O00139 (KIF2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIF2A

Alternative name(s):
Kinesin-2
Short name=hK2

Gene names

Name:	KIF2A
Synonyms:	KIF2, KNS2

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	706 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity. Ref.7 Ref.8 Ref.9
Subunit structure	Interacts with AURKA, PSRC1 and PLK1. Ref.9 Ref.10
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole. Cytoplasm › cytoskeleton › spindle. Note: Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1. Ref.9 Ref.10
Miscellaneous	HeLa cells lacking KIF2A show asymmetric or monopolar mitotic spindles. Osteosarcoma cells (U2OS) lacking KIF2A or KIF2B show disorganised or monopolar mitotic spindles.
Sequence similarities	Belongs to the kinesin-like protein family. MCAK/KIF2 subfamily. Contains 1 kinesin-motor domain.
Sequence caution	The sequence AAP84320.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Motor protein
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 differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome mitotic spindle organization Inferred from direct assay Ref.9. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro spindle pole 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 motor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: O00139-3)

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 1 (identifier: O00139-1)

Also known as: HK2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Isoform 2 (identifier: O00139-2)

Also known as: HK2s;

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     134-153: GSVSDISPVQAAKKEFGPPS → A

Isoform 4 (identifier: O00139-4)

The sequence of this isoform differs from the canonical sequence as follows:
     552-552: E → EFGISPSDIPFSQGSGSRPDLSPSYEYDDFSPSVTRVKE

Note: Contains a phosphoserine at position 579 (By similarity). No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 706

706

Kinesin-like protein KIF2A

PRO_0000125414

Regions

Domain

218 – 552

335

Kinesin-motor

Nucleotide binding

313 – 320

8

ATP

Region

1 – 217

217

Globular Potential

Coiled coil

660 – 699

40

Potential

Amino acid modifications

Modified residue

75

1

Phosphoserine Ref.11

Modified residue

78

1

Phosphothreonine Ref.11

Natural variations

Alternative sequence

1 – 27

27

Missing in isoform 1 and isoform 2.

VSP_028374

Alternative sequence

134 – 153

20

GSVSD…FGPPS → A in isoform 2.

VSP_028375

Alternative sequence

552

1

E → EFGISPSDIPFSQGSGSRPD LSPSYEYDDFSPSVTRVKE in isoform 4.

VSP_028376

Experimental info

Sequence conflict

143

1

Q → H in AAP84320. Ref.6

Sequence conflict

153

1

S → SHLFFSA in AAP84320. Ref.6

Sequence conflict

295

1

R → K in CAA69621. Ref.1

Secondary structure

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706

Helix Strand Turn

Details...

