FBX31_RAT
ID FBX31_RAT Reviewed; 507 AA.
AC B2RYN2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=F-box only protein 31;
GN Name=Fbxo31;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; BC166840; AAI66840.1; -; mRNA.
DR RefSeq; NP_001037724.2; NM_001044259.2.
DR AlphaFoldDB; B2RYN2; -.
DR SMR; B2RYN2; -.
DR STRING; 10116.ENSRNOP00000063581; -.
DR iPTMnet; B2RYN2; -.
DR PhosphoSitePlus; B2RYN2; -.
DR PaxDb; B2RYN2; -.
DR PeptideAtlas; B2RYN2; -.
DR Ensembl; ENSRNOT00000068764; ENSRNOP00000063581; ENSRNOG00000042274.
DR GeneID; 498959; -.
DR KEGG; rno:498959; -.
DR UCSC; RGD:1561069; rat.
DR CTD; 79791; -.
DR RGD; 1561069; Fbxo31.
DR eggNOG; ENOG502QR2A; Eukaryota.
DR GeneTree; ENSGT00390000001368; -.
DR HOGENOM; CLU_035961_0_0_1; -.
DR InParanoid; B2RYN2; -.
DR OMA; HIQIVKR; -.
DR OrthoDB; 484321at2759; -.
DR PhylomeDB; B2RYN2; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:B2RYN2; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000042274; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; B2RYN2; baseline and differential.
DR Genevisible; B2RYN2; RN.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; ISO:RGD.
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; IMP:CACAO.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:CACAO.
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_0000349261"
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 364..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 264
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q5XUX0"
SQ SEQUENCE 507 AA; 57399 MW; B4AEE043B0F9FD20 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 EGPAPHREPA VKDPEGPPAK ASKEAGPGAE AAEQSSTSGQ GQPFVLPAGV
SSRNEDYPRT CRLCFYGTGL IAGHGFTSPE RTPGVFVLFD EDRFGFLWLE LKSFSLYSRV
QATFQNADAP SPQAFDEMLR NIQSLTS
