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Q9UKA1

- FBXL5_HUMAN

UniProt

Q9UKA1 - FBXL5_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UKA1.
CleanExiHS_FBXL5.
ExpressionAtlasiQ9UKA1. baseline and differential.
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 – 83Combined sources
Helixi12 – 3120Combined sources
Helixi37 – 6428Combined sources
Helixi66 – 738Combined sources
Helixi85 – 9814Combined sources
Helixi102 – 13231Combined sources
Helixi134 – 1418Combined sources
Helixi144 – 15815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 329-419, 598-663.
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.
GeneTreeiENSGT00390000006172.
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

        10         20         30         40         50
MAPFPEEVDV FTAPHWRMKQ LVGLYCDKLS KTNFSNNNDF RALLQSLYAT
60 70 80 90 100
FKEFKMHEQI ENEYIIGLLQ QRSQTIYNVH SDNKLSEMLS LFEKGLKNVK
110 120 130 140 150
NEYEQLNYAK QLKERLEAFT RDFLPHMKEE EEVFQPMLME YFTYEELKDI
160 170 180 190 200
KKKVIAQHCS QKDTAELLRG LSLWNHAEER QKFFKYSVDE KSDKEAEVSE
210 220 230 240 250
HSTGITHLPP EVMLSIFSYL NPQELCRCSQ VSMKWSQLTK TGSLWKHLYP
260 270 280 290 300
VHWARGDWYS GPATELDTEP DDEWVKNRKD ESRAFHEWDE DADIDESEES
310 320 330 340 350
AEESIAISIA QMEKRLLHGL IHNVLPYVGT SVKTLVLAYS SAVSSKMVRQ
360 370 380 390 400
ILELCPNLEH LDLTQTDISD SAFDSWSWLG CCQSLRHLDL SGCEKITDVA
410 420 430 440 450
LEKISRALGI LTSHQSGFLK TSTSKITSTA WKNKDITMQS TKQYACLHDL
460 470 480 490 500
TNKGIGEEID NEHPWTKPVS SENFTSPYVW MLDAEDLADI EDTVEWRHRN
510 520 530 540 550
VESLCVMETA SNFSCSTSGC FSKDIVGLRT SVCWQQHCAS PAFAYCGHSF
560 570 580 590 600
CCTGTALRTM SSLPESSAMC RKAARTRLPR GKDLIYFGSE KSDQETGRVL
610 620 630 640 650
LFLSLSGCYQ ITDHGLRVLT LGGGLPYLEH LNLSGCLTIT GAGLQDLVSA
660 670 680 690
CPSLNDEYFY YCDNINGPHA DTASGCQNLQ CGFRACCRSG E
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. Curated
The sequence AAF67489.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH30656.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAW92737.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 329-419, 598-663.
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 GC04M015606.
H-InvDB HIX0004110.
HGNCi HGNC:13602. FBXL5.
MIMi 605655. gene.
neXtProti NX_Q9UKA1.
PharmGKBi PA28025.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG29620.
GeneTreei ENSGT00390000006172.
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

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

Gene expression databases

Bgeei Q9UKA1.
CleanExi HS_FBXL5.
ExpressionAtlasi Q9UKA1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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