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Q922S8 (KIF2C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF2C
Alternative name(s):
Mitotic centromere-associated kinesin
Short name=MCAK
Gene names
Name:Kif2c
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.3

Subunit structure

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.

Subcellular location

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.

Domain

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

Post-translational modification

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

Ubiquitinated By similarity.

Sequence similarities

Belongs to the kinesin-like protein family. MCAK/KIF2 subfamily.

Contains 1 kinesin-motor domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
Nucleus
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

establishment or maintenance of microtubule cytoskeleton polarity

Inferred from electronic annotation. Source: Ensembl

microtubule depolymerization

Inferred from electronic annotation. Source: Ensembl

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of chromosome segregation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome, centromeric region

Inferred from direct assay PubMed 19283064. Source: MGI

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

microtubule plus-end binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Kinesin-like protein KIF2C
PRO_0000125420

Regions

Domain251 – 514264Kinesin-motor
Nucleotide binding344 – 3518ATP
Region1 – 250250Globular Potential
Region203 – 23432Negative regulator of microtubule-binding
Coiled coil614 – 65239 Potential
Motif95 – 984Microtubule tip localization signal

Sites

Binding site2601ATP

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue921Phosphoserine; by AURKB By similarity
Modified residue1061Phosphoserine By similarity
Modified residue1081Phosphoserine By similarity
Modified residue1121Phosphoserine By similarity
Modified residue1621Phosphoserine By similarity
Modified residue1881Phosphoserine By similarity
Modified residue6261Phosphoserine By similarity

Experimental info

Mutagenesis2931K → A: Loss of microtubule depolymerization activity. Ref.3
Mutagenesis2941V → A: Loss of microtubule depolymerization activity. Ref.3
Mutagenesis2951D → A: Loss of microtubule depolymerization activity. Ref.3

Secondary structure

......................................................... 721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q922S8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 92FFBFFDA05B7E35

FASTA72181,085
        10         20         30         40         50         60 
MESLHARLFP GLSINIQRSN GLIHPANIST VNVEKSCVSV EWIEGGTTKG KEIDIDDVAA 

        70         80         90        100        110        120 
INPELLQLLP LRPKDSLPLQ ENVTVPKQKR KSVNSKIPAL KEGLRSRSTR MSTVSEVRIP 

       130        140        150        160        170        180 
AQENEMEVEL PVPTNSRKQF AIPSHPRASC STVTELPLLM VSEEAEEQAH STRSTSSANP 

       190        200        210        220        230        240 
GNSVRRKSCI VKEMEKMKNK REEKRAQNSE LRIKRAQEYD SSFPNWEFAR MIKEFRVTME 

       250        260        270        280        290        300 
CSPLTVTDPI EEHRICVCVR KRPLNKQELA KKEIDVISVP SKCLLLVHEP KLKVDLTKYL 

       310        320        330        340        350        360 
ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK THTMGGDLSG 

       370        380        390        400        410        420 
KSQNASKGIY AMASRDVFLL KNQPRYRNLN LEVYVTFFEI YNGKVFDLLN KKAKLRVLED 

       430        440        450        460        470        480 
SRQQVQVVGL QEYLVTCADD VIKMINMGSA CRTSGQTFAN SNSSRSHACF QILLRTKGRL 

       490        500        510        520        530        540 
HGKFSLVDLA GNERGADTSS ADRQTRMEGA EINKSLLALK ECIRALGQNK AHTPFRESKL 

       550        560        570        580        590        600 
TQVLRDSFIG ENSRTCMIAM ISPGISSCEY TLNTLRYADR VKELSPHSGP SGEQPVQMET 

       610        620        630        640        650        660 
EVMEASSNGT SLTGNEEEEL SSQMSSFNEA MTQIRELEER ALEELREIIQ QGPNWLELSE 

       670        680        690        700        710        720 
MTDQPDYDLE TFVNKAESAL TQQAKQAKHF SALREVIKAL RLAMQLEEQA SKQINSKKRH 


Q 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL671866 Genomic DNA. Translation: CAM26318.1.
BC006841 mRNA. Translation: AAH06841.1.
RefSeqNP_608301.3. NM_134471.4.
UniGeneMm.247651.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8JX-ray3.24A183-585[»]
1V8KX-ray2.25A183-585[»]
ProteinModelPortalQ922S8.
SMRQ922S8. Positions 189-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216265. 1 interaction.

PTM databases

PhosphoSiteQ922S8.

Proteomic databases

PaxDbQ922S8.
PRIDEQ922S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065896; ENSMUSP00000064261; ENSMUSG00000028678.
GeneID73804.
KEGGmmu:73804.
UCSCuc008uie.2. mouse.

Organism-specific databases

CTD11004.
MGIMGI:1921054. Kif2c.

Phylogenomic databases

eggNOGCOG5059.
GeneTreeENSGT00740000114912.
HOGENOMHOG000231329.
HOVERGENHBG003875.
InParanoidA2AE71.
KOK10393.
OMADETASNE.
OrthoDBEOG7K9K2C.
PhylomeDBQ922S8.
TreeFamTF105222.

Gene expression databases

ArrayExpressQ922S8.
BgeeQ922S8.
CleanExMM_KIF2C.
GenevestigatorQ922S8.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ922S8.
NextBio339083.
PROQ922S8.
SOURCESearch...

Entry information

Entry nameKIF2C_MOUSE
AccessionPrimary (citable) accession number: Q922S8
Secondary accession number(s): A2AE71
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot