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Q9BYG3

- MK67I_HUMAN

UniProt

Q9BYG3 - MK67I_HUMAN

Protein

MKI67 FHA domain-interacting nucleolar phosphoprotein

Gene

NIFK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of phosphatase activity Source: UniProtKB
    2. protein complex assembly Source: UniProtKB
    3. rRNA metabolic process Source: UniProtKB
    4. rRNA transcription Source: UniProtKB

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MKI67 FHA domain-interacting nucleolar phosphoprotein
    Alternative name(s):
    Nucleolar phosphoprotein Nopp34
    Nucleolar protein interacting with the FHA domain of pKI-67
    Short name:
    hNIFK
    Gene namesi
    Name:NIFK
    Synonyms:MKI67IP, NOPP34
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17838. NIFK.

    Subcellular locationi

    Nucleusnucleolus. Chromosome
    Note: Localizes to mitotic chromosomes in conjunction with MKI67.

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi230 – 2301S → A: Loss of phosphorylation site. 1 Publication
    Mutagenesisi234 – 2341T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications
    Mutagenesisi235 – 2351P → A: Reduces phosphorylation at T-234. 1 Publication
    Mutagenesisi238 – 2381T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications
    Mutagenesisi239 – 2391P → A: Reduces phosphorylation at T-234 and T-238. 1 Publication

    Organism-specific databases

    PharmGKBiPA38470.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 293292MKI67 FHA domain-interacting nucleolar phosphoproteinPRO_0000081629Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei218 – 2181Phosphoserine3 Publications
    Modified residuei223 – 2231Phosphothreonine4 Publications
    Modified residuei230 – 2301Phosphoserine2 Publications
    Modified residuei234 – 2341Phosphothreonine4 Publications
    Modified residuei238 – 2381Phosphothreonine3 Publications
    Modified residuei247 – 2471Phosphoserine2 Publications
    Modified residuei279 – 2791Phosphothreonine2 Publications

    Post-translational modificationi

    Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230. Thr-234 is phosphorylated only when Thr-238 is phosphorylated. Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated. Phosphorylation enhances MKI67 binding.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BYG3.
    PaxDbiQ9BYG3.
    PeptideAtlasiQ9BYG3.
    PRIDEiQ9BYG3.

    2D gel databases

    SWISS-2DPAGEQ9BYG3.

    PTM databases

    PhosphoSiteiQ9BYG3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BYG3.
    BgeeiQ9BYG3.
    CleanExiHS_MKI67IP.
    GenevestigatoriQ9BYG3.

    Organism-specific databases

    HPAiCAB015382.
    HPA035735.
    HPA035736.

    Interactioni

    Subunit structurei

    Binds to the FHA domain of MKI67; this interaction is enhanced in mitosis.1 Publication

    Protein-protein interaction databases

    BioGridi124066. 42 interactions.
    DIPiDIP-28134N.
    IntActiQ9BYG3. 6 interactions.
    MINTiMINT-1031770.
    STRINGi9606.ENSP00000285814.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi239 – 25113
    Helixi254 – 2574
    Beta strandi260 – 2656

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AFFNMR-B226-269[»]
    ProteinModelPortaliQ9BYG3.
    SMRiQ9BYG3. Positions 41-107, 228-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYG3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 12379RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni226 – 26944Interaction with MKI67Add
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG244773.
    HOGENOMiHOG000242795.
    HOVERGENiHBG057796.
    InParanoidiQ9BYG3.
    KOiK14838.
    OMAiGIDYNFP.
    OrthoDBiEOG7W6WNN.
    PhylomeDBiQ9BYG3.
    TreeFamiTF315137.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR021043. hNIFK_FHA_Ki67_binding.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF12196. hNIFK_binding. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BYG3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR    50
    HLPNLLDETQ IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK 100
    IVAETMNNYL FGERLLECHF MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN 150
    RNRTLTQKLR MEERFKKKER LLRKKLAKKG IDYDFPSLIL QKTESISKTN 200
    RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT FLERRKSQVA 250
    ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ 293
    Length:293
    Mass (Da):34,222
    Last modified:June 1, 2001 - v1
    Checksum:i9D288ECF2B4CE119
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441P → Q.1 Publication
    Corresponds to variant rs17852212 [ dbSNP | Ensembl ].
    VAR_027182

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB044971 mRNA. Translation: BAB41210.1.
    AK291903 mRNA. Translation: BAF84592.1.
    AC018737 Genomic DNA. Translation: AAY14830.1.
    CH471103 Genomic DNA. Translation: EAW95261.1.
    BC012457 mRNA. Translation: AAH12457.1.
    BC022990 mRNA. Translation: AAH22990.1.
    BC024238 mRNA. Translation: AAH24238.1.
    CCDSiCCDS2135.1.
    RefSeqiNP_115766.3. NM_032390.4.
    UniGeneiHs.367842.

