Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95239

- KIF4A_HUMAN

UniProt

O95239 - KIF4A_HUMAN

Protein

Chromosome-associated kinesin KIF4A

Gene

KIF4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 958ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. microtubule motor activity Source: ProtInc

    GO - Biological processi

    1. anterograde axon cargo transport Source: ProtInc
    2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. metabolic process Source: GOC
    6. microtubule-based movement Source: Reactome
    7. organelle organization Source: ProtInc

    Keywords - Molecular functioni

    Motor protein

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromosome-associated kinesin KIF4A
    Alternative name(s):
    Chromokinesin-A
    Gene namesi
    Name:KIF4A
    Synonyms:KIF4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13339. KIF4A.

    Subcellular locationi

    Nucleus matrix. Cytoplasmcytoskeletonspindle. Midbody. Chromosome
    Note: Not present in the nucleolus. In early mitosis, associated with the mitotic spindle, in anaphase, localized to the spindle midzone and, in telophase and cytokinesis, to the midbody. In late cytokinesis, found in the center of the midbody. Associated with chromosomes at all stages of mitosis.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. cytosol Source: Reactome
    4. kinesin complex Source: InterPro
    5. membrane Source: UniProtKB
    6. midbody Source: UniProtKB
    7. nuclear matrix Source: UniProtKB-SubCell
    8. nucleus Source: HPA
    9. spindle microtubule Source: ProtInc

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30105.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12321232Chromosome-associated kinesin KIF4APRO_0000125437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei799 – 7991Phosphothreonine2 Publications
    Modified residuei801 – 8011Phosphoserine2 Publications
    Modified residuei951 – 9511Phosphoserine1 Publication
    Modified residuei995 – 9951Phosphothreonine1 Publication
    Modified residuei1001 – 10011Phosphoserine3 Publications
    Modified residuei1013 – 10131Phosphoserine1 Publication
    Modified residuei1017 – 10171Phosphoserine1 Publication
    Modified residuei1028 – 10281Phosphoserine1 Publication
    Modified residuei1181 – 11811Phosphothreonine2 Publications
    Modified residuei1186 – 11861Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95239.
    PaxDbiO95239.
    PRIDEiO95239.

    PTM databases

    PhosphoSiteiO95239.

    Expressioni

    Tissue specificityi

    Highly expressed in hematopoietic tissues, fetal liver, spleen, thymus and adult thymus and bone marrow. Lower levels are found in heart, testis, kidney, colon and lung.1 Publication

    Gene expression databases

    BgeeiO95239.
    CleanExiHS_KIF4A.
    GenevestigatoriO95239.

    Organism-specific databases

    HPAiHPA034745.
    HPA034746.

    Interactioni

    Subunit structurei

    Interacts with unphosphorylated PRC1 during late mitosis.2 Publications

    Protein-protein interaction databases

    BioGridi117288. 14 interactions.
    IntActiO95239. 5 interactions.
    MINTiMINT-3002743.
    STRINGi9606.ENSP00000363524.

    Structurei

    3D structure databases

    ProteinModelPortaliO95239.
    SMRiO95239. Positions 4-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 336328Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni663 – 1232570Interaction with PRC1Add
    BLAST
    Regioni1000 – 1232233GlobularAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili350 – 999650Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi793 – 7986Nuclear localization signal

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    HOVERGENiHBG052256.
    InParanoidiO95239.
    KOiK10395.
    OMAiEVEVMVS.
    OrthoDBiEOG7P8P9J.
    PhylomeDBiO95239.
    TreeFamiTF105224.

    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95239-1) [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

