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Q9UKT7

- FBXL3_HUMAN

UniProt

Q9UKT7 - FBXL3_HUMAN

Protein

F-box/LRR-repeat protein 3

Gene

FBXL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex involved in circadian rhythm function. Plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. The SCF(FBXL3) complex mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2. Activity of the SCF(FBXL3) complex is counteracted by the SCF(FBXL21) complex.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. entrainment of circadian clock by photoperiod Source: UniProtKB
    2. protein destabilization Source: UniProtKB
    3. protein ubiquitination Source: UniProtKB
    4. regulation of circadian rhythm Source: UniProtKB
    5. rhythmic process Source: UniProtKB-KW
    6. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Biological rhythms, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    REACT_24941. Circadian Clock.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/LRR-repeat protein 3
    Alternative name(s):
    F-box and leucine-rich repeat protein 3A
    F-box/LRR-repeat protein 3A
    Gene namesi
    Name:FBXL3
    Synonyms:FBL3A, FBXL3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:13599. FBXL3.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. SCF ubiquitin ligase complex Source: UniProtKB
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi358 – 3581C → A: Loss of binding with CRY1. 1 Publication
    Mutagenesisi358 – 3581C → S: Decrease in binding efficiency with CRY2 and of CRY2 ubiquitination efficiency, loss of binding with CRY1. 1 Publication

    Organism-specific databases

    PharmGKBiPA28022.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428F-box/LRR-repeat protein 3PRO_0000119842Add
    BLAST

    Proteomic databases

    MaxQBiQ9UKT7.
    PaxDbiQ9UKT7.
    PRIDEiQ9UKT7.

    PTM databases

    PhosphoSiteiQ9UKT7.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9UKT7.
    BgeeiQ9UKT7.
    CleanExiHS_FBXL3.
    GenevestigatoriQ9UKT7.

    Organism-specific databases

    HPAiHPA049134.
    HPA060297.

    Interactioni

    Subunit structurei

    Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXL3) composed of CUL1, SKP1, RBX1 and FBXL3. Interacts with CRY1 and CRY2 (phosphorylated).1 Publication

    Protein-protein interaction databases

    BioGridi117615. 13 interactions.
    DIPiDIP-40770N.
    IntActiQ9UKT7. 3 interactions.
    MINTiMINT-108681.
    STRINGi9606.ENSP00000347834.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 487
    Helixi53 – 597
    Helixi64 – 674
    Turni68 – 714
    Helixi73 – 764
    Beta strandi77 – 837
    Turni86 – 883
    Beta strandi89 – 913
    Helixi96 – 10611
    Turni107 – 1093
    Beta strandi112 – 1176
    Helixi121 – 13111
    Beta strandi140 – 14910
    Helixi151 – 1544
    Helixi157 – 17014
    Beta strandi176 – 1783
    Helixi186 – 19611
    Turni197 – 1993
    Beta strandi202 – 2043
    Helixi213 – 22210
    Beta strandi228 – 2325
    Helixi233 – 2353
    Helixi238 – 2458
    Beta strandi246 – 2494
    Beta strandi253 – 2608
    Helixi274 – 28310
    Beta strandi288 – 2947
    Beta strandi303 – 3064
    Beta strandi312 – 3176
    Helixi321 – 3288
    Beta strandi335 – 3406
    Helixi348 – 35710
    Beta strandi363 – 3664
    Helixi373 – 38210
    Helixi384 – 3863
    Beta strandi388 – 3936
    Helixi394 – 3963
    Helixi405 – 41612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4I6JX-ray2.70B1-428[»]
    ProteinModelPortaliQ9UKT7.
    SMRiQ9UKT7. Positions 35-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 8148F-boxAdd
    BLAST
    Repeati119 – 14628LRR 1Add
    BLAST
    Repeati181 – 20727LRR 2Add
    BLAST
    Repeati208 – 23326LRR 3Add
    BLAST
    Repeati234 – 25926LRR 4Add
    BLAST
    Repeati316 – 34126LRR 5Add
    BLAST
    Repeati343 – 36826LRR 6Add
    BLAST
    Repeati369 – 39426LRR 7Add
    BLAST

