KIF2C_CRIGR
ID KIF2C_CRIGR Reviewed; 718 AA.
AC P70096;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Kinesin-like protein 6;
DE AltName: Full=Mitotic centromere-associated kinesin;
DE Short=MCAK;
GN Name=KIF2C; Synonyms=KNSL6;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=7822426; DOI=10.1083/jcb.128.1.95;
RA Wordeman L., Mitchison T.J.;
RT "Identification and partial characterization of mitotic centromere-
RT associated kinesin, a kinesin-related protein that associates with
RT centromeres during mitosis.";
RL J. Cell Biol. 128:95-105(1995).
RN [2]
RP SEQUENCE REVISION.
RA Wordeman L.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-92; SER-106;
RP SER-108; SER-112 AND SER-186, AND MUTAGENESIS OF SER-92; SER-106; SER-108;
RP SER-112 AND SER-186.
RX PubMed=14960279; DOI=10.1016/s1534-5807(04)00025-5;
RA Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K.,
RA Wordeman L., Swedlow J.R.;
RT "Aurora B regulates MCAK at the mitotic centromere.";
RL Dev. Cell 6:253-268(2004).
RN [4]
RP MUTAGENESIS OF GLY-489 AND GLU-491.
RX PubMed=19001124; DOI=10.1083/jcb.200805145;
RA Wagenbach M., Domnitz S., Wordeman L., Cooper J.;
RT "A kinesin-13 mutant catalytically depolymerizes microtubules in ADP.";
RL J. Cell Biol. 183:617-623(2008).
RN [5]
RP INTERACTION WITH MTUS2 AND MAPRE1, MUTAGENESIS OF SER-92, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19543227; DOI=10.1038/embor.2009.94;
RA Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F.,
RA Yao X.;
RT "TIP150 interacts with and targets MCAK at the microtubule plus ends.";
RL EMBO Rep. 10:857-865(2009).
CC -!- FUNCTION: In complex with KIF18B, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells (By similarity).
CC Regulates the turnover of microtubules at the kinetochore and functions
CC in chromosome segregation during mitosis (PubMed:14960279). Plays a
CC role in chromosome congression and is required for the lateral to end-
CC on conversion of the chromosome-microtubule attachment (By similarity).
CC {ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:14960279}.
CC -!- SUBUNIT: Interacts with CENPH (By similarity). Interacts with
CC MTUS2/TIP150; the interaction is direct (PubMed:19543227). Interacts
CC with MAPRE1; the interaction is direct, regulated by phosphorylation
CC and is probably required for targeting to growing microtubule plus ends
CC (PubMed:19543227). Interacts with KIF18B at microtubule tips; this
CC interaction increases the affinity of both partners for microtubule
CC plus ends and is required for robust microtubule depolymerization.
CC Phosphorylation by AURKA or AURKB strongly reduces KIF18B-binding (By
CC similarity). {ECO:0000250|UniProtKB:Q99661,
CC ECO:0000269|PubMed:19543227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19543227}. Nucleus {ECO:0000269|PubMed:7822426}.
CC Chromosome, centromere {ECO:0000269|PubMed:14960279,
CC ECO:0000269|PubMed:7822426}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:7822426}.
CC Note=Associates with the microtubule network at the growing distal tip
CC (the plus-end) of microtubules, through interaction with MTUS2/TIP150
CC and MAPRE1 (PubMed:19543227). Association with microtubule plus ends is
CC also mediated by interaction with KIF18B (By similarity). Centromeric
CC localization requires the presence of BUB1 and SGO2 (By similarity).
CC {ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:19543227}.
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:0000269|PubMed:14960279}.
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; U11790; AAB17358.2; -; mRNA.
DR RefSeq; NP_001233671.1; NM_001246742.1.
DR AlphaFoldDB; P70096; -.
DR SMR; P70096; -.
DR BioGRID; 1613894; 1.
DR STRING; 10029.XP_007608905.1; -.
DR iPTMnet; P70096; -.
DR PRIDE; P70096; -.
DR Ensembl; ENSCGRT00001030117; ENSCGRP00001025871; ENSCGRG00001023322.
DR GeneID; 100689309; -.
DR KEGG; cge:100689309; -.
DR CTD; 11004; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR OMA; RTTLECH; -.
DR OrthoDB; 418348at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
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; IEA:Ensembl.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Ubl conjugation.
