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Protein

F-box only protein 31

Gene

Fbxo31

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 31
Gene namesi
Name:Fbxo31
ORF Names:MNCb-2609
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1354708. Fbxo31.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: Ensembl
  • neuronal cell body Source: UniProtKB
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507F-box only protein 31PRO_0000349260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei37 – 371PhosphothreonineCombined sources
Modified residuei264 – 2641Phosphoserine; by ATMBy similarity

Post-translational modificationi

Phosphorylation by ATM following gamma-irradiation results in its stabilization.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3TQF0.
PaxDbiQ3TQF0.
PRIDEiQ3TQF0.

PTM databases

iPTMnetiQ3TQF0.
PhosphoSiteiQ3TQF0.

Expressioni

Gene expression databases

BgeeiQ3TQF0.
ExpressionAtlasiQ3TQF0. baseline and differential.
GenevisibleiQ3TQF0. MM.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057573.

Structurei

3D structure databases

ProteinModelPortaliQ3TQF0.
SMRiQ3TQF0. Positions 51-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 9647F-boxPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FBXO31 family.Curated
Contains 1 F-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFQE. Eukaryota.
ENOG410XPRQ. LUCA.
GeneTreeiENSGT00390000001368.
HOGENOMiHOG000112543.
HOVERGENiHBG071549.
InParanoidiQ3TQF0.
KOiK10308.
OMAiPQAFEEM.
OrthoDBiEOG7CG6ZR.
PhylomeDBiQ3TQF0.
TreeFamiTF331818.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR026941. FBXO31.
[Graphical view]
PANTHERiPTHR10706:SF126. PTHR10706:SF126. 2 hits.
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3TQF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVCARLCGV GPARGCRRRQ QRRGPAETAA ADSEADTDPE EERIEAGPAR
60 70 80 90 100
CSLLELPPEL LVEIFASLPG TDLPSLAQVC SRFRRILHTD TIWRRRCREE
110 120 130 140 150
YGVCENLRKL EITGVSCRDV YAKLLHRYRH ILGLWQPDIG PYGGLLNVVV
160 170 180 190 200
DGLFIIGWMY LPPHDPHVGD PMRFKPLFRI HLMERKSATV ECMYGHKGPH
210 220 230 240 250
NGHIQIVKRD EFSTKCNQTD HHRMSGGRQE EFRTWLREEW GRTLEDIFHE
260 270 280 290 300
HMQELILMKF IYTSQYDNCL TYRRIYLPPS HPDDLIKPGL FKGTYGSHGL
310 320 330 340 350
EIVMLSFHGS RARGTKITGD PNIPAGQQTV EIDLQRRIQL PDVENLRNFN
360 370 380 390 400
ELSRIVLEVR EQVRQEQEAG EGAAPPREPS AKAADGPPAK DGKEPGGGAE
410 420 430 440 450
AAEQSASSGQ GQPFVLPVGV SSRNEDYPRT CRLCFYGTGL IAGHGFTSPE
460 470 480 490 500
RTPGVFVLFD EDRFGFLWLE LKSFSLYSRV QATFQNAAAP SPQAFDEMLR

NIQSLTS
Length:507
Mass (Da):57,191
Last modified:October 11, 2005 - v1
Checksum:iCF6880553F5ABB0C
GO

Sequence cautioni

The sequence AAH26929.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA95069.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071V → L in AAH26929 (PubMed:15489334).Curated
Sequence conflicti313 – 3131R → W in BAA95069 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK163641 mRNA. Translation: BAE37434.1.
BC026929 mRNA. Translation: AAH26929.1. Different initiation.
AB041586 mRNA. Translation: BAA95069.1. Different initiation.
CCDSiCCDS52693.1.
RefSeqiNP_598526.3. NM_133765.4.
UniGeneiMm.24829.

Genome annotation databases

EnsembliENSMUST00000059018; ENSMUSP00000057573; ENSMUSG00000052934.
GeneIDi76454.
KEGGimmu:76454.
UCSCiuc009nrv.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK163641 mRNA. Translation: BAE37434.1.
BC026929 mRNA. Translation: AAH26929.1. Different initiation.
AB041586 mRNA. Translation: BAA95069.1. Different initiation.
CCDSiCCDS52693.1.
RefSeqiNP_598526.3. NM_133765.4.
UniGeneiMm.24829.

3D structure databases

ProteinModelPortaliQ3TQF0.
SMRiQ3TQF0. Positions 51-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057573.

PTM databases

iPTMnetiQ3TQF0.
PhosphoSiteiQ3TQF0.

Proteomic databases

MaxQBiQ3TQF0.
PaxDbiQ3TQF0.
PRIDEiQ3TQF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059018; ENSMUSP00000057573; ENSMUSG00000052934.
GeneIDi76454.
KEGGimmu:76454.
UCSCiuc009nrv.3. mouse.

Organism-specific databases

CTDi79791.
MGIiMGI:1354708. Fbxo31.

Phylogenomic databases

eggNOGiENOG410IFQE. Eukaryota.
ENOG410XPRQ. LUCA.
GeneTreeiENSGT00390000001368.
HOGENOMiHOG000112543.
HOVERGENiHBG071549.
InParanoidiQ3TQF0.
KOiK10308.
OMAiPQAFEEM.
OrthoDBiEOG7CG6ZR.
PhylomeDBiQ3TQF0.
TreeFamiTF331818.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ3TQF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TQF0.
ExpressionAtlasiQ3TQF0. baseline and differential.
GenevisibleiQ3TQF0. MM.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR026941. FBXO31.
[Graphical view]
PANTHERiPTHR10706:SF126. PTHR10706:SF126. 2 hits.
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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: Medulla oblongata.
  2. "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.
  3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-507.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiFBX31_MOUSE
AccessioniPrimary (citable) accession number: Q3TQF0
Secondary accession number(s): Q8K1A7, Q9JJC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.