Helix

197 – 205

9

Beta strand

223 – 230

8

Helix

235 – 239

5

Beta strand

250 – 261

12

Beta strand

267 – 275

9

Beta strand

277 – 280

4

Helix

286 – 292

7

Helix

295 – 302

8

Beta strand

306 – 313

8

Helix

319 – 323

5

Helix

338 – 349

12

Helix

353 – 356

4

Turn

357 – 359

3

Beta strand

361 – 370

10

Beta strand

373 – 376

4

Turn

377 – 381

5

Beta strand

383 – 387

5

Beta strand

395 – 397

3

Helix

407 – 421

15

Beta strand

434 – 457

24

Helix

472 – 497

26

Helix

499 – 501

3

Helix

504 – 506

3

Helix

508 – 512

5

Helix

514 – 518

5

Beta strand

522 – 530

9

Helix

534 – 536

3

Helix

537 – 548

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified October 2, 2007. Version 3. Checksum: A407D84B6BD04ACF	FASTA	706	79,955
	10 20 30 40 50 60 MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF 70 80 90 100 110 120 SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS IKNDPPSRDN RVVGSARARP 130 140 150 160 170 180 SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL 190 200 210 220 230 240 REKRAQDVDA TNPNYEIMCM IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM 250 260 270 280 290 300 KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET 310 320 330 340 350 360 IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL 370 380 390 400 410 420 QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIDIGNSC 430 440 450 460 470 480 RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE 490 500 510 520 530 540 INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT 550 560 570 580 590 600 LNTLRYANRV KELTVDPTAA GDVRPIMHHP PNQIDDLETQ WGVGSSPQRD DLKLLCEQNE 610 620 630 640 650 660 EEVSPQLFTF HEAVSQMVEM EEQVVEDHRA VFQESIRWLE DEKALLEMTE EVDYDVDSYA 670 680 690 700 TQLEAILEQK IDILTELRDK VKSFRAALQE EEQASKQINP KRPRAL
	Isoform 1 (HK2) [UniParc]. Checksum: ABB522C323822AF6	FASTA	679	76,955
	10 20 30 40 50 60 MVTSLNEDNE SVTVEWIENG DTKGKEIDLE SIFSLNPDLV PDEEIEPSPE TPPPPASSAK 70 80 90 100 110 120 VNKIVKNRRT VASIKNDPPS RDNRVVGSAR ARPSQFPEQS SSAQQNGSVS DISPVQAAKK 130 140 150 160 170 180 EFGPPSRRKS NCVKEVEKLQ EKREKRRLQQ QELREKRAQD VDATNPNYEI MCMIRDFRGS 190 200 210 220 230 240 LDYRPLTTAD PIDEHRICVC VRKRPLNKKE TQMKDLDVIT IPSKDVVMVH EPKQKVDLTR 250 260 270 280 290 300 YLENQTFRFD YAFDDSAPNE MVYRFTARPL VETIFERGMA TCFAYGQTGS GKTHTMGGDF 310 320 330 340 350 360 SGKNQDCSKG IYALAARDVF LMLKKPNYKK LELQVYATFF EIYSGKVFDL LNRKTKLRVL 370 380 390 400 410 420 EDGKQQVQVV GLQEREVKCV EDVLKLIDIG NSCRTSGQTS ANAHSSRSHA VFQIILRRKG 430 440 450 460 470 480 KLHGKFSLID LAGNERGADT SSADRQTRLE GAEINKSLLA LKECIRALGR NKPHTPFRAS 490 500 510 520 530 540 KLTQVLRDSF IGENSRTCMI ATISPGMASC ENTLNTLRYA NRVKELTVDP TAAGDVRPIM 550 560 570 580 590 600 HHPPNQIDDL ETQWGVGSSP QRDDLKLLCE QNEEEVSPQL FTFHEAVSQM VEMEEQVVED 610 620 630 640 650 660 HRAVFQESIR WLEDEKALLE MTEEVDYDVD SYATQLEAIL EQKIDILTEL RDKVKSFRAA 670 LQEEEQASKQ INPKRPRAL
	Isoform 2 (HK2s) [UniParc]. Checksum: 8975B0872C83FED9	FASTA	660	75,043
	10 20 30 40 50 60 MVTSLNEDNE SVTVEWIENG DTKGKEIDLE SIFSLNPDLV PDEEIEPSPE TPPPPASSAK 70 80 90 100 110 120 VNKIVKNRRT VASIKNDPPS RDNRVVGSAR ARPSQFPEQS SSAQQNARRK SNCVKEVEKL 130 140 150 160 170 180 QEKREKRRLQ QQELREKRAQ DVDATNPNYE IMCMIRDFRG SLDYRPLTTA DPIDEHRICV 190 200 210 220 230 240 CVRKRPLNKK ETQMKDLDVI TIPSKDVVMV HEPKQKVDLT RYLENQTFRF DYAFDDSAPN 250 260 270 280 290 300 EMVYRFTARP LVETIFERGM ATCFAYGQTG SGKTHTMGGD FSGKNQDCSK GIYALAARDV 310 320 330 340 350 360 FLMLKKPNYK KLELQVYATF FEIYSGKVFD LLNRKTKLRV LEDGKQQVQV VGLQEREVKC 370 380 390 400 410 420 VEDVLKLIDI GNSCRTSGQT SANAHSSRSH AVFQIILRRK GKLHGKFSLI DLAGNERGAD 430 440 450 460 470 480 TSSADRQTRL EGAEINKSLL ALKECIRALG RNKPHTPFRA SKLTQVLRDS FIGENSRTCM 490 500 510 520 530 540 IATISPGMAS CENTLNTLRY ANRVKELTVD PTAAGDVRPI MHHPPNQIDD LETQWGVGSS 550 560 570 580 590 600 PQRDDLKLLC EQNEEEVSPQ LFTFHEAVSQ MVEMEEQVVE DHRAVFQESI RWLEDEKALL 610 620 630 640 650 660 EMTEEVDYDV DSYATQLEAI LEQKIDILTE LRDKVKSFRA ALQEEEQASK QINPKRPRAL
	Isoform 4 [UniParc]. Checksum: 9948FA52D473F3B0	FASTA	744	84,089
	10 20 30 40 50 60 MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF 70 80 90 100 110 120 SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS IKNDPPSRDN RVVGSARARP 130 140 150 160 170 180 SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL 190 200 210 220 230 240 REKRAQDVDA TNPNYEIMCM IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM 250 260 270 280 290 300 KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET 310 320 330 340 350 360 IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL 370 380 390 400 410 420 QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIDIGNSC 430 440 450 460 470 480 RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE 490 500 510 520 530 540 INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT 550 560 570 580 590 600 LNTLRYANRV KEFGISPSDI PFSQGSGSRP DLSPSYEYDD FSPSVTRVKE LTVDPTAAGD 610 620 630 640 650 660 VRPIMHHPPN QIDDLETQWG VGSSPQRDDL KLLCEQNEEE VSPQLFTFHE AVSQMVEMEE 670 680 690 700 710 720 QVVEDHRAVF QESIRWLEDE KALLEMTEEV DYDVDSYATQ LEAILEQKID ILTELRDKVK 730 740 SFRAALQEEE QASKQINPKR PRAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel human kinesin-related gene (HK2) by the cDNA differential display technique." Debernardi S., Fontanella E., de Gregorio L., Pierotti M.A., Delia D. Genomics 42:67-73(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). Tissue: Fetal brain and Salivary gland.
[4]	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].
[5]	"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: Brain.
[6]	Sha J.H., Zhou Z.M., Li J.M. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-706 (ISOFORMS 1/3). Tissue: Testis.
[7]	"Functional analysis of human microtubule-based motor proteins, the kinesins and dyneins, in mitosis/cytokinesis using RNA interference." Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B., Abraham R.T., Jiang W. Mol. Biol. Cell 16:3187-3199(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells." Manning A.L., Ganem N.J., Bakhoum S.F., Wagenbach M., Wordeman L., Compton D.A. Mol. Biol. Cell 18:2970-2979(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"DDA3 recruits microtubule depolymerase Kif2a to spindle poles and controls spindle dynamics and mitotic chromosome movement." Jang C.Y., Wong J., Coppinger J.A., Seki A., Yates J.R. III, Fang G. J. Cell Biol. 181:255-267(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSRC1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[10]	"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a." Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G. J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLK1 AND AURKA, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PHOSPHORYLATION.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-78, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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].
[13]	"Crystal structure of the human KIF2 motor domain in complex with ADP." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 153-553 IN COMPLEX WITH ADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y08319 mRNA. Translation: CAA69621.1.
AK302270 mRNA. Translation: BAG63616.1.
EF560716 mRNA. Translation: ABQ59026.1.
EF560728 mRNA. Translation: ABQ59038.1.
CH471137 Genomic DNA. Translation: EAW51388.1.
CH471137 Genomic DNA. Translation: EAW51390.1.
BC031828 mRNA. Translation: AAH31828.1.
AY317140 mRNA. Translation: AAP84320.1. Different initiation.