    Genome annotation databases

    EnsembliENST00000285814; ENSP00000285814; ENSG00000155438.
    GeneIDi84365.
    KEGGihsa:84365.
    UCSCiuc002tnk.3. human.

    Polymorphism databases

    DMDMi71151919.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB044971 mRNA. Translation: BAB41210.1 .
    AK291903 mRNA. Translation: BAF84592.1 .
    AC018737 Genomic DNA. Translation: AAY14830.1 .
    CH471103 Genomic DNA. Translation: EAW95261.1 .
    BC012457 mRNA. Translation: AAH12457.1 .
    BC022990 mRNA. Translation: AAH22990.1 .
    BC024238 mRNA. Translation: AAH24238.1 .
    CCDSi CCDS2135.1.
    RefSeqi NP_115766.3. NM_032390.4.
    UniGenei Hs.367842.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AFF NMR - B 226-269 [» ]
    ProteinModelPortali Q9BYG3.
    SMRi Q9BYG3. Positions 41-107, 228-267.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124066. 42 interactions.
    DIPi DIP-28134N.
    IntActi Q9BYG3. 6 interactions.
    MINTi MINT-1031770.
    STRINGi 9606.ENSP00000285814.

    PTM databases

    PhosphoSitei Q9BYG3.

    Polymorphism databases

    DMDMi 71151919.

    2D gel databases

    SWISS-2DPAGE Q9BYG3.

    Proteomic databases

    MaxQBi Q9BYG3.
    PaxDbi Q9BYG3.
    PeptideAtlasi Q9BYG3.
    PRIDEi Q9BYG3.

    Protocols and materials databases

    DNASUi 84365.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285814 ; ENSP00000285814 ; ENSG00000155438 .
    GeneIDi 84365.
    KEGGi hsa:84365.
    UCSCi uc002tnk.3. human.

    Organism-specific databases

    CTDi 84365.
    GeneCardsi GC02M122484.
    HGNCi HGNC:17838. NIFK.
    HPAi CAB015382.
    HPA035735.
    HPA035736.
    MIMi 611970. gene.
    neXtProti NX_Q9BYG3.
    PharmGKBi PA38470.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244773.
    HOGENOMi HOG000242795.
    HOVERGENi HBG057796.
    InParanoidi Q9BYG3.
    KOi K14838.
    OMAi GIDYNFP.
    OrthoDBi EOG7W6WNN.
    PhylomeDBi Q9BYG3.
    TreeFami TF315137.

    Miscellaneous databases

    EvolutionaryTracei Q9BYG3.
    GeneWikii MKI67IP.
    GenomeRNAii 84365.
    NextBioi 74141.
    PROi Q9BYG3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYG3.
    Bgeei Q9BYG3.
    CleanExi HS_MKI67IP.
    Genevestigatori Q9BYG3.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR021043. hNIFK_FHA_Ki67_binding.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF12196. hNIFK_binding. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis."
      Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.
      J. Biol. Chem. 276:25386-25391(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MKI67, MUTAGENESIS OF THR-234 AND THR-238, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT GLN-144.
      Tissue: Brain, Lung and Placenta.
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-24; 87-114; 180-192; 227-244 AND 272-284, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions."
      Li H., Byeon I.-J., Ju Y., Tsai M.-D.
      J. Mol. Biol. 335:371-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-234, INTERACTION WITH MKI67.
    9. "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 THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-238 AND THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-218; THR-223 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67."
      Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.
      Nat. Struct. Mol. Biol. 12:987-993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 226-269 IN COMPLEX WITH MKI67, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-230; THR-234; PRO-235; THR-238 AND PRO-239, PHOSPHORYLATION AT SER-230; THR-234 AND THR-238.

    Entry informationi

    Entry nameiMK67I_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYG3
    Secondary accession number(s): A8K788, Q8TB66, Q96ED4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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