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O00139

- KIF2A_HUMAN

UniProt

O00139 - KIF2A_HUMAN

Protein

Kinesin-like protein KIF2A

Gene

KIF2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (02 Oct 2007)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi313 – 3208ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: InterPro
    3. motor activity Source: ProtInc
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. blood coagulation Source: Reactome
    3. cell differentiation Source: UniProtKB-KW
    4. metabolic process Source: GOC
    5. microtubule-based movement Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic nuclear division Source: UniProtKB-KW
    8. mitotic spindle organization Source: UniProtKB
    9. nervous system development Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Motor protein

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis

    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 KIF2A
    Alternative name(s):
    Kinesin-2
    Short name:
    hK2
    Gene namesi
    Name:KIF2A
    Synonyms:KIF2, KNS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6318. KIF2A.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole. Cytoplasmcytoskeletonspindle
    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.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytosol Source: Reactome
    3. kinesin complex Source: InterPro
    4. membrane Source: UniProtKB
    5. microtubule Source: UniProtKB-KW
    6. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Cortical dysplasia, complex, with other brain malformations 3 (CDCBM3) [MIM:615411]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset epilepsy, and various malformations of cortical development such as agyria, posterior or frontal pachygyria, subcortical band heterotopia, and thin corpus callosum.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171S → N in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. 1 Publication
    VAR_070575
    Natural varianti321 – 3211H → D in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. 1 Publication
    VAR_070576

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615411. phenotype.
    PharmGKBiPA162393356.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 706706Kinesin-like protein KIF2APRO_0000125414Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphoserine2 Publications
    Modified residuei78 – 781Phosphothreonine2 Publications
    Modified residuei102 – 1021N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00139.
    PaxDbiO00139.
    PRIDEiO00139.

    PTM databases

    PhosphoSiteiO00139.

    Expressioni

    Gene expression databases

    ArrayExpressiO00139.
    BgeeiO00139.
    CleanExiHS_KIF2A.
    GenevestigatoriO00139.

    Organism-specific databases

    HPAiHPA004716.

    Interactioni

    Subunit structurei

    Interacts with AURKA, PSRC1 and PLK1.3 Publications

    Protein-protein interaction databases

    BioGridi109997. 7 interactions.
    IntActiO00139. 4 interactions.
    MINTiMINT-2997391.
    STRINGi9606.ENSP00000385000.

    Structurei

    Secondary structure

    1
    706
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi197 – 2059
    Beta strandi223 – 2308
    Helixi235 – 2395
    Beta strandi250 – 26112
    Beta strandi267 – 2759
    Beta strandi277 – 2804
    Helixi286 – 2927
    Helixi295 – 3028
    Beta strandi306 – 3138
    Helixi319 – 3235
    Helixi338 – 34912
    Helixi353 – 3564
    Turni357 – 3593
    Beta strandi361 – 37010
    Beta strandi373 – 3764
    Turni377 – 3815
    Beta strandi383 – 3875
    Beta strandi395 – 3973
    Helixi407 – 42115
    Beta strandi434 – 45724
    Helixi472 – 49726
    Helixi499 – 5013
    Helixi504 – 5063
    Helixi508 – 5125
    Helixi514 – 5185
    Beta strandi522 – 5309
    Helixi534 – 5363
    Helixi537 – 54812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GRYX-ray2.35A153-553[»]
    ProteinModelPortaliO00139.
    SMRiO00139. Positions 162-550.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00139.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini223 – 553331Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 217217GlobularSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili660 – 69940Sequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000231329.
    HOVERGENiHBG003875.
    KOiK10393.
    OMAiNKKETVM.
    OrthoDBiEOG7K9K2C.
    PhylomeDBiO00139.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: O00139-3) [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

    MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK    50
    GKEIDLESIF SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS 100
    IKNDPPSRDN RVVGSARARP SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG 150
    PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL REKRAQDVDA TNPNYEIMCM 200
    IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM KDLDVITIPS 250
    KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET 300
    IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML 350
    KKPNYKKLEL QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ 400
    EREVKCVEDV LKLIDIGNSC RTSGQTSANA HSSRSHAVFQ IILRRKGKLH 450
    GKFSLIDLAG NERGADTSSA DRQTRLEGAE INKSLLALKE CIRALGRNKP 500
    HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT LNTLRYANRV 550
    KELTVDPTAA GDVRPIMHHP PNQIDDLETQ WGVGSSPQRD DLKLLCEQNE 600
    EEVSPQLFTF HEAVSQMVEM EEQVVEDHRA VFQESIRWLE DEKALLEMTE 650
    EVDYDVDSYA TQLEAILEQK IDILTELRDK VKSFRAALQE EEQASKQINP 700
    KRPRAL 706
    Length:706
    Mass (Da):79,955
    Last modified:October 2, 2007 - v3
    Checksum:iA407D84B6BD04ACF
    GO
    Isoform 1 (identifier: O00139-1) [UniParc]FASTAAdd to Basket

    Also known as: HK2

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

    Show »
    Length:679
    Mass (Da):76,955
    Checksum:iABB522C323822AF6
    GO
    Isoform 2 (identifier: O00139-2) [UniParc]FASTAAdd to Basket

    Also known as: HK2s

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

    Show »
    Length:660
    Mass (Da):75,043
    Checksum:i8975B0872C83FED9
    GO
    Isoform 4 (identifier: O00139-4) [UniParc]FASTAAdd to Basket

    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.By similarity

    Show »
    Length:744
    Mass (Da):84,089
    Checksum:i9948FA52D473F3B0
    GO
    Isoform 5 (identifier: O00139-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MATANFGKIQIGIYVEIKRSD → M

    Note: Gene prediction based on EST data.

    Show »
    Length:686
    Mass (Da):77,749
    Checksum:iA7845ECBC1EDA7D9
    GO

    Sequence cautioni

    The sequence AAP84320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431Q → H in AAP84320. 1 PublicationCurated
    Sequence conflicti153 – 1531S → SHLFFSA in AAP84320. 1 PublicationCurated
    Sequence conflicti295 – 2951R → K in CAA69621. (PubMed:9177777)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171S → N in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. 1 Publication
    VAR_070575
    Natural varianti321 – 3211H → D in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. 1 Publication
    VAR_070576

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727Missing in isoform 1 and isoform 2. 3 PublicationsVSP_028374Add
    BLAST
    Alternative sequencei1 – 2121MATAN…IKRSD → M in isoform 5. CuratedVSP_047373Add
    BLAST
    Alternative sequencei134 – 15320GSVSD…FGPPS → A in isoform 2. 2 PublicationsVSP_028375Add
    BLAST
    Alternative sequencei552 – 5521E → EFGISPSDIPFSQGSGSRPD LSPSYEYDDFSPSVTRVKE in isoform 4. 1 PublicationVSP_028376

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08319 mRNA. Translation: CAA69621.1.
    AK302270 mRNA. Translation: BAG63616.1.
    EF560716 mRNA. Translation: ABQ59026.1.
    EF560728 mRNA. Translation: ABQ59038.1.
    AC016637 Genomic DNA. No translation available.
    AC034242 Genomic DNA. No translation available.
    AC114982 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51388.1.
    CH471137 Genomic DNA. Translation: EAW51390.1.
    BC031828 mRNA. Translation: AAH31828.1.
    AY317140 mRNA. Translation: AAP84320.1. Different initiation.
    CCDSiCCDS3980.2. [O00139-3]
    CCDS47216.1. [O00139-4]
    CCDS58949.1. [O00139-5]
    RefSeqiNP_001091981.1. NM_001098511.2. [O00139-4]
    NP_001230881.1. NM_001243952.1. [O00139-5]
    NP_004511.2. NM_004520.4. [O00139-3]
    UniGeneiHs.558351.

