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Q9Y3I1

- FBX7_HUMAN

UniProt

Q9Y3I1 - FBX7_HUMAN

Protein

F-box only protein 7

Gene

FBXO7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PARK2 to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination.3 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-protein transferase activity Source: ProtInc

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. mitochondrion degradation Source: UniProtKB
    3. protein targeting to mitochondrion Source: UniProtKB
    4. protein ubiquitination Source: UniProtKB
    5. regulation of protein stability Source: UniProtKB
    6. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box only protein 7
    Gene namesi
    Name:FBXO7
    Synonyms:FBX7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:13586. FBXO7.

    Subcellular locationi

    Cytoplasm. Nucleus. Mitochondrion. Cytoplasmcytosol
    Note: Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. mitochondrion Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. protein complex Source: LIFEdb
    5. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Parkinson disease 15 (PARK15) [MIM:260300]: A neurodegenerative disorder characterized by parkinsonian and pyramidal signs. Clinical manifestations include tremor, bradykinesia, rigidity, postural instability, spasticity, mainly in the lower limbs, and hyperreflexia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti378 – 3781R → G in PARK15; no effect on interaction with PARK2. 1 Publication
    Corresponds to variant rs71799110 [ dbSNP | Ensembl ].
    VAR_047938

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221T → M: Impairs interaction with PARK2. 1 Publication
    Mutagenesisi253 – 2531V → E: Abolishes interaction with PSMF1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Parkinsonism

    Organism-specific databases

    MIMi260300. phenotype.
    Orphaneti171695. Parkinsonian-pyramidal syndrome.
    PharmGKBiPA28047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522F-box only protein 7PRO_0000119885Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3I1.
    PaxDbiQ9Y3I1.
    PRIDEiQ9Y3I1.

    PTM databases

    PhosphoSiteiQ9Y3I1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3I1.
    BgeeiQ9Y3I1.
    CleanExiHS_FBXO7.
    GenevestigatoriQ9Y3I1.

    Organism-specific databases

    HPAiCAB034296.
    HPA032114.

    Interactioni

    Subunit structurei

    Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2. Interacts with CDK6 and promotes its interaction with D-type cyclin. Isoform 1 interacts (via the N-terminal Ubl domain) with PARK2. Isoforms that lack the ubiquitin-like domain do not interact with PARK2. Isoform 1 and isoform 2 interact (via N-terminal region) with PINK1. Isoform 3 does not interact with PINK1. Interacts with PSMF1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PARK2O6026010EBI-1161222,EBI-716346
    PINK1Q9BXM78EBI-1161222,EBI-2846068
    SKP1P632082EBI-1161222,EBI-307486

    Protein-protein interaction databases

    BioGridi117326. 20 interactions.
    DIPiDIP-36125N.
    IntActiQ9Y3I1. 8 interactions.
    MINTiMINT-108554.
    STRINGi9606.ENSP00000266087.

    Structurei

    Secondary structure

    1
    522
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi181 – 19010
    Helixi195 – 20915
    Beta strandi213 – 2164
    Turni220 – 2223
    Beta strandi228 – 2303
    Beta strandi233 – 2397
    Helixi241 – 2433
    Beta strandi247 – 2559
    Beta strandi258 – 26710
    Beta strandi270 – 27910
    Helixi281 – 2833
    Helixi287 – 2893
    Helixi294 – 2974
    Helixi301 – 31111
    Helixi313 – 32311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4L9CX-ray2.10A/B180-335[»]
    4L9HX-ray2.00A180-335[»]
    ProteinModelPortaliQ9Y3I1.
    SMRiQ9Y3I1. Positions 180-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini329 – 37547F-boxPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8888Ubiquitin-likeAdd
    BLAST
    Regioni92 – 12938Important for interaction with PINK1Add
    BLAST
    Regioni129 – 16941Important for interaction with CDK6Add
    BLAST
    Regioni180 – 324145Important for dimerization and interaction with PSMF1Add
    BLAST
    Regioni381 – 522142Important for interaction with CDK6Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi481 – 4844RFDP motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi423 – 51492Pro-richAdd
    BLAST

    Domaini

    The ubiquitin-like region mediates interaction with PARK2.
    The proline-rich region is important for protein-protein interactions.

