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Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK)

 KIF2C_CRIGR             Reviewed;         718 AA.
P70096;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
25-OCT-2017, entry version 109.
RecName: Full=Kinesin-like protein KIF2C;
AltName: Full=Kinesin-like protein 6;
AltName: Full=Mitotic centromere-associated kinesin;
Short=MCAK;
Name=KIF2C; Synonyms=KNSL6;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7822426; DOI=10.1083/jcb.128.1.95;
Wordeman L., Mitchison T.J.;
"Identification and partial characterization of mitotic centromere-
associated kinesin, a kinesin-related protein that associates with
centromeres during mitosis.";
J. Cell Biol. 128:95-105(1995).
[2]
SEQUENCE REVISION.
Wordeman L.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-92; SER-106;
SER-108; SER-112 AND SER-186, AND MUTAGENESIS OF SER-92; SER-106;
SER-108; SER-112 AND SER-186.
PubMed=14960279; DOI=10.1016/S1534-5807(04)00025-5;
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K.,
Wordeman L., Swedlow J.R.;
"Aurora B regulates MCAK at the mitotic centromere.";
Dev. Cell 6:253-268(2004).
[4]
MUTAGENESIS OF GLY-489 AND GLU-491.
PubMed=19001124; DOI=10.1083/jcb.200805145;
Wagenbach M., Domnitz S., Wordeman L., Cooper J.;
"A kinesin-13 mutant catalytically depolymerizes microtubules in
ADP.";
J. Cell Biol. 183:617-623(2008).
[5]
INTERACTION WITH MTUS2 AND MAPRE1, MUTAGENESIS OF SER-92, AND
SUBCELLULAR LOCATION.
PubMed=19543227; DOI=10.1038/embor.2009.94;
Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F.,
Yao X.;
"TIP150 interacts with and targets MCAK at the microtubule plus
ends.";
EMBO Rep. 10:857-865(2009).
-!- FUNCTION: In complex with KIF18B, constitutes the major
microtubule plus-end depolymerizing activity in mitotic cells (By
similarity). Regulates the turnover of microtubules at the
kinetochore and functions in chromosome segregation during mitosis
(PubMed:14960279). Plays a role in chromosome congression and is
required for the lateral to end-on conversion of the chromosome-
microtubule attachment (By similarity).
{ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:14960279}.
-!- SUBUNIT: Interacts with CENPH (By similarity). Interacts with
MTUS2/TIP150; the interaction is direct (PubMed:19543227).
Interacts with MAPRE1; the interaction is direct, regulated by
phosphorylation and is probably required for targeting to growing
microtubule plus ends (PubMed:19543227). Interacts with KIF18B at
microtubule tips; this interaction increases the affinity of both
partners for microtubule plus ends and is required for robust
microtubule depolymerization. Phosphorylation by AURKA or AURKB
strongly reduces KIF18B-binding (By similarity).
{ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:19543227}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19543227}. Nucleus
{ECO:0000269|PubMed:7822426}. Chromosome, centromere
{ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:7822426}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14960279,
ECO:0000269|PubMed:7822426}. Note=Associates with the microtubule
network at the growing distal tip (the plus-end) of microtubules,
through interaction with MTUS2/TIP150 and MAPRE1
(PubMed:19543227). Association with microtubule plus ends is also
mediated by interaction with KIF18B (By similarity). Centromeric
localization requires the presence of BUB1 and SGO2 (By
similarity). {ECO:0000250|UniProtKB:Q99661,
ECO:0000269|PubMed:19543227}.
-!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
mediates interaction with MAPRE1 and targeting to the growing
microtubule plus ends. {ECO:0000250|UniProtKB:Q99661}.
-!- PTM: Phosphorylation by AURKB, regulates association with
centromeres and kinetochores and the microtubule depolymerization
activity. {ECO:0000269|PubMed:14960279}.
-!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99661}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. MCAK/KIF2 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00283}.
