFNDQFEQL INKHNMLKDN
IKNSITSTHS HITNVDDIYN TIENIMKNYG NKENATKDEM IENILKEIPN LSKKMPLRLS
NINSNSVQSV ISPKKHAIED ENKSSENVDN EGSRKMLKIE