    Sequence similaritiesi

    Contains 1 F-box domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG78399.
    HOGENOMiHOG000112551.
    HOVERGENiHBG005648.
    KOiK10293.
    OMAiPLCEGGS.
    OrthoDBiEOG7S7SDG.
    PhylomeDBiQ9Y3I1.
    TreeFamiTF329830.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    IPR021625. FP_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    PF11566. PI31_Prot_N. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF81383. SSF81383. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y3I1-1) [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

    MRLRVRLLKR TWPLEVPETE PTLGHLRSHL RQSLLCTWGY SSNTRFTITL    50
    NYKDPLTGDE ETLASYGIVS GDLICLILQD DIPAPNIPSS TDSEHSSLQN 100
    NEQPSLATSS NQTSMQDEQP SDSFQGQAAQ SGVWNDDSML GPSQNFEAES 150
    IQDNAHMAEG TGFYPSEPML CSESVEGQVP HSLETLYQSA DCSDANDALI 200
    VLIHLLMLES GYIPQGTEAK ALSMPEKWKL SGVYKLQYMH PLCEGSSATL 250
    TCVPLGNLIV VNATLKINNE IRSVKRLQLL PESFICKEKL GENVANIYKD 300
    LQKLSRLFKD QLVYPLLAFT RQALNLPDVF GLVVLPLELK LRIFRLLDVR 350
    SVLSLSAVCR DLFTASNDPL LWRFLYLRDF RDNTVRVQDT DWKELYRKRH 400
    IQRKESPKGR FVMLLPSSTH TIPFYPNPLH PRPFPSSRLP PGIIGGEYDQ 450
    RPTLPYVGDP ISSLIPGPGE TPSQFPPLRP RFDPVGPLPG PNPILPGRGG 500
    PNDRFPFRPS RGRPTDGRLS FM 522
    Length:522
    Mass (Da):58,503
    Last modified:November 1, 1999 - v1
    Checksum:iC4E5E70A0747287A
    GO
    Isoform 2 (identifier: Q9Y3I1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         80-91: DDIPAPNIPSST → MARPPGGSGPLL

    Show »
    Length:443
    Mass (Da):49,358
    Checksum:i263A319CE0096FFB
    GO
    Isoform 3 (identifier: Q9Y3I1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-114: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:408
    Mass (Da):45,781
    Checksum:iFE4FE5ECFEAC37C5
    GO

    Sequence cautioni

    The sequence AAF04471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791Q → H in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti84 – 841A → P in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti154 – 1541N → S in BAG63187. (PubMed:14702039)Curated
    Sequence conflicti169 – 1691M → L in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti224 – 2241M → L in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti241 – 2411P → H in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti328 – 3281D → N in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti413 – 4131M → L in AAF04471. (PubMed:10531035)Curated
    Sequence conflicti475 – 4751F → L in AAF04471. (PubMed:10531035)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151M → I.4 Publications
    Corresponds to variant rs11107 [ dbSNP | Ensembl ].
    VAR_021408
    Natural varianti378 – 3781R → G in PARK15; no effect on interaction with PARK2. 1 Publication
    Corresponds to variant rs71799110 [ dbSNP | Ensembl ].
    VAR_047938
    Natural varianti481 – 4811R → C Found in two patients with Kufor-Rakeb syndrome also carrying R-877 in ATP13A2. 1 Publication
    VAR_066022

