KIF2B_RAT
ID KIF2B_RAT Reviewed; 664 AA.
AC Q5XI51;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Kinesin-like protein KIF2B;
GN Name=Kif2b {ECO:0000312|EMBL:AAH83841.1, ECO:0000312|RGD:1359248};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH83841.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-359.
RC TISSUE=Testis {ECO:0000312|EMBL:AAH83841.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC spindle assembly and chromosome movement. Has microtubule
CC depolymerization activity. Plays a role in chromosome congression.
CC {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; AABR03074230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083841; AAH83841.1; -; mRNA.
DR RefSeq; NP_001005874.2; NM_001005874.2.
DR AlphaFoldDB; Q5XI51; -.
DR SMR; Q5XI51; -.
DR BioGRID; 252263; 1.
DR IntAct; Q5XI51; 1.
DR MINT; Q5XI51; -.
DR STRING; 10116.ENSRNOP00000003421; -.
DR PhosphoSitePlus; Q5XI51; -.
DR PaxDb; Q5XI51; -.
DR PRIDE; Q5XI51; -.
DR GeneID; 287624; -.
DR KEGG; rno:287624; -.
DR CTD; 84643; -.
DR RGD; 1359248; Kif2b.
DR eggNOG; KOG0246; Eukaryota.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q5XI51; -.
DR OMA; EMSLQRD; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q5XI51; -.
DR TreeFam; TF105222; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q5XI51; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002535; Expressed in testis and 1 other tissue.
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..664
FT /note="Kinesin-like protein KIF2B"
FT /id="PRO_0000306276"
FT DOMAIN 213..543
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 583..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..177
FT /evidence="ECO:0000255"
FT COILED 642..663
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 664 AA; 75004 MW; 109BB199948EC7FB CRC64;
MASQFCLPLA PRLSPLKPLK SHFTDFQVGI CVAIQRSDKR IHLAVVTEIN RENSWVTVEW
VEKGVKKGKK IELETVLLLN PALASTEHQR SRRPLRPVSV IPATAIGDQR TATKWIAMIP
HRNETPSGDS QTLVIPSNPC LMKRKKSPCL REIEKLQKQR EKRRRLQLEI RARRALDINT
GNPNFETMRM IEEYRRHLDS SKMSRLEPPE DHRICVCVRK RPLNERETTM KDLDIITIPS
HNVVMVHESK QKVDLTRYLE NQTFCFDHAF DDTASNELVY QFTARPLVES IFRKGMATCF
AYGQTGSGKT HTMGGAFSGK AQECSKGIYA LVAQDVFLLL RTPAYEKLEL KVYGTFFEIY
GGKVYDLLNW KKKLQVLEDG NQQIQVVGLQ EQEVGCVEEV LNLVELGNSC RTSGQTSVNA
HSSRSHAVFQ LILKCGGKLH GKFSLVDLAG NERGADTAKA TRKRQLEGAE INKSLLALKE
CIRALGKNKS HTPFRASKLT QVLRDSFIGQ NSYTCMIATI SPGMTSCENT LNTLRYANRV
KELALEARPY PPTDHEMPLT LENGNTNSEK SLQKDDIIQI PTVQKEEEKE SDELTSTKEP
AASWSRSGPW WEAIQETAEG VNCDVDFCIA QSLSILEQKI GVLTEIQKKL QLLRDDLQKK
SQAE
