ID FBX17_HUMAN Reviewed; 278 AA. AC Q96EF6; Q96LQ4; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=F-box only protein 17; DE AltName: Full=F-box only protein 26; GN Name=FBXO17; Synonyms=FBG4, FBX17, FBX26, FBXO26; 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], AND TISSUE SPECIFICITY. RX PubMed=12383498; DOI=10.1016/s0378-1119(02)00867-3; RA Ilyin G.P., Serandour A.L., Pigeon C., Rialland M., Glaise D., RA Guguen-Guillouzo C.; RT "A new subfamily of structurally related human F-box proteins."; RL Gene 296:11-20(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [4] RP SUGAR-BINDING, INTERACTION WITH CUL1 AND SKP1, IDENTIFICATION IN RP SCF-COMPLEX, AND MUTAGENESIS OF 257-SER-TRP-258. RX PubMed=18203720; DOI=10.1074/jbc.m709508200; RA Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.; RT "Diversity in tissue expression, substrate binding, and SCF complex RT formation for a lectin family of ubiquitin ligases."; RL J. Biol. Chem. 283:12717-12729(2008). CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box CC protein)-type E3 ubiquitin ligase complex. Able to recognize and bind CC denatured glycoproteins, which are modified with complex-type CC oligosaccharides. Also recognizes sulfated glycans. Does not bind high- CC mannose glycoproteins. CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. CC Interacts with SKP1 and CUL1. {ECO:0000269|PubMed:18203720}. CC -!- INTERACTION: CC Q96EF6; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2510157, EBI-10173507; CC Q96EF6; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-2510157, EBI-11524851; CC Q96EF6; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-2510157, EBI-979174; CC Q96EF6; Q13616: CUL1; NbExp=8; IntAct=EBI-2510157, EBI-359390; CC Q96EF6; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-2510157, EBI-948630; CC Q96EF6; Q15056-2: EIF4H; NbExp=3; IntAct=EBI-2510157, EBI-12222405; CC Q96EF6; O75564-2: JRK; NbExp=3; IntAct=EBI-2510157, EBI-17181882; CC Q96EF6; Q5T749: KPRP; NbExp=3; IntAct=EBI-2510157, EBI-10981970; CC Q96EF6; O95678: KRT75; NbExp=3; IntAct=EBI-2510157, EBI-2949715; CC Q96EF6; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-2510157, EBI-11953846; CC Q96EF6; Q14847-2: LASP1; NbExp=5; IntAct=EBI-2510157, EBI-9088686; CC Q96EF6; P29728-2: OAS2; NbExp=3; IntAct=EBI-2510157, EBI-12270678; CC Q96EF6; Q16825: PTPN21; NbExp=3; IntAct=EBI-2510157, EBI-2860264; CC Q96EF6; Q7L804: RAB11FIP2; NbExp=3; IntAct=EBI-2510157, EBI-1049676; CC Q96EF6; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-2510157, EBI-12001422; CC Q96EF6; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-2510157, EBI-3957636; CC Q96EF6; Q658L1: SAXO2; NbExp=3; IntAct=EBI-2510157, EBI-18394432; CC Q96EF6; P63208: SKP1; NbExp=16; IntAct=EBI-2510157, EBI-307486; CC Q96EF6; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-2510157, EBI-11975223; CC Q96EF6; O14771: ZNF213; NbExp=3; IntAct=EBI-2510157, EBI-12838388; CC Q96EF6; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-2510157, EBI-18036029; CC Q96EF6; O15535: ZSCAN9; NbExp=3; IntAct=EBI-2510157, EBI-751531; CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, liver and CC kidney. Expressed at lower levels in spleen and brain. CC {ECO:0000269|PubMed:12383498}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71616.1; Type=Erroneous initiation; 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; AF386743; AAL37625.1; -; mRNA. DR EMBL; AK057934; BAB71616.1; ALT_INIT; mRNA. DR EMBL; BC012385; AAH12385.1; -; mRNA. DR