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Q99661

- KIF2C_HUMAN

UniProt

Q99661 - KIF2C_HUMAN

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Protein

Kinesin-like protein KIF2C

Gene

KIF2C

Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei264 – 2641ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi348 – 3558ATP

GO - Molecular functioni

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. centromeric DNA binding Source: ProtInc
  4. microtubule motor activity Source: RefGenome
  5. microtubule plus-end binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. ATP catabolic process Source: GOC
  3. blood coagulation Source: Reactome
  4. cell proliferation Source: ProtInc
  5. chromosome segregation Source: UniProtKB-KW
  6. establishment or maintenance of microtubule cytoskeleton polarity Source: HGNC
  7. metabolic process Source: GOC
  8. microtubule-based movement Source: RefGenome
  9. microtubule depolymerization Source: UniProtKB
  10. mitotic cell cycle Source: Reactome
  11. mitotic nuclear division Source: ProtInc
  12. regulation of chromosome segregation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_25201. Kinesins.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF2C
Alternative name(s):
Kinesin-like protein 6
Mitotic centromere-associated kinesin
Short name:
MCAK
Gene namesi
Name:KIF2C
Synonyms:KNSL6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6393. KIF2C.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. cytosol Source: Reactome
  3. kinesin complex Source: RefGenome
  4. kinetochore Source: UniProtKB-KW
  5. membrane Source: UniProtKB
  6. microtubule cytoskeleton Source: LIFEdb
  7. microtubule plus-end Source: UniProtKB
  8. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-109 and E-111. 1 Publication
Mutagenesisi100 – 1012IP → NN: Loss of interaction with MAPRE1 and association with microtubule growing ends. 1 Publication
Mutagenesisi109 – 1091S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-111. 1 Publication
Mutagenesisi111 – 1111S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-109. 1 Publication

Organism-specific databases

PharmGKBiPA30182.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 725724Kinesin-like protein KIF2CPRO_0000125418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei95 – 951Phosphoserine; by AURKB1 Publication
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei621 – 6211Phosphoserine1 Publication
Modified residuei633 – 6331Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by AURKB, regulates association with centromeres and kinetochores and the microtubule depolymerization activity.3 Publications
Ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ99661.
PaxDbiQ99661.
PRIDEiQ99661.

PTM databases

PhosphoSiteiQ99661.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Isoform 2 is expressed in fetal testis.1 Publication

Gene expression databases

BgeeiQ99661.
CleanExiHS_KIF2C.
ExpressionAtlasiQ99661. baseline and differential.
GenevestigatoriQ99661.

Organism-specific databases

HPAiHPA006432.

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPRE1Q156915EBI-1642317,EBI-1004115
MTUS2Q5JR594EBI-1642317,EBI-742948

Protein-protein interaction databases

BioGridi116195. 17 interactions.
IntActiQ99661. 12 interactions.
MINTiMINT-4725759.
STRINGi9606.ENSP00000361298.

Structurei

Secondary structure

1
725
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi230 – 24213
Beta strandi258 – 2658
Helixi270 – 2745
Beta strandi285 – 29612
Beta strandi302 – 3109
Beta strandi312 – 3154
Helixi321 – 3277
Helixi330 – 3378
Beta strandi341 – 3488
Helixi354 – 3585
Helixi373 – 38513
Helixi388 – 3914
Turni392 – 3943
Beta strandi396 – 40510
Beta strandi408 – 4114
Turni412 – 4165
Beta strandi420 – 4234
Beta strandi429 – 4324
Beta strandi437 – 4415
Helixi442 – 45514
Helixi467 – 4693
Beta strandi470 – 49223
Helixi514 – 53118
Helixi539 – 5413
Helixi543 – 5475
Helixi549 – 5524
Beta strandi557 – 5659
Helixi569 – 5713
Helixi572 – 58514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HEHX-ray2.15A225-593[»]
ProteinModelPortaliQ99661.
SMRiQ99661. Positions 192-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99661.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 588331Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 254253GlobularSequence AnalysisAdd
BLAST
Regioni207 – 23832Negative regulator of microtubule-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili618 – 65841Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi98 – 1014Microtubule tip localization signal
Motifi415 – 4184Nuclear localization signalSequence Analysis

