KLH20_HUMAN
ID KLH20_HUMAN Reviewed; 609 AA.
AC Q9Y2M5; B3KMA0; B4DUR0; Q5TZF2; Q5ZF45; Q9H457;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Kelch-like protein 20;
DE AltName: Full=Kelch-like ECT2-interacting protein;
DE AltName: Full=Kelch-like protein X;
GN Name=KLHL20; Synonyms=KLEIP, KLHLX;
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), AND INTERACTION WITH ACTIN.
RX PubMed=14668487; DOI=10.1091/mbc.e03-07-0531;
RA Hara T., Ishida H., Raziuddin R., Dorkhom S., Kamijo K., Miki T.;
RT "Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-
RT cell contact sites of Madin-Darby canine kidney cells.";
RL Mol. Biol. Cell 15:1172-1184(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yoshida K., Sugano S.;
RT "Kelch motif containing protein.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [7]
RP FUNCTION.
RX PubMed=17395875; DOI=10.1161/01.res.0000265844.56493.ac;
RA Nacak T.G., Alajati A., Leptien K., Fulda C., Weber H., Miki T.,
RA Czepluch F.S., Waltenberger J., Wieland T., Augustin H.G., Kroll J.;
RT "The BTB-Kelch protein KLEIP controls endothelial migration and sprouting
RT angiogenesis.";
RL Circ. Res. 100:1155-1163(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3
RP UBIQUITIN LIGASE COMPLEX, INTERACTION WITH DAPK1 AND IFNG, AND MUTAGENESIS
RP OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
RX PubMed=20389280; DOI=10.1038/emboj.2010.62;
RA Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.;
RT "The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to
RT control interferon responses.";
RL EMBO J. 29:1748-1761(2010).
RN [9]
RP FUNCTION, INTERACTION WITH PML, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3
RP UBIQUITIN LIGASE COMPLEX, INDUCTION, AND MUTAGENESIS OF VAL-109; ILE-111;
RP ASP-113; CYS-146; LEU-148 AND LEU-150.
RX PubMed=21840486; DOI=10.1016/j.ccr.2011.07.008;
RA Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C.,
RA Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H., Gu D.L.,
RA Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.;
RT "A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to
RT potentiate HIF-1 signaling and prostate cancer progression.";
RL Cancer Cell 20:214-228(2011).
RN [10]
RP FUNCTION, INTERACTION WITH ARHGEF11, IDENTIFICATION IN A BCR
RP (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, AND MUTAGENESIS OF VAL-109;
RP ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
RX PubMed=21670212; DOI=10.1083/jcb.201103015;
RA Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.;
RT "PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced
RT neurite outgrowth.";
RL J. Cell Biol. 193:985-994(2011).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3
RP UBIQUITIN LIGASE COMPLEX, INTERACTION WITH CORO7, AND MUTAGENESIS OF
RP VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
RX PubMed=24768539; DOI=10.1016/j.molcel.2014.03.035;
RA Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C.,
RA Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.;
RT "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3
RT ligase regulates protein trafficking.";
RL Mol. Cell 54:586-600(2014).
RN [12]
RP INTERACTION WITH IVNS1ABP.
RX PubMed=25619834; DOI=10.1038/onc.2014.435;
RA Chen H.Y., Hu J.Y., Chen T.H., Lin Y.C., Liu X., Lin M.Y., Lang Y.D.,
RA Yen Y., Chen R.H.;
RT "KLHL39 suppresses colon cancer metastasis by blocking KLHL20-mediated PML
RT and DAPK ubiquitination.";
RL Oncogene 34:5141-5151(2015).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex involved in interferon response and
CC anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin
CC ligase complex mediates the ubiquitination of DAPK1, leading to its
CC degradation by the proteasome, thereby acting as a negative regulator
CC of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase
CC complex also specifically mediates 'Lys-33'-linked ubiquitination
CC (PubMed:24768539). Involved in anterograde Golgi to endosome transport
CC by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting
CC interaction between CORO7 and EPS15, thereby facilitating actin
CC polymerization and post-Golgi trafficking (PubMed:24768539). Also acts
CC as a regulator of endothelial migration during angiogenesis by
CC controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin
CC ligase complex acts as a regulator of neurite outgrowth by mediating
CC ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11
CC (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin
CC ligase complex is involved in tumor hypoxia: following hypoxia, the
CC BCR(KLHL20)complex mediates ubiquitination and degradation of PML,
CC potentiating HIF-1 signaling and cancer progression (PubMed:21840486).
