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Q9UKT4

- FBX5_HUMAN

UniProt

Q9UKT4 - FBX5_HUMAN

Protein

F-box only protein 5

Gene

FBXO5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri357 – 41963IBR-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. G1/S transition of mitotic cell cycle Source: Reactome
    3. inhibition of mitotic anaphase-promoting complex activity Source: UniProtKB
    4. metaphase/anaphase transition of mitotic cell cycle Source: Reactome
    5. microtubule polymerization Source: Ensembl
    6. mitotic cell cycle Source: Reactome
    7. negative regulation of meiosis Source: Ensembl
    8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: UniProtKB
    9. oocyte maturation Source: Ensembl
    10. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. regulation of mitotic cell cycle Source: UniProtKB
    12. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    13. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. spindle assembly involved in female meiosis I Source: Ensembl
    15. vesicle organization Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1016. Mitotic Metaphase/Anaphase Transition.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_683. G1/S-Specific Transcription.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6875. Phosphorylation of Emi1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box only protein 5
    Alternative name(s):
    Early mitotic inhibitor 1
    Gene namesi
    Name:FBXO5
    Synonyms:EMI1, FBX5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:13584. FBXO5.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle
    Note: In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431E → A: Delays degradation. 2 Publications
    Mutagenesisi145 – 1451S → E: Degraded in similar manner to wild-type. 4 Publications
    Mutagenesisi145 – 1451S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149. 4 Publications
    Mutagenesisi148 – 1481S → A: Degraded in similar manner to wild-type. 2 Publications
    Mutagenesisi149 – 1491S → E: Degraded in similar manner to wild-type. 4 Publications
    Mutagenesisi149 – 1491S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145. 4 Publications
    Mutagenesisi182 – 1821S → A: Shows impaired interaction with BTRC. 2 Publications
    Mutagenesisi210 – 2167KRNPKVD → AAAAAAA: Loss of interaction with EVI5. 1 Publication
    Mutagenesisi401 – 4011C → S: Reduced inhibition of APC. 2 Publications

    Organism-specific databases

    PharmGKBiPA28045.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447F-box only protein 5PRO_0000119881Add
    BLAST

    Post-translational modificationi

    Phosphorylation by CDK2 and subsequently by PLK1 triggers degradation during early mitosis through ubiquitin-mediated proteolysis by the SCF ubiquitin ligase complex containing the F-box protein BTRC. This degradation is necessary for the activation of APC in late mitosis and subsequent mitotic progression.
    Ubiquitinated by the by the SCF(BTRC) complex following phosphorylation by PLK1.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UKT4.
    PaxDbiQ9UKT4.
    PRIDEiQ9UKT4.

    PTM databases

    PhosphoSiteiQ9UKT4.

    Expressioni

    Developmental stagei

    Accumulates in late G1 phase, levels rise during S phase and drop in early mitosis.1 Publication

    Gene expression databases

    BgeeiQ9UKT4.
    CleanExiHS_FBXO5.
    GenevestigatoriQ9UKT4.

    Organism-specific databases

    HPAiCAB008106.
    HPA029048.

    Interactioni

    Subunit structurei

    Part of a SCF (SKP1-cullin-F-box) protein ligase complex By similarity. Interacts with BTRC, FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20. Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC27P302602EBI-852298,EBI-994813
    EVI5O604476EBI-852298,EBI-852291

    Protein-protein interaction databases

    BioGridi117655. 32 interactions.
    DIPiDIP-38023N.
    IntActiQ9UKT4. 10 interactions.
    MINTiMINT-4789777.
    STRINGi9606.ENSP00000229758.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni379 – 3813
    Beta strandi384 – 3885
    Turni389 – 3924
    Beta strandi393 – 3964
    Beta strandi404 – 4063
    Turni407 – 4093
    Beta strandi410 – 4123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M6NNMR-A364-447[»]
    ProteinModelPortaliQ9UKT4.
    SMRiQ9UKT4. Positions 374-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini250 – 29647F-boxAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni135 – 244110Interaction with EVI5Add
    BLAST

    Domaini

    The C-terminal region is required for inhibition of APC activity.

