ID   FBX40_HUMAN             Reviewed;         709 AA.
AC   Q9UH90; B2RAX7; Q32M70; Q9ULM5;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUN-2026, entry version 172.
DE   RecName: Full=F-box only protein 40;
DE   AltName: Full=Muscle disease-related protein;
GN   Name=FBXO40; Synonyms=FBX40, KIAA1195;
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].
RC   TISSUE=Muscle;
RA   Zhou Z.G., Wu Y.Q., Ren H.M., Lu C.Z.;
RT   "Cloning of a novel human gene related to muscle disease.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   TISSUE SPECIFICITY.
RX   PubMed=17928169; DOI=10.1016/j.gene.2007.08.020;
RA   Ye J., Zhang Y., Xu J., Zhang Q., Zhu D.;
RT   "FBXO40, a gene encoding a novel muscle-specific F-box protein, is
RT   upregulated in denervation-related muscle atrophy.";
RL   Gene 404:53-60(2007).
CC   -!- FUNCTION: Probable substrate-recognition component of the SCF (SKP1-
CC       CUL1-F-box protein)-type E3 ubiquitin ligase complex that may function
CC       in myogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed only in heart and skeletal muscle.
CC       {ECO:0000269|PubMed:17928169}.
CC   -!- MISCELLANEOUS: The expression decreases in the dystrophic muscle of
CC       Limb-girdle muscular dystrophy (LGMD) patient.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86509.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF204674; AAF17085.1; -; mRNA.
DR   EMBL; AB033021; BAA86509.1; ALT_INIT; mRNA.
DR   EMBL; AK314400; BAG37024.1; -; mRNA.
DR   EMBL; AC063920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79508.1; -; Genomic_DNA.
DR   EMBL; BC109275; AAI09276.1; -; mRNA.
DR   EMBL; BC109276; AAI09277.1; -; mRNA.
DR   CCDS; CCDS33835.1; -.
DR   RefSeq; NP_057382.2; NM_016298.4.
DR   AlphaFoldDB; Q9UH90; -.
DR   SMR; Q9UH90; -.
DR   BioGRID; 119698; 16.
DR   ComplexPortal; CPX-7981; SCF E3 ubiquitin ligase complex, FBXO40 variant.
DR   FunCoup; Q9UH90; 108.
DR   IntAct; Q9UH90; 12.
DR   STRING; 9606.ENSP00000337510; -.
DR   iPTMnet; Q9UH90; -.
DR   PhosphoSitePlus; Q9UH90; -.
DR   BioMuta; FBXO40; -.
DR   DMDM; 124012094; -.
DR   MassIVE; Q9UH90; -.
DR   PaxDb; 9606-ENSP00000337510; -.
DR   PeptideAtlas; Q9UH90; -.
DR   ProteomicsDB; 84285; -.
DR   Antibodypedia; 1237; 117 antibodies from 19 providers.
DR   DNASU; 51725; -.
DR   Ensembl; ENST00000338040.6; ENSP00000337510.4; ENSG00000163833.9.
DR   Ensembl; ENST00000868808.1; ENSP00000538867.1; ENSG00000163833.9.
DR   Ensembl; ENST00000868809.1; ENSP00000538868.1; ENSG00000163833.9.
DR   Ensembl; ENST00000868810.1; ENSP00000538869.1; ENSG00000163833.9.
DR   Ensembl; ENST00000868811.1; ENSP00000538870.1; ENSG00000163833.9.
DR   Ensembl; ENST00000968418.1; ENSP00000638477.1; ENSG00000163833.9.
DR   Ensembl; ENST00000968419.1; ENSP00000638478.1; ENSG00000163833.9.
DR   Ensembl; ENST00000968420.1; ENSP00000638479.1; ENSG00000163833.9.
DR   Ensembl; ENST00000968421.1; ENSP00000638480.1; ENSG00000163833.9.
DR   Ensembl; ENST00000968422.1; ENSP00000638481.1; ENSG00000163833.9.
DR   GeneID; 51725; -.
DR   KEGG; hsa:51725; -.
