KIF2B_HUMAN
ID KIF2B_HUMAN Reviewed; 673 AA.
AC Q8N4N8; Q96MA2; Q9BXG6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Kinesin-like protein KIF2B;
GN Name=KIF2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-112; SER-417 AND GLY-437.
RC TISSUE=Testis;
RA Sha J.H., Zhou Z.M., Li J.M.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-112; SER-417 AND
RP GLY-437.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-417 AND GLY-437.
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17538014; DOI=10.1091/mbc.e07-02-0110;
RA Manning A.L., Ganem N.J., Bakhoum S.F., Wagenbach M., Wordeman L.,
RA Compton D.A.;
RT "The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles
RT during mitosis in human cells.";
RL Mol. Biol. Cell 18:2970-2979(2007).
RN [6]
RP PHOSPHORYLATION AT THR-125 AND SER-204.
RX PubMed=22535524; DOI=10.1091/mbc.e11-12-1013;
RA Hood E.A., Kettenbach A.N., Gerber S.A., Compton D.A.;
RT "Plk1 regulates the kinesin-13 protein Kif2b to promote faithful chromosome
RT segregation.";
RL Mol. Biol. Cell 23:2264-2274(2012).
RN [7]
RP FUNCTION.
RX PubMed=23891108; DOI=10.1016/j.cub.2013.06.040;
RA Shrestha R.L., Draviam V.M.;
RT "Lateral to end-on conversion of chromosome-microtubule attachment requires
RT kinesins CENP-E and MCAK.";
RL Curr. Biol. 23:1514-1526(2013).
RN [8]
RP ERRATUM OF PUBMED:23891108.
RA Shrestha R.L., Draviam V.M.;
RL Curr. Biol. 23:2440-2441(2013).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC spindle assembly and chromosome movement. Has microtubule
CC depolymerization activity (PubMed:17538014). Plays a role in chromosome
CC congression (PubMed:23891108). {ECO:0000269|PubMed:17538014,
CC ECO:0000269|PubMed:23891108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17538014}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:17538014}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:17538014}. Note=Association
CC with kinetochore is transient.
CC -!- TISSUE SPECIFICITY: Highest level in lung. High level in ovary,
CC moderate levels in heart, kidney, placenta, skeletal muscle and spleen
CC (at protein level). Pancreas and spleen express a shorter isoform (at
CC protein level). {ECO:0000269|PubMed:17538014}.
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:0000269|PubMed:22535524}.
CC -!- MISCELLANEOUS: Osteosarcoma cells (U2OS) lacking KIF2B show
CC disorganised often monopolar mitotic spindles, severely reduced
CC velocity of chromosome movement and blocked cytokinesis. Bipolar
CC mitotic spindles can be restored by simultaneous depletion of KIF2B,
CC KIFC1 and NUMA1.
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; AF333335; AAK20830.2; -; mRNA.
DR EMBL; AK057272; BAB71406.1; -; mRNA.
DR EMBL; AC019315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033802; AAH33802.1; -; mRNA.
DR CCDS; CCDS32685.1; -.
DR RefSeq; NP_115948.4; NM_032559.4.
DR AlphaFoldDB; Q8N4N8; -.
DR SMR; Q8N4N8; -.
DR BioGRID; 124167; 50.
DR IntAct; Q8N4N8; 47.
DR MINT; Q8N4N8; -.
DR STRING; 9606.ENSP00000268919; -.
DR GlyGen; Q8N4N8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N4N8; -.
DR PhosphoSitePlus; Q8N4N8; -.
DR BioMuta; KIF2B; -.
DR DMDM; 308153588; -.
DR EPD; Q8N4N8; -.
DR jPOST; Q8N4N8; -.
DR MassIVE; Q8N4N8; -.
DR MaxQB; Q8N4N8; -.
DR PaxDb; Q8N4N8; -.
DR PeptideAtlas; Q8N4N8; -.
DR PRIDE; Q8N4N8; -.
DR ProteomicsDB; 71951; -.
DR Antibodypedia; 30815; 164 antibodies from 25 providers.
DR DNASU; 84643; -.
DR Ensembl; ENST00000268919.6; ENSP00000268919.4; ENSG00000141200.8.
DR GeneID; 84643; -.
DR KEGG; hsa:84643; -.
