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P52732

- KIF11_HUMAN

UniProt

P52732 - KIF11_HUMAN

Protein

Kinesin-like protein KIF11

Gene

KIF11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi105 – 1128ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule motor activity Source: ProtInc
    3. protein complex binding Source: UniProtKB
    4. protein kinase 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. metabolic process Source: GOC
    4. microtubule-based movement Source: Reactome
    5. mitotic centrosome separation Source: Ensembl
    6. mitotic nuclear division Source: ProtInc
    7. mitotic spindle organization Source: ProtInc
    8. spindle assembly involved in mitosis Source: UniProtKB
    9. spindle organization 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_25201. Kinesins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF11
    Alternative name(s):
    Kinesin-like protein 1
    Kinesin-like spindle protein HKSP
    Kinesin-related motor protein Eg5
    Thyroid receptor-interacting protein 5
    Short name:
    TR-interacting protein 5
    Short name:
    TRIP-5
    Gene namesi
    Name:KIF11
    Synonyms:EG5, KNSL1, TRIP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6388. KIF11.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. kinesin complex Source: ProtInc
    4. membrane Source: UniProtKB
    5. microtubule Source: UniProtKB
    6. spindle Source: UniProtKB
    7. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]: An autosomal dominant disorder that involves an overlapping but variable spectrum of central nervous system and ocular developmental anomalies. Microcephaly ranges from mild to severe and is often associated with mild to moderate developmental delay and a characteristic facial phenotype with upslanting palpebral fissures, broad nose with rounded tip, long philtrum with thin upper lip, prominent chin, and prominent ears. Chorioretinopathy is the most common eye abnormality, but retinal folds, microphthalmia, and myopic and hypermetropic astigmatism have also been reported, and some individuals have no overt ocular phenotype. Congenital lymphedema, when present, is typically confined to the dorsa of the feet, and lymphoscintigraphy reveals the absence of radioactive isotope uptake from the webspaces between the toes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441F → L in MCLMR. 1 Publication
    VAR_067829
    Natural varianti234 – 2341R → C in MCLMR. 1 Publication
    VAR_067830
    Natural varianti235 – 2351S → C in MCLMR. 1 Publication
    VAR_067831
    Natural varianti944 – 9441R → C in MCLMR. 1 Publication
    VAR_067832

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi926 – 9261T → A: No mitotic phosphorylation. No binding to spindle apparatus. 2 Publications
    Mutagenesisi1033 – 10331S → A: Still binds to the mitotic spindle but mitotic progression is impaired. 2 Publications
    Mutagenesisi1033 – 10331S → D: Still binds to the mitotic spindle but mitotic progression is impaired. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi152950. phenotype.
    Orphaneti2526. Microcephaly - lymphedema - chorioretinopathy.
    PharmGKBiPA30177.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10561056Kinesin-like protein KIF11PRO_0000125372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei146 – 1461N6-acetyllysine1 Publication
    Modified residuei458 – 4581Phosphothreonine1 Publication
    Modified residuei926 – 9261Phosphothreonine; by CDK13 Publications
    Modified residuei1033 – 10331Phosphoserine; by NEK61 Publication

    Post-translational modificationi

    Phosphorylated exclusively on serine during S phase, but on both serine and Thr-926 during mitosis, so controlling the association of KIF11 with the spindle apparatus (probably during early prophase).3 Publications
    A subset of this protein primarily localized at the spindle pole is phosphorylated by NEK6 during mitosis; phosphorylation is required for mitotic function.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52732.
    PaxDbiP52732.
    PeptideAtlasiP52732.
    PRIDEiP52732.

    PTM databases

    PhosphoSiteiP52732.

    Expressioni

    Gene expression databases

    BgeeiP52732.
    CleanExiHS_KIF11.
    GenevestigatoriP52732.

    Organism-specific databases

    HPAiCAB017617.
    HPA006916.
    HPA010568.

