FBX17_HUMAN
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 03-AUG-2022, entry version 151.
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};
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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; 58.
DR CORUM; Q96EF6; -.
DR IntAct; Q96EF6; 35.
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; Q96EF6; -.
DR PeptideAtlas; Q96EF6; -.
DR PRIDE; Q96EF6; -.
DR ProteomicsDB; 76403; -.
DR Antibodypedia; 68422; 54 antibodies from 17 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 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; 922544at2759; -.
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; 15 hits in 1114 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 96 other tissues.
DR ExpressionAtlas; Q96EF6; baseline and differential.
DR Genevisible; Q96EF6; HS.
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:0016567; P:protein ubiquitination; IEA:GOC.
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 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; PTHR12125; 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; SSF49785; SSF49785; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS51114; FBA; 1.
DR PROSITE; PS50181; FBOX; 1.
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
