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Q99661 (KIF2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF2C
Alternative name(s):
Kinesin-like protein 6
Mitotic centromere-associated kinesin
Short name=MCAK
Gene names
Name:KIF2C
Synonyms:KNSL6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16 Ref.21

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. 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. Ref.9 Ref.14 Ref.15 Ref.21

Subcellular location

Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Chromosomecentromere. Chromosomecentromerekinetochore. Note: Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1 By similarity. Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGOL2. Ref.10 Ref.11 Ref.14

Tissue specificity

Expressed at high levels in thymus and testis, at low levels in small intestine, the mucosal lining of colon, and placenta, and at very low levels in spleen and ovary; expression is not detected in prostate, peripheral blood Leukocytes, heart, brain, lung, liver, skeletal muscle, kidney or pancreas. Isoform 2 is testis-specific. Ref.1 Ref.2

Developmental stage

Isoform 2 is expressed in fetal testis. Ref.2

Domain

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. Ref.14

Post-translational modification

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

Ubiquitinated. Ref.18

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
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

establishment or maintenance of microtubule cytoskeleton polarity

Inferred from mutant phenotype PubMed 14718566. Source: HGNC

metabolic process

Traceable author statement Ref.1. Source: GOC

microtubule depolymerization

Inferred from direct assay Ref.21. Source: UniProtKB

microtubule-based movement

Traceable author statement. Source: Reactome

mitosis

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

regulation of chromosome segregation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from direct assay Ref.10. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Traceable author statement Ref.1. Source: ProtInc

microtubule cytoskeleton

Inferred from direct assay. Source: LIFEdb

microtubule plus-end

Inferred from direct assay Ref.21. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

centromeric DNA binding

Traceable author statement Ref.1. Source: ProtInc

microtubule motor activity

Traceable author statement Ref.1. Source: ProtInc

microtubule plus-end binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAPRE1Q156915EBI-1642317,EBI-1004115
MTUS2Q5JR594EBI-1642317,EBI-742948

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99661-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99661-2)

Also known as: tsMCAK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKE → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 725724Kinesin-like protein KIF2C
PRO_0000125418

Regions

Domain255 – 518264Kinesin-motor
Nucleotide binding348 – 3558ATP
Region2 – 254253Globular Potential
Region207 – 23832Negative regulator of microtubule-binding By similarity
Coiled coil618 – 65841 Potential
Motif98 – 1014Microtubule tip localization signal
Motif415 – 4184Nuclear localization signal Potential

Sites

Binding site2641ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.22
Modified residue221Phosphoserine Ref.19
Modified residue951Phosphoserine; by AURKB Ref.10
Modified residue1091Phosphoserine By similarity
Modified residue1111Phosphoserine By similarity
Modified residue1151Phosphoserine By similarity
Modified residue1661Phosphoserine Ref.13
Modified residue1921Phosphoserine By similarity
Modified residue6211Phosphoserine Ref.19
Modified residue6331Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 5555MAMDS…TKGKE → M in isoform 2.
VSP_002866
Natural variant4491I → L. Ref.1 Ref.2 Ref.5
Corresponds to variant rs4342887 [ dbSNP | Ensembl ].
VAR_049683

Experimental info

Mutagenesis951S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-109 and E-111. Ref.14
Mutagenesis100 – 1012IP → NN: Loss of interaction with MAPRE1 and association with microtubule growing ends.
Mutagenesis1091S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-111. Ref.14
Mutagenesis1111S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-109. Ref.14
Sequence conflict6981R → P in AAH08764. Ref.8

Secondary structure

...................................................... 725
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 5BDECC133AB4B55C

FASTA72581,313
        10         20         30         40         50         60 
MAMDSSLQAR LFPGLAIKIQ RSNGLIHSAN VRTVNLEKSC VSVEWAEGGA TKGKEIDFDD 

        70         80         90        100        110        120 
VAAINPELLQ LLPLHPKDNL PLQENVTIQK QKRRSVNSKI PAPKESLRSR STRMSTVSEL 

       130        140        150        160        170        180 
RITAQENDME VELPAAANSR KQFSVPPAPT RPSCPAVAEI PLRMVSEEME EQVHSIRGSS 

       190        200        210        220        230        240 
SANPVNSVRR KSCLVKEVEK MKNKREEKKA QNSEMRMKRA QEYDSSFPNW EFARMIKEFR 

       250        260        270        280        290        300 
ATLECHPLTM TDPIEEHRIC VCVRKRPLNK QELAKKEIDV ISIPSKCLLL VHEPKLKVDL 

       310        320        330        340        350        360 
TKYLENQAFC FDFAFDETAS NEVVYRFTAR PLVQTIFEGG KATCFAYGQT GSGKTHTMGG 

       370        380        390        400        410        420 
DLSGKAQNAS KGIYAMASRD VFLLKNQPCY RKLGLEVYVT FFEIYNGKLF DLLNKKAKLR 

       430        440        450        460        470        480 
VLEDGKQQVQ VVGLQEHLVN SADDVIKMID MGSACRTSGQ TFANSNSSRS HACFQIILRA 

       490        500        510        520        530        540 
KGRMHGKFSL VDLAGNERGA DTSSADRQTR MEGAEINKSL LALKECIRAL GQNKAHTPFR 

       550        560        570        580        590        600 
ESKLTQVLRD SFIGENSRTC MIATISPGIS SCEYTLNTLR YADRVKELSP HSGPSGEQLI 

       610        620        630        640        650        660 
QMETEEMEAC SNGALIPGNL SKEEEELSSQ MSSFNEAMTQ IRELEEKAME ELKEIIQQGP 

       670        680        690        700        710        720 
DWLELSEMTE QPDYDLETFV NKAESALAQQ AKHFSALRDV IKALRLAMQL EEQASRQISS 


KKRPQ 

« Hide

Isoform 2 (tsMCAK) [UniParc].

