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Protein

Kinesin-like protein KIF2C

Gene

Kif2c

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

Functioni

In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (PubMed:14980225). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei260ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi344 – 351ATP8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, Chromosome partition, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-983189 Kinesins

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1921054 Kif2c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi293K → A: Loss of microtubule depolymerization activity. 1 Publication1
Mutagenesisi294V → A: Loss of microtubule depolymerization activity. 1 Publication1
Mutagenesisi295D → A: Loss of microtubule depolymerization activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001254201 – 721Kinesin-like protein KIF2CAdd BLAST721

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei92Phosphoserine; by AURKBBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei112PhosphoserineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei171PhosphoserineBy similarity1
Modified residuei183PhosphoserineBy similarity1
Modified residuei188PhosphoserineBy similarity1
Modified residuei515PhosphoserineBy similarity1
Modified residuei626PhosphoserineBy similarity1

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

EPDiQ922S8
MaxQBiQ922S8
PaxDbiQ922S8
PRIDEiQ922S8

PTM databases

iPTMnetiQ922S8
PhosphoSitePlusiQ922S8

Expressioni

Gene expression databases

BgeeiENSMUSG00000028678
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. 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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216265, 17 interactors
IntActiQ922S8, 14 interactors
STRINGi10090.ENSMUSP00000064261

Structurei

Secondary structure

1721
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi226 – 239Combined sources14
Turni243 – 247Combined sources5
Beta strandi249 – 251Combined sources3
Beta strandi255 – 261Combined sources7
Helixi266 – 270Combined sources5
Beta strandi281 – 292Combined sources12
Beta strandi298 – 306Combined sources9
Beta strandi308 – 311Combined sources4
Helixi317 – 323Combined sources7
Helixi326 – 328Combined sources3
Helixi329 – 333Combined sources5
Beta strandi337 – 345Combined sources9
Helixi350 – 355Combined sources6
Helixi365 – 367Combined sources3
Helixi369 – 381Combined sources13
Helixi384 – 387Combined sources4
Beta strandi392 – 401Combined sources10
Beta strandi404 – 407Combined sources4
Turni408 – 412Combined sources5
Beta strandi414 – 419Combined sources6
Beta strandi421 – 423Combined sources3
Beta strandi425 – 428Combined sources4
Beta strandi433 – 437Combined sources5
Helixi438 – 450Combined sources13
Beta strandi465 – 488Combined sources24
Helixi506 – 508Combined sources3
Helixi509 – 526Combined sources18
Helixi539 – 543Combined sources5
Helixi546 – 549Combined sources4
Beta strandi550 – 561Combined sources12
Helixi565 – 567Combined sources3
Helixi568 – 582Combined sources15

3D structure databases

ProteinModelPortaliQ922S8
SMRiQ922S8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922S8

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini254 – 584Kinesin motorPROSITE-ProRule annotationAdd BLAST331

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 250GlobularSequence analysisAdd BLAST250
Regioni203 – 234Negative regulator of microtubule-bindingAdd BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili614 – 652Sequence analysisAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi95 – 98Microtubule tip localization signal4

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0246 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00920000148953
HOGENOMiHOG000231329
HOVERGENiHBG003875
InParanoidiQ922S8
KOiK10393
OMAiFAFDETA
OrthoDBiEOG091G06V3
PhylomeDBiQ922S8
TreeFamiTF105222

Family and domain databases

Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR027640 Kinesin-like_fam
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
PANTHERiPTHR24115 PTHR24115, 1 hit
PfamiView protein in Pfam
PF00225 Kinesin, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00129 KISc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit

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 No translation available.
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.3 mouse

Similar proteinsi

Entry informationi

Entry nameiKIF2C_MOUSE
AccessioniPrimary (citable) accession number: Q922S8
Secondary accession number(s): A2AE71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: June 20, 2018
This is version 146 of the entry and version 1 of the sequence. See 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

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