    Sequence similaritiesi

    Contains 1 F-box domain.Curated
    Contains 1 IBR-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri357 – 41963IBR-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG45978.
    HOGENOMiHOG000035122.
    HOVERGENiHBG010089.
    InParanoidiQ9UKT4.
    KOiK10292.
    OMAiSTTWKKI.
    OrthoDBiEOG783MXX.
    PhylomeDBiQ9UKT4.
    TreeFamiTF101170.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKT4-1) [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

    MSRRPCSCAL RPPRCSCSAS PSAVTAAGRP RPSDSCKEES STLSVKMKCD    50
    FNCNHVHSGL KLVKPDDIGR LVSYTPAYLE GSCKDCIKDY ERLSCIGSPI 100
    VSPRIVQLET ESKRLHNKEN QHVQQTLNST NEIEALETSR LYEDSGYSSF 150
    SLQSGLSEHE EGSLLEENFG DSLQSCLLQI QSPDQYPNKN LLPVLHFEKV 200
    VCSTLKKNAK RNPKVDREML KEIIARGNFR LQNIIGRKMG LECVDILSEL 250
    FRRGLRHVLA TILAQLSDMD LINVSKVSTT WKKILEDDKG AFQLYSKAIQ 300
    RVTENNNKFS PHASTREYVM FRTPLASVQK SAAQTSLKKD AQTKLSNQGD 350
    QKGSTYSRHN EFSEVAKTLK KNESLKACIR CNSPAKYDCY LQRATCKREG 400
    CGFDYCTKCL CNYHTTKDCS DGKLLKASCK IGPLPGTKKS KKNLRRL 447
    Length:447
    Mass (Da):50,146
    Last modified:May 1, 2000 - v1
    Checksum:i196FBC2578F92120
    GO
    Isoform 2 (identifier: Q9UKT4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: Missing.

    Show »
    Length:401
    Mass (Da):45,353
    Checksum:i8E9E775625E62A4F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121N → D in BAG51487. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071Q → E.2 Publications
    Corresponds to variant rs2073260 [ dbSNP | Ensembl ].
    VAR_024440
    Natural varianti164 – 1641L → F.
    Corresponds to variant rs7763565 [ dbSNP | Ensembl ].
    VAR_049038

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_041362Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129535 mRNA. Translation: AAF04469.1.
    AY079515 mRNA. Translation: AAL86610.1.
    AK055221 mRNA. Translation: BAG51487.1.
    AL080276 Genomic DNA. Translation: CAI18894.1.
    AL080276 Genomic DNA. Translation: CAI18895.1.
    CH471051 Genomic DNA. Translation: EAW47719.1.
    BC018905 mRNA. Translation: AAH18905.1.
    CCDSiCCDS47501.1. [Q9UKT4-2]
    CCDS5242.1. [Q9UKT4-1]
    RefSeqiNP_001135994.1. NM_001142522.1. [Q9UKT4-2]
    NP_036309.1. NM_012177.3. [Q9UKT4-1]
    UniGeneiHs.520506.

    Genome annotation databases

    EnsembliENST00000229758; ENSP00000229758; ENSG00000112029. [Q9UKT4-1]
    ENST00000367241; ENSP00000356210; ENSG00000112029. [Q9UKT4-2]
    GeneIDi26271.
    KEGGihsa:26271.
    UCSCiuc003qpg.3. human. [Q9UKT4-1]

