Q922S8 (KIF2C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIF2C

Alternative name(s):
Mitotic centromere-associated kinesin
Short name=MCAK

Gene names

Name:

Kif2c

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	721 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 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	Cytoplasm › cytoskeleton By similarity. Nucleus By similarity. Chromosome › centromere By similarity. Chromosome › centromere › kinetochore 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.
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
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW establishment or maintenance of microtubule cytoskeleton polarity Inferred from electronic annotation. Source: Compara microtubule depolymerization Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	chromosome, 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 microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 721

721

Kinesin-like protein KIF2C

PRO_0000125420

Regions

Domain

251 – 514

264

Kinesin-motor

Nucleotide binding

344 – 351

8

ATP

Region

1 – 250

250

Globular Potential

Region

203 – 234

32

Negative regulator of microtubule-binding

Coiled coil

614 – 652

39

Potential

Motif

95 – 98

4

Microtubule tip localization signal

Sites

Binding site

260

1

ATP

Amino acid modifications

Modified residue

19

1

Phosphoserine By similarity

Modified residue

92

1

Phosphoserine; by AURKB By similarity

Modified residue

106

1

Phosphoserine By similarity

Modified residue

108

1

Phosphoserine By similarity

Modified residue

112

1

Phosphoserine By similarity

Modified residue

162

1

Phosphoserine By similarity

Modified residue

188

1

Phosphoserine By similarity

Modified residue

626

1

Phosphoserine By similarity

Experimental info

Mutagenesis

293

1

K → A: Loss of microtubule depolymerization activity. Ref.3

Mutagenesis

294

1

V → A: Loss of microtubule depolymerization activity. Ref.3

Mutagenesis

295

1

D → A: Loss of microtubule depolymerization activity. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

721

Helix Strand Turn

Details...

Helix

226 – 239

14

Turn

243 – 247

5

Beta strand

255 – 261

7

Helix

266 – 270

5

Beta strand

281 – 292

12

Beta strand

298 – 306

9

Beta strand

308 – 311

4

Helix

317 – 323

7

Helix

326 – 328

3

Helix

329 – 333

5

Beta strand

337 – 345

9

Helix

350 – 355

6

Helix

365 – 367

3

Helix

369 – 381

13

Helix

384 – 387

4

Beta strand

392 – 401

10

Beta strand

404 – 407

4

Turn

408 – 412

5

Beta strand

414 – 419

6

Beta strand

421 – 423

3

Beta strand

425 – 428

4

Beta strand

433 – 437

5

Helix

438 – 450

13

Beta strand

465 – 488

24

Helix

506 – 508

3

Helix

509 – 526

18

Helix

539 – 543

5

Helix

546 – 549

4

Beta strand

550 – 561

12

Helix

565 – 567

3

Helix

568 – 582

15

Sequences

	Sequence		Length	Mass (Da)
	Q922S8 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 92FFBFFDA05B7E35	FASTA	721	81,085
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00123365.

RefSeq

NP_608301.3. NM_134471.4.

UniGene

Mm.247651.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V8J	X-ray	3.24	A	183-585	[»]
1V8K	X-ray	2.25	A	183-585	[»]

ProteinModelPortal

Q922S8.

SMR

Q922S8. Positions 224-585.

ModBase

Search...

PTM databases

PhosphoSite

Q922S8.

Proteomic databases

PaxDb

Q922S8.

PRIDE

Q922S8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000065896; ENSMUSP00000064261; ENSMUSG00000028678.

GeneID

73804.

KEGG

mmu:73804.

UCSC

uc008uie.2. mouse.

Organism-specific databases

CTD

11004.

MGI

MGI:1921054. Kif2c.

Phylogenomic databases

eggNOG

COG5059.

GeneTree

ENSGT00680000099804.

HOGENOM

HOG000231329.

HOVERGEN

HBG003875.

InParanoid

A2AE71.

KO

K10393.

OMA

DETASNE.

OrthoDB

EOG43JC44.

Gene expression databases

ArrayExpress

Q922S8.

Bgee

Q922S8.

CleanEx

MM_KIF2C.

Genevestigator

Q922S8.

GermOnline

ENSMUSG00000028678. Mus musculus.

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

EvolutionaryTrace

Q922S8.

NextBio

339083.

SOURCE

Search...

Entry information

Entry name

KIF2C_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program