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FBX50_MOUSE
ID   FBX50_MOUSE             Reviewed;         266 AA.
AC   G3X9C2; Q8BT24;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=F-box only protein 50;
DE   AltName: Full=NCC receptor protein 1;
DE            Short=NCCRP-1;
DE   AltName: Full=Non-specific cytotoxic cell receptor protein 1 homolog;
GN   Name=Nccrp1; Synonyms=Fbxo50;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-266.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-37; SER-40; SER-43
RP   AND THR-46, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Lung;
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).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=22087255; DOI=10.1371/journal.pone.0027152;
RA   Kallio H., Tolvanen M., Janis J., Pan P.W., Laurila E., Kallioniemi A.,
RA   Kilpinen S., Tuominen V.J., Isola J., Valjakka J., Pastorekova S.,
RA   Pastorek J., Parkkila S.;
RT   "Characterization of non-specific cytotoxic cell receptor protein 1: a new
RT   member of the lectin-type subfamily of F-box proteins.";
RL   PLoS ONE 6:E27152-E27152(2011).
CC   -!- FUNCTION: Promotes cell proliferation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney. Weakly expressed in
CC       stomach, colon, duodenum and prostate. {ECO:0000269|PubMed:22087255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDL24129.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC136456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466593; EDL24129.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK028022; BAC25704.1; -; mRNA.
DR   CCDS; CCDS39862.2; -.
DR   RefSeq; NP_001074584.1; NM_001081115.1.
DR   AlphaFoldDB; G3X9C2; -.
DR   SMR; G3X9C2; -.
DR   BioGRID; 231354; 4.
DR   IntAct; G3X9C2; 1.
DR   MINT; G3X9C2; -.
DR   STRING; 10090.ENSMUSP00000055562; -.
DR   iPTMnet; G3X9C2; -.
DR   PhosphoSitePlus; G3X9C2; -.
DR   jPOST; G3X9C2; -.
DR   MaxQB; G3X9C2; -.
DR   PaxDb; G3X9C2; -.
DR   PeptideAtlas; G3X9C2; -.
DR   PRIDE; G3X9C2; -.
DR   ProteomicsDB; 271886; -.
DR   Antibodypedia; 45009; 73 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000239002; ENSMUSP00000159104; ENSMUSG00000047586.
DR   GeneID; 233038; -.
DR   KEGG; mmu:233038; -.
DR   CTD; 342897; -.
DR   MGI; MGI:2685009; Nccrp1.
DR   VEuPathDB; HostDB:ENSMUSG00000047586; -.
DR   eggNOG; KOG3248; Eukaryota.
DR   GeneTree; ENSGT00940000161313; -.
DR   InParanoid; G3X9C2; -.
DR   OrthoDB; 922544at2759; -.
DR   TreeFam; TF320527; -.
DR   BioGRID-ORCS; 233038; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Nccrp1; mouse.
DR   PRO; PR:G3X9C2; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; G3X9C2; protein.
DR   Bgee; ENSMUSG00000047586; Expressed in esophagus and 24 other tissues.
DR   ExpressionAtlas; G3X9C2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR039752; F-box_only.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12125; PTHR12125; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM01198; FBA; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   PROSITE; PS51114; FBA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..266
FT                   /note="F-box only protein 50"
FT                   /id="PRO_0000421450"
FT   DOMAIN          86..264
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..51
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        53
FT                   /note="N -> D (in Ref. 3; BAC25704)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  30408 MW;  23E1532A240EE700 CRC64;
     MEKTQDRDTL SGRMEAEGSL NSEELPPHPQ SPPPPPSPRS PTSPVTPELP QPNAPTEVEA
     RQLLVEEWGP LSGKLELPPR ISWQLLFLER PLYRNLLSSP NPEGINIYQP APPTGPTRKP
     LKELGNFRGW YITTQNLQGP LSWTVKEQCV NLLAKKLWEE LLDDEQPDIT IMDWFEDSRL
     DQCVYELHVW LLAADRRTVI AQHHVAPRTN GRGPPGRWIQ VSHVFRQYGP GVRFVYFQHK
     AKNRMEPGGL RRTRVTDSSV SVQLRE
 
 
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