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Protein

Kinesin-like protein KIF2C

Gene

Kif2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei260 – 2601ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi344 – 3518ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_316383. MHC class II antigen presentation.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342780. Kinesins.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF2C
Alternative name(s):
Mitotic centromere-associated kinesin
Short name:
MCAK
Gene namesi
Name:Kif2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1921054. Kif2c.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Nucleus By similarity
  • Chromosomecentromere By similarity
  • Chromosomecentromerekinetochore By similarity

  • Note: Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1. Association with microtubule plus ends is also mediated by interaction with KIF18B (By similarity). Centromeric localization requires the presence of BUB1 and SGOL2 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi293 – 2931K → A: Loss of microtubule depolymerization activity. 1 Publication
Mutagenesisi294 – 2941V → A: Loss of microtubule depolymerization activity. 1 Publication
Mutagenesisi295 – 2951D → A: Loss of microtubule depolymerization activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Kinesin-like protein KIF2CPRO_0000125420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei92 – 921Phosphoserine; by AURKBBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei112 – 1121PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei626 – 6261PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by AURKB, regulates association with centromeres and kinetochores and the microtubule depolymerization activity.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ922S8.
PaxDbiQ922S8.
PRIDEiQ922S8.

PTM databases

PhosphoSiteiQ922S8.

Expressioni

Gene expression databases

BgeeiQ922S8.
CleanExiMM_KIF2C.
ExpressionAtlasiQ922S8. baseline and differential.
GenevisibleiQ922S8. MM.

Interactioni

Subunit structurei

Interacts with CENPH. Interacts with MTUS2/TIP150; the interaction is direct. Interacts with MAPRE1; the interaction is direct, regulated by phosphorylation and is probably required for targeting to growing microtubule plus ends (By similarity). 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).By similarity

Protein-protein interaction databases

BioGridi216265. 2 interactions.
STRINGi10090.ENSMUSP00000064261.

Structurei

Secondary structure

1
721
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi226 – 23914Combined sources
Turni243 – 2475Combined sources
Beta strandi255 – 2617Combined sources
Helixi266 – 2705Combined sources
Beta strandi281 – 29212Combined sources
Beta strandi298 – 3069Combined sources
Beta strandi308 – 3114Combined sources
Helixi317 – 3237Combined sources
Helixi326 – 3283Combined sources
Helixi329 – 3335Combined sources
Beta strandi337 – 3459Combined sources
Helixi350 – 3556Combined sources
Helixi365 – 3673Combined sources
Helixi369 – 38113Combined sources
Helixi384 – 3874Combined sources
Beta strandi392 – 40110Combined sources
Beta strandi404 – 4074Combined sources
Turni408 – 4125Combined sources
Beta strandi414 – 4196Combined sources
Beta strandi421 – 4233Combined sources
Beta strandi425 – 4284Combined sources
Beta strandi433 – 4375Combined sources
Helixi438 – 45013Combined sources
Beta strandi465 – 48824Combined sources
Helixi506 – 5083Combined sources
Helixi509 – 52618Combined sources
Helixi539 – 5435Combined sources
Helixi546 – 5494Combined sources
Beta strandi550 – 56112Combined sources
Helixi565 – 5673Combined sources
Helixi568 – 58215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8JX-ray3.24A183-585[»]
1V8KX-ray2.25A183-585[»]
ProteinModelPortaliQ922S8.
SMRiQ922S8. Positions 224-585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922S8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 584331Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 250250GlobularSequence AnalysisAdd
BLAST
Regioni203 – 23432Negative regulator of microtubule-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili614 – 65239Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi95 – 984Microtubule tip localization signal

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

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

eggNOGiCOG5059.
GeneTreeiENSGT00790000122962.
HOGENOMiHOG000231329.
HOVERGENiHBG003875.
InParanoidiQ922S8.
KOiK10393.
OMAiDETASNE.
OrthoDBiEOG7K9K2C.
PhylomeDBiQ922S8.
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. 1 hit.
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.