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 114114Missing in isoform 3. 1 PublicationVSP_044723Add
    BLAST
    Alternative sequencei1 – 7979Missing in isoform 2. 1 PublicationVSP_041073Add
    BLAST
    Alternative sequencei80 – 9112DDIPA…IPSST → MARPPGGSGPLL in isoform 2. 1 PublicationVSP_041074Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233225 mRNA. Translation: AAF67155.1.
    AL050254 mRNA. Translation: CAB43356.1.
    CR456491 mRNA. Translation: CAG30377.1.
    AK297841 mRNA. Translation: BAG60175.1.
    AK301716 mRNA. Translation: BAG63187.1.
    AL021937, AL035068, Z71183 Genomic DNA. Translation: CAI19587.1.
    AL021937, AL035068, Z71183 Genomic DNA. Translation: CAI19588.2.
    AL035068, AL021937, Z71183 Genomic DNA. Translation: CAI19333.1.
    AL035068, AL021937, Z71183 Genomic DNA. Translation: CAI19334.2.
    Z71183, AL021937, AL035068 Genomic DNA. Translation: CAI18782.1.
    Z71183, AL021937, AL035068 Genomic DNA. Translation: CAI18783.2.
    BC008361 mRNA. Translation: AAH08361.1.
    AF129537 mRNA. Translation: AAF04471.1. Different initiation.
    CCDSiCCDS13907.1. [Q9Y3I1-1]
    CCDS46695.1. [Q9Y3I1-2]
    CCDS58806.1. [Q9Y3I1-3]
    RefSeqiNP_001028196.1. NM_001033024.1. [Q9Y3I1-2]
    NP_001244919.1. NM_001257990.1. [Q9Y3I1-3]
    NP_036311.3. NM_012179.3. [Q9Y3I1-1]
    UniGeneiHs.5912.

    Genome annotation databases

    EnsembliENST00000266087; ENSP00000266087; ENSG00000100225. [Q9Y3I1-1]
    ENST00000397426; ENSP00000380571; ENSG00000100225. [Q9Y3I1-3]
    GeneIDi25793.
    KEGGihsa:25793.
    UCSCiuc003amq.3. human. [Q9Y3I1-1]
    uc003amt.3. human. [Q9Y3I1-2]

    Polymorphism databases

    DMDMi13124249.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233225 mRNA. Translation: AAF67155.1 .
    AL050254 mRNA. Translation: CAB43356.1 .
    CR456491 mRNA. Translation: CAG30377.1 .
    AK297841 mRNA. Translation: BAG60175.1 .
    AK301716 mRNA. Translation: BAG63187.1 .
    AL021937 , AL035068 , Z71183 Genomic DNA. Translation: CAI19587.1 .
    AL021937 , AL035068 , Z71183 Genomic DNA. Translation: CAI19588.2 .
    AL035068 , AL021937 , Z71183 Genomic DNA. Translation: CAI19333.1 .
    AL035068 , AL021937 , Z71183 Genomic DNA. Translation: CAI19334.2 .
    Z71183 , AL021937 , AL035068 Genomic DNA. Translation: CAI18782.1 .
    Z71183 , AL021937 , AL035068 Genomic DNA. Translation: CAI18783.2 .
    BC008361 mRNA. Translation: AAH08361.1 .
    AF129537 mRNA. Translation: AAF04471.1 . Different initiation.
    CCDSi CCDS13907.1. [Q9Y3I1-1 ]
    CCDS46695.1. [Q9Y3I1-2 ]
    CCDS58806.1. [Q9Y3I1-3 ]
    RefSeqi NP_001028196.1. NM_001033024.1. [Q9Y3I1-2 ]
    NP_001244919.1. NM_001257990.1. [Q9Y3I1-3 ]
    NP_036311.3. NM_012179.3. [Q9Y3I1-1 ]
    UniGenei Hs.5912.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4L9C X-ray 2.10 A/B 180-335 [» ]
    4L9H X-ray 2.00 A 180-335 [» ]
    ProteinModelPortali Q9Y3I1.
    SMRi Q9Y3I1. Positions 180-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117326. 20 interactions.
    DIPi DIP-36125N.
    IntActi Q9Y3I1. 8 interactions.
    MINTi MINT-108554.
    STRINGi 9606.ENSP00000266087.

    PTM databases

    PhosphoSitei Q9Y3I1.

    Polymorphism databases

    DMDMi 13124249.

    Proteomic databases

    MaxQBi Q9Y3I1.
    PaxDbi Q9Y3I1.
    PRIDEi Q9Y3I1.