    Genome annotation databases

    EnsembliENST00000381103; ENSP00000370493; ENSG00000068796. [O00139-5]
    ENST00000401507; ENSP00000385622; ENSG00000068796. [O00139-3]
    ENST00000407818; ENSP00000385000; ENSG00000068796. [O00139-4]
    ENST00000506857; ENSP00000423772; ENSG00000068796. [O00139-2]
    GeneIDi3796.
    KEGGihsa:3796.
    UCSCiuc003jsy.4. human. [O00139-3]
    uc003jsz.4. human. [O00139-4]
    uc010iwp.3. human. [O00139-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08319 mRNA. Translation: CAA69621.1 .
    AK302270 mRNA. Translation: BAG63616.1 .
    EF560716 mRNA. Translation: ABQ59026.1 .
    EF560728 mRNA. Translation: ABQ59038.1 .
    AC016637 Genomic DNA. No translation available.
    AC034242 Genomic DNA. No translation available.
    AC114982 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51388.1 .
    CH471137 Genomic DNA. Translation: EAW51390.1 .
    BC031828 mRNA. Translation: AAH31828.1 .
    AY317140 mRNA. Translation: AAP84320.1 . Different initiation.
    CCDSi CCDS3980.2. [O00139-3 ]
    CCDS47216.1. [O00139-4 ]
    CCDS58949.1. [O00139-5 ]
    RefSeqi NP_001091981.1. NM_001098511.2. [O00139-4 ]
    NP_001230881.1. NM_001243952.1. [O00139-5 ]
    NP_004511.2. NM_004520.4. [O00139-3 ]
    UniGenei Hs.558351.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GRY X-ray 2.35 A 153-553 [» ]
    ProteinModelPortali O00139.
    SMRi O00139. Positions 162-550.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109997. 7 interactions.
    IntActi O00139. 4 interactions.
    MINTi MINT-2997391.
    STRINGi 9606.ENSP00000385000.

    PTM databases

    PhosphoSitei O00139.

    Proteomic databases

    MaxQBi O00139.
    PaxDbi O00139.
    PRIDEi O00139.

    Protocols and materials databases

    DNASUi 3796.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381103 ; ENSP00000370493 ; ENSG00000068796 . [O00139-5 ]
    ENST00000401507 ; ENSP00000385622 ; ENSG00000068796 . [O00139-3 ]
    ENST00000407818 ; ENSP00000385000 ; ENSG00000068796 . [O00139-4 ]
    ENST00000506857 ; ENSP00000423772 ; ENSG00000068796 . [O00139-2 ]
    GeneIDi 3796.
    KEGGi hsa:3796.
    UCSCi uc003jsy.4. human. [O00139-3 ]
    uc003jsz.4. human. [O00139-4 ]
    uc010iwp.3. human. [O00139-2 ]

    Organism-specific databases

    CTDi 3796.
    GeneCardsi GC05P061601.
    H-InvDB HIX0020778.
    HGNCi HGNC:6318. KIF2A.
    HPAi HPA004716.
    MIMi 602591. gene.
    615411. phenotype.
    neXtProti NX_O00139.
    PharmGKBi PA162393356.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000231329.
    HOVERGENi HBG003875.
    KOi K10393.
    OMAi NKKETVM.
    OrthoDBi EOG7K9K2C.
    PhylomeDBi O00139.
    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 O00139.
    GeneWikii KIF2A.
    GenomeRNAii 3796.
    NextBioi 14903.
    PROi O00139.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00139.
    Bgeei O00139.
    CleanExi HS_KIF2A.
    Genevestigatori O00139.

    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

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
      Tissue: Fetal brain and Salivary gland.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. 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.
    8. "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.
    9. "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.
    10. "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, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
    15. Cited for: VARIANTS CDCBM3 ASN-317 AND ASP-321, CHARACTERIZATION OF VARIANTS CDCBM3 ASN-317 AND ASP-321.

    Entry informationi

    Entry nameiKIF2A_HUMAN
    AccessioniPrimary (citable) accession number: O00139
    Secondary accession number(s): A5YM42
    , A5YM54, B4DY54, D3DW97, E9PB70, Q7Z5I3, Q8N5Q7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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

    Miscellaneous

    HeLa cells lacking KIF2A show asymmetric or monopolar mitotic spindles. Osteosarcoma cells (U2OS) lacking KIF2A or KIF2B show disorganised or monopolar mitotic spindles.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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

    Dasty 3