FBX7_HUMAN
ID FBX7_HUMAN Reviewed; 522 AA.
AC Q9Y3I1; B4DNB3; B4DWX5; Q5TGC4; Q5TI86; Q96HM6; Q9UF21; Q9UKT2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=F-box only protein 7;
GN Name=FBXO7; Synonyms=FBX7;
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 [MRNA] (ISOFORM 1).
RX PubMed=10945468; DOI=10.1006/geno.2000.6211;
RA Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.;
RT "cDNA cloning and expression analysis of new members of the mammalian F-box
RT protein family.";
RL Genomics 67:40-47(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ILE-115.
RC TISSUE=Heart, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-115.
RC TISSUE=Pancreas;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-522 (ISOFORM 1), AND VARIANT ILE-115.
RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA Pagano M.;
RT "Identification of a family of human F-box proteins.";
RL Curr. Biol. 9:1177-1179(1999).
RN [8]
RP INTERACTION WITH DLGAP5, AND IDENTIFICATION IN SCF COMPLEX.
RX PubMed=12527899; DOI=10.1038/sj.onc.1206129;
RA Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G.,
RA Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H.,
RA Chou C.-K.;
RT "Identification of a novel cell cycle regulated gene, HURP, overexpressed
RT in human hepatocellular carcinoma.";
RL Oncogene 22:298-307(2003).
RN [9]
RP INTERACTION WITH DLGAP5; CUL1 AND SKP1, AND FUNCTION IN UBIQUITINATION OF
RP DLGAP5.
RX PubMed=15145941; DOI=10.1074/jbc.m404950200;
RA Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
RT "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated
RT hepatoma up-regulated protein (HURP) proteolysis by a proline-rich
RT region.";
RL J. Biol. Chem. 279:32592-32602(2004).
RN [10]
RP INTERACTION WITH CDK6, AND SUBCELLULAR LOCATION.
RX PubMed=16096642; DOI=10.1038/sj.emboj.7600775;
RA Laman H., Funes J.M., Ye H., Henderson S., Galinanes-Garcia L., Hara E.,
RA Knowles P., McDonald N., Boshoff C.;
RT "Transforming activity of Fbxo7 is mediated specifically through regulation
RT of cyclin D/cdk6.";
RL EMBO J. 24:3104-3116(2005).
RN [11]
RP INTERACTION WITH BIRC2, AND FUNCTION IN UBIQUITINATION OF BIRC2.
RX PubMed=16510124; DOI=10.1016/j.bbrc.2006.02.061;
RA Chang Y.F., Cheng C.M., Chang L.K., Jong Y.J., Yuo C.Y.;
RT "The F-box protein Fbxo7 interacts with human inhibitor of apoptosis
RT protein cIAP1 and promotes cIAP1 ubiquitination.";
RL Biochem. Biophys. Res. Commun. 342:1022-1026(2006).
RN [12]
RP INTERACTION WITH SKP1; PSMF1 AND CDK6, SUBCELLULAR LOCATION, SUBUNIT,
RP IDENTIFICATION IN A COMPLEX WITH SKP1 AND CUL1, AND MUTAGENESIS OF VAL-253.
RX PubMed=18495667; DOI=10.1074/jbc.m709900200;
RA Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M.,
RA Meziane E.K., McDonald N.Q.;
RT "Structure of a conserved dimerization domain within the F-box protein
RT Fbxo7 and the PI31 proteasome inhibitor.";
RL J. Biol. Chem. 283:22325-22335(2008).
RN [13]
RP FUNCTION, INTERACTION WITH PRKN AND PINK1, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF THR-22, AND CHARACTERIZATION OF VARIANT PARK15 GLY-378.
RX PubMed=23933751; DOI=10.1038/nn.3489;
RA Burchell V.S., Nelson D.E., Sanchez-Martinez A., Delgado-Camprubi M.,
RA Ivatt R.M., Pogson J.H., Randle S.J., Wray S., Lewis P.A., Houlden H.,
RA Abramov A.Y., Hardy J., Wood N.W., Whitworth A.J., Laman H.,
RA Plun-Favreau H.;
RT "The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to
RT mediate mitophagy.";
RL Nat. Neurosci. 16:1257-1265(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 180-335.
RX PubMed=24419388; DOI=10.1107/s1399004713025820;
RA Shang J., Wang G., Yang Y., Huang X., Du Z.;
RT "Structure of the FP domain of Fbxo7 reveals a novel mode of protein-
RT protein interaction.";
RL Acta Crystallogr. D 70:155-164(2014).
RN [15]
RP VARIANT PARK15 GLY-378, AND VARIANT ILE-115.
