KIP1_YEAST
ID KIP1_YEAST Reviewed; 1111 AA.
AC P28742; D6VPT7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kinesin-like protein KIP1;
DE AltName: Full=Chromosome instability protein 9;
GN Name=KIP1; Synonyms=CIN9; OrderedLocusNames=YBL063W;
GN ORFNames=YBL0504, YBL0521;
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=1618910; DOI=10.1083/jcb.118.1.95;
RA Roof D.M., Meluh P.B., Rose M.D.;
RT "Kinesin-related proteins required for assembly of the mitotic spindle.";
RL J. Cell Biol. 118:95-108(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
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 CHARACTERIZATION.
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 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).
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 mediate by KAR3.
CC -!- SUBUNIT: Might be dimeric.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Note=Spindle
CC microtubules that lie between the poles.
CC -!- MISCELLANEOUS: Present with 56 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}.
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DR EMBL; Z11962; CAA78019.1; -; Genomic_DNA.
DR EMBL; Z23261; CAA80785.1; -; Genomic_DNA.
DR EMBL; Z35824; CAA84883.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07057.1; -; Genomic_DNA.
DR PIR; A42640; A42640.
DR RefSeq; NP_009490.1; NM_001178303.1.
DR AlphaFoldDB; P28742; -.
DR SMR; P28742; -.
DR BioGRID; 32636; 75.
DR DIP; DIP-174N; -.
DR IntAct; P28742; 1.
DR MINT; P28742; -.
DR STRING; 4932.YBL063W; -.
DR iPTMnet; P28742; -.
DR MaxQB; P28742; -.
DR PaxDb; P28742; -.
DR PRIDE; P28742; -.
DR EnsemblFungi; YBL063W_mRNA; YBL063W; YBL063W.
DR GeneID; 852216; -.
DR KEGG; sce:YBL063W; -.
DR SGD; S000000159; KIP1.
DR VEuPathDB; FungiDB:YBL063W; -.
DR eggNOG; KOG0243; Eukaryota.
DR GeneTree; ENSGT00940000175563; -.
DR HOGENOM; CLU_001485_33_2_1; -.
DR InParanoid; P28742; -.
DR BioCyc; YEAST:G3O-28960-MON; -.
DR PRO; PR:P28742; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P28742; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; TAS:SGD.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030543; P:2-micrometer plasmid partitioning; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IGI: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: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; 1.
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; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1111
FT /note="Kinesin-like protein KIP1"
FT /id="PRO_0000125369"
FT DOMAIN 52..410
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..510
FT /evidence="ECO:0000255"
FT COILED 648..670
FT /evidence="ECO:0000255"
FT COILED 710..780
FT /evidence="ECO:0000255"
FT COILED 808..828
FT /evidence="ECO:0000255"
FT COMPBIAS 1016..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1111 AA; 125795 MW; 212F8279766137FC CRC64;
MARSSLPNRR TAQFEANKRR TIAHAPSPSL SNGMHTLTPP TCNNGAATSD SNIHVYVRCR
SRNKREIEEK SSVVISTLGP QGKEIILSNG SHQSYSSSKK TYQFDQVFGA ESDQETVFNA
TAKNYIKEML HGYNCTIFAY GQTGTGKTYT MSGDINILGD VQSTDNLLLG EHAGIIPRVL
VDLFKELSSL NKEYSVKISF LELYNENLKD LLSDSEDDDP AVNDPKRQIR IFDNNNNNSS
IMVKGMQEIF INSAHEGLNL LMQGSLKRKV AATKCNDLSS RSHTVFTITT NIVEQDSKDH
GQNKNFVKIG KLNLVDLAGS ENINRSGAEN KRAQEAGLIN KSLLTLGRVI NALVDHSNHI
PYRESKLTRL LQDSLGGMTK TCIIATISPA KISMEETAST LEYATRAKSI KNTPQVNQSL
SKDTCLKDYI QEIEKLRNDL KNSRNKQGIF ITQDQLDLYE SNSILIDEQN LKIHNLREQI
KKFKENYLNQ LDINNLLQSE KEKLIAIIQN FNVDFSNFYS EIQKIHHTNL ELMNEVIQQR
DFSLENSQKQ YNTNQNMQLK ISQQVLQTLN TLQGSLNNYN SKCSEVIKGV TEELTRNVNT
HKAKHDSTLK SLLNITTNLL MNQMNELVRS ISTSLEIFQS DSTSHYRKDL NEIYQSHQQF
LKNLQNDIKS CLDSIGSSIL TSINEISQNC TTNLNSMNVL IENQQSGSSK LIKEQDLEIK
KLKNDLINER RISNQFNQQL AEMKRYFQDH VSRTRSEFHD ELNKCIDNLK DKQSKLDQDI
WQKTASIFNE TDIVVNKIHS DSIASLAHNA ENTLKTVSQN NESFTNDLIS LSRGMNMDIS
SKLRSLPINE FLNKISQTIC ETCGDDNTIA SNPVLTSIKK FQNIICSDIA LTNEKIMSLI
DEIQSQIETI SNENNINLIA INENFNSLCN FILTDYDENI MQISKTQDEV LSEHCEKLQS
LKILGMDIFT AHSIEKPLHE HTRPEASVIK ALPLLDYPKQ FQIYRDAENK SKDDTSNSRT
CIPNLSTNEN FPLSQFSPKT PVPVPDQPLP KVLIPKSINS AKSNRSKTLP NTEGTGRESQ
NNLKRRFTTE PILKGEETEN NDILQNKKLH Q
