FBX31_MOUSE
ID FBX31_MOUSE Reviewed; 507 AA.
AC Q3TQF0; Q8K1A7; Q9JJC4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=F-box only protein 31;
GN Name=Fbxo31; ORFNames=MNCb-2609;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-507.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC complex that plays a central role in G1 arrest following DNA damage.
CC Specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its
CC ubiquitination and degradation by the proteasome, resulting in G1
CC arrest (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation by ATM following gamma-irradiation results in its
CC stabilization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBXO31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA95069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK163641; BAE37434.1; -; mRNA.
DR EMBL; BC026929; AAH26929.1; ALT_INIT; mRNA.
DR EMBL; AB041586; BAA95069.1; ALT_INIT; mRNA.
DR CCDS; CCDS52693.1; -.
DR RefSeq; NP_598526.3; NM_133765.4.
DR AlphaFoldDB; Q3TQF0; -.
DR SMR; Q3TQF0; -.
DR BioGRID; 218134; 1.
DR STRING; 10090.ENSMUSP00000057573; -.
DR iPTMnet; Q3TQF0; -.
DR PhosphoSitePlus; Q3TQF0; -.
DR EPD; Q3TQF0; -.
DR MaxQB; Q3TQF0; -.
DR PaxDb; Q3TQF0; -.
DR PRIDE; Q3TQF0; -.
DR ProteomicsDB; 271673; -.
DR Antibodypedia; 30677; 247 antibodies from 24 providers.
DR DNASU; 76454; -.
DR Ensembl; ENSMUST00000059018; ENSMUSP00000057573; ENSMUSG00000052934.
DR GeneID; 76454; -.
DR KEGG; mmu:76454; -.
DR UCSC; uc009nrv.3; mouse.
DR CTD; 79791; -.
DR MGI; MGI:1354708; Fbxo31.
DR VEuPathDB; HostDB:ENSMUSG00000052934; -.
DR eggNOG; ENOG502QR2A; Eukaryota.
DR GeneTree; ENSGT00390000001368; -.
DR HOGENOM; CLU_035961_0_0_1; -.
DR InParanoid; Q3TQF0; -.
DR OMA; HIQIVKR; -.
DR OrthoDB; 484321at2759; -.
DR PhylomeDB; Q3TQF0; -.
DR TreeFam; TF331818; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76454; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Fbxo31; mouse.
DR PRO; PR:Q3TQF0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TQF0; protein.
DR Bgee; ENSMUSG00000052934; Expressed in hindlimb stylopod muscle and 215 other tissues.
DR ExpressionAtlas; Q3TQF0; baseline and differential.
DR Genevisible; Q3TQF0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR026941; FBXO31.
DR InterPro; IPR045048; FBXO31/39.
DR PANTHER; PTHR10706; PTHR10706; 1.
DR PANTHER; PTHR10706:SF130; PTHR10706:SF130; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA damage; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..507
FT /note="F-box only protein 31"
FT /id="PRO_0000349260"
FT DOMAIN 50..96
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 264
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q5XUX0"
FT CONFLICT 207
FT /note="V -> L (in Ref. 2; AAH26929)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="R -> W (in Ref. 3; BAA95069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 57191 MW; CF6880553F5ABB0C CRC64;
MAVCARLCGV GPARGCRRRQ QRRGPAETAA ADSEADTDPE EERIEAGPAR CSLLELPPEL
LVEIFASLPG TDLPSLAQVC SRFRRILHTD TIWRRRCREE YGVCENLRKL EITGVSCRDV
YAKLLHRYRH ILGLWQPDIG PYGGLLNVVV DGLFIIGWMY LPPHDPHVGD PMRFKPLFRI
HLMERKSATV ECMYGHKGPH NGHIQIVKRD EFSTKCNQTD HHRMSGGRQE EFRTWLREEW
GRTLEDIFHE HMQELILMKF IYTSQYDNCL TYRRIYLPPS HPDDLIKPGL FKGTYGSHGL
EIVMLSFHGS RARGTKITGD PNIPAGQQTV EIDLQRRIQL PDVENLRNFN ELSRIVLEVR
EQVRQEQEAG EGAAPPREPS AKAADGPPAK DGKEPGGGAE AAEQSASSGQ GQPFVLPVGV
SSRNEDYPRT CRLCFYGTGL IAGHGFTSPE RTPGVFVLFD EDRFGFLWLE LKSFSLYSRV
QATFQNAAAP SPQAFDEMLR NIQSLTS