    Interactioni

    Subunit structurei

    Interacts with the thyroid hormone receptor in the presence of thyroid hormone. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Interacts (via C-terminus) with the kinase NEK6 in both interphase and mitosis.2 Publications

    Protein-protein interaction databases

    BioGridi110030. 20 interactions.
    IntActiP52732. 5 interactions.
    MINTiMINT-1152202.
    STRINGi9606.ENSP00000260731.

    Structurei

    Secondary structure

    1
    1056
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 257
    Helixi30 – 345
    Beta strandi41 – 444
    Turni45 – 484
    Beta strandi49 – 535
    Beta strandi58 – 603
    Beta strandi63 – 675
    Beta strandi69 – 724
    Helixi78 – 9417
    Beta strandi98 – 1069
    Helixi111 – 1155
    Helixi121 – 1233
    Turni127 – 1293
    Helixi130 – 1323
    Helixi135 – 14814
    Turni149 – 1513
    Beta strandi153 – 16412
    Beta strandi167 – 1715
    Beta strandi174 – 1763
    Beta strandi183 – 1864
    Beta strandi188 – 1903
    Beta strandi194 – 1974
    Beta strandi202 – 2043
    Helixi207 – 22317
    Helixi226 – 2338
    Beta strandi235 – 24814
    Beta strandi250 – 2523
    Beta strandi254 – 26512
    Helixi269 – 2713
    Helixi272 – 2754
    Helixi280 – 2834
    Turni287 – 2893
    Helixi290 – 30415
    Helixi311 – 3133
    Helixi315 – 3206
    Helixi321 – 3233
    Beta strandi324 – 3274
    Beta strandi330 – 3367
    Helixi340 – 3423
    Helixi343 – 35715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1II6X-ray2.10A/B1-368[»]
    1Q0BX-ray1.90A/B2-368[»]
    1X88X-ray1.80A/B10-368[»]
    1YRSX-ray2.50A/B1-368[»]
    2FKYX-ray2.30A/B2-368[»]
    2FL2X-ray2.50A/B2-368[»]
    2FL6X-ray2.50A/B2-368[»]
    2FMEX-ray2.10A/B1-368[»]
    2G1QX-ray2.51A/B1-368[»]
    2GM1X-ray2.30A/B/D/E1-368[»]
    2IEHX-ray2.70A/B2-368[»]
    2PG2X-ray1.85A/B1-368[»]
    2Q2YX-ray2.50A/B2-368[»]
    2Q2ZX-ray3.00A/B2-368[»]
    2UYIX-ray2.10A/B1-368[»]
    2UYMX-ray2.11A/B1-368[»]
    2WOGX-ray2.00A/B/C1-368[»]
    2X2RX-ray2.20A/B/C1-368[»]
    2X7CX-ray1.90A/B1-368[»]
    2X7DX-ray2.30A/B1-368[»]
    2X7EX-ray2.40A/B1-368[»]
    2XAEX-ray2.60A/B/C1-368[»]
    3CJOX-ray2.28A/B2-368[»]
    3HQDX-ray2.19A/B1-369[»]
    3K3BX-ray2.40A/B1-368[»]
    3K5EX-ray1.97A/B1-368[»]
    3KENX-ray2.50A1-369[»]
    3L9HX-ray2.00A/B1-368[»]
    3ZCWX-ray1.69A16-363[»]
    4A1ZX-ray2.80A/B1-368[»]
    4A28X-ray2.55A/B1-368[»]
    4A50X-ray2.75A1-368[»]
    4A51X-ray2.75A/B/C/D/E/F/G1-368[»]
    4A5YX-ray2.45A/B/C1-368[»]
    4AP0X-ray2.59A/B/C/D1-368[»]
    4AQVelectron microscopy9.70C1-367[»]
    4AQWelectron microscopy9.50C1-367[»]
    4AS7X-ray2.40A1-368[»]
    4B7BX-ray2.50A1-368[»]
    4BBGX-ray2.75A1-368[»]
    4BXNX-ray2.79A/B1-368[»]
    4CK5electron microscopy10.00C1-367[»]
    4CK6electron microscopy9.20C1-367[»]
    4CK7electron microscopy9.20C1-367[»]
    ProteinModelPortaliP52732.
    SMRiP52732. Positions 15-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52732.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 359342Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili364 – 480117Sequence AnalysisAdd
    BLAST
    Coiled coili736 – 76328Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    HOGENOMiHOG000116164.
    HOVERGENiHBG005572.
    InParanoidiP52732.
    KOiK10398.
    OMAiQPNSSAK.
    OrthoDBiEOG7VX8V8.
    PhylomeDBiP52732.
    TreeFamiTF105230.

