KIF2C_MOUSE
ID KIF2C_MOUSE Reviewed; 721 AA.
AC Q922S8; A2AE71;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Mitotic centromere-associated kinesin;
DE Short=MCAK;
GN Name=Kif2c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 183-585 IN COMPLEX WITH ADP AND
RP ATP ANALOG, FUNCTION, AND MUTAGENESIS OF LYS-293; VAL-294 AND ASP-295.
RX PubMed=14980225; DOI=10.1016/s0092-8674(04)00129-1;
RA Ogawa T., Nitta R., Okada Y., Hirokawa N.;
RT "A common mechanism for microtubule destabilizers-M type kinesins stabilize
RT curling of the protofilament using the class-specific neck and loops.";
RL Cell 116:591-602(2004).
CC -!- FUNCTION: In complex with KIF18B, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells (PubMed:14980225).
CC Regulates the turnover of microtubules at the kinetochore and functions
CC in chromosome segregation during mitosis. Plays a role in chromosome
CC congression and is required for the lateral to end-on conversion of the
CC chromosome-microtubule attachment (By similarity).
CC {ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:14980225}.
CC -!- SUBUNIT: Interacts with CENPH. Interacts with MTUS2/TIP150; the
CC interaction is direct. Interacts with MAPRE1; the interaction is
CC direct, regulated by phosphorylation and is probably required for
CC targeting to growing microtubule plus ends. Interacts with KIF18B at
CC microtubule tips; this interaction increases the affinity of both
CC partners for microtubule plus ends and is required for robust
CC microtubule depolymerization. Phosphorylation by AURKA or AURKB
CC strongly reduces KIF18B-binding. {ECO:0000250|UniProtKB:Q99661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q99661}. Nucleus {ECO:0000250|UniProtKB:P70096}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q99661}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q99661}. Note=Associates
CC with the microtubule network at the growing distal tip (the plus-end)
CC of microtubules, probably through interaction with MTUS2/TIP150 and
CC MAPRE1. Association with microtubule plus ends is also mediated by
CC interaction with KIF18B. Centromeric localization requires the presence
CC of BUB1 and SGO2. {ECO:0000250|UniProtKB:P70096,
CC ECO:0000250|UniProtKB:Q99661}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250|UniProtKB:Q99661}.
CC -!- PTM: Phosphorylation by AURKB, regulates association with centromeres
CC and kinetochores and the microtubule depolymerization activity.
CC {ECO:0000250|UniProtKB:Q99661}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99661}.
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; AL671866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006841; AAH06841.1; -; mRNA.
DR CCDS; CCDS18531.1; -.
DR RefSeq; NP_608301.3; NM_134471.4.
DR PDB; 1V8J; X-ray; 3.24 A; A=183-585.
DR PDB; 1V8K; X-ray; 2.25 A; A=183-585.
DR PDB; 3EDL; EM; 28.00 A; D=255-585.
DR PDB; 5XJA; X-ray; 3.43 A; A/B=183-585.
DR PDB; 5XJB; X-ray; 3.10 A; A/B=184-585.
DR PDBsum; 1V8J; -.
DR PDBsum; 1V8K; -.
DR PDBsum; 3EDL; -.
DR PDBsum; 5XJA; -.
DR PDBsum; 5XJB; -.
DR AlphaFoldDB; Q922S8; -.
DR SMR; Q922S8; -.
DR BioGRID; 216265; 21.
DR IntAct; Q922S8; 14.
DR STRING; 10090.ENSMUSP00000064261; -.
DR iPTMnet; Q922S8; -.
DR PhosphoSitePlus; Q922S8; -.
DR EPD; Q922S8; -.
DR jPOST; Q922S8; -.
DR MaxQB; Q922S8; -.
DR PaxDb; Q922S8; -.
DR PRIDE; Q922S8; -.
DR ProteomicsDB; 263604; -.
DR Antibodypedia; 1212; 393 antibodies from 34 providers.