RX PubMed=18513678; DOI=10.1016/j.ajhg.2008.05.005;
RA Shojaee S., Sina F., Banihosseini S.S., Kazemi M.H., Kalhor R.,
RA Shahidi G.-A., Fakhrai-Rad H., Ronaghi M., Elahi E.;
RT "Genome-wide linkage analysis of a Parkinsonian-pyramidal syndrome pedigree
RT by 500 K SNP arrays.";
RL Am. J. Hum. Genet. 82:1375-1384(2008).
RN [16]
RP VARIANT CYS-481.
RX PubMed=20853184; DOI=10.1007/s10048-010-0259-0;
RA Santoro L., Breedveld G.J., Manganelli F., Iodice R., Pisciotta C.,
RA Nolano M., Punzo F., Quarantelli M., Pappata S., Di Fonzo A., Oostra B.A.,
RA Bonifati V.;
RT "Novel ATP13A2 (PARK9) homozygous mutation in a family with marked
RT phenotype variability.";
RL Neurogenetics 12:33-39(2011).
RN [17]
RP VARIANT PARK15 ARG-34.
RX PubMed=32892229; DOI=10.1007/s00401-020-02219-6;
RA Tesson C., Lohmann E., Devos D., Bertrand H., Lesage S., Brice A.;
RT "Segregation of ATP10B variants in families with autosomal recessive
RT parkinsonism.";
RL Acta Neuropathol. 140:783-785(2020).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1
CC in the clearance of damaged mitochondria via selective autophagy
CC (mitophagy) by targeting PRKN to dysfunctional depolarized
CC mitochondria. Promotes MFN1 ubiquitination.
CC {ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:16510124,
CC ECO:0000269|PubMed:23933751}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via
CC its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2.
CC Interacts with CDK6 and promotes its interaction with D-type cyclin.
CC Interacts with PSMF1. {ECO:0000269|PubMed:12527899,
CC ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:16096642,
CC ECO:0000269|PubMed:16510124, ECO:0000269|PubMed:18495667,
CC ECO:0000269|PubMed:23933751}.
CC -!- SUBUNIT: [Isoform 1]: Interacts (via the N-terminal Ubl domain) with
CC PRKN (PubMed:23933751). Interact (via N-terminal region) with PINK1
CC (PubMed:23933751). {ECO:0000269|PubMed:23933751}.
CC -!- SUBUNIT: [Isoform 2]: Interact (via N-terminal region) with PINK1.
CC {ECO:0000269|PubMed:23933751}.
CC -!- INTERACTION:
CC Q9Y3I1; P22607: FGFR3; NbExp=3; IntAct=EBI-1161222, EBI-348399;
CC Q9Y3I1; Q9BXM7: PINK1; NbExp=8; IntAct=EBI-1161222, EBI-2846068;
CC Q9Y3I1; O60260: PRKN; NbExp=10; IntAct=EBI-1161222, EBI-716346;
CC Q9Y3I1; P25788: PSMA3; NbExp=6; IntAct=EBI-1161222, EBI-348380;
CC Q9Y3I1; P61289: PSME3; NbExp=3; IntAct=EBI-1161222, EBI-355546;
CC Q9Y3I1; Q92530: PSMF1; NbExp=9; IntAct=EBI-1161222, EBI-945916;
CC Q9Y3I1; P63208: SKP1; NbExp=8; IntAct=EBI-1161222, EBI-307486;
CC Q9Y3I1; Q9Y649; NbExp=3; IntAct=EBI-1161222, EBI-25900580;
CC Q9Y3I1-1; Q9BXM7: PINK1; NbExp=2; IntAct=EBI-9102965, EBI-2846068;
CC Q9Y3I1-1; O60260: PRKN; NbExp=2; IntAct=EBI-9102965, EBI-716346;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16096642,
CC ECO:0000269|PubMed:18495667}. Nucleus {ECO:0000269|PubMed:16096642,
CC ECO:0000269|PubMed:18495667}. Mitochondrion
CC {ECO:0000269|PubMed:23933751}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23933751}. Note=Predominantly cytoplasmic
CC (PubMed:16096642). A minor proportion is detected in the nucleus
CC (PubMed:16096642). Relocates from the cytosol to depolarized
CC mitochondria (PubMed:23933751). {ECO:0000269|PubMed:16096642,
CC ECO:0000269|PubMed:23933751}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y3I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3I1-2; Sequence=VSP_041073, VSP_041074;
CC Name=3;
CC IsoId=Q9Y3I1-3; Sequence=VSP_044723;
CC -!- DOMAIN: The ubiquitin-like region mediates interaction with PRKN.
CC {ECO:0000269|PubMed:23933751}.
CC -!- DOMAIN: The proline-rich region is important for protein-protein
CC interactions.
