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O95235

- KI20A_HUMAN

UniProt

O95235 - KI20A_HUMAN

Protein

Kinesin-like protein KIF20A

Gene

KIF20A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi160 – 1678ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. microtubule-based movement Source: InterPro
    3. microtubule bundle formation Source: UniProtKB
    4. mitotic cell cycle Source: Reactome
    5. protein transport Source: UniProtKB-KW
    6. vesicle-mediated transport Source: ProtInc

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Protein transport, Transport

    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 KIF20A
    Alternative name(s):
    GG10_2
    Mitotic kinesin-like protein 2
    Short name:
    MKlp2
    Rab6-interacting kinesin-like protein
    Rabkinesin-6
    Gene namesi
    Name:KIF20A
    Synonyms:MKLP2, RAB6KIFL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9787. KIF20A.

    Subcellular locationi

    Golgi apparatus By similarity. Cytoplasmcytoskeletonspindle 1 Publication

    GO - Cellular componenti

    1. Golgi apparatus Source: ProtInc
    2. kinesin complex Source: InterPro
    3. microtubule Source: UniProtKB-KW
    4. nucleoplasm Source: Reactome
    5. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Golgi apparatus, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi528 – 5281S → A: Impairs phosphorylation by PLK1 and recruitment of PLK1 to the spindle. 1 Publication

    Organism-specific databases

    PharmGKBiPA34149.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 890889Kinesin-like protein KIF20APRO_0000125460Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei7 – 71Phosphoserine1 Publication
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei528 – 5281Phosphoserine; by PLK12 Publications
    Modified residuei532 – 5321Phosphoserine3 Publications
    Modified residuei662 – 6621Phosphoserine1 Publication
    Modified residuei668 – 6681Phosphoserine1 Publication
    Modified residuei825 – 8251Phosphoserine1 Publication
    Modified residuei857 – 8571Phosphothreonine1 Publication
    Modified residuei867 – 8671Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by PLK1 at Ser-528 during mitosis, creating a docking site for PLK1 and recruiting PLK1 at central spindle.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95235.
    PaxDbiO95235.
    PeptideAtlasiO95235.
    PRIDEiO95235.

    PTM databases

    PhosphoSiteiO95235.

    Expressioni

    Gene expression databases

    ArrayExpressiO95235.
    BgeeiO95235.
    CleanExiHS_KIF20A.
    GenevestigatoriO95235.

    Organism-specific databases

    HPAiHPA036909.
    HPA036910.

    Interactioni

    Protein-protein interaction databases

    BioGridi115418. 11 interactions.
    IntActiO95235. 4 interactions.
    MINTiMINT-4989469.
    STRINGi9606.ENSP00000378356.

    Structurei

    3D structure databases

    ProteinModelPortaliO95235.
    SMRiO95235. Positions 56-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 507444Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni763 – 890128GlobularSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili611 – 762152Sequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000054207.
    HOVERGENiHBG052246.
    InParanoidiO95235.
    KOiK10402.
    OMAiRLCEDQN.
    OrthoDBiEOG74BJR9.
    PhylomeDBiO95235.
    TreeFamiTF105232.

    Family and domain databases

    Gene3Di3.40.850.10. 2 hits.
    InterProiIPR027326. KIF20A.
    IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR24115. PTHR24115. 1 hit.
    PTHR24115:SF352. PTHR24115:SF352. 1 hit.
    PfamiPF00225. Kinesin. 1 hit.
    [Graphical view]
    PRINTSiPR00380. KINESINHEAVY.
    SMARTiSM00129. KISc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95235-1) [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

    MSQGILSPPA GLLSDDDVVV SPMFESTAAD LGSVVRKNLL SDCSVVSTSL    50
    EDKQQVPSED SMEKVKVYLR VRPLLPSELE RQEDQGCVRI ENVETLVLQA 100
    PKDSFALKSN ERGIGQATHR FTFSQIFGPE VGQASFFNLT VKEMVKDVLK 150
    GQNWLIYTYG VTNSGKTHTI QGTIKDGGIL PRSLALIFNS LQGQLHPTPD 200
    LKPLLSNEVI WLDSKQIRQE EMKKLSLLNG GLQEEELSTS LKRSVYIESR 250
    IGTSTSFDSG IAGLSSISQC TSSSQLDETS HRWAQPDTAP LPVPANIRFS 300
    IWISFFEIYN ELLYDLLEPP SQQRKRQTLR LCEDQNGNPY VKDLNWIHVQ 350
    DAEEAWKLLK VGRKNQSFAS THLNQNSSRS HSIFSIRILH LQGEGDIVPK 400
    ISELSLCDLA GSERCKDQKS GERLKEAGNI NTSLHTLGRC IAALRQNQQN 450
    RSKQNLVPFR DSKLTRVFQG FFTGRGRSCM IVNVNPCAST YDETLHVAKF 500
    SAIASQLVHA PPMQLGFPSL HSFIKEHSLQ VSPSLEKGAK ADTGLDDDIE 550
    NEADISMYGK EELLQVVEAM KTLLLKERQE KLQLEMHLRD EICNEMVEQM 600
    QQREQWCSEH LDTQKELLEE MYEEKLNILK ESLTSFYQEE IQERDEKIEE 650
    LEALLQEARQ QSVAHQQSGS ELALRRSQRL AASASTQQLQ EVKAKLQQCK 700
    AELNSTTEEL HKYQKMLEPP PSAKPFTIDV DKKLEEGQKN IRLLRTELQK 750
    LGESLQSAER ACCHSTGAGK LRQALTTCDD ILIKQDQTLA ELQNNMVLVK 800
    LDLRKKAACI AEQYHTVLKL QGQVSAKKRL GTNQENQQPN QQPPGKKPFL 850
    RNLLPRTPTC QSSTDCSPYA RILRSRRSPL LKSGPFGKKY 890
    Length:890
    Mass (Da):100,278
    Last modified:May 1, 1999 - v1
    Checksum:i6620264615496051
    GO
    Isoform 2 (identifier: O95235-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         65-82: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:872
    Mass (Da):98,100
    Checksum:i3E7BB0907A62A23B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631E → K.
    Corresponds to variant rs3734116 [ dbSNP | Ensembl ].
    VAR_049704
    Natural varianti839 – 8391P → L.
    Corresponds to variant rs3172747 [ dbSNP | Ensembl ].
    VAR_049705

