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Protein

Kinesin-like protein KIF2B

Gene

Kif2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 3108ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-2132295. MHC class II antigen presentation.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.
R-RNO-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF2B
Gene namesi
Name:Kif2bImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1359248. Kif2b.

Subcellular locationi

  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Chromosomecentromerekinetochore By similarity

  • Note: Association with kinetochore is transient.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664Kinesin-like protein KIF2BPRO_0000306276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphothreonine; by PLK1By similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei204 – 2041Phosphoserine; by PLK1By similarity

Post-translational modificationi

Phosphorylation at Thr-125 by PLK1 is required for activity in the correction of kinetochore-microtubules attachment errors, while phosphorylation at Ser-204 also by PLK1 is required for the kinetochore localization and activity in prometaphase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5XI51.
PRIDEiQ5XI51.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003421.

Structurei

3D structure databases

ProteinModelPortaliQ5XI51.
SMRiQ5XI51. Positions 186-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini213 – 543331Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili149 – 17729Sequence analysisAdd
BLAST
Coiled coili642 – 66322Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. MCAK/KIF2 subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0246. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00830000128292.
HOGENOMiHOG000231329.
HOVERGENiHBG003875.
InParanoidiQ5XI51.
KOiK10393.
OMAiQTFCFDH.
OrthoDBiEOG7K9K2C.
PhylomeDBiQ5XI51.
TreeFamiTF105222.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XI51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQFCLPLA PRLSPLKPLK SHFTDFQVGI CVAIQRSDKR IHLAVVTEIN
60 70 80 90 100
RENSWVTVEW VEKGVKKGKK IELETVLLLN PALASTEHQR SRRPLRPVSV
110 120 130 140 150
IPATAIGDQR TATKWIAMIP HRNETPSGDS QTLVIPSNPC LMKRKKSPCL
160 170 180 190 200
REIEKLQKQR EKRRRLQLEI RARRALDINT GNPNFETMRM IEEYRRHLDS
210 220 230 240 250
SKMSRLEPPE DHRICVCVRK RPLNERETTM KDLDIITIPS HNVVMVHESK
260 270 280 290 300
QKVDLTRYLE NQTFCFDHAF DDTASNELVY QFTARPLVES IFRKGMATCF
310 320 330 340 350
AYGQTGSGKT HTMGGAFSGK AQECSKGIYA LVAQDVFLLL RTPAYEKLEL
360 370 380 390 400
KVYGTFFEIY GGKVYDLLNW KKKLQVLEDG NQQIQVVGLQ EQEVGCVEEV
410 420 430 440 450
LNLVELGNSC RTSGQTSVNA HSSRSHAVFQ LILKCGGKLH GKFSLVDLAG
460 470 480 490 500
NERGADTAKA TRKRQLEGAE INKSLLALKE CIRALGKNKS HTPFRASKLT
510 520 530 540 550
QVLRDSFIGQ NSYTCMIATI SPGMTSCENT LNTLRYANRV KELALEARPY
560 570 580 590 600
PPTDHEMPLT LENGNTNSEK SLQKDDIIQI PTVQKEEEKE SDELTSTKEP
610 620 630 640 650
AASWSRSGPW WEAIQETAEG VNCDVDFCIA QSLSILEQKI GVLTEIQKKL
660
QLLRDDLQKK SQAE
Length:664
Mass (Da):75,004
Last modified:October 2, 2007 - v2
Checksum:i109BB199948EC7FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03074230 Genomic DNA. No translation available.
BC083841 mRNA. Translation: AAH83841.1.
RefSeqiNP_001005874.2. NM_001005874.2.
UniGeneiRn.113616.

Genome annotation databases

EnsembliENSRNOT00000003421; ENSRNOP00000003421; ENSRNOG00000002535.
GeneIDi287624.
KEGGirno:287624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03074230 Genomic DNA. No translation available.
BC083841 mRNA. Translation: AAH83841.1.
RefSeqiNP_001005874.2. NM_001005874.2.
UniGeneiRn.113616.

3D structure databases

ProteinModelPortaliQ5XI51.
SMRiQ5XI51. Positions 186-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003421.

Proteomic databases

PaxDbiQ5XI51.
PRIDEiQ5XI51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003421; ENSRNOP00000003421; ENSRNOG00000002535.
GeneIDi287624.
KEGGirno:287624.

Organism-specific databases

CTDi84643.
RGDi1359248. Kif2b.

Phylogenomic databases

eggNOGiKOG0246. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00830000128292.
HOGENOMiHOG000231329.
HOVERGENiHBG003875.
InParanoidiQ5XI51.
KOiK10393.
OMAiQTFCFDH.
OrthoDBiEOG7K9K2C.
PhylomeDBiQ5XI51.
TreeFamiTF105222.

Enzyme and pathway databases

ReactomeiR-RNO-2132295. MHC class II antigen presentation.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.
R-RNO-983189. Kinesins.

Miscellaneous databases

PROiQ5XI51.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-359.
    Tissue: TestisImported.

Entry informationi

Entry nameiKIF2B_RAT
AccessioniPrimary (citable) accession number: Q5XI51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 11, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.