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   10-JUN-2026, entry version 185.
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   -!- INTERACTION:
CC       Q8TB52; Q9UM54: MYO6; NbExp=2; IntAct=EBI-2556210, EBI-350606;
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_001348092.2.
DR   RefSeq; NP_115521.3; NM_032145.4.
DR   PDB; 2YRE; NMR; -; A=1-87.
DR   PDBsum; 2YRE; -.
DR   AlphaFoldDB; Q8TB52; -.
DR   SMR; Q8TB52; -.
DR   BioGRID; 123879; 57.
DR   ComplexPortal; CPX-7968; SCF E3 ubiquitin ligase complex, FBXO30 variant.
DR   FunCoup; Q8TB52; 1499.
DR   IntAct; Q8TB52; 37.
DR   MINT; Q8TB52; -.
DR   NDEx; MUSIC2-C5192-FBXO30; Osteosarcoma (U2OS) cell map - Cytoskeletal dynamics and intracellular transport (47 proteins).
DR   STRING; 9606.ENSP00000237281; -.
DR   GlyGen; Q8TB52; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TB52; -.
DR   PhosphoSitePlus; Q8TB52; -.
DR   BioMuta; FBXO30; -.
DR   DMDM; 51704325; -.
DR   jPOST; Q8TB52; -.
DR   MassIVE; Q8TB52; -.
DR   PaxDb; 9606-ENSP00000237281; -.
DR   PeptideAtlas; Q8TB52; -.
DR   ProteomicsDB; 73962; -.
DR   Pumba; Q8TB52; -.
DR   Antibodypedia; 33222; 51 antibodies from 13 providers.
DR   DNASU; 84085; -.
DR   Ensembl; ENST00000237281.5; ENSP00000237281.3; ENSG00000118496.6.
DR   Ensembl; ENST00000894020.1; ENSP00000564079.1; ENSG00000118496.6.
DR   Ensembl; ENST00000894021.1; ENSP00000564080.1; ENSG00000118496.6.
DR   Ensembl; ENST00000894022.1; ENSP00000564081.1; ENSG00000118496.6.
DR   Ensembl; ENST00000894023.1; ENSP00000564082.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929661.1; ENSP00000599720.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929662.1; ENSP00000599721.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929663.1; ENSP00000599722.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929664.1; ENSP00000599723.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929665.1; ENSP00000599724.1; ENSG00000118496.6.
DR   Ensembl; ENST00000929666.1; ENSP00000599725.1; ENSG00000118496.6.
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   AGR; HGNC:15600; -.
DR   ClinPGx; PA28041; -.
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   OpenTargets; ENSG00000118496; -.
DR   VEuPathDB; HostDB:ENSG00000118496; -.
DR   eggNOG; ENOG502QTD9; Eukaryota.
DR   GeneTree; ENSGT00950000183204; -.
DR   HOGENOM; CLU_013357_0_0_1; -.
DR   InParanoid; Q8TB52; -.
DR   OMA; SSWQVKE; -.
DR   OrthoDB; 5918172at2759; -.
DR   PAN-GO; Q8TB52; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8TB52; -.
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   Agora; ENSG00000118496; -.
DR   BioGRID-ORCS; 84085; 10 hits in 1196 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 191 other cell types or tissues.
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:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; NAS:ComplexPortal.
DR   CDD; cd22174; F-box_FBXO30; 1.
DR   FunFam; 3.30.40.150:FF:000001; F-box only protein 30; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 3.30.40.150; TRAF-like zinc-finger, N-terminal subdomain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF13; F-BOX ONLY PROTEIN 30; 1.
DR   PANTHER; PTHR15933; PROTEIN CBG16327; 1.
DR   Pfam; PF15966; F-box_4; 1.
DR   Pfam; PF15965; zf-TRAF_2; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS50145; ZF_TRAF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Proteomics identification; Reference proteome;
KW   Ubl conjugation; 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   COMPBIAS        222..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..314
FT                   /note="Polar residues"
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..66
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
//