Checksum: 6A493B16911472C8
Show »

FASTA67175,561

References

« Hide 'large scale' references
[1]"Cloning and expression of human mitotic centromere-associated kinesin gene."
Kim I.-G., Jun D.Y., Sohn U., Kim Y.H.
Biochim. Biophys. Acta 1359:181-186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-449, TISSUE SPECIFICITY.
Tissue: T-cell.
[2]"Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in human testis."
Cheng L.J., Zhou Z.M., Li J.M., Zhu H., Zhu H., Zhou Y.D., Wang L.R., Lin M., Sha J.H.
Life Sci. 71:2741-2757(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-449, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Testis.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"MCAK/KIF2c V1."
Katagiri T., Shimo A.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-449.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Kidney and Uterus.
[9]"Human CENP-H multimers colocalize with CENP-A and CENP-C at active centromere-kinetochore complexes."
Sugata N., Li S., Earnshaw W.C., Yen T.J., Yoda K., Masumoto H., Munekata E., Warburton P.E., Todokoro K.
Hum. Mol. Genet. 9:2919-2926(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CENPH.
[10]"Aurora B regulates MCAK at the mitotic centromere."
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K., Wordeman L., Swedlow J.R.
Dev. Cell 6:253-268(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-95 BY AURKB, SUBCELLULAR LOCATION.
[11]"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF SER-95; 100-ILE-PRO-101; SER-109 AND SER-111.
[15]"TIP150 interacts with and targets MCAK at the microtubule plus ends."
Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F., Yao X.
EMBO Rep. 10:857-865(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTUS2 AND MAPRE1.
[16]"Genome stability is ensured by temporal control of kinetochore-microtubule dynamics."
Bakhoum S.F., Thompson S.L., Manning A.L., Compton D.A.
Nat. Cell Biol. 11:27-35(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-621 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases."
Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A., Medema R.H.
Curr. Biol. 21:1356-1365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KIF18B.
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[23]"Crystal structure of the KIF2C motor domain."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 225-593 IN COMPLEX WITH ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63743 mRNA. Translation: AAC27660.1.
AY026505 mRNA. Translation: AAK20168.1.
BT006759 mRNA. Translation: AAP35405.1.
CR450302 mRNA. Translation: CAG29298.1.
AB264115 mRNA. Translation: BAG50306.1.
AL592166 Genomic DNA. Translation: CAI12997.1.
AL592166 Genomic DNA. Translation: CAI12999.1.
CH471059 Genomic DNA. Translation: EAX07025.1.
BC008764 mRNA. Translation: AAH08764.1.
BC014924 mRNA. Translation: AAH14924.1.
RefSeqNP_006836.2. NM_006845.3.
XP_005270453.1. XM_005270396.1.
UniGeneHs.720061.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HEHX-ray2.15A225-593[»]
ProteinModelPortalQ99661.
SMRQ99661. Positions 192-587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116195. 15 interactions.
IntActQ99661. 12 interactions.
MINTMINT-4725759.
STRING9606.ENSP00000361298.

Chemistry

BindingDBQ99661.
ChEMBLCHEMBL5967.

PTM databases

PhosphoSiteQ99661.

Polymorphism databases

DMDM20141607.

Proteomic databases

PaxDbQ99661.
PRIDEQ99661.

Protocols and materials databases

DNASU11004.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372217; ENSP00000361291; ENSG00000142945. [Q99661-2]
ENST00000372224; ENSP00000361298; ENSG00000142945. [Q99661-1]
GeneID11004.
KEGGhsa:11004.
UCSCuc001cmg.4. human. [Q99661-1]
uc001cmh.4. human. [Q99661-2]

Organism-specific databases

CTD11004.
GeneCardsGC01P045208.
HGNCHGNC:6393. KIF2C.
HPAHPA006432.
MIM604538. gene.
neXtProtNX_Q99661.
PharmGKBPA30182.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG003875.
InParanoidQ99661.
KOK10393.
OMADETASNE.
PhylomeDBQ99661.
TreeFamTF105222.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ99661.
BgeeQ99661.
CleanExHS_KIF2C.
GenevestigatorQ99661.

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

EvolutionaryTraceQ99661.
GeneWikiKIF2C.
GenomeRNAi11004.
NextBio41799.
PROQ99661.
SOURCESearch...

Entry information

Entry nameKIF2C_HUMAN
AccessionPrimary (citable) accession number: Q99661
Secondary accession number(s): B3ITR9 expand/collapse secondary AC list , Q5JR88, Q6ICU1, Q96C18, Q96HB8, Q9BWV8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM