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Q9UKT7

- FBXL3_HUMAN

UniProt

Q9UKT7 - FBXL3_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UKT7.
CleanExiHS_FBXL3.
ExpressionAtlasiQ9UKT7. baseline and differential.
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. 15 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 – 487Combined sources
Helixi53 – 597Combined sources
Helixi64 – 674Combined sources
Turni68 – 714Combined sources
Helixi73 – 764Combined sources
Beta strandi77 – 837Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 10611Combined sources
Turni107 – 1093Combined sources
Beta strandi112 – 1176Combined sources
Helixi121 – 13111Combined sources
Beta strandi140 – 14910Combined sources
Helixi151 – 1544Combined sources
Helixi157 – 17014Combined sources
Beta strandi176 – 1783Combined sources
Helixi186 – 19611Combined sources
Turni197 – 1993Combined sources
Beta strandi202 – 2043Combined sources
Helixi213 – 22210Combined sources
Beta strandi228 – 2325Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 2458Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi253 – 2608Combined sources
Helixi274 – 28310Combined sources
Beta strandi288 – 2947Combined sources
Beta strandi303 – 3064Combined sources
Beta strandi312 – 3176Combined sources
Helixi321 – 3288Combined sources
Beta strandi335 – 3406Combined sources
Helixi348 – 35710Combined sources
Beta strandi363 – 3664Combined sources
Helixi373 – 38210Combined sources
Helixi384 – 3863Combined sources
Beta strandi388 – 3936Combined sources
Helixi394 – 3963Combined sources
Helixi405 – 41612Combined sources

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.
GeneTreeiENSGT00390000007432.
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

        10         20         30         40         50
MKRGGRDSDR NSSEEGTAEK SKKLRTTNEH SQTCDWGNLL QDIILQVFKY
60 70 80 90 100
LPLLDRAHAS QVCRNWNQVF HMPDLWRCFE FELNQPATSY LKATHPELIK
110 120 130 140 150
QIIKRHSNHL QYVSFKVDSS KESAEAACDI LSQLVNCSLK TLGLISTARP
160 170 180 190 200
SFMDLPKSHF ISALTVVFVN SKSLSSLKID DTPVDDPSLK VLVANNSDTL
210 220 230 240 250
KLLKMSSCPH VSPAGILCVA DQCHGLRELA LNYHLLSDEL LLALSSEKHV
260 270 280 290 300
RLEHLRIDVV SENPGQTHFH TIQKSSWDAF IRHSPKVNLV MYFFLYEEEF
310 320 330 340 350
DPFFRYEIPA THLYFGRSVS KDVLGRVGMT CPRLVELVVC ANGLRPLDEE
360 370 380 390 400
LIRIAERCKN LSAIGLGECE VSCSAFVEFV KMCGGRLSQL SIMEEVLIPD
410 420
QKYSLEQIHW EVSKHLGRVW FPDMMPTW
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. 15 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.
GeneTreei ENSGT00390000007432.
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

Bgeei Q9UKT7.
CleanExi HS_FBXL3.
ExpressionAtlasi Q9UKT7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 109 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