    Polymorphism databases

    DMDMi24636847.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129535 mRNA. Translation: AAF04469.1 .
    AY079515 mRNA. Translation: AAL86610.1 .
    AK055221 mRNA. Translation: BAG51487.1 .
    AL080276 Genomic DNA. Translation: CAI18894.1 .
    AL080276 Genomic DNA. Translation: CAI18895.1 .
    CH471051 Genomic DNA. Translation: EAW47719.1 .
    BC018905 mRNA. Translation: AAH18905.1 .
    CCDSi CCDS47501.1. [Q9UKT4-2 ]
    CCDS5242.1. [Q9UKT4-1 ]
    RefSeqi NP_001135994.1. NM_001142522.1. [Q9UKT4-2 ]
    NP_036309.1. NM_012177.3. [Q9UKT4-1 ]
    UniGenei Hs.520506.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M6N NMR - A 364-447 [» ]
    ProteinModelPortali Q9UKT4.
    SMRi Q9UKT4. Positions 374-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117655. 32 interactions.
    DIPi DIP-38023N.
    IntActi Q9UKT4. 10 interactions.
    MINTi MINT-4789777.
    STRINGi 9606.ENSP00000229758.

    PTM databases

    PhosphoSitei Q9UKT4.

    Polymorphism databases

    DMDMi 24636847.

    Proteomic databases

    MaxQBi Q9UKT4.
    PaxDbi Q9UKT4.
    PRIDEi Q9UKT4.

    Protocols and materials databases

    DNASUi 26271.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229758 ; ENSP00000229758 ; ENSG00000112029 . [Q9UKT4-1 ]
    ENST00000367241 ; ENSP00000356210 ; ENSG00000112029 . [Q9UKT4-2 ]
    GeneIDi 26271.
    KEGGi hsa:26271.
    UCSCi uc003qpg.3. human. [Q9UKT4-1 ]

    Organism-specific databases

    CTDi 26271.
    GeneCardsi GC06M153291.
    HGNCi HGNC:13584. FBXO5.
    HPAi CAB008106.
    HPA029048.
    MIMi 606013. gene.
    neXtProti NX_Q9UKT4.
    PharmGKBi PA28045.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45978.
    HOGENOMi HOG000035122.
    HOVERGENi HBG010089.
    InParanoidi Q9UKT4.
    KOi K10292.
    OMAi STTWKKI.
    OrthoDBi EOG783MXX.
    PhylomeDBi Q9UKT4.
    TreeFami TF101170.

    Enzyme and pathway databases

    Reactomei REACT_1016. Mitotic Metaphase/Anaphase Transition.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_683. G1/S-Specific Transcription.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6875. Phosphorylation of Emi1.

    Miscellaneous databases

    GeneWikii FBXO5.
    GenomeRNAii 26271.
    NextBioi 48561.
    PROi Q9UKT4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UKT4.
    CleanExi HS_FBXO5.
    Genevestigatori Q9UKT4.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1)."
      Hsu J.Y., Reimann J.D.R., Sorensen C.S., Lukas J., Jackson P.K.
      Nat. Cell Biol. 4:358-366(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH FZR1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    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), VARIANT GLU-107.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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), VARIANT GLU-107.
      Tissue: Placenta.
    7. "Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase."
      Margottin-Goguet F., Hsu J.Y., Loktev A., Hsieh H.-M., Reimann J.D.R., Jackson P.K.
      Dev. Cell 4:813-826(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BTRC; PHOSPHORYLATION, DEGRADATION, MUTAGENESIS OF SER-145; SER-149 AND SER-182.
    8. "Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC inhibitor Emi1."
      Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K.
      Mol. Biol. Cell 15:5623-5634(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF GLU-143; SER-145; SER-148 AND SER-149.
    9. "Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome."
      Moshe Y., Boulaire J., Pagano M., Hershko A.
      Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF SER-145 AND SER-149.
    10. "The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1."
      Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., Jackson P.K.
      Cell 124:367-380(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EVI5, MUTAGENESIS OF 210-LYS--ASP-216.
    11. "Emi1 stably binds and inhibits the anaphase-promoting complex/cyclosome as a pseudosubstrate inhibitor."
      Miller J.J., Summers M.K., Hansen D.V., Nachury M.V., Lehman N.L., Loktev A., Jackson P.K.
      Genes Dev. 20:2410-2420(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-401.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiFBX5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKT4
    Secondary accession number(s): B3KNX5
    , Q5TF47, Q8WV29, Q9UGC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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