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Q02241

- KIF23_HUMAN

UniProt

Q02241 - KIF23_HUMAN

Protein

Kinesin-like protein KIF23

Gene

KIF23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi112 – 1198ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule binding Source: UniProtKB
    3. microtubule 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. cytokinesis Source: UniProtKB
    4. metabolic process Source: GOC
    5. microtubule-based movement Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic spindle elongation Source: ProtInc
    8. positive regulation of cytokinesis Source: UniProtKB
    9. spindle midzone assembly involved in mitosis Source: UniProtKB

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_25201. Kinesins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF23
    Alternative name(s):
    Kinesin-like protein 5
    Mitotic kinesin-like protein 1
    Gene namesi
    Name:KIF23
    Synonyms:KNSL5, MKLP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6392. KIF23.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonspindle. Midbody
    Note: Localizes to the interzone of mitotic spindles. Detected at the midbody during later stages of mitotic cytokinesis.

    GO - Cellular componenti

    1. centralspindlin complex Source: UniProtKB
    2. centrosome Source: MGI
    3. cytosol Source: Reactome
    4. intercellular bridge Source: Ensembl
    5. kinesin complex Source: ProtInc
    6. microtubule Source: UniProtKB-KW
    7. midbody Source: UniProtKB
    8. mitotic spindle Source: UniProtKB
    9. nucleoplasm Source: Reactome
    10. nucleus Source: UniProtKB
    11. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti98870. Congenital dyserythropoietic anemia type III.
    PharmGKBiPA30181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 960960Kinesin-like protein KIF23PRO_0000125434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei155 – 1551Phosphoserine1 Publication
    Modified residuei160 – 1601Phosphoserine1 Publication
    Modified residuei605 – 6051Phosphoserine1 Publication
    Modified residuei738 – 7381Phosphothreonine1 Publication
    Modified residuei814 – 8141Phosphoserine1 Publication
    Modified residuei867 – 8671Phosphoserine3 Publications
    Modified residuei902 – 9021Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated. Deubiquitinated by USP8/UBPY.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ02241.
    PaxDbiQ02241.
    PRIDEiQ02241.

    PTM databases

    PhosphoSiteiQ02241.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02241.
    BgeeiQ02241.
    CleanExiHS_KIF23.
    GenevestigatoriQ02241.

    Organism-specific databases

    HPAiCAB010414.
    HPA045208.

    Interactioni

    Subunit structurei

    Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Interacts with RACGAP1; the interaction is direct. Interacts with ECT2 and PRC1. Interacts with ANXA11 during cytokinesis. Interacts with BIRC6/bruce and USP8/UBPY. Interacts with ARF6, forming heterodimers and heterotetramers.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARF6P6233023EBI-306852,EBI-638181
    Arf6P6233110EBI-306852,EBI-988682From a different organism.
    BIRC6Q9NR094EBI-306852,EBI-1765160
    RACGAP1Q9H0H54EBI-306852,EBI-717233
    YWHAZP631045EBI-306852,EBI-347088

    Protein-protein interaction databases

    BioGridi114873. 27 interactions.
    DIPiDIP-40359N.
    IntActiQ02241. 19 interactions.
    MINTiMINT-1631617.
    STRINGi9606.ENSP00000260363.

    Structurei

    Secondary structure

    1
    960
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi814 – 8163
    Beta strandi819 – 8224
    Beta strandi833 – 8364
    Beta strandi841 – 8466
    Helixi849 – 8546
    Beta strandi856 – 86510
    Beta strandi871 – 88212
    Beta strandi888 – 90114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VHXX-ray2.81B/D/F/H794-911[»]
    ProteinModelPortaliQ02241.
    SMRiQ02241. Positions 21-455, 799-904.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 436412Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni794 – 911118Interaction with ARF6Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili535 – 62086Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi7 – 115Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    HOGENOMiHOG000273893.
    HOVERGENiHBG052253.
    InParanoidiQ02241.
    KOiK17387.
    OMAiQTSLKDP.
    OrthoDBiEOG7PCJG5.
    PhylomeDBiQ02241.
    TreeFamiTF105232.