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei65 – 8218Missing in isoform 2. 1 PublicationVSP_056007Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070672 mRNA. Translation: AAC83230.1.
    AF153329 mRNA. Translation: AAD37806.1.
    AK296879 mRNA. Translation: BAG59441.1.
    AC106752 Genomic DNA. No translation available.
    AC109442 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62157.1.
    CH471062 Genomic DNA. Translation: EAW62158.1.
    BC012999 mRNA. Translation: AAH12999.1.
    CCDSiCCDS4199.1.
    RefSeqiNP_005724.1. NM_005733.2.
    XP_006714577.1. XM_006714514.1.
    UniGeneiHs.718626.

    Genome annotation databases

    EnsembliENST00000394894; ENSP00000378356; ENSG00000112984.
    ENST00000508792; ENSP00000420880; ENSG00000112984.
    GeneIDi10112.
    KEGGihsa:10112.
    UCSCiuc003lcj.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070672 mRNA. Translation: AAC83230.1 .
    AF153329 mRNA. Translation: AAD37806.1 .
    AK296879 mRNA. Translation: BAG59441.1 .
    AC106752 Genomic DNA. No translation available.
    AC109442 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62157.1 .
    CH471062 Genomic DNA. Translation: EAW62158.1 .
    BC012999 mRNA. Translation: AAH12999.1 .
    CCDSi CCDS4199.1.
    RefSeqi NP_005724.1. NM_005733.2.
    XP_006714577.1. XM_006714514.1.
    UniGenei Hs.718626.

    3D structure databases

    ProteinModelPortali O95235.
    SMRi O95235. Positions 56-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115418. 11 interactions.
    IntActi O95235. 4 interactions.
    MINTi MINT-4989469.
    STRINGi 9606.ENSP00000378356.

    Chemistry

    ChEMBLi CHEMBL2021753.

    PTM databases

    PhosphoSitei O95235.

    Proteomic databases

    MaxQBi O95235.
    PaxDbi O95235.
    PeptideAtlasi O95235.
    PRIDEi O95235.

    Protocols and materials databases

    DNASUi 10112.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394894 ; ENSP00000378356 ; ENSG00000112984 .
    ENST00000508792 ; ENSP00000420880 ; ENSG00000112984 .
    GeneIDi 10112.
    KEGGi hsa:10112.
    UCSCi uc003lcj.3. human.

    Organism-specific databases

    CTDi 10112.
    GeneCardsi GC05P137542.
    HGNCi HGNC:9787. KIF20A.
    HPAi HPA036909.
    HPA036910.
    MIMi 605664. gene.
    neXtProti NX_O95235.
    PharmGKBi PA34149.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000054207.
    HOVERGENi HBG052246.
    InParanoidi O95235.
    KOi K10402.
    OMAi RLCEDQN.
    OrthoDBi EOG74BJR9.
    PhylomeDBi O95235.
    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 KIF20A.
    GenomeRNAii 10112.
    NextBioi 38255.
    PROi O95235.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95235.
    Bgeei O95235.
    CleanExi HS_KIF20A.
    Genevestigatori O95235.

    Family and domain databases

    Gene3Di 3.40.850.10. 2 hits.
    InterProi IPR027326. KIF20A.
    IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    PTHR24115:SF352. PTHR24115:SF352. 1 hit.
    Pfami PF00225. Kinesin. 1 hit.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00129. KISc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes."
      Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., ten Cate J.W., Pannekoek H.
      Blood 93:3418-3431(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Endothelial cell.
    2. "cDNA cloning, expression pattern, genomic structure and chromosomal location of RAB6KIFL, a human kinesin-like gene."
      Lai F., Fernald A.A., Zhao N., Le Beau M.M.
      Gene 248:117-125(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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: Tongue.
    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: Uterus.
    7. "Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis."
      Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., Barr F.A.
      J. Cell Biol. 162:863-875(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-528; SER-662 AND SER-668, MUTAGENESIS OF SER-528, FUNCTION.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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.
    10. "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.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-532; THR-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-14; SER-21; SER-532 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKI20A_HUMAN
    AccessioniPrimary (citable) accession number: O95235
    Secondary accession number(s): B4DL79, D3DQB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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