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Q9UKA1

- FBXL5_HUMAN

UniProt

Q9UKA1 - FBXL5_HUMAN

Protein

F-box/LRR-repeat protein 5

Gene

FBXL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi15 – 151Iron 1
    Metal bindingi57 – 571Iron 1
    Metal bindingi58 – 581Iron 1
    Metal bindingi61 – 611Iron 1
    Metal bindingi61 – 611Iron 2
    Metal bindingi80 – 801Iron 2
    Metal bindingi126 – 1261Iron 2
    Metal bindingi130 – 1301Iron 1
    Metal bindingi130 – 1301Iron 2

    GO - Molecular functioni

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

    GO - Biological processi

    1. iron ion homeostasis Source: UniProtKB
    2. protein ubiquitination Source: UniProtKB
    3. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/LRR-repeat protein 5
    Alternative name(s):
    F-box and leucine-rich repeat protein 5
    F-box protein FBL4/FBL5
    p45SKP2-like protein
    Gene namesi
    Name:FBXL5
    Synonyms:FBL4, FBL5, FLR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:13602. FBXL5.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication

    GO - Cellular componenti

    1. perinuclear region of cytoplasm Source: UniProtKB
    2. SCF ubiquitin ligase complex Source: UniProtKB
    3. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151H → A: Abolishes iron-binding and promotes its degradation. 1 Publication
    Mutagenesisi57 – 571H → A: Abolishes iron-binding and promotes its degradation. 2 Publications
    Mutagenesisi61 – 611E → A: Abolishes iron-binding and promotes its degradation. 1 Publication

    Organism-specific databases

    PharmGKBiPA28025.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 691691F-box/LRR-repeat protein 5PRO_0000119845Add
    BLAST

    Post-translational modificationi

    Polybiquitinated upon iron and oxygen depletion, leading to its degradation by the proteasome. Ubiquitination is regulated by the hemerythrin-like region that acts as an oxygen and iron sensor.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9UKA1.
    PRIDEiQ9UKA1.

    PTM databases

    PhosphoSiteiQ9UKA1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UKA1.
    BgeeiQ9UKA1.
    CleanExiHS_FBXL5.
    GenevestigatoriQ9UKA1.

    Interactioni

    Subunit structurei

    Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with ACO1/IRP1, IREB2/IRP2; the interaction depends on the 4Fe-4S cluster. Interacts with DCTN1/p150-glued.3 Publications

    Protein-protein interaction databases

    BioGridi117625. 21 interactions.
    IntActiQ9UKA1. 7 interactions.
    MINTiMINT-8247431.

    Structurei

    Secondary structure

    1
    691
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Helixi12 – 3120
    Helixi37 – 6428
    Helixi66 – 738
    Helixi85 – 9814
    Helixi102 – 13231
    Helixi134 – 1418
    Helixi144 – 15815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U9JX-ray1.60A/B1-160[»]
    3U9MX-ray1.95A/C/E/G1-160[»]
    3V5XX-ray1.85A/B1-161[»]
    3V5YX-ray2.10A/B/C/D1-161[»]
    3V5ZX-ray2.18A/B1-161[»]
    ProteinModelPortaliQ9UKA1.
    SMRiQ9UKA1. Positions 4-160, 343-409, 595-676.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini202 – 24847F-boxPROSITE-ProRule annotationAdd
    BLAST
    Repeati340 – 36425LRR 1Add
    BLAST
    Repeati365 – 39228LRR 2Add
    BLAST
    Repeati393 – 41826LRR 3Add
    BLAST
    Repeati479 – 50830LRR 4Add
    BLAST
    Repeati576 – 60732LRR 5Add
    BLAST
    Repeati608 – 63528LRR 6Add
    BLAST
    Repeati636 – 66126LRR 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 159159Hemerythrin-likeAdd
    BLAST

    Domaini

    The hemerythrin-like region acts as an oxygen and iron sensor by binding oxygen through a diiron metal-center. In absence of oxygen and iron, the protein is ubiquitinated and degraded.2 Publications

    Sequence similaritiesi

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

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG29620.
    HOVERGENiHBG051589.
    InParanoidiQ9UKA1.
    KOiK10271.
    OMAiTKQYACL.
    OrthoDBiEOG76MK7S.
    PhylomeDBiQ9UKA1.
    TreeFamiTF331105.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    IPR012312. Haemerythrin/HHE_cat-bd_motif.
    IPR006553. Leu-rich_rpt_Cys-con_subtyp.
    [Graphical view]
    PfamiPF12937. F-box-like. 1 hit.
    PF01814. Hemerythrin. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    SM00367. LRR_CC. 1 hit.
    [Graphical view]
    SUPFAMiSSF81383. SSF81383. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKA1-1) [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

