Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UKT7 (FBXL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FBXL3
Synonyms:FBL3A, FBXL3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. FBXL3 probably recognizes and binds phosphorylated CRY1 and CRY2. Ref.5 Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.5

Subcellular location

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

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Contains 1 F-box domain.

Contains 7 LRR (leucine-rich) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428F-box/LRR-repeat protein 3
PRO_0000119842

Regions

Domain34 – 8148F-box
Repeat119 – 14628LRR 1
Repeat181 – 20727LRR 2
Repeat208 – 23326LRR 3
Repeat234 – 25926LRR 4
Repeat316 – 34126LRR 5
Repeat343 – 36826LRR 6
Repeat369 – 39426LRR 7

Experimental info

Mutagenesis3581C → A: Loss of binding with CRY1. Ref.5
Mutagenesis3581C → S: Decrease in binding efficiency with CRY2 and of CRY2 ubiquitination efficiency, loss of binding with CRY1. Ref.5
Sequence conflict101R → H in AAF37383. Ref.2
Sequence conflict131S → A in AAF37383. Ref.2
Sequence conflict3531R → A in AAF37383. Ref.2
Sequence conflict3641I → V in BAG37051. Ref.3
Sequence conflict4121V → A in BAG37051. Ref.3

Secondary structure

..................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UKT7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AAEAB31BAF0EA5A5

FASTA42848,707
        10         20         30         40         50         60 
MKRGGRDSDR NSSEEGTAEK SKKLRTTNEH SQTCDWGNLL QDIILQVFKY LPLLDRAHAS 

        70         80         90        100        110        120 
QVCRNWNQVF HMPDLWRCFE FELNQPATSY LKATHPELIK QIIKRHSNHL QYVSFKVDSS 

       130        140        150        160        170        180 
KESAEAACDI LSQLVNCSLK TLGLISTARP SFMDLPKSHF ISALTVVFVN SKSLSSLKID 

       190        200        210        220        230        240 
DTPVDDPSLK VLVANNSDTL KLLKMSSCPH VSPAGILCVA DQCHGLRELA LNYHLLSDEL 

       250        260        270        280        290        300 
LLALSSEKHV RLEHLRIDVV SENPGQTHFH TIQKSSWDAF IRHSPKVNLV MYFFLYEEEF 

       310        320        330        340        350        360 
DPFFRYEIPA THLYFGRSVS KDVLGRVGMT CPRLVELVVC ANGLRPLDEE LIRIAERCKN 

       370        380        390        400        410        420 
LSAIGLGECE VSCSAFVEFV KMCGGRLSQL SIMEEVLIPD QKYSLEQIHW EVSKHLGRVW 


FPDMMPTW 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a family of human F-box proteins."
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., Pagano M.
Curr. Biol. 9:1177-1179(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129532 mRNA. Translation: AAF04466.1.
AF126028 mRNA. Translation: AAF37383.1.
AK314442 mRNA. Translation: BAG37051.1.
BC072448 mRNA. Translation: AAH72448.1.
RefSeqNP_036290.1. NM_012158.2.
XP_005266393.1. XM_005266336.1.
UniGeneHs.508284.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6JX-ray2.70B1-428[»]
ProteinModelPortalQ9UKT7.
SMRQ9UKT7. Positions 35-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117615. 13 interactions.
DIPDIP-40770N.
IntActQ9UKT7. 3 interactions.
MINTMINT-108681.
STRING9606.ENSP00000347834.

PTM databases

PhosphoSiteQ9UKT7.

Polymorphism databases

DMDM37537866.

Proteomic databases

PaxDbQ9UKT7.
PRIDEQ9UKT7.

Protocols and materials databases

DNASU26224.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355619; ENSP00000347834; ENSG00000005812.
GeneID26224.
KEGGhsa:26224.
UCSCuc001vkd.3. human.

Organism-specific databases

CTD26224.
GeneCardsGC13M077566.
HGNCHGNC:13599. FBXL3.
HPAHPA049134.
HPA060297.
MIM605653. gene.
neXtProtNX_Q9UKT7.
PharmGKBPA28022.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71260.
HOGENOMHOG000060185.
HOVERGENHBG051587.
InParanoidQ9UKT7.
KOK10269.
OMASWDAFIK.
OrthoDBEOG7HB596.
PhylomeDBQ9UKT7.
TreeFamTF352583.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_24941. Circadian Clock.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UKT7.
BgeeQ9UKT7.
CleanExHS_FBXL3.
GenevestigatorQ9UKT7.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
ProtoNetSearch...

Other

ChiTaRSFBXL3. human.
GeneWikiFBXL3.
GenomeRNAi26224.
NextBio48369.
PROQ9UKT7.
SOURCESearch...

Entry information

Entry nameFBXL3_HUMAN
AccessionPrimary (citable) accession number: Q9UKT7
Secondary accession number(s): B2RB04, Q9P122
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM