KIP2_YEAST
ID KIP2_YEAST Reviewed; 706 AA.
AC P28743; D6W3L3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Kinesin-like protein KIP2;
GN Name=KIP2; OrderedLocusNames=YPL155C; ORFNames=P2581;
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 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 [6]
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).
CC -!- FUNCTION: Required for assembly of the mitotic spindle.
CC -!- SUBUNIT: Might be dimeric.
CC -!- INTERACTION:
CC P28743; P33419: SPC29; NbExp=4; IntAct=EBI-9749, EBI-12041;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 656 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. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; Z11963; CAA78021.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65566.1; -; Genomic_DNA.
DR EMBL; Z73511; CAA97860.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11279.1; -; Genomic_DNA.
DR PIR; C42640; C42640.
DR RefSeq; NP_015170.1; NM_001183969.1.
DR AlphaFoldDB; P28743; -.
DR SMR; P28743; -.
DR BioGRID; 36028; 111.
DR DIP; DIP-3012N; -.
DR IntAct; P28743; 3.
DR MINT; P28743; -.
DR STRING; 4932.YPL155C; -.
DR iPTMnet; P28743; -.
DR MaxQB; P28743; -.
DR PaxDb; P28743; -.
DR PRIDE; P28743; -.
DR EnsemblFungi; YPL155C_mRNA; YPL155C; YPL155C.
DR GeneID; 855948; -.
DR KEGG; sce:YPL155C; -.
DR SGD; S000006076; KIP2.
DR VEuPathDB; FungiDB:YPL155C; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000160597; -.
DR HOGENOM; CLU_001485_24_1_1; -.
DR InParanoid; P28743; -.
DR OMA; LCTIHMG; -.
DR BioCyc; YEAST:G3O-34051-MON; -.
DR PRO; PR:P28743; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P28743; protein.
DR GO; GO:1903754; C:cortical microtubule plus-end; IDA:SGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046785; P:microtubule polymerization; IDA:SGD.
DR GO; GO:0007018; P:microtubule-based movement; IDA:SGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:SGD.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
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..706
FT /note="Kinesin-like protein KIP2"
FT /id="PRO_0000125453"
FT DOMAIN 102..493
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 507..541
FT /evidence="ECO:0000255"
FT COILED 569..589
FT /evidence="ECO:0000255"
FT COILED 612..689
FT /evidence="ECO:0000255"
FT COMPBIAS 1..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 706 AA; 78378 MW; 1E94C004C4E3BF08 CRC64;
MIQKMSPSLR RPSTRSSSGS SNIPQSPSVR STSSFSNLTR NSIRSTSNSG SQSISASSTR
SNSPLRSVSA KSDPFLHPGR IRIRRSDSIN NNSRKNDTYT GSITVTIRPK PRSVGTSRDH
VGLKSPRYSQ PRSNSHHGSN TFVRDPWFIT NDKTIVHEEI GEFKFDHVFA SHCTNLEVYE
RTSKPMIDKL LMGFNATIFA YGMTGSGKTF TMSGNEQELG LIPLSVSYLF TNIMEQSMNG
DKKFDVIISY LEIYNERIYD LLESGLEESG SRISTPSRLY MSKSNSNGLG VELKIRDDSQ
YGVKVIGLTE RRCESSEELL RWIAVGDKSR KIGETDYNAR SSRSHAIVLI RLTSTNVKNG
TSRSSTLSLC DLAGSERATG QQERRKEGSF INKSLLALGT VISKLSADKM NSVGSNIPSP
SASGSSSSSG NATNNGTSPS NHIPYRDSKL TRLLQPALSG DSIVTTICTV DTRNDAAAET
MNTLRFASRA KNVALHVSKK SIISNGNNDG DKDRTIELLR RQLEEQRRMI SELKNRSNIG
EPLTKSSNES TYKDIKATGN DGDPNLALMR AENRVLKYKL ENCEKLLDKD VVDLQDSEIM
EIVEMLPFEV GTLLETKFQG LESQIRQYRK YTQKLEDKIM ALEKSGHTAM SLTGCDGTEV
IELQKMLERK DKMIEALQSA KRLRDRALKP LINTQQSPHP VVDNDK