CCDS; CCDS12526.1; -. DR RefSeq; NP_079183.4; NM_024907.6. DR RefSeq; NP_680474.1; NM_148169.2. DR AlphaFoldDB; Q96EF6; -. DR SMR; Q96EF6; -. DR BioGRID; 125424; 59. DR ComplexPortal; CPX-7927; SCF E3 ubiquitin ligase complex, FBXO17 variant. DR CORUM; Q96EF6; -. DR IntAct; Q96EF6; 36. DR MINT; Q96EF6; -. DR STRING; 9606.ENSP00000292852; -. DR BioMuta; FBXO17; -. DR DMDM; 21263617; -. DR EPD; Q96EF6; -. DR jPOST; Q96EF6; -. DR MassIVE; Q96EF6; -. DR MaxQB; Q96EF6; -. DR PaxDb; 9606-ENSP00000292852; -. DR PeptideAtlas; Q96EF6; -. DR ProteomicsDB; 76403; -. DR Pumba; Q96EF6; -. DR Antibodypedia; 68422; 65 antibodies from 18 providers. DR DNASU; 115290; -. DR Ensembl; ENST00000292852.9; ENSP00000292852.3; ENSG00000269190.6. DR Ensembl; ENST00000595329.5; ENSP00000470361.1; ENSG00000269190.6. DR Ensembl; ENST00000634982.2; ENSP00000488997.1; ENSG00000282954.2. DR Ensembl; ENST00000635115.1; ENSP00000489327.1; ENSG00000282954.2. DR GeneID; 115290; -. DR KEGG; hsa:115290; -. DR MANE-Select; ENST00000292852.9; ENSP00000292852.3; NM_024907.7; NP_079183.4. DR UCSC; uc002okg.3; human. DR AGR; HGNC:18754; -. DR CTD; 115290; -. DR DisGeNET; 115290; -. DR GeneCards; FBXO17; -. DR HGNC; HGNC:18754; FBXO17. DR HPA; ENSG00000269190; Tissue enhanced (liver). DR MIM; 609094; gene. DR neXtProt; NX_Q96EF6; -. DR OpenTargets; ENSG00000269190; -. DR PharmGKB; PA38676; -. DR VEuPathDB; HostDB:ENSG00000269190; -. DR eggNOG; ENOG502RZA6; Eukaryota. DR GeneTree; ENSGT00940000162455; -. DR HOGENOM; CLU_068548_0_0_1; -. DR InParanoid; Q96EF6; -. DR OMA; YAVVQRC; -. DR OrthoDB; 587001at2759; -. DR PhylomeDB; Q96EF6; -. DR PathwayCommons; Q96EF6; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q96EF6; -. DR BioGRID-ORCS; 115290; 16 hits in 1193 CRISPR screens. DR GenomeRNAi; 115290; -. DR Pharos; Q96EF6; Tbio. DR PRO; PR:Q96EF6; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q96EF6; Protein. DR Bgee; ENSG00000269190; Expressed in right lobe of liver and 97 other cell types or tissues. DR ExpressionAtlas; Q96EF6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR CDD; cd22169; F-box_FBXO17-like; 1. DR Gene3D; 1.20.1280.50; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR007397; F-box-assoc_dom. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR039752; F-box_only. DR InterPro; IPR008979; Galactose-bd-like_sf. DR PANTHER; PTHR12125:SF7; F-BOX ONLY PROTEIN 17; 1. DR PANTHER; PTHR12125; F-BOX ONLY PROTEIN 6-LIKE PROTEIN; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF04300; FBA; 1. DR SMART; SM01198; FBA; 1. DR SMART; SM00256; FBOX; 1. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS51114; FBA; 1. DR PROSITE; PS50181; FBOX; 1. DR Genevisible; Q96EF6; HS. PE 1: Evidence at protein level; KW Reference proteome; Ubl conjugation pathway. FT CHAIN 1..278 FT /note="F-box only protein 17" FT /id="PRO_0000119898" FT DOMAIN 15..62 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT DOMAIN 99..275 FT /note="FBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00482" FT MUTAGEN 257..258 FT /note="SW->AA: Reduces interaction with glycosylated FT concanavalin-A in vitro." FT /evidence="ECO:0000269|PubMed:18203720" SQ SEQUENCE 278 AA; 31479 MW; B44E577D6F3529D4 CRC64; MGARLSRRRL PADPSLALDA LPPELLVQVL SHVPPRSLVT RCRPVCRAWR DIVDGPTVWL LQLARDRSAE GRALYAVAQR CLPSNEDKEE FPLCALARYC LRAPFGRNLI FNSCGEQGFR GWEVEHGGNG WAIEKNLTPV PGAPSQTCFV TSFEWCSKRQ LVDLVMEGVW QELLDSAQIE ICVADWWGAR ENCGCVYQLR VRLLDVYEKE VVKFSASPDP VLQWTERGCR QVSHVFTNFG KGIRYVSFEQ YGRDVSSWVG HYGALVTHSS VRVRIRLS //