CC -!- DISEASE: Parkinson disease 15 (PARK15) [MIM:260300]: A
CC neurodegenerative disorder characterized by parkinsonian and pyramidal
CC signs. Clinical manifestations include tremor, bradykinesia, rigidity,
CC postural instability, spasticity, mainly in the lower limbs, and
CC hyperreflexia. {ECO:0000269|PubMed:18513678,
CC ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:32892229}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF04471.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF233225; AAF67155.1; -; mRNA.
DR EMBL; AL050254; CAB43356.1; -; mRNA.
DR EMBL; CR456491; CAG30377.1; -; mRNA.
DR EMBL; AK297841; BAG60175.1; -; mRNA.
DR EMBL; AK301716; BAG63187.1; -; mRNA.
DR EMBL; AL021937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z71183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008361; AAH08361.1; -; mRNA.
DR EMBL; AF129537; AAF04471.1; ALT_INIT; mRNA.
DR CCDS; CCDS13907.1; -. [Q9Y3I1-1]
DR CCDS; CCDS46695.1; -. [Q9Y3I1-2]
DR CCDS; CCDS58806.1; -. [Q9Y3I1-3]
DR RefSeq; NP_001028196.1; NM_001033024.1. [Q9Y3I1-2]
DR RefSeq; NP_001244919.1; NM_001257990.1. [Q9Y3I1-3]
DR RefSeq; NP_036311.3; NM_012179.3. [Q9Y3I1-1]
DR PDB; 4L9C; X-ray; 2.10 A; A/B=180-335.
DR PDB; 4L9H; X-ray; 2.00 A; A=180-335.
DR PDBsum; 4L9C; -.
DR PDBsum; 4L9H; -.
DR AlphaFoldDB; Q9Y3I1; -.
DR SMR; Q9Y3I1; -.
DR BioGRID; 117326; 594.
DR DIP; DIP-36125N; -.
DR IntAct; Q9Y3I1; 68.
DR MINT; Q9Y3I1; -.
DR STRING; 9606.ENSP00000266087; -.
DR GlyGen; Q9Y3I1; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y3I1; -.
DR PhosphoSitePlus; Q9Y3I1; -.
DR SwissPalm; Q9Y3I1; -.
DR BioMuta; FBXO7; -.
DR DMDM; 13124249; -.
DR EPD; Q9Y3I1; -.
DR jPOST; Q9Y3I1; -.
DR MassIVE; Q9Y3I1; -.
DR MaxQB; Q9Y3I1; -.
DR PaxDb; Q9Y3I1; -.
DR PeptideAtlas; Q9Y3I1; -.
DR PRIDE; Q9Y3I1; -.
DR ProteomicsDB; 65179; -.
DR ProteomicsDB; 86039; -. [Q9Y3I1-1]
DR ProteomicsDB; 86040; -. [Q9Y3I1-2]
DR Antibodypedia; 25270; 179 antibodies from 32 providers.
DR DNASU; 25793; -.
DR Ensembl; ENST00000266087.12; ENSP00000266087.7; ENSG00000100225.18. [Q9Y3I1-1]
DR Ensembl; ENST00000397426.5; ENSP00000380571.1; ENSG00000100225.18. [Q9Y3I1-3]
DR Ensembl; ENST00000452138.3; ENSP00000388547.2; ENSG00000100225.18. [Q9Y3I1-2]
DR GeneID; 25793; -.
DR KEGG; hsa:25793; -.
DR MANE-Select; ENST00000266087.12; ENSP00000266087.7; NM_012179.4; NP_036311.3.
DR UCSC; uc003amq.4; human. [Q9Y3I1-1]
DR CTD; 25793; -.
DR DisGeNET; 25793; -.
DR GeneCards; FBXO7; -.
DR GeneReviews; FBXO7; -.
DR HGNC; HGNC:13586; FBXO7.
DR HPA; ENSG00000100225; Tissue enhanced (bone).
DR MalaCards; FBXO7; -.
DR MIM; 260300; phenotype.
DR MIM; 605648; gene.
DR neXtProt; NX_Q9Y3I1; -.
DR OpenTargets; ENSG00000100225; -.
DR Orphanet; 171695; Parkinsonian-pyramidal syndrome.
DR PharmGKB; PA28047; -.
DR VEuPathDB; HostDB:ENSG00000100225; -.
DR eggNOG; ENOG502QTNJ; Eukaryota.
DR GeneTree; ENSGT00390000006670; -.
DR HOGENOM; CLU_039588_0_0_1; -.
DR InParanoid; Q9Y3I1; -.
DR OMA; ICLVLED; -.
DR OrthoDB; 999024at2759; -.
DR PhylomeDB; Q9Y3I1; -.
DR TreeFam; TF329830; -.
DR PathwayCommons; Q9Y3I1; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9Y3I1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25793; 39 hits in 1121 CRISPR screens.
DR ChiTaRS; FBXO7; human.
DR GeneWiki; FBXO7; -.
DR GenomeRNAi; 25793; -.
