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FXL12_MOUSE
ID   FXL12_MOUSE             Reviewed;         326 AA.
AC   Q9EPX5; Q3UVH7; Q8CDX0; Q9CY04; Q9QZN5;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=F-box/LRR-repeat protein 12;
DE   AltName: Full=F-box and leucine-rich repeat protein 12;
DE   AltName: Full=F-box protein FBL12;
GN   Name=Fbxl12; Synonyms=Fbl12;
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 [MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ilyin G.P.;
RT   "F-box protein FBL12 containing leucine-rich repeats.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver, Head, and Urinary bladder;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complex. Mediates the
CC       polyubiquitination and proteasomal degradation of CAMK1 leading to
CC       disruption of cyclin D1/CDK4 complex assembly which results in G1 cell
CC       cycle arrest in lung epithelia (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF09134.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF176525; AAF09134.1; ALT_FRAME; mRNA.
DR   EMBL; AF313405; AAG37272.1; -; mRNA.
DR   EMBL; AK011081; BAB27385.1; -; mRNA.
DR   EMBL; AK029429; BAC26448.1; -; mRNA.
DR   EMBL; AK030910; BAC27180.1; -; mRNA.
DR   EMBL; AK137282; BAE23292.1; -; mRNA.
DR   EMBL; BC005699; AAH05699.1; -; mRNA.
DR   EMBL; BC054471; AAH54471.1; -; mRNA.
DR   CCDS; CCDS22880.1; -.
DR   RefSeq; NP_001002846.1; NM_001002846.2.
DR   RefSeq; NP_001273458.1; NM_001286529.1.
DR   RefSeq; NP_001273459.1; NM_001286530.1.
DR   RefSeq; NP_038939.2; NM_013911.3.
DR   RefSeq; XP_006510460.1; XM_006510397.2.
DR   RefSeq; XP_006510461.1; XM_006510398.2.
DR   RefSeq; XP_006510462.1; XM_006510399.2.
DR   AlphaFoldDB; Q9EPX5; -.
DR   SMR; Q9EPX5; -.
DR   BioGRID; 205979; 4.
DR   MINT; Q9EPX5; -.
DR   STRING; 10090.ENSMUSP00000083649; -.
DR   PhosphoSitePlus; Q9EPX5; -.
DR   jPOST; Q9EPX5; -.
DR   MaxQB; Q9EPX5; -.
DR   PaxDb; Q9EPX5; -.
DR   PeptideAtlas; Q9EPX5; -.
DR   PRIDE; Q9EPX5; -.
DR   ProteomicsDB; 267532; -.
DR   Antibodypedia; 25087; 155 antibodies from 27 providers.
DR   DNASU; 30843; -.
DR   Ensembl; ENSMUST00000086459; ENSMUSP00000083650; ENSMUSG00000066892.
DR   Ensembl; ENSMUST00000148631; ENSMUSP00000119124; ENSMUSG00000066892.
DR   GeneID; 30843; -.
DR   KEGG; mmu:30843; -.
DR   UCSC; uc009oiz.2; mouse.
DR   CTD; 54850; -.
DR   MGI; MGI:1354738; Fbxl12.
DR   VEuPathDB; HostDB:ENSMUSG00000066892; -.
DR   eggNOG; KOG1947; Eukaryota.
DR   GeneTree; ENSGT00390000003354; -.
DR   HOGENOM; CLU_024577_1_0_1; -.
DR   InParanoid; Q9EPX5; -.
DR   OMA; SCLAMPK; -.
DR   OrthoDB; 1046098at2759; -.
DR   PhylomeDB; Q9EPX5; -.
DR   TreeFam; TF313434; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 30843; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Fbxl12; mouse.
DR   PRO; PR:Q9EPX5; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9EPX5; protein.
DR   Bgee; ENSMUSG00000066892; Expressed in thymus and 222 other tissues.
DR   ExpressionAtlas; Q9EPX5; baseline and differential.
DR   Genevisible; Q9EPX5; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IPI:MGI.
DR   GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IPI:MGI.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..326
FT                   /note="F-box/LRR-repeat protein 12"
FT                   /id="PRO_0000119858"
FT   DOMAIN          1..47
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          51..78
FT                   /note="LRR 1"
FT   REPEAT          86..111
FT                   /note="LRR 2"
FT   REPEAT          113..133
FT                   /note="LRR 3"
FT   REPEAT          161..185
FT                   /note="LRR 4"
FT   REPEAT          186..211
FT                   /note="LRR 5"
FT   REPEAT          212..236
FT                   /note="LRR 6"
FT   REPEAT          237..261
FT                   /note="LRR 7"
FT   REPEAT          266..291
FT                   /note="LRR 8"
SQ   SEQUENCE   326 AA;  37231 MW;  5A670BCDBF87CC5B CRC64;
     MATLFDLPDL VLLEIFSYLP VRDRIRISRV CHRWKRLVDD RWLWRHVDLT LYTMRPKVMW
     HLLRRYMASR LYSLRMGGYL FSGSQAPQLS PALMRALGQK CPNLKRLCLH VADLSMVPIT
     SLPSTLRTLE LHSCEISMIW LQKEQDPTVL PLLECIVLDR VPAFRDEHLQ GLTRFRALRS
     LVLGGTYRVT ETGLDASLQE LSYLQRLEVL GCTLSADSTL LAISRHLRDV RKIRLTVGGL
     SAQGLVFLEG MPVLESLCFQ GPLITPDMPT PTQIVSSCLT MPKLRVLEVQ GLGWEGQEAE
     KILCKGLPHC IVIVRACPKE SMDWWM
 
 
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