    Family and domain databases

    Gene3Di3.40.850.10. 1 hit.
    InterProiIPR025901. Kinesin-assoc_MT-bd_dom.
    IPR027640. 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.
    PF13931. Microtub_bind. 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]

    Sequencei

    Sequence statusi: Complete.

    P52732-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASQPNSSAK KKEEKGKNIQ VVVRCRPFNL AERKASAHSI VECDPVRKEV     50
    SVRTGGLADK SSRKTYTFDM VFGASTKQID VYRSVVCPIL DEVIMGYNCT 100
    IFAYGQTGTG KTFTMEGERS PNEEYTWEED PLAGIIPRTL HQIFEKLTDN 150
    GTEFSVKVSL LEIYNEELFD LLNPSSDVSE RLQMFDDPRN KRGVIIKGLE 200
    EITVHNKDEV YQILEKGAAK RTTAATLMNA YSSRSHSVFS VTIHMKETTI 250
    DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT 300
    ALVERTPHVP YRESKLTRIL QDSLGGRTRT SIIATISPAS LNLEETLSTL 350
    EYAHRAKNIL NKPEVNQKLT KKALIKEYTE EIERLKRDLA AAREKNGVYI 400
    SEENFRVMSG KLTVQEEQIV ELIEKIGAVE EELNRVTELF MDNKNELDQC 450
    KSDLQNKTQE LETTQKHLQE TKLQLVKEEY ITSALESTEE KLHDAASKLL 500
    NTVEETTKDV SGLHSKLDRK KAVDQHNAEA QDIFGKNLNS LFNNMEELIK 550
    DGSSKQKAML EVHKTLFGNL LSSSVSALDT ITTVALGSLT SIPENVSTHV 600
    SQIFNMILKE QSLAAESKTV LQELINVLKT DLLSSLEMIL SPTVVSILKI 650
    NSQLKHIFKT SLTVADKIED QKKELDGFLS ILCNNLHELQ ENTICSLVES 700
    QKQCGNLTED LKTIKQTHSQ ELCKLMNLWT ERFCALEEKC ENIQKPLSSV 750
    QENIQQKSKD IVNKMTFHSQ KFCADSDGFS QELRNFNQEG TKLVEESVKH 800
    SDKLNGNLEK ISQETEQRCE SLNTRTVYFS EQWVSSLNER EQELHNLLEV 850
    VSQCCEASSS DITEKSDGRK AAHEKQHNIF LDQMTIDEDK LIAQNLELNE 900
    TIKIGLTKLN CFLEQDLKLD IPTGTTPQRK SYLYPSTLVR TEPREHLLDQ 950
    LKRKQPELLM MLNCSENNKE ETIPDVDVEE AVLGQYTEEP LSQEPSVDAG 1000
    VDCSSIGGVP FFQHKKSHGK DKENRGINTL ERSKVEETTE HLVTKSRLPL 1050
    RAQINL 1056
    Length:1,056
    Mass (Da):119,159
    Last modified:October 17, 2006 - v2
    Checksum:iC7F2606FE68DA8EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti674 – 6752EL → RNS in CAA59449. (PubMed:8548803)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441F → L in MCLMR. 1 Publication
    VAR_067829
    Natural varianti234 – 2341R → C in MCLMR. 1 Publication
    VAR_067830
    Natural varianti235 – 2351S → C in MCLMR. 1 Publication
    VAR_067831
    Natural varianti944 – 9441R → C in MCLMR. 1 Publication
    VAR_067832
    Natural varianti1042 – 10421L → F.
    Corresponds to variant rs34417963 [ dbSNP | Ensembl ].
    VAR_049682

