FBW1A_MOUSE
ID FBW1A_MOUSE Reviewed; 605 AA.
AC Q3ULA2; Q3U0Q4; Q571K6; Q9QUI5; Q9R1G7; Q9Z159;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=F-box/WD repeat-containing protein 1A {ECO:0000250|UniProtKB:Q9Y297, ECO:0000312|EMBL:AAL40929.1};
DE AltName: Full=Beta-TrCP protein E3RS-IkappaB {ECO:0000312|EMBL:AAD08701.1};
DE AltName: Full=Beta-transducin repeat-containing protein {ECO:0000312|EMBL:BAE26547.1};
DE Short=Beta-TrCP {ECO:0000303|PubMed:9990853};
DE AltName: Full=E3RSIkappaB {ECO:0000250|UniProtKB:Q9Y297};
DE Short=mE3RS-IkappaB {ECO:0000303|PubMed:9859996};
DE AltName: Full=F-box and WD repeats protein beta-TrCP {ECO:0000250|UniProtKB:Q9Y297};
DE AltName: Full=HOS {ECO:0000303|PubMed:11735228};
DE AltName: Full=Ubiquitin ligase FWD1 {ECO:0000303|PubMed:10097128, ECO:0000312|EMBL:AAD17755.1};
DE AltName: Full=pIkappaB-E3 receptor subunit {ECO:0000303|PubMed:9859996};
GN Name=Btrc {ECO:0000312|MGI:MGI:1338871};
GN Synonyms=Fbw1, Fbxw1 {ECO:0000312|EMBL:AAL40929.1}, Fwd1, Kiaa4123;
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] {ECO:0000305, ECO:0000312|EMBL:AAD08701.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, AND INTERACTION
RP WITH PHOSPHORYLATED NFKBIA.
RX PubMed=9859996; DOI=10.1038/25159;
RA Yaron A., Hatzubai A., Davis M., Lavon I., Amit S., Manning A.M.,
RA Andersen J.S., Mann M., Mercurio F., Ben-Neriah Y.;
RT "Identification of the receptor component of the IkappaBalpha-ubiquitin
RT ligase.";
RL Nature 396:590-594(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD41025.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT "A family of mammalian F-box proteins.";
RL Curr. Biol. 9:1180-1182(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD04181.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, AND
RP IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; SKP1 AND RELA.
RC TISSUE=Embryo {ECO:0000269|PubMed:9990853};
RX PubMed=9990853; DOI=10.1101/gad.13.3.284;
RA Spencer E., Jiang J., Chen Z.J.;
RT "Signal-induced ubiquitination of IkappaBalpha by the F-box protein
RT Slimb/beta-TrCP.";
RL Genes Dev. 13:284-294(1999).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAD17755.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, AND
RP IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; SKP1 AND CUL1.
RX PubMed=10097128; DOI=10.1073/pnas.96.7.3859;
RA Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
RA Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
RA Nakayama K.;
RT "Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin
RT ligase Skp1/Cul 1/F-box protein FWD1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAL40929.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN A COMPLEX WITH SKP1
RP AND CUL1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000269|PubMed:11735228};
RX PubMed=11735228; DOI=10.1006/geno.2001.6658;
RA Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K.,
RA Nakayama K.;
RT "Characterization of a mouse gene (Fbxw6) that encodes a homologue of
RT Caenorhabditis elegans SEL-10.";
RL Genomics 78:214-222(2001).
RN [6] {ECO:0000312|EMBL:BAE26547.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 53-605 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE26547.1}, and
RC NOD {ECO:0000312|EMBL:BAE33798.1};
RC TISSUE=Blastocyst {ECO:0000312|EMBL:BAE26547.1}, and
RC Spleen {ECO:0000312|EMBL:BAE33798.1};
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 [7] {ECO:0000312|EMBL:BAD90368.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAD90368.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000312|EMBL:BAD90368.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000312|EMBL:AAH03989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH03989.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH03989.1};
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 [10]
RP INTERACTION WITH PER3.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH GLI3.
RX PubMed=16371461; DOI=10.1073/pnas.0509927103;
RA Wang B., Li Y.;
RT "Evidence for the direct involvement of {beta}TrCP in Gli3 protein
RT processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:33-38(2006).
RN [12]
RP FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18782782; DOI=10.1093/jb/mvn112;
RA Ohsaki K., Oishi K., Kozono Y., Nakayama K., Nakayama K.I., Ishida N.;
RT "The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation
RT by mediating degradation of clock protein PER2.";
RL J. Biochem. 144:609-618(2008).
