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FBX42_HUMAN
ID   FBX42_HUMAN             Reviewed;         717 AA.
AC   Q6P3S6; B3KP30; Q5TEU8; Q86XI0; Q8N3N4; Q8N5F8; Q9BRM0; Q9P2L4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=F-box only protein 42;
DE   AltName: Full=Just one F-box and Kelch domain-containing protein;
GN   Name=FBXO42; Synonyms=FBX42, JFK, KIAA1332;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-471.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-471.
RC   TISSUE=Brain, PNS, and Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-717.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-717, AND VARIANT ALA-471.
RC   TISSUE=Melanoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-373 AND THR-378, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN THE SCF COMPLEX, AND INTERACTION WITH TP53.
RX   PubMed=19509332; DOI=10.1073/pnas.0901864106;
RA   Sun L., Shi L., Li W., Yu W., Liang J., Zhang H., Yang X., Wang Y., Li R.,
RA   Yao X., Yi X., Shang Y.;
RT   "JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53
RT   regulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:10195-10200(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-373, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complex. Specifically recognizes
CC       p53/TP53, promoting its ubiquitination and degradation.
CC       {ECO:0000269|PubMed:19509332}.
CC   -!- SUBUNIT: Component of some SCF complex, composed of CUL1, SKP1, RBX1
CC       and FBXO42. Interacts (via the kelch domain) with p53/TP53; interaction
CC       is direct. {ECO:0000269|PubMed:19509332}.
CC   -!- INTERACTION:
CC       Q6P3S6; P50570-2: DNM2; NbExp=3; IntAct=EBI-2506081, EBI-10968534;
CC       Q6P3S6; P49821: NDUFV1; NbExp=3; IntAct=EBI-2506081, EBI-748312;
CC       Q6P3S6; Q06330: RBPJ; NbExp=3; IntAct=EBI-2506081, EBI-632552;
CC       Q6P3S6; O14773: TPP1; NbExp=3; IntAct=EBI-2506081, EBI-2800203;
CC       Q6P3S6; O76024: WFS1; NbExp=3; IntAct=EBI-2506081, EBI-720609;
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DR   EMBL; AK055598; BAG51542.1; -; mRNA.
DR   EMBL; AL109627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006174; AAH06174.1; -; mRNA.
DR   EMBL; BC032439; AAH32439.1; -; mRNA.
DR   EMBL; BC043410; AAH43410.1; -; mRNA.
DR   EMBL; BC063864; AAH63864.1; -; mRNA.
DR   EMBL; AB037753; BAA92570.1; -; mRNA.
DR   EMBL; AL833874; CAD38731.1; -; mRNA.
DR   CCDS; CCDS30613.1; -.
DR   RefSeq; NP_061867.1; NM_018994.2.
DR   RefSeq; XP_006710761.1; XM_006710698.3.
DR   AlphaFoldDB; Q6P3S6; -.
DR   SMR; Q6P3S6; -.
DR   BioGRID; 119962; 26.
DR   IntAct; Q6P3S6; 15.
DR   MINT; Q6P3S6; -.
DR   STRING; 9606.ENSP00000364742; -.
DR   GlyConnect; 2039; 1 N-Linked glycan (1 site).
DR   GlyGen; Q6P3S6; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; Q6P3S6; -.
DR   PhosphoSitePlus; Q6P3S6; -.
DR   BioMuta; FBXO42; -.
DR   DMDM; 51701398; -.
DR   EPD; Q6P3S6; -.
DR   jPOST; Q6P3S6; -.
DR   MassIVE; Q6P3S6; -.
DR   MaxQB; Q6P3S6; -.
DR   PaxDb; Q6P3S6; -.
DR   PeptideAtlas; Q6P3S6; -.
DR   PRIDE; Q6P3S6; -.
DR   ProteomicsDB; 66931; -.
DR   Antibodypedia; 14535; 325 antibodies from 21 providers.
DR   DNASU; 54455; -.
DR   Ensembl; ENST00000375592.8; ENSP00000364742.3; ENSG00000037637.11.
DR   GeneID; 54455; -.
DR   KEGG; hsa:54455; -.
DR   MANE-Select; ENST00000375592.8; ENSP00000364742.3; NM_018994.3; NP_061867.1.