Q922S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLHARLFP GLSINIQRSN GLIHPANIST VNVEKSCVSV EWIEGGTTKG
60 70 80 90 100
KEIDIDDVAA INPELLQLLP LRPKDSLPLQ ENVTVPKQKR KSVNSKIPAL
110 120 130 140 150
KEGLRSRSTR MSTVSEVRIP AQENEMEVEL PVPTNSRKQF AIPSHPRASC
160 170 180 190 200
STVTELPLLM VSEEAEEQAH STRSTSSANP GNSVRRKSCI VKEMEKMKNK
210 220 230 240 250
REEKRAQNSE LRIKRAQEYD SSFPNWEFAR MIKEFRVTME CSPLTVTDPI
260 270 280 290 300
EEHRICVCVR KRPLNKQELA KKEIDVISVP SKCLLLVHEP KLKVDLTKYL
310 320 330 340 350
ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK
360 370 380 390 400
THTMGGDLSG KSQNASKGIY AMASRDVFLL KNQPRYRNLN LEVYVTFFEI
410 420 430 440 450
YNGKVFDLLN KKAKLRVLED SRQQVQVVGL QEYLVTCADD VIKMINMGSA
460 470 480 490 500
CRTSGQTFAN SNSSRSHACF QILLRTKGRL HGKFSLVDLA GNERGADTSS
510 520 530 540 550
ADRQTRMEGA EINKSLLALK ECIRALGQNK AHTPFRESKL TQVLRDSFIG
560 570 580 590 600
ENSRTCMIAM ISPGISSCEY TLNTLRYADR VKELSPHSGP SGEQPVQMET
610 620 630 640 650
EVMEASSNGT SLTGNEEEEL SSQMSSFNEA MTQIRELEER ALEELREIIQ
660 670 680 690 700
QGPNWLELSE MTDQPDYDLE TFVNKAESAL TQQAKQAKHF SALREVIKAL
710 720
RLAMQLEEQA SKQINSKKRH Q
Length:721
Mass (Da):81,085
Last modified:December 1, 2001 - v1
Checksum:i92FFBFFDA05B7E35
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671866 Genomic DNA. Translation: CAM26318.1.
BC006841 mRNA. Translation: AAH06841.1.
CCDSiCCDS18531.1.
RefSeqiNP_608301.3. NM_134471.4.
UniGeneiMm.247651.

Genome annotation databases

EnsembliENSMUST00000065896; ENSMUSP00000064261; ENSMUSG00000028678.
GeneIDi73804.
KEGGimmu:73804.
UCSCiuc008uie.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671866 Genomic DNA. Translation: CAM26318.1.
BC006841 mRNA. Translation: AAH06841.1.
CCDSiCCDS18531.1.
RefSeqiNP_608301.3. NM_134471.4.
UniGeneiMm.247651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8JX-ray3.24A183-585[»]
1V8KX-ray2.25A183-585[»]
ProteinModelPortaliQ922S8.
SMRiQ922S8. Positions 224-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216265. 2 interactions.
STRINGi10090.ENSMUSP00000064261.

PTM databases

PhosphoSiteiQ922S8.

Proteomic databases

MaxQBiQ922S8.
PaxDbiQ922S8.
PRIDEiQ922S8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065896; ENSMUSP00000064261; ENSMUSG00000028678.
GeneIDi73804.
KEGGimmu:73804.
UCSCiuc008uie.2. mouse.

Organism-specific databases

CTDi11004.
MGIiMGI:1921054. Kif2c.

Phylogenomic databases

eggNOGiCOG5059.
GeneTreeiENSGT00790000122962.
HOGENOMiHOG000231329.
HOVERGENiHBG003875.
InParanoidiQ922S8.
KOiK10393.
OMAiDETASNE.
OrthoDBiEOG7K9K2C.
PhylomeDBiQ922S8.
TreeFamiTF105222.

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_316383. MHC class II antigen presentation.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342780. Kinesins.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

EvolutionaryTraceiQ922S8.
NextBioi339083.
PROiQ922S8.
SOURCEiSearch...

Gene expression databases

BgeeiQ922S8.
CleanExiMM_KIF2C.
ExpressionAtlasiQ922S8. baseline and differential.
GenevisibleiQ922S8. MM.

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. 1 hit.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
  3. "A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops."
    Ogawa T., Nitta R., Okada Y., Hirokawa N.
    Cell 116:591-602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 183-585 IN COMPLEX WITH ADP AND ATP ANALOG, FUNCTION, MUTAGENESIS OF LYS-293; VAL-294 AND ASP-295.

Entry informationi

Entry nameiKIF2C_MOUSE
AccessioniPrimary (citable) accession number: Q922S8
Secondary accession number(s): A2AE71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.