RN [13]
RP INTERACTION WITH ZC3H12A.
RX PubMed=22037600; DOI=10.1038/ni.2137;
RA Iwasaki H., Takeuchi O., Teraguchi S., Matsushita K., Uehata T.,
RA Kuniyoshi K., Satoh T., Saitoh T., Matsushita M., Standley D.M., Akira S.;
RT "The IkappaB kinase complex regulates the stability of cytokine-encoding
RT mRNA induced by TLR-IL-1R by controlling degradation of regnase-1.";
RL Nat. Immunol. 12:1167-1175(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH NFE2L1.
RX PubMed=21911472; DOI=10.1128/mcb.05663-11;
RA Tsuchiya Y., Morita T., Kim M., Iemura S., Natsume T., Yamamoto M.,
RA Kobayashi A.;
RT "Dual regulation of the transcriptional activity of Nrf1 by beta-TrCP- and
RT Hrd1-dependent degradation mechanisms.";
RL Mol. Cell. Biol. 31:4500-4512(2011).
RN [15]
RP FUNCTION, PATHWAY, AND INTERACTION WITH KLF4.
RX PubMed=29593216; DOI=10.1038/s41467-018-03008-2;
RA Ye B., Liu B., Hao L., Zhu X., Yang L., Wang S., Xia P., Du Y., Meng S.,
RA Huang G., Qin X., Wang Y., Yan X., Li C., Hao J., Zhu P., He L., Tian Y.,
RA Fan Z.;
RT "Klf4 glutamylation is required for cell reprogramming and early embryonic
RT development in mice.";
RL Nat. Commun. 9:1261-1261(2018).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (PubMed:10097128, PubMed:16371461, PubMed:18782782,
CC PubMed:9859996, PubMed:9990853, PubMed:21911472, PubMed:29593216).
CC Recognizes and binds to phosphorylated target proteins
CC (PubMed:10097128, PubMed:16371461, PubMed:18782782, PubMed:9859996,
CC PubMed:9990853, PubMed:21911472). SCF(BTRC) mediates the ubiquitination
CC of phosphorylated NFKB, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4,
CC SNAI1 and probably NFKB2. SCF(BTRC) mediates the ubiquitination of
CC CTNNB1 and participates in Wnt signaling (By similarity). SCF(BTRC)
CC mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the
CC degradation frees the associated NFKB1 to translocate into the nucleus
CC and to activate transcription (PubMed:9859996, PubMed:10097128).
CC Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22'
CC (PubMed:9859996, PubMed:10097128). SCF(BTRC) mediates the
CC ubiquitination of CEP68; this is required for centriole separation
CC during mitosis (By similarity). SCF(BTRC) mediates the ubiquitination
CC and subsequent degradation of nuclear NFE2L1 (PubMed:21911472). Has an
CC essential role in the control of the clock-dependent transcription via
CC degradation of phosphorylated PER1 and PER2 (PubMed:18782782). May be
CC involved in ubiquitination and subsequent proteasomal degradation
CC through a DBB1-CUL4 E3 ubiquitin-protein ligase (By similarity).
CC Required for activation of NFKB-mediated transcription by IL1B,
CC MAP3K14, MAP3K1, IKBKB and TNF (By similarity). Required for
CC proteolytic processing of GLI3 (PubMed:16371461). Mediates
CC ubiquitination of REST, thereby leading to its proteasomal degradation
CC (By similarity). SCF(BTRC) mediates the ubiquitination and subsequent
CC proteasomal degradation of KLF4; thereby negatively regulating cell
CC pluripotency maintenance and embryogenesis (PubMed:29593216).
CC {ECO:0000250|UniProtKB:Q9Y297, ECO:0000269|PubMed:10097128,
CC ECO:0000269|PubMed:16371461, ECO:0000269|PubMed:18782782,
CC ECO:0000269|PubMed:21911472, ECO:0000269|PubMed:29593216,
CC ECO:0000269|PubMed:9859996, ECO:0000269|PubMed:9990853}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:21911472,
CC ECO:0000269|PubMed:29593216, ECO:0000269|PubMed:9859996,
CC ECO:0000269|PubMed:9990853}.