    Family and domain databases

    Gene3Di3.40.850.10. 2 hits.
    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. 3 hits.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02241-1) [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

    MKSARAKTPR KPTVKKGSQT NLKDPVGVYC RVRPLGFPDQ ECCIEVINNT    50
    TVQLHTPEGY RLNRNGDYKE TQYSFKQVFG THTTQKELFD VVANPLVNDL 100
    IHGKNGLLFT YGVTGSGKTH TMTGSPGEGG LLPRCLDMIF NSIGSFQAKR 150
    YVFKSNDRNS MDIQCEVDAL LERQKREAMP NPKTSSSKRQ VDPEFADMIT 200
    VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVPFD PIKPKPPQSK 250
    LLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR 300
    SHSVFNIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTRAE 350
    GNRLREAGNI NQSLMTLRTC MDVLRENQMY GTNKMVPYRD SKLTHLFKNY 400
    FDGEGKVRMI VCVNPKAEDY EENLQVMRFA EVTQEVEVAR PVDKAICGLT 450
    PGRRYRNQPR GPVGNEPLVT DVVLQSFPPL PSCEILDIND EQTLPRLIEA 500
    LEKRHNLRQM MIDEFNKQSN AFKALLQEFD NAVLSKENHM QGKLNEKEKM 550
    ISGQKLEIER LEKKNKTLEY KIEILEKTTT IYEEDKRNLQ QELETQNQKL 600
    QRQFSDKRRL EARLQGMVTE TTMKWEKECE RRVAAKQLEM QNKLWVKDEK 650
    LKQLKAIVTE PKTEKPERPS RERDREKVTQ RSVSPSPVPL SSNYIAQISN 700
    GQQLMSQPQL HRRSNSCSSI SVASCISEWE QKIPTYNTPL KVTSIARRRQ 750
    QEPGQSKTCI VSDRRRGMYW TEGREVVPTF RNEIEIEEDH CGRLLFQPDQ 800
    NAPPIRLRHR RSRSAGDRWV DHKPASNMQT ETVMQPHVPH AITVSVANEK 850
    ALAKCEKYML THQELASDGE IETKLIKGDI YKTRGGGQSV QFTDIETLKQ 900
    ESPNGSRKRR SSTVAPAQPD GAESEWTDVE TRCSVAVEMR AGSQLGPGYQ 950
    HHAQPKRKKP 960
    Length:960
    Mass (Da):110,059
    Last modified:November 28, 2006 - v3
    Checksum:iB2AA784D2D236A90
    GO
    Isoform 2 (identifier: Q02241-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         690-793: Missing.

    Show »
    Length:856
    Mass (Da):98,105
    Checksum:iDDE7CEB480ABE58A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti515 – 5151F → L.
    Corresponds to variant rs17310879 [ dbSNP | Ensembl ].
    VAR_049686

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei690 – 793104Missing in isoform 2. 2 PublicationsVSP_021801Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67155 mRNA. Translation: CAA47628.2.
    BC017705 mRNA. Translation: AAH17705.2.
    BC051826 mRNA. Translation: AAH51826.1.
    CCDSiCCDS32278.1. [Q02241-1]
    CCDS32279.1. [Q02241-2]
    PIRiS28262.
    RefSeqiNP_004847.2. NM_004856.6. [Q02241-2]
    NP_612565.1. NM_138555.3. [Q02241-1]
    UniGeneiHs.270845.

    Genome annotation databases

    EnsembliENST00000260363; ENSP00000260363; ENSG00000137807. [Q02241-1]
    ENST00000352331; ENSP00000304978; ENSG00000137807. [Q02241-2]
    ENST00000559279; ENSP00000453386; ENSG00000137807. [Q02241-2]
    GeneIDi9493.
    KEGGihsa:9493.
    UCSCiuc002asb.3. human. [Q02241-1]
    uc002asc.3. human. [Q02241-2]