DR DNASU; 73804; -.
DR Ensembl; ENSMUST00000065896; ENSMUSP00000064261; ENSMUSG00000028678.
DR GeneID; 73804; -.
DR KEGG; mmu:73804; -.
DR UCSC; uc008uie.3; mouse.
DR CTD; 11004; -.
DR MGI; MGI:1921054; Kif2c.
DR VEuPathDB; HostDB:ENSMUSG00000028678; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR InParanoid; Q922S8; -.
DR OMA; RTTLECH; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q922S8; -.
DR TreeFam; TF105222; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 73804; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Kif2c; mouse.
DR EvolutionaryTrace; Q922S8; -.
DR PRO; PR:Q922S8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q922S8; protein.
DR Bgee; ENSMUSG00000028678; Expressed in otic placode and 198 other tissues.
DR ExpressionAtlas; Q922S8; baseline and differential.
DR Genevisible; Q922S8; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISO:MGI.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; ISO:MGI.
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 3D-structure; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton;
KW Kinetochore; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..721
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125420"
FT DOMAIN 254..584
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..250
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 164..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..234
FT /note="Negative regulator of microtubule-binding"
FT COILED 614..652
FT /evidence="ECO:0000255"
FT MOTIF 95..98
FT /note="Microtubule tip localization signal"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 344..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 92
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MUTAGEN 293
FT /note="K->A: Loss of microtubule depolymerization
FT activity."
FT /evidence="ECO:0000269|PubMed:14980225"
FT MUTAGEN 294
FT /note="V->A: Loss of microtubule depolymerization
FT activity."
FT /evidence="ECO:0000269|PubMed:14980225"
FT MUTAGEN 295
FT /note="D->A: Loss of microtubule depolymerization
FT activity."
FT /evidence="ECO:0000269|PubMed:14980225"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:1V8K"
FT TURN 243..247
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5XJB"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:1V8K"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1V8J"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 465..488
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1V8J"
FT HELIX 509..526
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 539..543
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:1V8K"
FT STRAND 550..561
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:1V8K"
FT HELIX 568..582
FT /evidence="ECO:0007829|PDB:1V8K"
SQ SEQUENCE 721 AA; 81085 MW; 92FFBFFDA05B7E35 CRC64;
MESLHARLFP GLSINIQRSN GLIHPANIST VNVEKSCVSV EWIEGGTTKG KEIDIDDVAA
INPELLQLLP LRPKDSLPLQ ENVTVPKQKR KSVNSKIPAL KEGLRSRSTR MSTVSEVRIP
AQENEMEVEL PVPTNSRKQF AIPSHPRASC STVTELPLLM VSEEAEEQAH STRSTSSANP
GNSVRRKSCI VKEMEKMKNK REEKRAQNSE LRIKRAQEYD SSFPNWEFAR MIKEFRVTME
CSPLTVTDPI EEHRICVCVR KRPLNKQELA KKEIDVISVP SKCLLLVHEP KLKVDLTKYL
ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK THTMGGDLSG
KSQNASKGIY AMASRDVFLL KNQPRYRNLN LEVYVTFFEI YNGKVFDLLN KKAKLRVLED
SRQQVQVVGL QEYLVTCADD VIKMINMGSA CRTSGQTFAN SNSSRSHACF QILLRTKGRL
HGKFSLVDLA GNERGADTSS ADRQTRMEGA EINKSLLALK ECIRALGQNK AHTPFRESKL
TQVLRDSFIG ENSRTCMIAM ISPGISSCEY TLNTLRYADR VKELSPHSGP SGEQPVQMET
EVMEASSNGT SLTGNEEEEL SSQMSSFNEA MTQIRELEER ALEELREIIQ QGPNWLELSE
MTDQPDYDLE TFVNKAESAL TQQAKQAKHF SALREVIKAL RLAMQLEEQA SKQINSKKRH
Q
