Q99661 (KIF2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Protein existence	Evidence 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.20
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.20
Subcellular location	Cytoplasm › cytoskeleton By similarity. Nucleus By similarity. Chromosome › centromere. Chromosome › centromere › kinetochore. 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.
Sequence similarities	Belongs to the kinesin-like protein family. MCAK/KIF2 subfamily. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW 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 microtubule depolymerization Inferred from mutant phenotype Ref.16. Source: UniProtKB microtubule-based movement Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome regulation of chromosome segregation Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular_component	chromosome, 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 Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 725

725

Kinesin-like protein KIF2C

PRO_0000125418

Regions

Domain

255 – 518

264

Kinesin-motor

Nucleotide binding

348 – 355

8

ATP

Region

1 – 254

254

Globular Potential

Region

207 – 238

32

Negative regulator of microtubule-binding By similarity

Coiled coil

618 – 658

41

Potential

Motif

98 – 101

4

Microtubule tip localization signal

Motif

415 – 418

4

Nuclear localization signal Potential

Sites

Binding site

264

1

ATP By similarity

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.18

Modified residue

95

1

Phosphoserine; by AURKB Ref.10

Modified residue

109

1

Phosphoserine By similarity

Modified residue

111

1

Phosphoserine By similarity

Modified residue

115

1

Phosphoserine By similarity

Modified residue

166

1

Phosphoserine Ref.13

Modified residue

192

1

Phosphoserine By similarity

Modified residue

621

1

Phosphoserine Ref.18

Modified residue

633

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

1 – 55

55

MAMDS…TKGKE → M in isoform 2.

VSP_002866

Natural variant

449

1

I → L. Ref.1 Ref.2 Ref.5
Corresponds to variant rs4342887 [ dbSNP | Ensembl ].

VAR_049683

Experimental info

Mutagenesis

95

1

S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-109 and E-111. Ref.14

Mutagenesis

100 – 101

2

IP → NN: Loss of interaction with MAPRE1 and association with microtubule growing ends.

Mutagenesis

109

1

S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-111. Ref.14

Mutagenesis

111

1

S → E: Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-109. Ref.14

Sequence conflict

698

1

R → P in AAH08764. Ref.8

Secondary structure

1

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725

Helix Strand Turn

Details...

Helix

230 – 242

13

Beta strand

258 – 265

8

Helix

270 – 274

5

Beta strand

285 – 296

12

Beta strand

302 – 310

9

Beta strand

312 – 315

4

Helix

321 – 327

7

Helix

330 – 337

8

Beta strand

341 – 348

8

Helix

354 – 358

5

Helix

373 – 385

13

Helix

388 – 391

4

Turn

392 – 394

3

Beta strand

396 – 405

10

Beta strand

408 – 411

4

Turn

412 – 416

5

Beta strand

420 – 423

4

Beta strand

429 – 432

4

Beta strand

437 – 441

5

Helix

442 – 455

14

Helix

467 – 469

3

Beta strand

470 – 492

23

Helix

514 – 531

18

Helix

539 – 541

3

Helix

543 – 547

5

Helix

549 – 552

4

Beta strand

557 – 565

9

Helix

569 – 571

3

Helix

572 – 585

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 5BDECC133AB4B55C	FASTA	725	81,313
	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
	Isoform 2 (tsMCAK) [UniParc]. Checksum: 6A493B16911472C8	FASTA	671	75,561
	10 20 30 40 50 60 MIDFDDVAAI NPELLQLLPL HPKDNLPLQE NVTIQKQKRR SVNSKIPAPK ESLRSRSTRM 70 80 90 100 110 120 STVSELRITA QENDMEVELP AAANSRKQFS VPPAPTRPSC PAVAEIPLRM VSEEMEEQVH 130 140 150 160 170 180 SIRGSSSANP VNSVRRKSCL VKEVEKMKNK REEKKAQNSE MRMKRAQEYD SSFPNWEFAR 190 200 210 220 230 240 MIKEFRATLE CHPLTMTDPI EEHRICVCVR KRPLNKQELA KKEIDVISIP SKCLLLVHEP 250 260 270 280 290 300 KLKVDLTKYL ENQAFCFDFA FDETASNEVV YRFTARPLVQ TIFEGGKATC FAYGQTGSGK 310 320 330 340 350 360 THTMGGDLSG KAQNASKGIY AMASRDVFLL KNQPCYRKLG LEVYVTFFEI YNGKLFDLLN 370 380 390 400 410 420 KKAKLRVLED GKQQVQVVGL QEHLVNSADD VIKMIDMGSA CRTSGQTFAN SNSSRSHACF 430 440 450 460 470 480 QIILRAKGRM HGKFSLVDLA GNERGADTSS ADRQTRMEGA EINKSLLALK ECIRALGQNK 490 500 510 520 530 540 AHTPFRESKL TQVLRDSFIG ENSRTCMIAT ISPGISSCEY TLNTLRYADR VKELSPHSGP 550 560 570 580 590 600 SGEQLIQMET EEMEACSNGA LIPGNLSKEE EELSSQMSSF NEAMTQIREL EEKAMEELKE 610 620 630 640 650 660 IIQQGPDWLE LSEMTEQPDY DLETFVNKAE SALAQQAKHF SALRDVIKAL RLAMQLEEQA 670 SRQISSKKRP Q

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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].
[20]	"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.
[21]	"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.

IPI

IPI00216113.
IPI00290435.

RefSeq

NP_006836.2. NM_006845.3.

UniGene

Hs.720061.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HEH	X-ray	2.15	A	225-593	[»]

ProteinModelPortal

Q99661.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99661. 5 interactions.

MINT

MINT-4725759.

STRING

9606.ENSP00000361298.

PTM databases

PhosphoSite

Q99661.

Polymorphism databases

DMDM

20141607.

Proteomic databases

PaxDb

Q99661.

PRIDE

Q99661.

Protocols and materials databases

DNASU

11004.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372217; ENSP00000361291; ENSG00000142945.
ENST00000372224; ENSP00000361298; ENSG00000142945.

GeneID

11004.

KEGG

hsa:11004.

UCSC

uc001cmg.4. human.
uc001cmh.4. human.

Organism-specific databases

CTD

11004.

GeneCards

GC01P045208.

HGNC

HGNC:6393. KIF2C.

HPA

HPA006432.

MIM

604538. gene.

neXtProt

NX_Q99661.

PharmGKB

PA30182.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOVERGEN

HBG003875.

InParanoid

Q99661.

KO

K10393.

OMA

DETASNE.

OrthoDB

EOG43JC44.

PhylomeDB

Q99661.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q99661.

Bgee

Q99661.

CleanEx

HS_KIF2C.

Genevestigator

Q99661.

GermOnline

ENSG00000142945. Homo sapiens.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q99661.

ChEMBL

CHEMBL5967.

EvolutionaryTrace

Q99661.

GenomeRNAi

11004.

NextBio

41799.

SOURCE

Search...

Entry information

Entry name

KIF2C_HUMAN

Accession

Primary (citable) accession number: Q99661
Secondary accession number(s): B3ITR9 , Q5JR88, Q6ICU1, Q96C18, Q96HB8, Q9BWV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.