    MAPFPEEVDV FTAPHWRMKQ LVGLYCDKLS KTNFSNNNDF RALLQSLYAT    50
    FKEFKMHEQI ENEYIIGLLQ QRSQTIYNVH SDNKLSEMLS LFEKGLKNVK 100
    NEYEQLNYAK QLKERLEAFT RDFLPHMKEE EEVFQPMLME YFTYEELKDI 150
    KKKVIAQHCS QKDTAELLRG LSLWNHAEER QKFFKYSVDE KSDKEAEVSE 200
    HSTGITHLPP EVMLSIFSYL NPQELCRCSQ VSMKWSQLTK TGSLWKHLYP 250
    VHWARGDWYS GPATELDTEP DDEWVKNRKD ESRAFHEWDE DADIDESEES 300
    AEESIAISIA QMEKRLLHGL IHNVLPYVGT SVKTLVLAYS SAVSSKMVRQ 350
    ILELCPNLEH LDLTQTDISD SAFDSWSWLG CCQSLRHLDL SGCEKITDVA 400
    LEKISRALGI LTSHQSGFLK TSTSKITSTA WKNKDITMQS TKQYACLHDL 450
    TNKGIGEEID NEHPWTKPVS SENFTSPYVW MLDAEDLADI EDTVEWRHRN 500
    VESLCVMETA SNFSCSTSGC FSKDIVGLRT SVCWQQHCAS PAFAYCGHSF 550
    CCTGTALRTM SSLPESSAMC RKAARTRLPR GKDLIYFGSE KSDQETGRVL 600
    LFLSLSGCYQ ITDHGLRVLT LGGGLPYLEH LNLSGCLTIT GAGLQDLVSA 650
    CPSLNDEYFY YCDNINGPHA DTASGCQNLQ CGFRACCRSG E 691
    Length:691
    Mass (Da):78,555
    Last modified:October 3, 2003 - v2
    Checksum:i923A1B31590E5145
    GO
    Isoform 2 (identifier: Q9UKA1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         29-45: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:674
    Mass (Da):76,590
    Checksum:iB114C4C0F0A37AE9
    GO

    Sequence cautioni

    The sequence AAF66616.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF67489.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH30656.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW92737.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521K → T in AAH30656. (PubMed:15489334)Curated
    Sequence conflicti195 – 1951Missing in AAF09249. (PubMed:10945468)Curated
    Sequence conflicti242 – 2421G → R in AAH30656. (PubMed:15489334)Curated
    Sequence conflicti532 – 5321V → I in BAA90978. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei29 – 4517Missing in isoform 2. 2 PublicationsVSP_008417Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176700 mRNA. Translation: AAF03700.1.
    AF199420 mRNA. Translation: AAF09249.1.
    AF142481 mRNA. Translation: AAF66616.1. Different initiation.
    AK000153 mRNA. Translation: BAA90978.1.
    AK295510 mRNA. Translation: BAG58427.1.
    BX537957 mRNA. Translation: CAD97924.1.
    AC114744 Genomic DNA. Translation: AAY40929.1.
    AC116651 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92737.1. Sequence problems.
    CH471069 Genomic DNA. Translation: EAW92739.1.
    BC030656 mRNA. Translation: AAH30656.1. Different initiation.
    AF157323 mRNA. Translation: AAF67489.1. Different initiation.
    AF174591 mRNA. Translation: AAF04512.1.
    CCDSiCCDS3415.1. [Q9UKA1-1]
    CCDS54745.1. [Q9UKA1-2]
    RefSeqiNP_001180463.1. NM_001193534.1.
    NP_001180464.1. NM_001193535.1. [Q9UKA1-2]
    NP_036293.1. NM_012161.3. [Q9UKA1-1]
    UniGeneiHs.643433.
    Hs.714386.

    Genome annotation databases

    EnsembliENST00000341285; ENSP00000344866; ENSG00000118564. [Q9UKA1-1]
    ENST00000412094; ENSP00000408679; ENSG00000118564. [Q9UKA1-2]
    GeneIDi26234.
    KEGGihsa:26234.
    UCSCiuc003gob.2. human. [Q9UKA1-1]
    uc003god.2. human. [Q9UKA1-2]

    Polymorphism databases

    DMDMi37537864.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176700 mRNA. Translation: AAF03700.1 .
    AF199420 mRNA. Translation: AAF09249.1 .
    AF142481 mRNA. Translation: AAF66616.1 . Different initiation.
    AK000153 mRNA. Translation: BAA90978.1 .
    AK295510 mRNA. Translation: BAG58427.1 .
    BX537957 mRNA. Translation: CAD97924.1 .
    AC114744 Genomic DNA. Translation: AAY40929.1 .
    AC116651 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92737.1 . Sequence problems.
    CH471069 Genomic DNA. Translation: EAW92739.1 .
    BC030656 mRNA. Translation: AAH30656.1 . Different initiation.
    AF157323 mRNA. Translation: AAF67489.1 . Different initiation.
    AF174591 mRNA. Translation: AAF04512.1 .
    CCDSi CCDS3415.1. [Q9UKA1-1 ]
    CCDS54745.1. [Q9UKA1-2 ]
    RefSeqi NP_001180463.1. NM_001193534.1.
    NP_001180464.1. NM_001193535.1. [Q9UKA1-2 ]
    NP_036293.1. NM_012161.3. [Q9UKA1-1 ]
    UniGenei Hs.643433.
    Hs.714386.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U9J X-ray 1.60 A/B 1-160 [» ]
    3U9M X-ray 1.95 A/C/E/G 1-160 [» ]
    3V5X X-ray 1.85 A/B 1-161 [» ]
    3V5Y X-ray 2.10 A/B/C/D 1-161 [» ]
    3V5Z X-ray 2.18 A/B 1-161 [» ]
    ProteinModelPortali Q9UKA1.
    SMRi Q9UKA1. Positions 4-160, 343-409, 595-676.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117625. 21 interactions.
    IntActi Q9UKA1. 7 interactions.
    MINTi MINT-8247431.

