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Q8QZS3 (FLCN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Folliculin
Gene names
Name:Flcn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be a tumor suppressor. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1 By similarity.

Subunit structure

Interacts (via C-terminus) with FNIP1 and FNIP2 (via C-terminus). This mediates indirect interaction with the PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Mainly localized in the nucleus. Colocalizes with FNIP1 and FNIP2 in the cytoplasm By similarity.

Sequence similarities

Belongs to the folliculin family.

Sequence caution

The sequence BAC30240.1 differs from that shown. Reason: Frameshift at position 42.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DiseaseTumor suppressor
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTOR signaling

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction assembly

Inferred from mutant phenotype PubMed 22965878. Source: UniProtKB

hemopoiesis

Inferred from mutant phenotype PubMed 21258407. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 21258407. Source: MGI

negative regulation of ATP biosynthetic process

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 18182616PubMed 21258407. Source: MGI

negative regulation of Rho protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of TOR signaling

Inferred from mutant phenotype PubMed 18182616PubMed 18974783PubMed 21258407. Source: MGI

negative regulation of angiogenesis

Non-traceable author statement PubMed 23150719. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation involved in kidney development

Inferred from mutant phenotype PubMed 18182616PubMed 18974783PubMed 19843504PubMed 19850877. Source: MGI

negative regulation of cellular respiration

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of energy homeostasis

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of gene expression

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of mitochondrial DNA metabolic process

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of mitochondrion organization

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of muscle tissue development

Inferred from mutant phenotype PubMed 23150719. Source: UniProtKB

negative regulation of post-translational protein modification

Inferred from mutant phenotype PubMed 21209915. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19850877. Source: MGI

negative regulation of protein localization to nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21209915. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 21209915. Source: UniProtKB

positive regulation of TOR signaling

Inferred from mutant phenotype PubMed 19234517. Source: MGI

positive regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 22965878. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21258407. Source: MGI

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 21209915. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 21258407. Source: MGI

regulation of TOR signaling

Inferred from mutant phenotype PubMed 19843504. Source: MGI

regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of histone acetylation

Inferred from mutant phenotype PubMed 21258407. Source: MGI

regulation of pro-B cell differentiation

Inferred from mutant phenotype PubMed 22709692. Source: MGI

regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 23582324. Source: IntAct

protein complex binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fnip1Q68FD73EBI-6911093,EBI-6911068

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Folliculin
PRO_0000223941

Regions

Coiled coil287 – 31024 Potential

Amino acid modifications

Modified residue621Phosphoserine Ref.4
Modified residue731Phosphoserine Ref.4

Experimental info

Sequence conflict291L → M in BAE28418. Ref.1
Sequence conflict2401S → Y in BAE28418. Ref.1
Sequence conflict3281E → G in BAE32332. Ref.1
Sequence conflict3771K → R in BAC30240. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8QZS3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: DD20DB9F7AFAC81C

FASTA57964,327
        10         20         30         40         50         60 
MNAIVALCHF CELHGPRTLF CTEVLHAPLP QGAGSGDSPD QVEQAEEEEG GIQMSSRVRA 

        70         80         90        100        110        120 
HSPAEGASSE SSSPGPKKSD MCEGCRSLAV GHPGYISHDK ETSIKYVSHQ HPNHPQLFSI 

       130        140        150        160        170        180 
VRQACVRSLS CEVCPGREGP IFFGDEQHGF VFSHTFFIKD SLARGFQRWY SIIAIMMDRI 

       190        200        210        220        230        240 
YLINSWPFLL GRIRGIISEL QAKAFKVFEA EQFGCPQRAQ RMNTAFTPFL HQRNGNAARS 

       250        260        270        280        290        300 
LTSLTSDDNL WACLHTSFAW LLKACGSRLT EKLLEGAPTE DTLVQMEKLA DLEEESESWD 

       310        320        330        340        350        360 
NSEAEEEEKA PVTPEGAEGR ELTSCPTESS FLSACGSWQP PKLTGFKSLR HMRQVLGAPS 

       370        380        390        400        410        420 
FRMLAWHVLM GNQVIWKSRD VNLVHSAFEV LRTMLPVGCV RIIPYSSQYE EAYRCNFLGL 

       430        440        450        460        470        480 
SPPVPIPAHV LASEFVVVVE VHTATRSNLH PAGCEDDQSL SKYEFVVTSG SPVAADRVGP 

       490        500        510        520        530        540 
TILNKIEAAL TNQNLSVDVV DQCLICLKEE WMNKVKVLFK FTKVDSRPKE DTQKLLSVLG 

       550        560        570 
ASEEDNVKLL KFWMTGLSKT YKSHLMSTVR SPTATESRS 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adipose tissue, Egg, Hypothalamus and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Strain: FVB/N.
Tissue: Liver.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK039106 mRNA. Translation: BAC30240.1. Frameshift.
AK080933 mRNA. Translation: BAC38084.1.
AK136071 mRNA. Translation: BAE22806.1.
AK148216 mRNA. Translation: BAE28418.1.
AK154040 mRNA. Translation: BAE32332.1.
AL596204 Genomic DNA. Translation: CAI24295.1.
AL596204 Genomic DNA. Translation: CAI24297.1.
BC025820 mRNA. Translation: AAH25820.1.
CCDSCCDS24777.1.
RefSeqNP_001258285.1. NM_001271356.1.
NP_001258286.1. NM_001271357.1.
NP_666130.1. NM_146018.2.
UniGeneMm.339640.
Mm.401724.
Mm.491488.

3D structure databases

ProteinModelPortalQ8QZS3.
SMRQ8QZS3. Positions 346-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8QZS3. 1 interaction.
STRING10090.ENSMUSP00000091696.

PTM databases

PhosphoSiteQ8QZS3.

Proteomic databases

PaxDbQ8QZS3.
PRIDEQ8QZS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091246; ENSMUSP00000091696; ENSMUSG00000032633.
ENSMUST00000102697; ENSMUSP00000099758; ENSMUSG00000032633.
GeneID216805.
KEGGmmu:216805.
UCSCuc007jew.1. mouse.

Organism-specific databases

CTD201163.
MGIMGI:2442184. Flcn.

Phylogenomic databases

eggNOGNOG319853.
GeneTreeENSGT00390000009864.
HOVERGENHBG081531.
InParanoidQ8QZS3.
KOK09594.
OMADENLWAC.
OrthoDBEOG7PS1FX.
PhylomeDBQ8QZS3.
TreeFamTF315084.

Gene expression databases

BgeeQ8QZS3.
CleanExMM_FLCN.
GenevestigatorQ8QZS3.

Family and domain databases

InterProIPR021713. Folliculin.
[Graphical view]
PfamPF11704. Folliculin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio375332.
PROQ8QZS3.
SOURCESearch...

Entry information

Entry nameFLCN_MOUSE
AccessionPrimary (citable) accession number: Q8QZS3
Secondary accession number(s): Q3U4U8 expand/collapse secondary AC list , Q3UFZ1, Q5SWZ2, Q5SX01, Q5SX02, Q8CAC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot