(data stored in ACNUC7421 zone)

SWISSPROT: KIP2_ASHGO

ID   KIP2_ASHGO              Reviewed;         685 AA.
AC   Q8J1G1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=Kinesin-like protein KIP2;
GN   Name=KIP2; OrderedLocusNames=ACR145W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Alberti-Segui C., Dietrich F.S., Philippsen P.;
RT   "Identification of kinesin-related proteins in the filamentous fungus
RT   Ashbya gossypii.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Required for assembly of the mitotic spindle. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
DR   EMBL; AF378570; AAN87140.1; -; Genomic_DNA.
DR   EMBL; AE016816; AAS51371.1; -; Genomic_DNA.
DR   RefSeq; NP_983547.1; NM_208900.1.
DR   SMR; Q8J1G1; -.
DR   STRING; 33169.AAS51371; -.
DR   PRIDE; Q8J1G1; -.
DR   EnsemblFungi; AAS51371; AAS51371; AGOS_ACR145W.
DR   GeneID; 4619679; -.
DR   KEGG; ago:AGOS_ACR145W; -.
DR   HOGENOM; HOG000000988; -.
DR   InParanoid; Q8J1G1; -.
DR   OMA; TSKPMID; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:1903754; C:cortical microtubule plus-end; IEA:EnsemblFungi.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; IEA:EnsemblFungi.
DR   GO; GO:0016887; F:ATPase 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:EnsemblFungi.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:EnsemblFungi.
DR   GO; GO:0030473; P:nuclear migration along microtubule; IEA:EnsemblFungi.
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   3: Inferred from homology;
DR   PRODOM; Q8J1G1.
DR   SWISS-2DPAGE; Q8J1G1.
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..685
FT                   /note="Kinesin-like protein KIP2"
FT                   /id="PRO_0000125452"
FT   DOMAIN          113..446
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   NP_BIND         185..192
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          464..486
FT                   /evidence="ECO:0000255"
FT   COILED          520..663
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   685 AA;  74696 MW;  A627E5BA4E151DDF CRC64;
     MMMVARVATA EHVGSAGASL PQTPGSRSFA LGAHPGPQKR IGGPAQGQTA FITPLVTPDG
     IYSRPSSPYM QASPLLKGSE SGGSAGSPQS PDAPSSASGA SVGNAIGSGY TGNVSVAIRI
     KPSESSTKDP WYASNDRLIH TEFGEFQFDH VFTKGVCNQE VYQALGVPII DKLFEGYNAT
     IFAYGMTGSG KTFTMSGNKQ EPGLIPQCVG NIFDRISSEH HGASLAYEVK VSYLEIYNEK
     IYDLLNYVDR QAGSTGQPSR NATGLKIRDD SKYGVKVVDL TEQLVSSHED VMKWIATGDR
     NRKTGETDFN TRSSRSHAIV LLRLTRYDLK TGSEATSTLS LCDLAGSERA VTQIVRRKEG
     AFINKSLLAL GTVIAKLSML GSQANGLQPS PAAGHIPYRD SKLTRILQPA LTGDSIITTI
     CTIDSKAESS TETTNTVRFA SRAKNIALNV RKNEMDSHAE KDTIIQNLRK QLDEQHETIV
     MLRRSAAAPS GNGSTSPLDS PGVGGTSLSE RTHNMEKGLL EVENSILKTK LEHCEKLLDK
     DMMVLEDPHV REIVEMLPLD IASVLESKVQ GMESQLRQYR VYVQKLESDL LKAQRNIITT
     HSVQFNRQST ANVQEKYGSD VDIELLLEEQ EAELMELRNA LKRKDKMIEA LQSARRLRDS
     ALSPTTTVLL QRKESVIDPR DPQPV
//

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