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EMBL; U11790; AAB17358.2; -; mRNA.
RefSeq; NP_001233671.1; NM_001246742.1.
ProteinModelPortal; P70096; -.
SMR; P70096; -.
BioGrid; 1613894; 1.
iPTMnet; P70096; -.
PRIDE; P70096; -.
Ensembl; ENSCGRT00000005321; ENSCGRP00000005229; ENSCGRG00000003827.
Ensembl; ENSCGRT00001030117; ENSCGRP00001025871; ENSCGRG00001023322.
GeneID; 100689309; -.
KEGG; cge:100689309; -.
CTD; 11004; -.
HOVERGEN; HBG003875; -.
KO; K10393; -.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:Ensembl.
GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115; PTHR24115; 1.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton;
Kinetochore; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
Phosphoprotein; Ubl conjugation.
CHAIN 1 718 Kinesin-like protein KIF2C.
/FTId=PRO_0000125417.
DOMAIN 252 582 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 342 349 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
REGION 1 248 Globular. {ECO:0000255}.
REGION 201 232 Negative regulator of microtubule-
binding. {ECO:0000250}.
COILED 613 651 {ECO:0000255}.
COILED 689 716 {ECO:0000255}.
MOTIF 95 98 Microtubule tip localization signal.
MOTIF 409 412 Nuclear localization signal.
{ECO:0000255}.
BINDING 258 258 ATP. {ECO:0000250}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:Q99661}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q99661}.
MOD_RES 92 92 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:Q99661}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000269|PubMed:14960279}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000269|PubMed:14960279}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000269|PubMed:14960279}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000250|UniProtKB:Q99661}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000269|PubMed:14960279}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:Q99661}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000250|UniProtKB:Q99661}.
MUTAGEN 92 92 S->A: Increased frequency of metaphase
figures; when associated with A-106; A-
108; A-112 and A-186.
{ECO:0000269|PubMed:14960279,
ECO:0000269|PubMed:19543227}.
MUTAGEN 92 92 S->E: Altered interaction with
MTUS2/TIP150 and association with
microtubules. Altered localization,
reduced microtubule depolymerizing
activity and increased frequency of
prometaphase figures; when associated
with E-106; E-108; E-112 and E-186.
{ECO:0000269|PubMed:14960279,
ECO:0000269|PubMed:19543227}.
MUTAGEN 106 106 S->A: Increased frequency of metaphase
figures; when associated with A-92; A-
108; A-112 and A-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 106 106 S->E: Altered localization, reduced
microtubule depolymerizing activity and
increased frequency of prometaphase
figures; when associated with E-92; E-
108; E-112 and E-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 108 108 S->A: Increased frequency of metaphase
figures; when associated with A-92; A-
106; A-112 and A-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 108 108 S->E: Altered localization, reduced
microtubule depolymerizing activity and
increased frequency of prometaphase
figures; when associated with E-92; E-
106; E-112 and E-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 112 112 S->A: Increased frequency of metaphase
figures; when associated with A-92; A-
106; A-108 and A-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 112 112 S->E: Altered localization, reduced
microtubule depolymerizing activity and
increased frequency of prometaphase
figures; when associated with E-92; E-
106; E-108 and E-186.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 186 186 S->A: Increased frequency of metaphase
figures; when associated with A-92; A-
106; A-108 and A-112.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 186 186 S->E: Altered localization, reduced
microtubule depolymerizing activity and
increased frequency of prometaphase
figures; when associated with E-92; E-
106; E-108 and E-112.
{ECO:0000269|PubMed:14960279}.
MUTAGEN 489 489 G->A: No effect on microtubule
depolymerization but unable to release
tubulin dimers to recycle catalytically.
{ECO:0000269|PubMed:19001124}.
MUTAGEN 491 491 E->A: No effect on microtubule
depolymerization but unable to release
tubulin dimers to recycle catalytically.
{ECO:0000269|PubMed:19001124}.
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


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