DR   MANE-Select; ENST00000338040.6; ENSP00000337510.4; NM_016298.4; NP_057382.2.
DR   UCSC; uc003eeg.3; human.
DR   AGR; HGNC:29816; -.
DR   ClinPGx; PA134971542; -.
DR   CTD; 51725; -.
DR   DisGeNET; 51725; -.
DR   GeneCards; FBXO40; -.
DR   HGNC; HGNC:29816; FBXO40.
DR   HPA; ENSG00000163833; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MalaCards; FBXO40; -.
DR   MIM; 609107; gene.
DR   OpenTargets; ENSG00000163833; -.
DR   VEuPathDB; HostDB:ENSG00000163833; -.
DR   eggNOG; ENOG502QVHX; Eukaryota.
DR   GeneTree; ENSGT00950000183204; -.
DR   HOGENOM; CLU_013357_0_0_1; -.
DR   InParanoid; Q9UH90; -.
DR   OMA; RKKIWQF; -.
DR   OrthoDB; 5918172at2759; -.
DR   PAN-GO; Q9UH90; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q9UH90; -.
DR   PathwayCommons; Q9UH90; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9UH90; -.
DR   Agora; ENSG00000163833; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 51725; 11 hits in 1191 CRISPR screens.
DR   GenomeRNAi; 51725; -.
DR   Pharos; Q9UH90; Tbio.
DR   PRO; PR:Q9UH90; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9UH90; protein.
DR   Bgee; ENSG00000163833; Expressed in gluteal muscle and 92 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; NAS:ComplexPortal.
DR   CDD; cd22175; F-box_FBXO40; 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:SF1; F-BOX ONLY PROTEIN 40; 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   Cytoplasm; Metal-binding; Proteomics identification; Reference proteome;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..709
FT                   /note="F-box only protein 40"
FT                   /id="PRO_0000119938"
FT   DOMAIN          570..624
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   ZN_FING         53..112
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   REGION          232..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         87
FT                   /note="V -> A (in dbSNP:rs4676684)"
FT                   /id="VAR_030005"
FT   CONFLICT        45
FT                   /note="T -> A (in Ref. 1; AAF17085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="L -> P (in Ref. 1; AAF17085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="E -> G (in Ref. 1; AAF17085)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   709 AA;  79782 MW;  4B69F51EA78D78E3 CRC64;
     MGKARRSPPG HHRHCEGCFN RHCHIPVEPN TSCLVISCHL LCGATFHMCK EAEHQLLCPL
     EQVPCLNSEY GCPLSMSRHK LAKHLQVCPA SVVCCSMEWN RWPNVDSETT LHENIMKETP
     SEECLDTALA LQDQKVLFRS LKMVELFPET REATEEEPTM NGETSVEEMG GAVGGVDIGL
     VPHGLSATNG EMAELSQEER EVLAKTKEGM DLVKFGQWEN IFSKEHAASA LTNSSASCES
     KNKNDSEKEQ ISSGHNMVEG EGAPKKKEPQ ENQKQQDVRT AMETTGLAPW QDGVLERLKT
     AVDAKDYNMY LVHNGRMLIH FGQMPACTPK ERDFVYGKLE AQEVKTVYTF KVPVSYCGKR
     ARLGDAMLSC KPSEHKAVDT SDLGITVEDL PKSDLIKTTL QCALERELKG HVISESRSID
     GLFMDFATQT YNFEPEQFSS GTVLADLTAA TPGGLHVELH SECVTRRHNK SSSAFTFTCN
     KFFRRDEFPL HFKNVHTDIQ SCLNGWFQHR CPLAYLGCTF VQNHFRPPGQ KAKVIYSQEL
     KTFAIKPEVA PELSEGRKNN HLLGHGGKSQ NSLTSLPLEI LKYIAGFLDS VSLAQLSQVS
     VLMRNICATL LQERGMVLLQ WKKKRYSHGG TSWRVHREIW QFSSLFSKIK SWEFNEVTSM
     SEHLKSCPFN IVEHKTDPIL LTSMCQPREQ ARESLVSTFR IRPRGRYVS
//