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85137 mRNA. Translation: CAA59449.1.
    U37426 mRNA. Translation: AAA86132.1.
    AL360222, AL356128 Genomic DNA. Translation: CAH72288.1.
    AL356128, AL360222 Genomic DNA. Translation: CAI13671.1.
    BC126211 mRNA. Translation: AAI26212.1.
    BC136474 mRNA. Translation: AAI36475.1.
    L40372 mRNA. Translation: AAC41739.1.
    CCDSiCCDS7422.1.
    PIRiG02157.
    RefSeqiNP_004514.2. NM_004523.3.
    UniGeneiHs.8878.

    Genome annotation databases

    EnsembliENST00000260731; ENSP00000260731; ENSG00000138160.
    GeneIDi3832.
    KEGGihsa:3832.
    UCSCiuc001kic.3. human.

    Polymorphism databases

    DMDMi116242604.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85137 mRNA. Translation: CAA59449.1 .
    U37426 mRNA. Translation: AAA86132.1 .
    AL360222 , AL356128 Genomic DNA. Translation: CAH72288.1 .
    AL356128 , AL360222 Genomic DNA. Translation: CAI13671.1 .
    BC126211 mRNA. Translation: AAI26212.1 .
    BC136474 mRNA. Translation: AAI36475.1 .
    L40372 mRNA. Translation: AAC41739.1 .
    CCDSi CCDS7422.1.
    PIRi G02157.
    RefSeqi NP_004514.2. NM_004523.3.
    UniGenei Hs.8878.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1II6 X-ray 2.10 A/B 1-368 [» ]
    1Q0B X-ray 1.90 A/B 2-368 [» ]
    1X88 X-ray 1.80 A/B 10-368 [» ]
    1YRS X-ray 2.50 A/B 1-368 [» ]
    2FKY X-ray 2.30 A/B 2-368 [» ]
    2FL2 X-ray 2.50 A/B 2-368 [» ]
    2FL6 X-ray 2.50 A/B 2-368 [» ]
    2FME X-ray 2.10 A/B 1-368 [» ]
    2G1Q X-ray 2.51 A/B 1-368 [» ]
    2GM1 X-ray 2.30 A/B/D/E 1-368 [» ]
    2IEH X-ray 2.70 A/B 2-368 [» ]
    2PG2 X-ray 1.85 A/B 1-368 [» ]
    2Q2Y X-ray 2.50 A/B 2-368 [» ]
    2Q2Z X-ray 3.00 A/B 2-368 [» ]
    2UYI X-ray 2.10 A/B 1-368 [» ]
    2UYM X-ray 2.11 A/B 1-368 [» ]
    2WOG X-ray 2.00 A/B/C 1-368 [» ]
    2X2R X-ray 2.20 A/B/C 1-368 [» ]
    2X7C X-ray 1.90 A/B 1-368 [» ]
    2X7D X-ray 2.30 A/B 1-368 [» ]
    2X7E X-ray 2.40 A/B 1-368 [» ]
    2XAE X-ray 2.60 A/B/C 1-368 [» ]
    3CJO X-ray 2.28 A/B 2-368 [» ]
    3HQD X-ray 2.19 A/B 1-369 [» ]
    3K3B X-ray 2.40 A/B 1-368 [» ]
    3K5E X-ray 1.97 A/B 1-368 [» ]
    3KEN X-ray 2.50 A 1-369 [» ]
    3L9H X-ray 2.00 A/B 1-368 [» ]
    3ZCW X-ray 1.69 A 16-363 [» ]
    4A1Z X-ray 2.80 A/B 1-368 [» ]
    4A28 X-ray 2.55 A/B 1-368 [» ]
    4A50 X-ray 2.75 A 1-368 [» ]
    4A51 X-ray 2.75 A/B/C/D/E/F/G 1-368 [» ]
    4A5Y X-ray 2.45 A/B/C 1-368 [» ]
    4AP0 X-ray 2.59 A/B/C/D 1-368 [» ]
    4AQV electron microscopy 9.70 C 1-367 [» ]
    4AQW electron microscopy 9.50 C 1-367 [» ]
    4AS7 X-ray 2.40 A 1-368 [» ]
    4B7B X-ray 2.50 A 1-368 [» ]
    4BBG X-ray 2.75 A 1-368 [» ]
    4BXN X-ray 2.79 A/B 1-368 [» ]
    4CK5 electron microscopy 10.00 C 1-367 [» ]
    4CK6 electron microscopy 9.20 C 1-367 [» ]
    4CK7 electron microscopy 9.20 C 1-367 [» ]
    ProteinModelPortali P52732.
    SMRi P52732. Positions 15-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110030. 20 interactions.
    IntActi P52732. 5 interactions.
    MINTi MINT-1152202.
    STRINGi 9606.ENSP00000260731.

