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Q5XUX0 (FBX31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box only protein 31
Gene names
Name:FBXO31
Synonyms:FBX14, FBX31
ORF Names:PP2386
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. May act as a tumor suppressor. Ref.7 Ref.8

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Ref.7 Ref.8

Tissue specificity

Highly expressed in brain. Expressed at moderate levels in most tissues, except bone marrow. Ref.7

Developmental stage

Expression is cell-cycle regulated, and peaks at late G2 to early G1 phase (at protein level). Ref.7

Induction

By DNA damage. Increases after UV irradiation, X-ray irradiation, oxidative stress (H2O2) or addition of the chemotherapeutic DNA-damaging agents etoposide, adriamycin, cisplatin or fluorouracil. Ref.8

Post-translational modification

Phosphorylation at Ser-278 by ATM following gamma-irradiation results in its stabilization.

Sequence similarities

Belongs to the FBXO31 family.

Contains 1 F-box domain.

Sequence caution

The sequence AAH12748.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL55855.1 differs from that shown. Reason: Frameshift at position 496.

The sequence CAB55929.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5XUX0-1)

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.
Isoform 2 (identifier: Q5XUX0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: MAVCARLCGV...DTIWRRRCRE → MFLVT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539F-box only protein 31
PRO_0000119921

Regions

Domain64 – 11047F-box
Compositional bias58 – 636Poly-Pro

Amino acid modifications

Modified residue331Phosphoserine By similarity
Modified residue371Phosphothreonine By similarity
Modified residue2781Phosphoserine; by ATM Ref.8

Natural variations

Alternative sequence1 – 113113MAVCA…RRCRE → MFLVT in isoform 2.
VSP_037469

Experimental info

Mutagenesis2781S → A: Fails to accumulate following gamma-irradiation. Ref.8
Mutagenesis4001S → A: No effect following gamma-irradiation. Ref.8
Sequence conflict1381L → V in AAU50679. Ref.1
Sequence conflict2811D → E in AAU50679. Ref.1
Sequence conflict4661C → S in AAU50679. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: E833D63A361E7381

FASTA53960,664
        10         20         30         40         50         60 
MAVCARLCGV GPSRGCRRRQ QRRGPAETAA ADSEPDTDPE EERIEASAGV GGGLCAGPSP 

        70         80         90        100        110        120 
PPPRCSLLEL PPELLVEIFA SLPGTDLPSL AQVCTKFRRI LHTDTIWRRR CREEYGVCEN 

       130        140        150        160        170        180 
LRKLEITGVS CRDVYAKLLH RYRHILGLWQ PDIGPYGGLL NVVVDGLFII GWMYLPPHDP 

       190        200        210        220        230        240 
HVDDPMRFKP LFRIHLMERK AATVECMYGH KGPHHGHIQI VKKDEFSTKC NQTDHHRMSG 

       250        260        270        280        290        300 
GRQEEFRTWL REEWGRTLED IFHEHMQELI LMKFIYTSQY DNCLTYRRIY LPPSRPDDLI 

       310        320        330        340        350        360 
KPGLFKGTYG SHGLEIVMLS FHGRRARGTK ITGDPNIPAG QQTVEIDLRH RIQLPDLENQ 

       370        380        390        400        410        420 
RNFNELSRIV LEVRERVRQE QQEGGHEAGE GRGRQGPRES QPSPAQPRAE APSKGPDGTP 

       430        440        450        460        470        480 
GEDGGEPGDA VAAAEQPAQC GQGQPFVLPV GVSSRNEDYP RTCRMCFYGT GLIAGHGFTS 

       490        500        510        520        530 
PERTPGVFIL FDEDRFGFVW LELKSFSLYS RVQATFRNAD APSPQAFDEM LKNIQSLTS 

« Hide

Isoform 2 [UniParc].

Checksum: 69E7352F7253F32C
Show »

FASTA43149,039

References

« Hide 'large scale' references
[1]"Systematic analysis and nomenclature of mammalian F-box proteins."
Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M., Harper J.W.
Genes Dev. 18:2573-2580(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A novel F-box protein is differentially expressed in hematopoietic malignancies."
Banham A.H., Cordell J.L., Jones M., Liggins A.P., Pulford K., Mason D.Y.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Choriocarcinoma.
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Placenta.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-539 (ISOFORM 1).
Tissue: Testis.
[7]"FBXO31 is the chromosome 16q24.3 senescence gene, a candidate breast tumor suppressor, and a component of an SCF complex."
Kumar R., Neilsen P.M., Crawford J., McKirdy R., Lee J., Powell J.A., Saif Z., Martin J.M., Lombaerts M., Cornelisse C.J., Cleton-Jansen A.-M., Callen D.F.
Cancer Res. 65:11304-11313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBUNIT, FUNCTION, DEVELOPMENTAL STAGE.
[8]"F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage."
Santra M.K., Wajapeyee N., Green M.R.
Nature 459:722-725(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INDUCTION, INTERACTION WITH CCND1, PHOSPHORYLATION AT SER-278, MUTAGENESIS OF SER-278 AND SER-400.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY736035 mRNA. Translation: AAU50679.1.
AF428140 mRNA. Translation: AAQ04213.1.
AF318348 mRNA. Translation: AAL55855.1. Frameshift.
AC010531 Genomic DNA. No translation available.
BC012748 mRNA. Translation: AAH12748.1. Different initiation.
AL117444 mRNA. Translation: CAB55929.2. Different initiation.
PIRT17239.
RefSeqNP_001269612.1. NM_001282683.1.
NP_079011.3. NM_024735.4.
UniGeneHs.567582.
Hs.658034.
Hs.733212.

3D structure databases

ProteinModelPortalQ5XUX0.
SMRQ5XUX0. Positions 66-137.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122890. 7 interactions.
DIPDIP-60449N.
IntActQ5XUX0. 1 interaction.
STRING9606.ENSP00000310841.

PTM databases

PhosphoSiteQ5XUX0.

Polymorphism databases

DMDM146345419.

Proteomic databases

PaxDbQ5XUX0.
PRIDEQ5XUX0.

Protocols and materials databases

DNASU79791.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311635; ENSP00000310841; ENSG00000103264. [Q5XUX0-1]
GeneID79791.
KEGGhsa:79791.
UCSCuc002fjv.3. human. [Q5XUX0-2]
uc002fjw.3. human. [Q5XUX0-1]

Organism-specific databases

CTD79791.
GeneCardsGC16M087365.
HGNCHGNC:16510. FBXO31.
HPAHPA030150.
MIM609102. gene.
neXtProtNX_Q5XUX0.
PharmGKBPA28042.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43393.
HOGENOMHOG000112543.
HOVERGENHBG071549.
InParanoidQ5XUX0.
KOK10308.
OMAPERTPGV.
OrthoDBEOG7CG6ZR.
PhylomeDBQ5XUX0.
TreeFamTF331818.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ5XUX0.
BgeeQ5XUX0.
CleanExHS_FBXO31.
GenevestigatorQ5XUX0.

Family and domain databases

InterProIPR001810. F-box_dom.
IPR026941. FBXO31.
[Graphical view]
PANTHERPTHR10706:SF117. PTHR10706:SF117. 1 hit.
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBXO31. human.
GeneWikiFBXO31.
GenomeRNAi79791.
NextBio69320.
PROQ5XUX0.
SOURCESearch...

Entry information

Entry nameFBX31_HUMAN
AccessionPrimary (citable) accession number: Q5XUX0
Secondary accession number(s): Q5K680 expand/collapse secondary AC list , Q8WYV1, Q96D73, Q9UFV4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM