FBX30_HUMAN
ID FBX30_HUMAN Reviewed; 745 AA.
AC Q8TB52; Q9BXZ7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=F-box only protein 30;
GN Name=FBXO30; Synonyms=FBX30;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 333-745, AND VARIANTS MET-375 AND GLN-583.
RC TISSUE=Nasopharyngeal epithelium;
RA Li Z.-H., Li G.-Y.;
RT "A new gene associated nasopharyngeal carcinoma.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
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).
RN [7]
RP STRUCTURE BY NMR OF 1-87.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the zinc finger domains (1-87) from human F-box only
RT protein.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-8.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Required for muscle atrophy
CC following denervation. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with SKP1, CUL1 and RBX1/ROC1 (By similarity). {ECO:0000250}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
CC -!- PTM: May be neddylated. Neddylation may be required for E3 ligase
CC activity (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK30299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK30299.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AL356599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024326; AAH24326.3; -; mRNA.
DR EMBL; AF248640; AAK30299.1; ALT_INIT; mRNA.
DR CCDS; CCDS5208.1; -.
DR RefSeq; NP_001335021.1; NM_001348092.1.
DR RefSeq; NP_115521.3; NM_032145.4.
DR RefSeq; XP_011534479.1; XM_011536177.2.
DR RefSeq; XP_016866842.1; XM_017011353.1.
DR PDB; 2YRE; NMR; -; A=1-87.
DR PDBsum; 2YRE; -.
DR AlphaFoldDB; Q8TB52; -.
DR SMR; Q8TB52; -.
DR BioGRID; 123879; 43.
DR IntAct; Q8TB52; 18.
DR STRING; 9606.ENSP00000237281; -.
DR GlyGen; Q8TB52; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TB52; -.
DR PhosphoSitePlus; Q8TB52; -.
DR BioMuta; FBXO30; -.
DR DMDM; 51704325; -.
DR EPD; Q8TB52; -.
DR jPOST; Q8TB52; -.
DR MassIVE; Q8TB52; -.
DR MaxQB; Q8TB52; -.
DR PaxDb; Q8TB52; -.
DR PeptideAtlas; Q8TB52; -.
DR PRIDE; Q8TB52; -.
DR ProteomicsDB; 73962; -.
DR Antibodypedia; 33222; 53 antibodies from 14 providers.
DR DNASU; 84085; -.
DR Ensembl; ENST00000237281.5; ENSP00000237281.3; ENSG00000118496.5.
DR GeneID; 84085; -.
DR KEGG; hsa:84085; -.
DR MANE-Select; ENST00000237281.5; ENSP00000237281.3; NM_032145.5; NP_115521.3.
DR UCSC; uc003qla.4; human.
DR CTD; 84085; -.
DR DisGeNET; 84085; -.
DR GeneCards; FBXO30; -.
DR HGNC; HGNC:15600; FBXO30.
DR HPA; ENSG00000118496; Low tissue specificity.
DR MIM; 609101; gene.
DR neXtProt; NX_Q8TB52; -.
DR OpenTargets; ENSG00000118496; -.
DR PharmGKB; PA28041; -.
DR VEuPathDB; HostDB:ENSG00000118496; -.
DR eggNOG; ENOG502QTD9; Eukaryota.
DR GeneTree; ENSGT00950000183204; -.
DR HOGENOM; CLU_013357_0_0_1; -.
DR InParanoid; Q8TB52; -.
DR OMA; HTPSFKF; -.
DR OrthoDB; 1009974at2759; -.
DR PhylomeDB; Q8TB52; -.
DR TreeFam; TF343227; -.
DR PathwayCommons; Q8TB52; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8TB52; -.
DR SIGNOR; Q8TB52; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84085; 8 hits in 1118 CRISPR screens.
DR ChiTaRS; FBXO30; human.
DR EvolutionaryTrace; Q8TB52; -.
DR GenomeRNAi; 84085; -.
DR Pharos; Q8TB52; Tdark.
DR PRO; PR:Q8TB52; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TB52; protein.
DR Bgee; ENSG00000118496; Expressed in secondary oocyte and 189 other tissues.
DR Genevisible; Q8TB52; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.40.150; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR031890; Fbxo30/Fbxo40.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001293; Znf_TRAF.
DR InterPro; IPR043013; Znf_TRAF_N.
DR PANTHER; PTHR15933; PTHR15933; 1.
DR Pfam; PF15966; F-box_4; 1.
DR Pfam; PF15965; zf-TRAF_2; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..745
FT /note="F-box only protein 30"
FT /id="PRO_0000119918"
FT DOMAIN 610..658
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT ZN_FING 48..109
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 8
FT /note="S -> C (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036072"
FT VARIANT 375
FT /note="V -> M (in dbSNP:rs9373475)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_024443"
FT VARIANT 382
FT /note="S -> C (in dbSNP:rs17075385)"
FT /id="VAR_049044"
FT VARIANT 583
FT /note="H -> Q (in dbSNP:rs3811102)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020410"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2YRE"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2YRE"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2YRE"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2YRE"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:2YRE"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2YRE"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2YRE"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2YRE"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:2YRE"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YRE"
SQ SEQUENCE 745 AA; 82304 MW; C2C010CF28568F9F CRC64;
MEEELQHSHC VNCVSRRCMT RPEPGISCDL IGCPLVCGAV FHSCKADEHR LLCPFERVPC
LNSDFGCPFT MARNKVAEHL EMCPASVVCC TMEWNRWPVS YADRKSYENL SRDVDEVAQL
DMALALQDQR MLLESLKVAT MMSKATDKVS KPREQISVKS SVPEIPHANG LVSVDEESYG
ALYQATVETT RSLAAALDIL NTATRDIGML NTSVPNDMDE QQNARESLED QNLKDQDHLY
EEEIGAVGGI DYNDTNQNAQ SEQNGSSDLL CDLNTSSYDT SALCNGFPLE NICTQVIDQN
QNLHGDSKQS NLTNGDCVAS SDGTSKPSSS LAVAAQLREI IPSSALPNGT VQHILMPDDE
GEGELCWKKV DLGDVKNVDV LSFSHAPSFN FLSNSCWSKP KEDKAVDTSD LEVAEDPMGL
QGIDLITAAL LFCLGDSPGG RGISDSRMAD IYHIDVGTQT FSLPSAILAT STMVGEIASA
SACDHANPQL SNPSPFQTLG LDLVLECVAR YQPKQRSMFT FVCGQLFRRK EFSSHFKNVH
GDIHAGLNGW MEQRCPLAYY GCTYSQRRFC PSIQGAKIIH DRHLRSFGVQ PCVSTVLVEP
ARNCVLGLHN DHLSSLPFEV LQHIAGFLDG FSLCQLSCVS KLMRDVCGSL LQSRGMVILQ
WGKRKYPEGN SSWQIKEKVW RFSTAFCSVN EWKFADILSM ADHLKKCSYN VVEKREEAIP
LPCMCVTREL TKEGRSLRSV LKPVL