    PTM databases

    PhosphoSitei Q9UKA1.

    Polymorphism databases

    DMDMi 37537864.

    Proteomic databases

    PaxDbi Q9UKA1.
    PRIDEi Q9UKA1.

    Protocols and materials databases

    DNASUi 26234.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341285 ; ENSP00000344866 ; ENSG00000118564 . [Q9UKA1-1 ]
    ENST00000412094 ; ENSP00000408679 ; ENSG00000118564 . [Q9UKA1-2 ]
    GeneIDi 26234.
    KEGGi hsa:26234.
    UCSCi uc003gob.2. human. [Q9UKA1-1 ]
    uc003god.2. human. [Q9UKA1-2 ]

    Organism-specific databases

    CTDi 26234.
    GeneCardsi GC04M015548.
    H-InvDB HIX0004110.
    HGNCi HGNC:13602. FBXL5.
    MIMi 605655. gene.
    neXtProti NX_Q9UKA1.
    PharmGKBi PA28025.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29620.
    HOVERGENi HBG051589.
    InParanoidi Q9UKA1.
    KOi K10271.
    OMAi TKQYACL.
    OrthoDBi EOG76MK7S.
    PhylomeDBi Q9UKA1.
    TreeFami TF331105.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii FBXL5.
    GenomeRNAii 26234.
    NextBioi 48417.
    PROi Q9UKA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKA1.
    Bgeei Q9UKA1.
    CleanExi HS_FBXL5.
    Genevestigatori Q9UKA1.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    IPR012312. Haemerythrin/HHE_cat-bd_motif.
    IPR006553. Leu-rich_rpt_Cys-con_subtyp.
    [Graphical view ]
    Pfami PF12937. F-box-like. 1 hit.
    PF01814. Hemerythrin. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    SM00367. LRR_CC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81383. SSF81383. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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).
    3. "cDNA cloning of a new human protein, FLR1, containing both motifs of F-box and leucine-rich repeat."
      Shimbara N.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-691 (ISOFORMS 1/2).
      Tissue: Colon and Hippocampus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Cervix.
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Testis.
    9. "A novel gene expressed in the human adrenal gland."
      Huang C., Zhang C., Wu T., Peng Y., Gu Y., Jin Y., Jiang C., Li Y., Han Z., Wang Y., Chen Z., Fu G.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-691 (ISOFORM 1).
      Tissue: Adrenal gland.
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-691 (ISOFORMS 1/2).
    11. "FBXL5 interacts with p150Glued and regulates its ubiquitination."
      Zhang N., Liu J., Ding X., Aikhionbare F., Jin C., Yao X.
      Biochem. Biophys. Res. Commun. 359:34-39(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DCTN1.
    12. Cited for: FUNCTION, INTERACTION WITH ACO1 AND IREB2, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, IRON-BINDING, DOMAIN HEMERYTHRIN-LIKE, UBIQUITINATION, MUTAGENESIS OF HIS-15 AND HIS-57.
    13. "An E3 ligase possessing an iron responsive hemerythrin domain is a regulator of iron homeostasis."
      Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q., Grishin N.V., Bruick R.K.
      Science 326:722-726(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACO1 AND IREB2, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, IRON-BINDING, DOMAIN HEMERYTHRIN-LIKE, UBIQUITINATION, MUTAGENESIS OF HIS-57 AND GLU-61.
    14. "The structural basis of iron sensing by the human F-box protein FBXL5."
      Shu C., Sung M.W., Stewart M.D., Igumenova T.I., Tan X., Li P.
      ChemBioChem 13:788-791(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-160, IRON-BINDING SITES.
    15. "Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5)."
      Thompson J.W., Salahudeen A.A., Chollangi S., Ruiz J.C., Brautigam C.A., Makris T.M., Lipscomb J.D., Tomchick D.R., Bruick R.K.
      J. Biol. Chem. 287:7357-7365(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-161, IRON-BINDING SITES.

    Entry informationi

    Entry nameiFBXL5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKA1
    Secondary accession number(s): A8MSK4
    , B4DIB5, Q4W5A8, Q8NHP3, Q9NXN2, Q9P0I0, Q9P0X5, Q9UJT7, Q9UKC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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 4
      Human chromosome 4: 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