    Polymorphism databases

    DMDMi118572664.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67155 mRNA. Translation: CAA47628.2 .
    BC017705 mRNA. Translation: AAH17705.2 .
    BC051826 mRNA. Translation: AAH51826.1 .
    CCDSi CCDS32278.1. [Q02241-1 ]
    CCDS32279.1. [Q02241-2 ]
    PIRi S28262.
    RefSeqi NP_004847.2. NM_004856.6. [Q02241-2 ]
    NP_612565.1. NM_138555.3. [Q02241-1 ]
    UniGenei Hs.270845.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VHX X-ray 2.81 B/D/F/H 794-911 [» ]
    ProteinModelPortali Q02241.
    SMRi Q02241. Positions 21-455, 799-904.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114873. 27 interactions.
    DIPi DIP-40359N.
    IntActi Q02241. 19 interactions.
    MINTi MINT-1631617.
    STRINGi 9606.ENSP00000260363.

    Chemistry

    BindingDBi Q02241.
    ChEMBLi CHEMBL5899.

    PTM databases

    PhosphoSitei Q02241.

    Polymorphism databases

    DMDMi 118572664.

    Proteomic databases

    MaxQBi Q02241.
    PaxDbi Q02241.
    PRIDEi Q02241.

    Protocols and materials databases

    DNASUi 9493.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260363 ; ENSP00000260363 ; ENSG00000137807 . [Q02241-1 ]
    ENST00000352331 ; ENSP00000304978 ; ENSG00000137807 . [Q02241-2 ]
    ENST00000559279 ; ENSP00000453386 ; ENSG00000137807 . [Q02241-2 ]
    GeneIDi 9493.
    KEGGi hsa:9493.
    UCSCi uc002asb.3. human. [Q02241-1 ]
    uc002asc.3. human. [Q02241-2 ]

    Organism-specific databases

    CTDi 9493.
    GeneCardsi GC15P069706.
    HGNCi HGNC:6392. KIF23.
    HPAi CAB010414.
    HPA045208.
    MIMi 605064. gene.
    neXtProti NX_Q02241.
    Orphaneti 98870. Congenital dyserythropoietic anemia type III.
    PharmGKBi PA30181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000273893.
    HOVERGENi HBG052253.
    InParanoidi Q02241.
    KOi K17387.
    OMAi QTSLKDP.
    OrthoDBi EOG7PCJG5.
    PhylomeDBi Q02241.
    TreeFami TF105232.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_25201. Kinesins.

    Miscellaneous databases

    GeneWikii KIF23.
    GenomeRNAii 9493.
    NextBioi 35566.
    PROi Q02241.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02241.
    Bgeei Q02241.
    CleanExi HS_KIF23.
    Genevestigatori Q02241.

    Family and domain databases

    Gene3Di 3.40.850.10. 2 hits.
    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. 3 hits.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles."
      Nislow C., Lombillo V.A., Kuriyama R., McIntosh J.R.
      Nature 359:543-547(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Gryka M.A.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-960 (ISOFORM 1).
      Tissue: Lymph and Uterus.
    4. "Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity."
      Mishima M., Kaitna S., Glotzer M.
      Dev. Cell 2:41-54(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO MICROTUBULES, INTERACTION WITH RACGAP1.
    5. "Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation."
      Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.
      EMBO J. 23:3237-3248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRC1.
    6. "Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis."
      Tomas A., Futter C., Moss S.E.
      J. Cell Biol. 165:813-822(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANXA11, SUBCELLULAR LOCATION.
    7. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
      Yuce O., Piekny A., Glotzer M.
      J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RACGAP1.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-814; SER-867 AND SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
      Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
      Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH ECT2 AND RACGAP1, SUBCELLULAR LOCATION.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
      Pohl C., Jentsch S.
      Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION, INTERACTION WITH BIRC6/BRUCE AND USP8/UBPY.
    12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-738; SER-867 AND SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation."
      Wolfe B.A., Takaki T., Petronczki M., Glotzer M.
      PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECT2.
    16. "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.
    17. "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-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis."
      Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A., Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M., Kawasaki M., Kato R., Wakatsuki S., Nakayama K.
      EMBO J. 31:2590-2603(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 794-911 IN COMPLEX WITH ARF6, INTERACTION WITH ARF6, FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiKIF23_HUMAN
    AccessioniPrimary (citable) accession number: Q02241
    Secondary accession number(s): Q8WVP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 148 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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