CC -!- SUBUNIT: Homodimer. Self-associates. Component of the SCF(BTRC)
CC complex, composed of SKP1, CUL1 and BTRC. Direct interaction with SKP1
CC with SKP1 occurs via the F-box domain. Interacts with phosphorylated
CC ubiquitination substrates SMAD3 and SMAD4. Interacts with
CC phosphorylated ubiquitination substrates CTNNB1, NFKBIA, NFKBIB,
CC NFKBIE, NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A,
CC DLG1, FBXO5 and SNAI1; the interaction requires the phosphorylation of
CC the 2 serine residues in the substrate destruction motif D-S-G-
CC X(2,3,4)-S. Binds UBQLN1. Interacts with CDC34 and UBE2R2. Interacts
CC with FBXW11. Interacts with CUL4A and DDB1. Part of a SCF(BTRC)-like
CC complex lacking CUL1, which is associated with phosphorylated NKBIA and
CC RELA; RELA interacts directly with NFKBIA. Interacts with the
CC phosphorylated form of GLI3. Interacts with CLU. Interacts with PER1
CC (phosphorylated), PER2 (phosphorylated) and PER3. Interacts with
CC phosphorylated ubiquitination substrate CEP68 (By similarity).
CC Interacts with ZC3H12A; this interaction occurs when ZC3H12A is
CC phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600).
CC Interacts with HSF1; this interaction occurs during mitosis and induces
CC HSF1 ubiquitin-dependent degradation, a process inhibited by CDC20 (By
CC similarity). Interacts with NFE2L1 (PubMed:21911472). Interacts with
CC INAVA (By similarity). Interacts with IL10RA; this interaction leads to
CC IL10RA ubiquitination and subsequent degradation (By similarity).
CC Interacts with REST (By similarity). Interacts with KLF4; this
CC interaction leads to KLF4 ubiquitination and subsequent degradation
CC (PubMed:29593216). {ECO:0000250|UniProtKB:Q9Y297,
CC ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:11735228,
CC ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16371461,
CC ECO:0000269|PubMed:18782782, ECO:0000269|PubMed:21911472,
CC ECO:0000269|PubMed:22037600, ECO:0000269|PubMed:29593216,
CC ECO:0000269|PubMed:9859996, ECO:0000269|PubMed:9990853}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11735228}. Nucleus
CC {ECO:0000269|PubMed:11735228}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072, ECO:0000269|Ref.7};
CC IsoId=Q3ULA2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10097128, ECO:0000269|PubMed:10531037,
CC ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9859996,
CC ECO:0000269|PubMed:9990853};
CC IsoId=Q3ULA2-2; Sequence=VSP_053208;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, skeletal muscle
CC and, most strongly, in testis. {ECO:0000269|PubMed:11735228}.
CC -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9Y297}.
CC -!- DISRUPTION PHENOTYPE: Mutants have normal circadian behavior with
CC normal PER2 expression in the suprachiasmatic nucleus.
CC {ECO:0000269|PubMed:18782782}.
CC -!- CAUTION: PubMed:10531037 wrongly lists the species as human.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90368.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF099932; AAD08701.1; -; mRNA.
DR EMBL; AF110396; AAD41025.1; -; mRNA.
DR EMBL; AF112979; AAD04181.1; -; mRNA.
DR EMBL; AF081887; AAD17755.1; -; mRNA.
DR EMBL; AF391190; AAL40929.1; -; Genomic_DNA.
DR EMBL; AF391178; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391179; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391180; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391181; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391182; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391183; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391184; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391185; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391186; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391187; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391188; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AF391189; AAL40929.1; JOINED; Genomic_DNA.
DR EMBL; AK145624; BAE26547.1; -; mRNA.
DR EMBL; AK156660; BAE33798.1; -; mRNA.
DR EMBL; AK220183; BAD90368.1; ALT_INIT; mRNA.
DR EMBL; CH466534; EDL41951.1; -; Genomic_DNA.
DR EMBL; BC003989; AAH03989.1; -; mRNA.
DR CCDS; CCDS29860.1; -. [Q3ULA2-1]
DR CCDS; CCDS38002.1; -. [Q3ULA2-2]
DR RefSeq; NP_001032847.2; NM_001037758.2. [Q3ULA2-1]
DR RefSeq; NP_001273394.1; NM_001286465.1. [Q3ULA2-1]
DR RefSeq; NP_001273395.1; NM_001286466.1.
DR RefSeq; NP_033901.1; NM_009771.3. [Q3ULA2-2]
DR AlphaFoldDB; Q3ULA2; -.
DR SMR; Q3ULA2; -.
DR BioGRID; 198403; 30.
DR CORUM; Q3ULA2; -.