    Chemistry

    BindingDBi P52732.
    ChEMBLi CHEMBL4581.

    PTM databases

    PhosphoSitei P52732.

    Polymorphism databases

    DMDMi 116242604.

    Proteomic databases

    MaxQBi P52732.
    PaxDbi P52732.
    PeptideAtlasi P52732.
    PRIDEi P52732.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260731 ; ENSP00000260731 ; ENSG00000138160 .
    GeneIDi 3832.
    KEGGi hsa:3832.
    UCSCi uc001kic.3. human.

    Organism-specific databases

    CTDi 3832.
    GeneCardsi GC10P094352.
    HGNCi HGNC:6388. KIF11.
    HPAi CAB017617.
    HPA006916.
    HPA010568.
    MIMi 148760. gene.
    152950. phenotype.
    neXtProti NX_P52732.
    Orphaneti 2526. Microcephaly - lymphedema - chorioretinopathy.
    PharmGKBi PA30177.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000116164.
    HOVERGENi HBG005572.
    InParanoidi P52732.
    KOi K10398.
    OMAi QPNSSAK.
    OrthoDBi EOG7VX8V8.
    PhylomeDBi P52732.
    TreeFami TF105230.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.

    Miscellaneous databases

    EvolutionaryTracei P52732.
    GeneWikii Kinesin_family_member_11.
    GenomeRNAii 3832.
    NextBioi 15061.
    PROi P52732.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52732.
    CleanExi HS_KIF11.
    Genevestigatori P52732.

    Family and domain databases

    Gene3Di 3.40.850.10. 1 hit.
    InterProi IPR025901. Kinesin-assoc_MT-bd_dom.
    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.
    PF13931. Microtub_bind. 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. "Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo."
      Blangy A., Lane H.A., D'Herin P., Harper M., Kress M., Nigg E.A.
      Cell 83:1159-1169(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-926, MUTAGENESIS.
    2. "Expanding the role of HsEg5 within the mitotic and post-mitotic phases of the cell cycle."
      Whitehead C.M., Rattner J.B.
      J. Cell Sci. 111:2551-2561(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Lung.
    5. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
      Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
      Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 818-867.
    6. "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.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation."
      Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C., Avruch J., Roig J.
      J. Cell Sci. 121:3912-3921(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEK6, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-926 AND SER-1033, MUTAGENESIS OF THR-926 AND SER-1033.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 THR-926, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker."
      Turner J., Anderson R., Guo J., Beraud C., Fletterick R., Sakowicz R.
      J. Biol. Chem. 276:25496-25502(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-368.
    15. "A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
      Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
      Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
    16. Cited for: VARIANTS MCLMR LEU-144; CYS-234; CYS-235 AND CYS-944.

    Entry informationi

    Entry nameiKIF11_HUMAN
    AccessioniPrimary (citable) accession number: P52732
    Secondary accession number(s): A0AV49
    , B2RMV3, Q15716, Q5VWX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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 10
      Human chromosome 10: 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