    Sequence similaritiesi

    Contains 1 F-box domain.Curated
    Contains 7 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG71260.
    HOGENOMiHOG000060185.
    HOVERGENiHBG051587.
    InParanoidiQ9UKT7.
    KOiK10269.
    OMAiSWDAFIK.
    OrthoDBiEOG7HB596.
    PhylomeDBiQ9UKT7.
    TreeFamiTF352583.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    [Graphical view]
    PfamiPF12937. F-box-like. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF81383. SSF81383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9UKT7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRGGRDSDR NSSEEGTAEK SKKLRTTNEH SQTCDWGNLL QDIILQVFKY    50
    LPLLDRAHAS QVCRNWNQVF HMPDLWRCFE FELNQPATSY LKATHPELIK 100
    QIIKRHSNHL QYVSFKVDSS KESAEAACDI LSQLVNCSLK TLGLISTARP 150
    SFMDLPKSHF ISALTVVFVN SKSLSSLKID DTPVDDPSLK VLVANNSDTL 200
    KLLKMSSCPH VSPAGILCVA DQCHGLRELA LNYHLLSDEL LLALSSEKHV 250
    RLEHLRIDVV SENPGQTHFH TIQKSSWDAF IRHSPKVNLV MYFFLYEEEF 300
    DPFFRYEIPA THLYFGRSVS KDVLGRVGMT CPRLVELVVC ANGLRPLDEE 350
    LIRIAERCKN LSAIGLGECE VSCSAFVEFV KMCGGRLSQL SIMEEVLIPD 400
    QKYSLEQIHW EVSKHLGRVW FPDMMPTW 428
    Length:428
    Mass (Da):48,707
    Last modified:May 1, 2000 - v1
    Checksum:iAAEAB31BAF0EA5A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101R → H in AAF37383. 1 PublicationCurated
    Sequence conflicti13 – 131S → A in AAF37383. 1 PublicationCurated
    Sequence conflicti353 – 3531R → A in AAF37383. 1 PublicationCurated
    Sequence conflicti364 – 3641I → V in BAG37051. (PubMed:14702039)Curated
    Sequence conflicti412 – 4121V → A in BAG37051. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129532 mRNA. Translation: AAF04466.1.
    AF126028 mRNA. Translation: AAF37383.1.
    AK314442 mRNA. Translation: BAG37051.1.
    BC072448 mRNA. Translation: AAH72448.1.
    CCDSiCCDS9457.1.
    RefSeqiNP_036290.1. NM_012158.2.
    XP_005266393.1. XM_005266336.1.
    UniGeneiHs.508284.

    Genome annotation databases

    EnsembliENST00000355619; ENSP00000347834; ENSG00000005812.
    GeneIDi26224.
    KEGGihsa:26224.
    UCSCiuc001vkd.3. human.

    Polymorphism databases

    DMDMi37537866.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129532 mRNA. Translation: AAF04466.1 .
    AF126028 mRNA. Translation: AAF37383.1 .
    AK314442 mRNA. Translation: BAG37051.1 .
    BC072448 mRNA. Translation: AAH72448.1 .
    CCDSi CCDS9457.1.
    RefSeqi NP_036290.1. NM_012158.2.
    XP_005266393.1. XM_005266336.1.
    UniGenei Hs.508284.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4I6J X-ray 2.70 B 1-428 [» ]
    ProteinModelPortali Q9UKT7.
    SMRi Q9UKT7. Positions 35-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117615. 13 interactions.
    DIPi DIP-40770N.
    IntActi Q9UKT7. 3 interactions.
    MINTi MINT-108681.
    STRINGi 9606.ENSP00000347834.

    PTM databases

    PhosphoSitei Q9UKT7.

    Polymorphism databases

    DMDMi 37537866.

    Proteomic databases

    MaxQBi Q9UKT7.
    PaxDbi Q9UKT7.
    PRIDEi Q9UKT7.

    Protocols and materials databases

    DNASUi 26224.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355619 ; ENSP00000347834 ; ENSG00000005812 .
    GeneIDi 26224.
    KEGGi hsa:26224.
    UCSCi uc001vkd.3. human.

    Organism-specific databases

    CTDi 26224.
    GeneCardsi GC13M077566.
    HGNCi HGNC:13599. FBXL3.
    HPAi HPA049134.
    HPA060297.
    MIMi 605653. gene.
    neXtProti NX_Q9UKT7.
    PharmGKBi PA28022.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71260.
    HOGENOMi HOG000060185.
    HOVERGENi HBG051587.
    InParanoidi Q9UKT7.
    KOi K10269.
    OMAi SWDAFIK.
    OrthoDBi EOG7HB596.
    PhylomeDBi Q9UKT7.
    TreeFami TF352583.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    REACT_24941. Circadian Clock.

    Miscellaneous databases

    ChiTaRSi FBXL3. human.
    GeneWikii FBXL3.
    GenomeRNAii 26224.
    NextBioi 48369.
    PROi Q9UKT7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKT7.
    Bgeei Q9UKT7.
    CleanExi HS_FBXL3.
    Genevestigatori Q9UKT7.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    [Graphical view ]
    Pfami PF12937. F-box-like. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81383. SSF81383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Transcript mapping on the CLN5 region on 13q22."
      Klockars T., Holmberg V., Savukoski M., Lander E.S., Peltonen L.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Placenta.
    4. "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].
      Tissue: Skin.
    5. "SCFFbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins."
      Busino L., Bassermann F., Maiolica A., Lee C., Nolan P.M., Godinho S.I., Draetta G.F., Pagano M.
      Science 316:900-904(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK, INTERACTION WITH CRY1 AND CRY2, MUTAGENESIS OF CYS-358.
    6. "Competing E3 ubiquitin ligases govern circadian periodicity by degradation of CRY in nucleus and cytoplasm."
      Yoo S.H., Mohawk J.A., Siepka S.M., Shan Y., Huh S.K., Hong H.K., Kornblum I., Kumar V., Koike N., Xu M., Nussbaum J., Liu X., Chen Z., Chen Z.J., Green C.B., Takahashi J.S.
      Cell 152:1091-1105(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.

    Entry informationi

    Entry nameiFBXL3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKT7
    Secondary accession number(s): B2RB04, Q9P122
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 108 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 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3