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Q9UKT7

- FBXL3_HUMAN

UniProt

Q9UKT7 - FBXL3_HUMAN

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Protein
F-box/LRR-repeat protein 3
Gene
FBXL3, FBL3A, FBXL3A
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. protein binding Source: UniProtKB
  2. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

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

GO - Cellular componenti

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

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 F-box domain.

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

Sequence conflict

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

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

« 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: September 3, 2014
This is version 107 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

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