ID   KIF2B_BOVIN             Reviewed;         683 AA.
AC   A6H750;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Kinesin-like protein KIF2B;
GN   Name=KIF2B {ECO:0000250|UniProtKB:Q8N4N8};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI46114.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI46114.1};
RC   TISSUE=Liver {ECO:0000312|EMBL:AAI46114.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC       spindle assembly and chromosome movement during mitosis. Has
CC       microtubule depolymerization activity. Plays a role in chromosome
CC       congression. {ECO:0000250|UniProtKB:Q8N4N8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q8N4N8}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8N4N8}. Chromosome,
CC       centromere, kinetochore {ECO:0000250|UniProtKB:Q8N4N8}.
CC       Note=Association with kinetochore is transient.
CC       {ECO:0000250|UniProtKB:Q8N4N8}.
CC   -!- PTM: Phosphorylation at Thr-125 by PLK1 is required for activity in the
CC       correction of kinetochore-microtubules attachment errors, while
CC       phosphorylation at Ser-204 also by PLK1 is required for the kinetochore
CC       localization and activity in prometaphase.
CC       {ECO:0000250|UniProtKB:Q8N4N8}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; BC146113; AAI46114.1; -; mRNA.
DR   RefSeq; NP_001094651.1; NM_001101181.1.
DR   AlphaFoldDB; A6H750; -.
DR   SMR; A6H750; -.
DR   STRING; 9913.ENSBTAP00000023059; -.
DR   PaxDb; A6H750; -.
DR   GeneID; 538921; -.
DR   KEGG; bta:538921; -.
DR   CTD; 84643; -.
DR   eggNOG; KOG0246; Eukaryota.
DR   InParanoid; A6H750; -.
DR   OrthoDB; 418348at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..683
FT                   /note="Kinesin-like protein KIF2B"
FT                   /id="PRO_0000306275"
FT   DOMAIN          213..543
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          141..176
FT                   /evidence="ECO:0000255"
FT   COILED          640..672
FT                   /evidence="ECO:0000255"
FT   BINDING         303..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         125
FT                   /note="Phosphothreonine; by PLK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4N8"
FT   MOD_RES         204
FT                   /note="Phosphoserine; by PLK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4N8"
SQ   SEQUENCE   683 AA;  76907 MW;  2BFDE54EE7481D52 CRC64;
     MASQLFRPLT PRLSSLTPVK PHFGHLQAGI SVAIQRTDGR IHLAVVTEVR RDNAWVTVEW
     AEKGVKKGKK VALETIFLLN PALALAGPAA QGRASRSVSL APPSVIGDQR TAARWAGKIP
     QRNETPSGDS LAVRVPSSPC LMTQRKSACL REIEKLQKQR ERRRRLHREI RAQRARDADT
     GNAHYEIRRL IEECRRRLRG GRISGPEPRD GRRICVCVRK RPLNRQEATR EDLDIVTIPS
     DNVVMVHESK QKVDLTRYLE NQTFCFDHAF DDTASNELVY QFTDQPLVES IFRHGMATCF
     AYGQTGSGKT HTMGGGFSGR DQDCSKGIYA MVAQDVFLLL KTSAYEKLNL KVYGTFFEIY
     GGKVYDLLNW KKKLQVLEDG SQQIQVVGLQ EQEVCCVEDM LNLVELGNSC RTSGQTSVNA
     HSSRSHAVFQ IILKSRGKLH GKFSLVDLAG NERGADTAKA NRKRQLEGAE INKSLLALKE
     CIRALGQNKS HTPFRASKLT QVLRDSFIGQ NSSTCMIATI SPGMASCENT LNTLRYANRV
     KEITLNLRPR HRCLYPAERE MPRVLENHIR NSEMSLQGDE FIRIPCLQSE EEKETEGIKV
     LSSPLVDTTI SWKEASQWPD NKIQDTSDEV NCNVDFCIAQ LLSILEKKID ILTEIRRKLK
     LLQADIQKEN RHGEVNGERS DLK