CC {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17395875,
CC ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212,
CC ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:24768539}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ-
CC RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin.
CC Interacts with IFN-gamma (IFNG). Interacts (via kelch repeats) with
CC IVNS1ABP (via kelch repeats); this interaction blocks the assembly of
CC CUL3-KLHL20 complex (PubMed:25619834). {ECO:0000269|PubMed:14528312,
CC ECO:0000269|PubMed:14668487, ECO:0000269|PubMed:20389280,
CC ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
CC ECO:0000269|PubMed:24768539, ECO:0000269|PubMed:25619834}.
CC -!- INTERACTION:
CC Q9Y2M5; Q86V38: ATN1; NbExp=3; IntAct=EBI-714379, EBI-11954292;
CC Q9Y2M5; P54253: ATXN1; NbExp=6; IntAct=EBI-714379, EBI-930964;
CC Q9Y2M5; P54252: ATXN3; NbExp=3; IntAct=EBI-714379, EBI-946046;
CC Q9Y2M5; P46379-2: BAG6; NbExp=3; IntAct=EBI-714379, EBI-10988864;
CC Q9Y2M5; P02489: CRYAA; NbExp=3; IntAct=EBI-714379, EBI-6875961;
CC Q9Y2M5; Q13618: CUL3; NbExp=6; IntAct=EBI-714379, EBI-456129;
CC Q9Y2M5; P53355: DAPK1; NbExp=11; IntAct=EBI-714379, EBI-358616;
CC Q9Y2M5; P09172: DBH; NbExp=3; IntAct=EBI-714379, EBI-8589586;
CC Q9Y2M5; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-714379, EBI-25840379;
CC Q9Y2M5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-714379, EBI-10976677;
CC Q9Y2M5; P00488: F13A1; NbExp=3; IntAct=EBI-714379, EBI-2565863;
CC Q9Y2M5; P22607: FGFR3; NbExp=3; IntAct=EBI-714379, EBI-348399;
CC Q9Y2M5; P14136: GFAP; NbExp=3; IntAct=EBI-714379, EBI-744302;
CC Q9Y2M5; O14908-2: GIPC1; NbExp=3; IntAct=EBI-714379, EBI-25913156;
CC Q9Y2M5; Q53GS7: GLE1; NbExp=3; IntAct=EBI-714379, EBI-1955541;
CC Q9Y2M5; P28799: GRN; NbExp=3; IntAct=EBI-714379, EBI-747754;
CC Q9Y2M5; P06396: GSN; NbExp=3; IntAct=EBI-714379, EBI-351506;
CC Q9Y2M5; P04792: HSPB1; NbExp=3; IntAct=EBI-714379, EBI-352682;
CC Q9Y2M5; O43464: HTRA2; NbExp=3; IntAct=EBI-714379, EBI-517086;
CC Q9Y2M5; P42858: HTT; NbExp=9; IntAct=EBI-714379, EBI-466029;
CC Q9Y2M5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-714379, EBI-10975473;
CC Q9Y2M5; O14901: KLF11; NbExp=3; IntAct=EBI-714379, EBI-948266;
CC Q9Y2M5; Q92876: KLK6; NbExp=3; IntAct=EBI-714379, EBI-2432309;
CC Q9Y2M5; P51608: MECP2; NbExp=3; IntAct=EBI-714379, EBI-1189067;
CC Q9Y2M5; P19404: NDUFV2; NbExp=3; IntAct=EBI-714379, EBI-713665;
CC Q9Y2M5; P29474: NOS3; NbExp=3; IntAct=EBI-714379, EBI-1391623;
CC Q9Y2M5; Q13153: PAK1; NbExp=3; IntAct=EBI-714379, EBI-1307;
CC Q9Y2M5; O14832: PHYH; NbExp=3; IntAct=EBI-714379, EBI-721853;
CC Q9Y2M5; P29590: PML; NbExp=9; IntAct=EBI-714379, EBI-295890;
CC Q9Y2M5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-714379, EBI-25882629;
CC Q9Y2M5; O60260-5: PRKN; NbExp=3; IntAct=EBI-714379, EBI-21251460;
CC Q9Y2M5; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-714379, EBI-912440;
CC Q9Y2M5; P60891: PRPS1; NbExp=3; IntAct=EBI-714379, EBI-749195;
CC Q9Y2M5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-714379, EBI-396669;
CC Q9Y2M5; P37840: SNCA; NbExp=3; IntAct=EBI-714379, EBI-985879;
CC Q9Y2M5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-714379, EBI-5235340;
CC Q9Y2M5; Q13148: TARDBP; NbExp=3; IntAct=EBI-714379, EBI-372899;
CC Q9Y2M5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-714379, EBI-12806590;
CC Q9Y2M5; P02766: TTR; NbExp=3; IntAct=EBI-714379, EBI-711909;
CC Q9Y2M5; O76024: WFS1; NbExp=3; IntAct=EBI-714379, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Golgi
CC apparatus, trans-Golgi network. Cell projection, axon {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Note=Localizes in the
CC perinuclear region in normal conditions. Following IFN-alpha or IFN-
CC gamma treatment, it is relocalized and sequestrated to the PML nuclear
CC bodies, preventing DAPK1 ubiquitination (PubMed:20389280).
CC {ECO:0000269|PubMed:20389280}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2M5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2M5-2; Sequence=VSP_057026, VSP_057027;
CC -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:21840486}.
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DR EMBL; AJ844466; CAH59617.1; -; mRNA.
DR EMBL; AB026190; BAA77027.1; -; mRNA.
DR EMBL; AK001430; BAG50912.1; -; mRNA.
DR EMBL; AK300755; BAG62422.1; -; mRNA.
DR EMBL; AL109921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063418; AAH63418.1; -; mRNA.
DR CCDS; CCDS1310.1; -. [Q9Y2M5-1]
DR RefSeq; NP_055273.2; NM_014458.3. [Q9Y2M5-1]
DR RefSeq; XP_005245150.1; XM_005245093.3. [Q9Y2M5-1]
DR PDB; 5YQ4; X-ray; 1.58 A; A=303-600.
DR PDB; 6GY5; X-ray; 1.09 A; A=303-605.
DR PDBsum; 5YQ4; -.
DR PDBsum; 6GY5; -.
DR AlphaFoldDB; Q9Y2M5; -.
DR SMR; Q9Y2M5; -.
DR BioGRID; 118100; 185.
DR CORUM; Q9Y2M5; -.
DR IntAct; Q9Y2M5; 101.
DR MINT; Q9Y2M5; -.
DR STRING; 9606.ENSP00000209884; -.
DR iPTMnet; Q9Y2M5; -.
DR PhosphoSitePlus; Q9Y2M5; -.
DR BioMuta; KLHL20; -.
DR DMDM; 257051084; -.
DR EPD; Q9Y2M5; -.
DR MassIVE; Q9Y2M5; -.
DR MaxQB; Q9Y2M5; -.
DR PaxDb; Q9Y2M5; -.
DR PeptideAtlas; Q9Y2M5; -.
DR PRIDE; Q9Y2M5; -.
DR ProteomicsDB; 5204; -.