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.1 Publication

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.
GeneTreeiENSGT00760000119175.
HOVERGENiHBG003875.
InParanoidiQ99661.
KOiK10393.
OMAiDETASNE.
PhylomeDBiQ99661.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99661-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAMDSSLQAR LFPGLAIKIQ RSNGLIHSAN VRTVNLEKSC VSVEWAEGGA
60 70 80 90 100
TKGKEIDFDD VAAINPELLQ LLPLHPKDNL PLQENVTIQK QKRRSVNSKI
110 120 130 140 150
PAPKESLRSR STRMSTVSEL RITAQENDME VELPAAANSR KQFSVPPAPT
160 170 180 190 200
RPSCPAVAEI PLRMVSEEME EQVHSIRGSS SANPVNSVRR KSCLVKEVEK
210 220 230 240 250
MKNKREEKKA QNSEMRMKRA QEYDSSFPNW EFARMIKEFR ATLECHPLTM
260 270 280 290 300
TDPIEEHRIC VCVRKRPLNK QELAKKEIDV ISIPSKCLLL VHEPKLKVDL
310 320 330 340 350
TKYLENQAFC FDFAFDETAS NEVVYRFTAR PLVQTIFEGG KATCFAYGQT
360 370 380 390 400
GSGKTHTMGG DLSGKAQNAS KGIYAMASRD VFLLKNQPCY RKLGLEVYVT
410 420 430 440 450
FFEIYNGKLF DLLNKKAKLR VLEDGKQQVQ VVGLQEHLVN SADDVIKMID
460 470 480 490 500
MGSACRTSGQ TFANSNSSRS HACFQIILRA KGRMHGKFSL VDLAGNERGA
510 520 530 540 550
DTSSADRQTR MEGAEINKSL LALKECIRAL GQNKAHTPFR ESKLTQVLRD
560 570 580 590 600
SFIGENSRTC MIATISPGIS SCEYTLNTLR YADRVKELSP HSGPSGEQLI
610 620 630 640 650
QMETEEMEAC SNGALIPGNL SKEEEELSSQ MSSFNEAMTQ IRELEEKAME
660 670 680 690 700
ELKEIIQQGP DWLELSEMTE QPDYDLETFV NKAESALAQQ AKHFSALRDV
710 720
IKALRLAMQL EEQASRQISS KKRPQ
Length:725
Mass (Da):81,313
Last modified:January 23, 2002 - v2
Checksum:i5BDECC133AB4B55C
GO
Isoform 2 (identifier: Q99661-2) [UniParc]FASTAAdd to Basket

Also known as: tsMCAK

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

Show »
Length:671
Mass (Da):75,561
Checksum:i6A493B16911472C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti698 – 6981R → P in AAH08764. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti449 – 4491I → L.3 Publications
Corresponds to variant rs4342887 [ dbSNP | Ensembl ].
VAR_049683

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5555MAMDS…TKGKE → M in isoform 2. 1 PublicationVSP_002866Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS512.1. [Q99661-1]
CCDS72774.1. [Q99661-2]
RefSeqiNP_006836.2. NM_006845.3. [Q99661-1]
UniGeneiHs.720061.

Genome annotation databases

EnsembliENST00000372217; ENSP00000361291; ENSG00000142945. [Q99661-2]
ENST00000372224; ENSP00000361298; ENSG00000142945. [Q99661-1]
GeneIDi11004.
KEGGihsa:11004.
UCSCiuc001cmg.4. human. [Q99661-1]
uc001cmh.4. human. [Q99661-2]

Polymorphism databases

DMDMi20141607.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS512.1. [Q99661-1 ]
CCDS72774.1. [Q99661-2 ]
RefSeqi NP_006836.2. NM_006845.3. [Q99661-1 ]
UniGenei Hs.720061.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HEH X-ray 2.15 A 225-593 [» ]
ProteinModelPortali Q99661.
SMRi Q99661. Positions 192-587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116195. 17 interactions.
IntActi Q99661. 12 interactions.
MINTi MINT-4725759.
STRINGi 9606.ENSP00000361298.

Chemistry

BindingDBi Q99661.
ChEMBLi CHEMBL5967.

PTM databases

PhosphoSitei Q99661.

Polymorphism databases

DMDMi 20141607.

Proteomic databases

MaxQBi Q99661.
PaxDbi Q99661.
PRIDEi Q99661.

Protocols and materials databases

DNASUi 11004.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372217 ; ENSP00000361291 ; ENSG00000142945 . [Q99661-2 ]
ENST00000372224 ; ENSP00000361298 ; ENSG00000142945 . [Q99661-1 ]
GeneIDi 11004.
KEGGi hsa:11004.
UCSCi uc001cmg.4. human. [Q99661-1 ]
uc001cmh.4. human. [Q99661-2 ]

Organism-specific databases

CTDi 11004.
GeneCardsi GC01P045208.
HGNCi HGNC:6393. KIF2C.
HPAi HPA006432.
MIMi 604538. gene.
neXtProti NX_Q99661.
PharmGKBi PA30182.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
GeneTreei ENSGT00760000119175.
HOVERGENi HBG003875.
InParanoidi Q99661.
KOi K10393.
OMAi DETASNE.
PhylomeDBi Q99661.
TreeFami TF105222.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_25201. Kinesins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTracei Q99661.
GeneWikii KIF2C.
GenomeRNAii 11004.
NextBioi 41799.
PROi Q99661.
SOURCEi Search...

Gene expression databases

Bgeei Q99661.
CleanExi HS_KIF2C.
ExpressionAtlasi Q99661. baseline and differential.
Genevestigatori Q99661.

Family and domain databases

Gene3Di 3.40.850.10. 1 hit.
InterProi IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. 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. 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. 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.

Entry informationi

Entry nameiKIF2C_HUMAN
AccessioniPrimary (citable) accession number: Q99661
Secondary accession number(s): B3ITR9
, Q5JR88, Q6ICU1, Q96C18, Q96HB8, Q9BWV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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