    Protocols and materials databases

    DNASUi 25793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266087 ; ENSP00000266087 ; ENSG00000100225 . [Q9Y3I1-1 ]
    ENST00000397426 ; ENSP00000380571 ; ENSG00000100225 . [Q9Y3I1-3 ]
    GeneIDi 25793.
    KEGGi hsa:25793.
    UCSCi uc003amq.3. human. [Q9Y3I1-1 ]
    uc003amt.3. human. [Q9Y3I1-2 ]

    Organism-specific databases

    CTDi 25793.
    GeneCardsi GC22P032870.
    GeneReviewsi FBXO7.
    HGNCi HGNC:13586. FBXO7.
    HPAi CAB034296.
    HPA032114.
    MIMi 260300. phenotype.
    605648. gene.
    neXtProti NX_Q9Y3I1.
    Orphaneti 171695. Parkinsonian-pyramidal syndrome.
    PharmGKBi PA28047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78399.
    HOGENOMi HOG000112551.
    HOVERGENi HBG005648.
    KOi K10293.
    OMAi PLCEGGS.
    OrthoDBi EOG7S7SDG.
    PhylomeDBi Q9Y3I1.
    TreeFami TF329830.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi FBXO7. human.
    GeneWikii FBXO7.
    GenomeRNAii 25793.
    NextBioi 46969.
    PROi Q9Y3I1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3I1.
    Bgeei Q9Y3I1.
    CleanExi HS_FBXO7.
    Genevestigatori Q9Y3I1.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    IPR021625. FP_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    PF11566. PI31_Prot_N. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF81383. SSF81383. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
      Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
      Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
      Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
      Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 2 AND 3), VARIANT ILE-115.
      Tissue: Heart and Testis.
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      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 ILE-115.
      Tissue: Pancreas.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-522 (ISOFORM 1), VARIANT ILE-115.
    8. "Identification of a novel cell cycle regulated gene, HURP, overexpressed in human hepatocellular carcinoma."
      Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G., Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H., Chou C.-K.
      Oncogene 22:298-307(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLGAP5, IDENTIFICATION IN SCF COMPLEX.
    9. "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
      Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
      J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLGAP5; CUL1 AND SKP1, FUNCTION IN UBIQUITINATION OF DLGAP5.
    10. "Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6."
      Laman H., Funes J.M., Ye H., Henderson S., Galinanes-Garcia L., Hara E., Knowles P., McDonald N., Boshoff C.
      EMBO J. 24:3104-3116(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK6, SUBCELLULAR LOCATION.
    11. "The F-box protein Fbxo7 interacts with human inhibitor of apoptosis protein cIAP1 and promotes cIAP1 ubiquitination."
      Chang Y.F., Cheng C.M., Chang L.K., Jong Y.J., Yuo C.Y.
      Biochem. Biophys. Res. Commun. 342:1022-1026(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC2, FUNCTION IN UBIQUITINATION OF BIRC2.
    12. "Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor."
      Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M., Meziane E.K., McDonald N.Q.
      J. Biol. Chem. 283:22325-22335(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKP1; PSMF1 AND CDK6, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH SKP1 AND CUL1, MUTAGENESIS OF VAL-253.
    13. Cited for: FUNCTION, INTERACTION WITH PARK2 AND PINK1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-22, CHARACTERIZATION OF VARIANT PARK15 GLY-378.
    14. "Structure of the FP domain of Fbxo7 reveals a novel mode of protein-protein interaction."
      Shang J., Wang G., Yang Y., Huang X., Du Z.
      Acta Crystallogr. D 70:155-164(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 180-335.
    15. "Genome-wide linkage analysis of a Parkinsonian-pyramidal syndrome pedigree by 500 K SNP arrays."
      Shojaee S., Sina F., Banihosseini S.S., Kazemi M.H., Kalhor R., Shahidi G.-A., Fakhrai-Rad H., Ronaghi M., Elahi E.
      Am. J. Hum. Genet. 82:1375-1384(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK15 GLY-378, VARIANT ILE-115.
    16. Cited for: VARIANT CYS-481.

    Entry informationi

    Entry nameiFBX7_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3I1
    Secondary accession number(s): B4DNB3
    , B4DWX5, Q5TGC4, Q5TI86, Q96HM6, Q9UF21, Q9UKT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 132 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 22
      Human chromosome 22: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3