IPI

IPI00010368.
IPI00848334.
IPI00867529.
IPI00867746.

RefSeq

NP_001091981.1. NM_001098511.2.
NP_004511.2. NM_004520.4.

UniGene

Hs.558351.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GRY	X-ray	2.35	A	153-553	[»]

ProteinModelPortal

O00139.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00139. 2 interactions.

STRING

9606.ENSP00000385000.

PTM databases

PhosphoSite

O00139.

Proteomic databases

PaxDb

O00139.

PRIDE

O00139.

Protocols and materials databases

DNASU

3796.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000401507; ENSP00000385622; ENSG00000068796.
ENST00000407818; ENSP00000385000; ENSG00000068796.
ENST00000506857; ENSP00000423772; ENSG00000068796.

GeneID

3796.

KEGG

hsa:3796.

UCSC

uc003jsy.4. human.
uc003jsz.4. human.
uc010iwp.3. human.

Organism-specific databases

CTD

3796.

GeneCards

GC05P061601.

H-InvDB

HIX0020778.

HGNC

HGNC:6318. KIF2A.

HPA

HPA004716.

MIM

602591. gene.

neXtProt

NX_O00139.

PharmGKB

PA162393356.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOGENOM

HOG000231329.

HOVERGEN

HBG003875.

KO

K10393.

OMA

KETVMKD.

OrthoDB

EOG44QT0D.

Enzyme and pathway databases

Reactome

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

Gene expression databases

ArrayExpress

O00139.

Bgee

O00139.

CleanEx

HS_KIF2A.

Genevestigator

O00139.

GermOnline

ENSG00000068796. 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

EvolutionaryTrace

O00139.

GenomeRNAi

3796.

NextBio

14903.

SOURCE

Search...

Entry information

Entry name

KIF2A_HUMAN

Accession

Primary (citable) accession number: O00139
Secondary accession number(s): A5YM42 , A5YM54, B4DY54, D3DW97, Q7Z5I3, Q8N5Q7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 2, 2007
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 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.