FT CHAIN 1..718
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125417"
FT DOMAIN 252..582
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..248
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 86..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..232
FT /note="Negative regulator of microtubule-binding"
FT /evidence="ECO:0000250"
FT COILED 613..651
FT /evidence="ECO:0000255"
FT COILED 689..716
FT /evidence="ECO:0000255"
FT MOTIF 95..98
FT /note="Microtubule tip localization signal"
FT MOTIF 409..412
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 342..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
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:0000269|PubMed:14960279"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14960279"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14960279"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14960279"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99661"
FT MUTAGEN 92
FT /note="S->A: Increased frequency of metaphase figures; when
FT associated with A-106; A-108; A-112 and A-186."
FT /evidence="ECO:0000269|PubMed:14960279,
FT ECO:0000269|PubMed:19543227"
FT MUTAGEN 92
FT /note="S->E: Altered interaction with MTUS2/TIP150 and
FT association with microtubules. Altered localization,
FT reduced microtubule depolymerizing activity and increased
FT frequency of prometaphase figures; when associated with E-
FT 106; E-108; E-112 and E-186."
FT /evidence="ECO:0000269|PubMed:14960279,
FT ECO:0000269|PubMed:19543227"
FT MUTAGEN 106
FT /note="S->A: Increased frequency of metaphase figures; when
FT associated with A-92; A-108; A-112 and A-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 106
FT /note="S->E: Altered localization, reduced microtubule
FT depolymerizing activity and increased frequency of
FT prometaphase figures; when associated with E-92; E-108; E-
FT 112 and E-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 108
FT /note="S->A: Increased frequency of metaphase figures; when
FT associated with A-92; A-106; A-112 and A-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 108
FT /note="S->E: Altered localization, reduced microtubule
FT depolymerizing activity and increased frequency of
FT prometaphase figures; when associated with E-92; E-106; E-
FT 112 and E-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 112
FT /note="S->A: Increased frequency of metaphase figures; when
FT associated with A-92; A-106; A-108 and A-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 112
FT /note="S->E: Altered localization, reduced microtubule
FT depolymerizing activity and increased frequency of
FT prometaphase figures; when associated with E-92; E-106; E-
FT 108 and E-186."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 186
FT /note="S->A: Increased frequency of metaphase figures; when
FT associated with A-92; A-106; A-108 and A-112."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 186
FT /note="S->E: Altered localization, reduced microtubule
FT depolymerizing activity and increased frequency of
FT prometaphase figures; when associated with E-92; E-106; E-
FT 108 and E-112."
FT /evidence="ECO:0000269|PubMed:14960279"
FT MUTAGEN 489
FT /note="G->A: No effect on microtubule depolymerization but
FT unable to release tubulin dimers to recycle catalytically."
FT /evidence="ECO:0000269|PubMed:19001124"
FT MUTAGEN 491
FT /note="E->A: No effect on microtubule depolymerization but
FT unable to release tubulin dimers to recycle catalytically."
FT /evidence="ECO:0000269|PubMed:19001124"
SQ SEQUENCE 718 AA; 80918 MW; 16ABD8BC66AD11B2 CRC64;
MESLPARLFP GLSIKIQRSN GLIHSANIST VNVEKSCVSV EWIEGGNTKG KEIDFDDVAA
INPELLQLLP LHPKDNLPLQ ENVTVPKQKR RSVNSKIPAP KEGLRSRSTR MSTVPEVRIA
TQENEMEVEL PVATNSRKQF SVATGLPRPS CPAMTELPLS MVSEEAEEQV HPTRSTSSAN
PARRKSCIVK EMEKMKNKRE EKRAQNSEIR IKRAQEYDSS FPNWEFARMI KEFRVTIECH
PLTLTDPTEE HRICVCVRKR PLNKQELAKK EIDVISVPSK CLLFVHEPKL KVDLTKYLEN
QAFCFDFAFD ETASNEVVYR FTARPLVQTI FEGGKATCFA YGQTGSGKTH TMGGDLSGKS
QNTSKGIYAM ASRDVFLLKS QPRYRNLNLE VYVTFFEIYN GKVFDLLNKK AKLRVLEDSK
QQVQVVGLQE YLVNCADDVI KMLNMGSACR TSGQTFANSN SSRSHACFQI LLRAKGRLHG
KFSLVDLAGN ERGADTSSAD RQTRMEGAEI NKSLLALKEC IRALGQNKAH TPFRESKLTQ
VLRDSFIGEN SRTCMIAMIS PGISSCEYTL NTLRYADRVK ELSPHSGLSG EQPIQMETEE
MEASSNGTSL AVNFKEEEEL SSQMSSFNEA MSQIRELEER AMEELREIIQ QGPGWLELSE
MTDQPDYDLE TFVNKAESAL TQQTKHFSAL REVIKALRVA MQLEEQASKQ MNSKKRHQ