    MKEEVKGIPV RVALRCRPLV PKEISEGCQM CLSFVPGEPQ VVVGTDKSFT     50
    YDFVFDPSTE QEEVFNTAVA PLIKGVFKGY NATVLAYGQT GSGKTYSMGG 100
    AYTAEQENEP TVGVIPRVIQ LLFKEIDKKS DFEFTLKVSY LEIYNEEILD 150
    LLCPSREKAQ INIREDPKEG IKIVGLTEKT VLVALDTVSC LEQGNNSRTV 200
    ASTAMNSQSS RSHAIFTISL EQRKKSDKNS SFRSKLHLVD LAGSERQKKT 250
    KAEGDRLKEG ININRGLLCL GNVISALGDD KKGGFVPYRD SKLTRLLQDS 300
    LGGNSHTLMI ACVSPADSNL EETLNTLRYA DRARKIKNKP IVNIDPQTAE 350
    LNHLKQQVQQ LQVLLLQAHG GTLPGSITVE PSENLQSLME KNQSLVEENE 400
    KLSRGLSEAA GQTAQMLERI ILTEQANEKM NAKLEELRQH AACKLDLQKL 450
    VETLEDQELK ENVEIICNLQ QLITQLSDET VACMAAAIDT AVEQEAQVET 500
    SPETSRSSDA FTTQHALRQA QMSKELVELN KALALKEALA RKMTQNDSQL 550
    QPIQYQYQDN IKELELEVIN LQKEKEELVL ELQTAKKDAN QAKLSERRRK 600
    RLQELEGQIA DLKKKLNEQS KLLKLKESTE RTVSKLNQEI RMMKNQRVQL 650
    MRQMKEDAEK FRQWKQKKDK EVIQLKERDR KRQYELLKLE RNFQKQSNVL 700
    RRKTEEAAAA NKRLKDALQK QREVADKRKE TQSRGMEGTA ARVKNWLGNE 750
    IEVMVSTEEA KRHLNDLLED RKILAQDVAQ LKEKKESGEN PPPKLRRRTF 800
    SLTEVRGQVS ESEDSITKQI ESLETEMEFR SAQIADLQQK LLDAESEDRP 850
    KQRWENIATI LEAKCALKYL IGELVSSKIQ VSKLESSLKQ SKTSCADMQK 900
    MLFEERNHFA EIETELQAEL VRMEQQHQEK VLYLLSQLQQ SQMAEKQLEE 950
    SVSEKEQQLL STLKCQDEEL EKMREVCEQN QQLLRENEII KQKLTLLQVA 1000
    SRQKHLPKDT LLSPDSSFEY VPPKPKPSRV KEKFLEQSMD IEDLKYCSEH 1050
    SVNEHEDGDG DDDEGDDEEW KPTKLVKVSR KNIQGCSCKG WCGNKQCGCR 1100
    KQKSDCGVDC CCDPTKCRNR QQGKDSLGTV ERTQDSEGSF KLEDPTEVTP 1150
    GLSFFNPVCA TPNSKILKEM CDVEQVLSKK TPPAPSPFDL PELKHVATEY 1200
    QENKAPGKKK KRALASNTSF FSGCSPIEEE AH 1232
    Length:1,232
    Mass (Da):139,881
    Last modified:April 12, 2005 - v3
    Checksum:iAD1B7C2A10AB24DB
    GO
    Isoform 2 (identifier: O95239-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1086-1127: CSCKGWCGNK...RNRQQGKDSL → VLLLTPVISA...RDPVSTKPKN
         1128-1232: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,127
    Mass (Da):128,459
    Checksum:i84D7ABE2CE39697A
    GO

    Sequence cautioni

    The sequence AAH49218.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231R → G in AAD05492. (PubMed:10978527)Curated
    Sequence conflicti231 – 2311S → T in AAF86334. (PubMed:9168136)Curated
    Sequence conflicti286 – 2861V → A in AAD05492. (PubMed:10978527)Curated
    Sequence conflicti564 – 5641L → H in AAF86334. (PubMed:9168136)Curated
    Sequence conflicti564 – 5641L → P in AAD05492. (PubMed:10978527)Curated
    Sequence conflicti600 – 6001K → E in CAB75427. 1 PublicationCurated
    Sequence conflicti668 – 6681K → R1 PublicationCurated
    Sequence conflicti668 – 6681K → R(PubMed:10978527)Curated
    Sequence conflicti928 – 9281Q → P in AAD51855. 1 PublicationCurated
    Sequence conflicti958 – 9581Q → R in CAB75427. 1 PublicationCurated
    Sequence conflicti960 – 9601L → Q in AAD51855. 1 PublicationCurated
    Sequence conflicti996 – 9972LL → S in AAF86334. (PubMed:9168136)Curated
    Sequence conflicti1003 – 101412QKHLP…TLLSP → RTLPRIPFYLQ in AAF86334. (PubMed:9168136)CuratedAdd
    BLAST
    Sequence conflicti1022 – 10221P → Q in AAD05492. (PubMed:10978527)Curated
    Sequence conflicti1077 – 10771K → N in AAD05492. (PubMed:10978527)Curated
    Sequence conflicti1138 – 11381G → S in AAD05492. (PubMed:10978527)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti422 – 4221L → W.2 Publications
    Corresponds to variant rs1199457 [ dbSNP | Ensembl ].
    VAR_021828
    Natural varianti491 – 4911A → V.
    Corresponds to variant rs2297871 [ dbSNP | Ensembl ].
    VAR_049693
    Natural varianti1193 – 11931L → S.
    Corresponds to variant rs1046485 [ dbSNP | Ensembl ].
    VAR_049694

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1086 – 112742CSCKG…GKDSL → VLLLTPVISALWEAEARGLL EARSSRPAWATWRDPVSTKP KN in isoform 2. 1 PublicationVSP_013375Add
    BLAST
    Alternative sequencei1128 – 1232105Missing in isoform 2. 1 PublicationVSP_013376Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179308 mRNA. Translation: AAD51855.1.
    AF071592 mRNA. Translation: AAD05492.2.
    AJ271784 mRNA. Translation: CAB75427.1.
    AK313133 mRNA. Translation: BAG35952.1.
    AL139398, AL357752 Genomic DNA. Translation: CAI41024.1.
    AL357752, AL139398 Genomic DNA. Translation: CAI41487.1.
    CH471132 Genomic DNA. Translation: EAX05341.1.
    CH471132 Genomic DNA. Translation: EAX05342.1.
    BC049218 mRNA. Translation: AAH49218.1. Sequence problems.
    BC050548 mRNA. Translation: AAH50548.1.
    AF277375 mRNA. Translation: AAF86334.1.
    CCDSiCCDS14401.1. [O95239-1]
    RefSeqiNP_036442.3. NM_012310.4. [O95239-1]
    UniGeneiHs.648326.