DR IntAct; Q3ULA2; 17.
DR MINT; Q3ULA2; -.
DR STRING; 10090.ENSMUSP00000070728; -.
DR iPTMnet; Q3ULA2; -.
DR PhosphoSitePlus; Q3ULA2; -.
DR EPD; Q3ULA2; -.
DR MaxQB; Q3ULA2; -.
DR PaxDb; Q3ULA2; -.
DR PeptideAtlas; Q3ULA2; -.
DR PRIDE; Q3ULA2; -.
DR ProteomicsDB; 267717; -. [Q3ULA2-1]
DR ProteomicsDB; 267718; -. [Q3ULA2-2]
DR Antibodypedia; 31277; 380 antibodies from 32 providers.
DR DNASU; 12234; -.
DR Ensembl; ENSMUST00000065601; ENSMUSP00000070728; ENSMUSG00000025217. [Q3ULA2-1]
DR Ensembl; ENSMUST00000111936; ENSMUSP00000107567; ENSMUSG00000025217. [Q3ULA2-2]
DR GeneID; 12234; -.
DR KEGG; mmu:12234; -.
DR UCSC; uc008hqx.2; mouse. [Q3ULA2-1]
DR UCSC; uc008hqz.2; mouse. [Q3ULA2-2]
DR CTD; 8945; -.
DR MGI; MGI:1338871; Btrc.
DR VEuPathDB; HostDB:ENSMUSG00000025217; -.
DR eggNOG; KOG0281; Eukaryota.
DR GeneTree; ENSGT00940000159672; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR InParanoid; Q3ULA2; -.
DR OMA; ENNWRMG; -.
DR OrthoDB; 666965at2759; -.
DR PhylomeDB; Q3ULA2; -.
DR TreeFam; TF105679; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 12234; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Btrc; mouse.
DR PRO; PR:Q3ULA2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3ULA2; protein.
DR Bgee; ENSMUSG00000025217; Expressed in spermatocyte and 240 other tissues.
DR ExpressionAtlas; Q3ULA2; baseline and differential.
DR Genevisible; Q3ULA2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0045309; F:protein phosphorylated amino acid binding; IDA:BHF-UCL.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021977; Beta-TrCP_D.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12125; Beta-TrCP_D; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01028; Beta-TrCP_D; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 6.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..605
FT /note="F-box/WD repeat-containing protein 1A"
FT /id="PRO_0000393571"
FT DOMAIN 182..228
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 301..338
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 341..378
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 381..418
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 424..461
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 464..503
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 505..541
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 553..590
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 128..177
FT /note="Homodimerization domain D"
FT /evidence="ECO:0000250"
FT REGION 190..228
FT /note="Required for down-regulation of SNAI1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 17..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10097128,
FT ECO:0000303|PubMed:10531037, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9859996, ECO:0000303|PubMed:9990853"
FT /id="VSP_053208"
FT CONFLICT 193
FT /note="A -> T (in Ref. 2; AAD41025)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="K -> E (in Ref. 6; BAE33798)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="H -> R (in Ref. 6; BAE26547)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="D -> G (in Ref. 3; AAD04181)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="N -> D (in Ref. 2; AAD41025)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="I -> T (in Ref. 2; AAD41025)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="A -> R (in Ref. 2; AAD41025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 68923 MW; 9E66D94D1EEEFF1B CRC64;
MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA FQNSSEREDC
NNGEPPRKII PEKNSLRQTY NSCARLCINQ ETVCLTSTAM KTENCVAKAK LANGTSSMIV
PKQRKLSASY EKEKELCVKY FEQWSESDQV EFVEHLISQM CHYQHGHINS YLKPMLQRDF
ITALPARGLD HIAENILSYL DAKSLCAAEL VCKEWYRVTS DGMLWKKLIE RMVRTDSLWR
GLAERRGWGQ YLFKNKPPDE NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS
ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK STLECKRILT GHTGSVLCLQ YDERVIITGS
SDSTVRVWDV NAGEMLNTLI HHCEAVLHLR FNNGMMVTCS KDRSIAVWDM ASPTDITLRR
VLVGHRAAVN VVDFDDKYIV SASGDRTIKV WNTSTCEFVR TLNGHKRGIA CLQYRDRLVV
SGSSDNTIRL WDIECGACLR VLEGHEELVR CIRFDNKRIV SGAYDGKIKV WDLMAALDPR
APAGTLCLRT LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAHA EPPRSPSRTY
TYISR