DR MANE-Select; ENST00000268919.6; ENSP00000268919.4; NM_032559.5; NP_115948.4.
DR UCSC; uc002iua.3; human.
DR CTD; 84643; -.
DR DisGeNET; 84643; -.
DR GeneCards; KIF2B; -.
DR HGNC; HGNC:29443; KIF2B.
DR HPA; ENSG00000141200; Tissue enriched (testis).
DR MIM; 615142; gene.
DR neXtProt; NX_Q8N4N8; -.
DR OpenTargets; ENSG00000141200; -.
DR PharmGKB; PA134928830; -.
DR VEuPathDB; HostDB:ENSG00000141200; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000163180; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q8N4N8; -.
DR OMA; EMSLQRD; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q8N4N8; -.
DR TreeFam; TF105222; -.
DR PathwayCommons; Q8N4N8; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q8N4N8; -.
DR SIGNOR; Q8N4N8; -.
DR BioGRID-ORCS; 84643; 10 hits in 1066 CRISPR screens.
DR GenomeRNAi; 84643; -.
DR Pharos; Q8N4N8; Tbio.
DR PRO; PR:Q8N4N8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N4N8; protein.
DR Bgee; ENSG00000141200; Expressed in sperm and 23 other tissues.
DR ExpressionAtlas; Q8N4N8; baseline and differential.
DR Genevisible; Q8N4N8; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
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:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
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; IMP:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP: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 1: Evidence at protein 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..673
FT /note="Kinesin-like protein KIF2B"
FT /id="PRO_0000253715"
FT DOMAIN 213..543
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 151..176
FT /evidence="ECO:0000255"
FT COILED 640..666
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:0000269|PubMed:22535524"
FT MOD_RES 204
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22535524"
FT VARIANT 112
FT /note="A -> V (in dbSNP:rs3803824)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_028717"
FT VARIANT 128
FT /note="G -> R (in dbSNP:rs9912492)"
FT /id="VAR_028718"
FT VARIANT 148
FT /note="P -> S (in dbSNP:rs59657238)"
FT /id="VAR_061279"
FT VARIANT 417
FT /note="P -> S (in dbSNP:rs4561518)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_028719"
FT VARIANT 437
FT /note="R -> G (in dbSNP:rs4561519)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_028720"
FT CONFLICT 32
FT /note="V -> A (in Ref. 1; AAK20830)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="I -> T (in Ref. 2; BAB71406)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> L (in Ref. 1; AAK20830)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> R (in Ref. 1; AAK20830)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="M -> V (in Ref. 1; AAK20830)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="T -> K (in Ref. 2; BAB71406)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="T -> A (in Ref. 1; AAK20830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 76254 MW; A0986D95FCF116F1 CRC64;
MASQFCLPES PCLSPLKPLK PHFGDIQEGI YVAIQRSDKR IHLAVVTEIN RENYWVTVEW
VEKAVKKGKK IDLETILLLN PALDSAEHPM PPPPLSPLAL APSSAIRDQR TATKWVAMIP
QKNQTASGDS LDVRVPSKPC LMKQKKSPCL WEIQKLQEQR EKRRRLQQEI RARRALDVNT
RNPNYEIMHM IEEYRRHLDS SKISVLEPPQ EHRICVCVRK RPLNQRETTL KDLDIITVPS
DNVVMVHESK QKVDLTRYLQ NQTFCFDHAF DDKASNELVY QFTAQPLVES IFRKGMATCF
AYGQTGSGKT YTMGGDFSGT AQDCSKGIYA LVAQDVFLLL RNSTYEKLDL KVYGTFFEIY
GGKVYDLLNW KKKLQVLEDG NQQIQVVGLQ EKEVCCVEEV LNLVEIGNSC RTSRQTPVNA
HSSRSHAVFQ IILKSGRIMH GKFSLVDLAG NERGADTTKA SRKRQLEGAE INKSLLALKE
CILALGQNKP HTPFRASKLT LVLRDSFIGQ NSSTCMIATI SPGMTSCENT LNTLRYANRV
KKLNVDVRPY HRGHYPIGHE APRMLKSHIG NSEMSLQRDE FIKIPYVQSE EQKEIEEVET
LPTLLGKDTT ISGKGSSQWL ENIQERAGGV HHDIDFCIAR SLSILEQKID ALTEIQKKLK
LLLADLHVKS KVE