DR   UCSC; uc001ayg.4; human.
DR   CTD; 54455; -.
DR   DisGeNET; 54455; -.
DR   GeneCards; FBXO42; -.
DR   HGNC; HGNC:29249; FBXO42.
DR   HPA; ENSG00000037637; Low tissue specificity.
DR   MIM; 609109; gene.
DR   neXtProt; NX_Q6P3S6; -.
DR   OpenTargets; ENSG00000037637; -.
DR   PharmGKB; PA134951560; -.
DR   VEuPathDB; HostDB:ENSG00000037637; -.
DR   eggNOG; KOG0379; Eukaryota.
DR   GeneTree; ENSGT00440000039706; -.
DR   HOGENOM; CLU_023579_0_0_1; -.
DR   InParanoid; Q6P3S6; -.
DR   OMA; EGCDLKM; -.
DR   OrthoDB; 838833at2759; -.
DR   PhylomeDB; Q6P3S6; -.
DR   TreeFam; TF324505; -.
DR   PathwayCommons; Q6P3S6; -.
DR   SignaLink; Q6P3S6; -.
DR   BioGRID-ORCS; 54455; 135 hits in 1128 CRISPR screens.
DR   ChiTaRS; FBXO42; human.
DR   GenomeRNAi; 54455; -.
DR   Pharos; Q6P3S6; Tbio.
DR   PRO; PR:Q6P3S6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q6P3S6; protein.
DR   Bgee; ENSG00000037637; Expressed in hair follicle and 208 other tissues.
DR   ExpressionAtlas; Q6P3S6; baseline and differential.
DR   Genevisible; Q6P3S6; HS.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IBA:GO_Central.
DR   Gene3D; 2.120.10.80; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Kelch repeat; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..717
FT                   /note="F-box only protein 42"
FT                   /id="PRO_0000119942"
FT   DOMAIN          44..93
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          132..184
FT                   /note="Kelch 1"
FT   REPEAT          186..242
FT                   /note="Kelch 2"
FT   REPEAT          244..293
FT                   /note="Kelch 3"
FT   REPEAT          295..342
FT                   /note="Kelch 4"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         378
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VARIANT         471
FT                   /note="P -> A (in dbSNP:rs12069239)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_024447"
FT   CONFLICT        454
FT                   /note="Missing (in Ref. 3; AAH43410)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="A -> T (in Ref. 5; CAD38731)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   717 AA;  77839 MW;  938D0A018FC3DCBD CRC64;
     MASSSDSEDD SFMAVDQEET VLEGTMDQDE EPHPVLEAEE TRHNRSMSEL PEEVLEYILS
     FLSPYQEHKT AALVCKQWYR LIKGVAHQCY HGFMKAVQEG NIQWESRTYP YPGTPITQRF
     SHSACYYDAN QSMYVFGGCT QSSCNAAFND LWRLDLNSKE WIRPLASGSY PSPKAGATLV
     VYKDLLVLFG GWTRPSPYPL HQPERFFDEI HTYSPSKNWW NCIVTTHGPP PMAGHSSCVI
     DDKMIVFGGS LGSRQMSNDV WVLDLEQWAW SKPNISGPSP HPRGGQSQIV IDDATILILG
     GCGGPNALFK DAWLLHMHSG PWAWQPLKVE NEEHGAPELW CHPACRVGQC VVVFSQAPSG
     RAPLSPSLNS RPSPISATPP ALVPETREYR SQSPVRSMDE APCVNGRWGT LRPRAQRQTP
     SGSREGSLSP ARGDGSPILN GGSLSPGTAA VGGSSLDSPV QAISPSTPSA PEGYDLKIGL
     SLAPRRGSLP DQKDLRLGSI DLNWDLKPAS SSNPMDGMDN RTVGGSMRHP PEQTNGVHTP
     PHVASALAGA VSPGALRRSL EAIKAMSSKG PSASAALSPP LGSSPGSPGS QSLSSGETVP
     IPRPGPAQGD GHSLPPIARR LGHHPPQSLN VGKPLYQSMN CKPMQMYVLD IKDTKEKGRV
     KWKVFNSSSV VGPPETSLHT VVQGRGELII FGGLMDKKQN VKYYPKTNAL YFVRAKR
 
 
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