DR Pharos; Q9Y3I1; Tbio.
DR PRO; PR:Q9Y3I1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9Y3I1; protein.
DR Bgee; ENSG00000100225; Expressed in trabecular bone tissue and 211 other tissues.
DR ExpressionAtlas; Q9Y3I1; baseline and differential.
DR Genevisible; Q9Y3I1; HS.
DR GO; GO:0097414; C:classical Lewy body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097409; C:glial cytoplasmic inclusion; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990037; C:Lewy body core; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990038; C:Lewy body corona; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097462; C:Lewy neurite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043130; F:ubiquitin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:UniProtKB.
DR GO; GO:0030098; P:lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045620; P:negative regulation of lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0040012; P:regulation of locomotion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR021625; PI31_Prot_N.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW Methylation; Mitochondrion; Neurodegeneration; Nucleus; Parkinson disease;
KW Parkinsonism; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..522
FT /note="F-box only protein 7"
FT /id="PRO_0000119885"
FT DOMAIN 329..375
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..88
FT /note="Ubiquitin-like"
FT REGION 85..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..129
FT /note="Important for interaction with PINK1"
FT /evidence="ECO:0000269|PubMed:23933751"
FT REGION 129..169
FT /note="Important for interaction with CDK6"
FT REGION 180..324
FT /note="Important for dimerization and interaction with
FT PSMF1"
FT /evidence="ECO:0000269|PubMed:18495667"
FT REGION 381..522
FT /note="Important for interaction with CDK6"
FT REGION 483..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 481..484
FT /note="RFDP motif"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
FT MOD_RES 451
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
FT MOD_RES 518
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044723"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041073"
FT VAR_SEQ 80..91
FT /note="DDIPAPNIPSST -> MARPPGGSGPLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041074"
FT VARIANT 34
FT /note="L -> R (in PARK15; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32892229"
FT /id="VAR_084192"
FT VARIANT 115
FT /note="M -> I (in dbSNP:rs11107)"
FT /evidence="ECO:0000269|PubMed:10531035,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18513678"
FT /id="VAR_021408"
FT VARIANT 378
FT /note="R -> G (in PARK15; no effect on interaction with
FT PRKN; dbSNP:rs71799110)"
FT /evidence="ECO:0000269|PubMed:18513678,
FT ECO:0000269|PubMed:23933751"
FT /id="VAR_047938"
FT VARIANT 481
FT /note="R -> C (found in two patients with Kufor-Rakeb
FT syndrome also carrying R-877 in ATP13A2;
FT dbSNP:rs148272407)"
FT /evidence="ECO:0000269|PubMed:20853184"
FT /id="VAR_066022"
FT MUTAGEN 22
FT /note="T->M: Impairs interaction with PRKN."
FT /evidence="ECO:0000269|PubMed:23933751"
FT MUTAGEN 253
FT /note="V->E: Abolishes interaction with PSMF1."
FT /evidence="ECO:0000269|PubMed:18495667"
FT CONFLICT 79
FT /note="Q -> H (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> P (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="N -> S (in Ref. 4; BAG63187)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="M -> L (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="M -> L (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="P -> H (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="D -> N (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="M -> L (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="F -> L (in Ref. 7; AAF04471)"
FT /evidence="ECO:0000305"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:4L9H"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4L9H"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4L9H"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4L9H"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4L9C"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:4L9H"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:4L9H"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:4L9H"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:4L9H"
SQ SEQUENCE 522 AA; 58503 MW; C4E5E70A0747287A CRC64;
MRLRVRLLKR TWPLEVPETE PTLGHLRSHL RQSLLCTWGY SSNTRFTITL NYKDPLTGDE
ETLASYGIVS GDLICLILQD DIPAPNIPSS TDSEHSSLQN NEQPSLATSS NQTSMQDEQP
SDSFQGQAAQ SGVWNDDSML GPSQNFEAES IQDNAHMAEG TGFYPSEPML CSESVEGQVP
HSLETLYQSA DCSDANDALI VLIHLLMLES GYIPQGTEAK ALSMPEKWKL SGVYKLQYMH
PLCEGSSATL TCVPLGNLIV VNATLKINNE IRSVKRLQLL PESFICKEKL GENVANIYKD
LQKLSRLFKD QLVYPLLAFT RQALNLPDVF GLVVLPLELK LRIFRLLDVR SVLSLSAVCR
DLFTASNDPL LWRFLYLRDF RDNTVRVQDT DWKELYRKRH IQRKESPKGR FVMLLPSSTH
TIPFYPNPLH PRPFPSSRLP PGIIGGEYDQ RPTLPYVGDP ISSLIPGPGE TPSQFPPLRP
RFDPVGPLPG PNPILPGRGG PNDRFPFRPS RGRPTDGRLS FM