    Genome annotation databases

    EnsembliENST00000374403; ENSP00000363524; ENSG00000090889. [O95239-1]
    GeneIDi24137.
    KEGGihsa:24137.
    UCSCiuc004dyf.2. human. [O95239-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179308 mRNA. Translation: AAD51855.1 .
    AF071592 mRNA. Translation: AAD05492.2 .
    AJ271784 mRNA. Translation: CAB75427.1 .
    AK313133 mRNA. Translation: BAG35952.1 .
    AL139398 , AL357752 Genomic DNA. Translation: CAI41024.1 .
    AL357752 , AL139398 Genomic DNA. Translation: CAI41487.1 .
    CH471132 Genomic DNA. Translation: EAX05341.1 .
    CH471132 Genomic DNA. Translation: EAX05342.1 .
    BC049218 mRNA. Translation: AAH49218.1 . Sequence problems.
    BC050548 mRNA. Translation: AAH50548.1 .
    AF277375 mRNA. Translation: AAF86334.1 .
    CCDSi CCDS14401.1. [O95239-1 ]
    RefSeqi NP_036442.3. NM_012310.4. [O95239-1 ]
    UniGenei Hs.648326.

    3D structure databases

    ProteinModelPortali O95239.
    SMRi O95239. Positions 4-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117288. 14 interactions.
    IntActi O95239. 5 interactions.
    MINTi MINT-3002743.
    STRINGi 9606.ENSP00000363524.

    Chemistry

    ChEMBLi CHEMBL6163.

    PTM databases

    PhosphoSitei O95239.

    Proteomic databases

    MaxQBi O95239.
    PaxDbi O95239.
    PRIDEi O95239.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374403 ; ENSP00000363524 ; ENSG00000090889 . [O95239-1 ]
    GeneIDi 24137.
    KEGGi hsa:24137.
    UCSCi uc004dyf.2. human. [O95239-1 ]

    Organism-specific databases

    CTDi 24137.
    GeneCardsi GC0XP069509.
    H-InvDB HIX0016851.
    HGNCi HGNC:13339. KIF4A.
    HPAi HPA034745.
    HPA034746.
    MIMi 300521. gene.
    neXtProti NX_O95239.
    PharmGKBi PA30105.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOVERGENi HBG052256.
    InParanoidi O95239.
    KOi K10395.
    OMAi EVEVMVS.
    OrthoDBi EOG7P8P9J.
    PhylomeDBi O95239.
    TreeFami TF105224.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.

    Miscellaneous databases

    ChiTaRSi KIF4A. human.
    GeneWikii KIF4A.
    GenomeRNAii 24137.
    NextBioi 46801.
    PROi O95239.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95239.
    CleanExi HS_KIF4A.
    Genevestigatori O95239.

    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. "Human KIF4 mRNA, complete coding sequence."
      Villard L.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymphocyte.
    2. "Identification of the human homologue of mouse KIF4, a kinesin superfamily motor protein."
      Oh S.J., Hahn H., Torrey T.A., Shin H., Choi W., Lee Y.M., Morse H.C. III, Kim W.
      Biochim. Biophys. Acta 1493:219-224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT TRP-422.
    3. Rentsch A., Neumann T., Rommerskirch W.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retinoblastoma.
    4. "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 1).
      Tissue: Tongue.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1-668 (ISOFORM 1), VARIANT TRP-422.
      Tissue: Lymph and Testis.
    8. "Increased chromokinesin immunoreactivity in retinoblastoma cells."
      Yan R.-T., Wang S.-Z.
      Gene 189:263-267(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-1232.
      Tissue: Retinoblastoma.
    9. "Human kinesin superfamily member 4 is dominantly localized in the nuclear matrix and is associated with chromosomes during mitosis."
      Lee Y.M., Lee S., Lee E., Shin H., Hahn H., Choi W., Kim W.
      Biochem. J. 360:549-556(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRC1.
    11. "Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is essential for midzone formation and cytokinesis."
      Zhu C., Jiang W.
      Proc. Natl. Acad. Sci. U.S.A. 102:343-348(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRC1.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-799; SER-801; SER-951; SER-1001; SER-1013; SER-1017 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995 AND SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "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].
    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 THR-799; SER-801; SER-1001; THR-1181 AND SER-1186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKIF4A_HUMAN
    AccessioniPrimary (citable) accession number: O95239
    Secondary accession number(s): B2R7V5
    , D3DVU4, Q86TN3, Q86XX7, Q9NNY6, Q9NY24, Q9UMW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 140 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3