FBSP1_HUMAN
ID FBSP1_HUMAN Reviewed; 286 AA.
AC P0C2W1; A6NF90; D3DXB5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE AltName: Full=F-box only protein 45;
DE Short=hFbxo45;
GN Name=FBXO45; Synonyms=FBX45;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-286.
RC TISSUE=Hepatoma;
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 NOMENCLATURE, AND IDENTIFICATION.
RX PubMed=15520277; DOI=10.1101/gad.1255304;
RA Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M., Harper J.W.;
RT "Systematic analysis and nomenclature of mammalian F-box proteins.";
RL Genes Dev. 18:2573-2580(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP FUNCTION, INDUCTION, AND INTERACTION WITH TP73.
RX PubMed=19581926; DOI=10.1038/onc.2009.177;
RA Peschiaroli A., Scialpi F., Bernassola F., Pagano M., Melino G.;
RT "The F-box protein FBXO45 promotes the proteasome-dependent degradation of
RT p73.";
RL Oncogene 28:3157-3166(2009).
RN [7]
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).
CC -!- FUNCTION: Component of E3 ubiquitin ligase complexes. Required for
CC normal neuromuscular synaptogenesis, axon pathfinding and neuronal
CC migration (By similarity). Plays a role in the regulation of
CC neurotransmission at mature neurons (By similarity). May control
CC synaptic activity by controlling UNC13A via ubiquitin dependent pathway
CC (By similarity). Specifically recognizes TP73, promoting its
CC ubiquitination and degradation. {ECO:0000250,
CC ECO:0000269|PubMed:19581926}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms a complex with MYCBP2 and SKP1 but does not appear to
CC form an authentic SCF (SKP1-CUL1-F-box protein) complex (By
CC similarity). Interacts (via B30.2/SPRY domain) with TP73 (via SAM
CC domain); leading to TP73 ubiquitination and degradation by proteasome.
CC Interacts (via SRY domain) with UNC13A; leading to degradation of
CC UNC13A by the proteasome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}.
CC Presynaptic cell membrane {ECO:0000250}.
CC -!- INDUCTION: Down-regulated in response to DNA-damage.
CC {ECO:0000269|PubMed:19581926}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {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; AC092933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471191; EAW53643.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53644.1; -; Genomic_DNA.
DR EMBL; AK025697; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS46985.1; -.
DR RefSeq; NP_001099043.1; NM_001105573.1.
DR AlphaFoldDB; P0C2W1; -.
DR SMR; P0C2W1; -.
DR BioGRID; 128358; 175.
DR IntAct; P0C2W1; 14.
DR STRING; 9606.ENSP00000310332; -.
DR iPTMnet; P0C2W1; -.
DR PhosphoSitePlus; P0C2W1; -.
DR BioMuta; FBXO45; -.
DR DMDM; 146286173; -.
DR EPD; P0C2W1; -.
DR jPOST; P0C2W1; -.
DR MassIVE; P0C2W1; -.
DR MaxQB; P0C2W1; -.
DR PaxDb; P0C2W1; -.
DR PeptideAtlas; P0C2W1; -.
DR PRIDE; P0C2W1; -.
DR ProteomicsDB; 52305; -.
DR Antibodypedia; 51201; 67 antibodies from 16 providers.
DR DNASU; 200933; -.
DR Ensembl; ENST00000311630.7; ENSP00000310332.6; ENSG00000174013.8.
DR GeneID; 200933; -.
DR KEGG; hsa:200933; -.
DR MANE-Select; ENST00000311630.7; ENSP00000310332.6; NM_001105573.2; NP_001099043.1.
DR UCSC; uc010iai.4; human.
DR CTD; 200933; -.
DR DisGeNET; 200933; -.
DR GeneCards; FBXO45; -.
DR HGNC; HGNC:29148; FBXO45.
DR HPA; ENSG00000174013; Low tissue specificity.
DR MIM; 609112; gene.
DR neXtProt; NX_P0C2W1; -.
DR OpenTargets; ENSG00000174013; -.
DR PharmGKB; PA134904114; -.
DR VEuPathDB; HostDB:ENSG00000174013; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_1_0_1; -.
DR InParanoid; P0C2W1; -.
DR OMA; YHAWNPN; -.
DR OrthoDB; 1027590at2759; -.
DR PhylomeDB; P0C2W1; -.
DR TreeFam; TF312822; -.
DR PathwayCommons; P0C2W1; -.
DR SignaLink; P0C2W1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 200933; 9 hits in 1110 CRISPR screens.
DR ChiTaRS; FBXO45; human.
DR GenomeRNAi; 200933; -.
DR Pharos; P0C2W1; Tbio.
DR PRO; PR:P0C2W1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P0C2W1; protein.
DR Bgee; ENSG00000174013; Expressed in secondary oocyte and 193 other tissues.
DR ExpressionAtlas; P0C2W1; baseline and differential.
DR Genevisible; P0C2W1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0021800; P:cerebral cortex tangential migration; IEA:Ensembl.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0060386; P:synapse assembly involved in innervation; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd12907; SPRY_Fbox; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035784; SPRY_FBXO45.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Developmental protein;
KW Membrane; Neurogenesis; Postsynaptic cell membrane; Reference proteome;
KW Synapse; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..286
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000285933"
FT DOMAIN 33..82
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 92..284
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
SQ SEQUENCE 286 AA; 30633 MW; C2CF11ED007CC837 CRC64;
MAAPAPGAGA ASGGAGCSGG GAGAGAGSGS GAAGAGGRLP SRVLELVFSY LELSELRSCA
LVCKHWYRCL HGDENSEVWR SLCARSLAEE ALRTDILCNL PSYKAKIRAF QHAFSTNDCS
RNVYIKKNGF TLHRNPIAQS TDGARTKIGF SEGRHAWEVW WEGPLGTVAV IGIATKRAPM
QCQGYVALLG SDDQSWGWNL VDNNLLHNGE VNGSFPQCNN APKYQIGERI RVILDMEDKT
LAFERGYEFL GVAFRGLPKV CLYPAVSAVY GNTEVTLVYL GKPLDG