DR ProteomicsDB; 85844; -. [Q9Y2M5-1]
DR Antibodypedia; 20562; 112 antibodies from 21 providers.
DR DNASU; 27252; -.
DR Ensembl; ENST00000209884.5; ENSP00000209884.4; ENSG00000076321.11. [Q9Y2M5-1]
DR GeneID; 27252; -.
DR KEGG; hsa:27252; -.
DR MANE-Select; ENST00000209884.5; ENSP00000209884.4; NM_014458.4; NP_055273.2.
DR UCSC; uc001gjc.5; human. [Q9Y2M5-1]
DR CTD; 27252; -.
DR DisGeNET; 27252; -.
DR GeneCards; KLHL20; -.
DR HGNC; HGNC:25056; KLHL20.
DR HPA; ENSG00000076321; Low tissue specificity.
DR MIM; 617679; gene.
DR neXtProt; NX_Q9Y2M5; -.
DR OpenTargets; ENSG00000076321; -.
DR PharmGKB; PA134982126; -.
DR VEuPathDB; HostDB:ENSG00000076321; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155161; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q9Y2M5; -.
DR OMA; NSWSPIV; -.
DR OrthoDB; 731760at2759; -.
DR PhylomeDB; Q9Y2M5; -.
DR TreeFam; TF329218; -.
DR PathwayCommons; Q9Y2M5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9Y2M5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 27252; 17 hits in 1131 CRISPR screens.
DR ChiTaRS; KLHL20; human.
DR GeneWiki; KLHL20; -.
DR GenomeRNAi; 27252; -.
DR Pharos; Q9Y2M5; Tbio.
DR PRO; PR:Q9Y2M5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2M5; protein.
DR Bgee; ENSG00000076321; Expressed in secondary oocyte and 206 other tissues.
DR Genevisible; Q9Y2M5; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0019964; F:interferon-gamma binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1990390; P:protein K33-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0035455; P:response to interferon-alpha; TAS:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030594; KLHL17/KLHL20.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF454; PTHR24412:SF454; 2.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW Cytoplasm; Golgi apparatus; Kelch repeat; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation pathway.
FT CHAIN 1..609
FT /note="Kelch-like protein 20"
FT /id="PRO_0000119123"
FT DOMAIN 68..135
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 170..272
FT /note="BACK"
FT REPEAT 319..365
FT /note="Kelch 1"
FT REPEAT 367..413
FT /note="Kelch 2"
FT REPEAT 414..460
FT /note="Kelch 3"
FT REPEAT 462..507
FT /note="Kelch 4"
FT REPEAT 509..554
FT /note="Kelch 5"
FT REPEAT 556..601
FT /note="Kelch 6"
FT VAR_SEQ 1..10
FT /note="MEGKPMRRCT -> MVHGRKANAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057026"
FT VAR_SEQ 11..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057027"
FT MUTAGEN 109
FT /note="V->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-111; A-113; A-146; A-148 and A-150."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT MUTAGEN 111
FT /note="I->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-109; A-113; A-146; A-148 and A-150."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT MUTAGEN 113
FT /note="D->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-109; A-111; A-146; A-148 and A-150."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT MUTAGEN 146
FT /note="C->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-109; A-111; A-113; A-148 and A-150."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT MUTAGEN 148
FT /note="L->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-109; A-111; A-113; A-146 and A-150."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT MUTAGEN 150
FT /note="L->A: In KLHL20m6; abolishes interaction with CUL3;
FT when associated with A-109; A-111; A-113; A-146 and A-148."
FT /evidence="ECO:0000269|PubMed:20389280,
FT ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486,
FT ECO:0000269|PubMed:24768539"
FT CONFLICT 171
FT /note="L -> Q (in Ref. 3; BAG50912)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="F -> S (in Ref. 3; BAG50912)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="S -> N (in Ref. 3; BAG50912)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="V -> M (in Ref. 3; BAG50912)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="G -> W (in Ref. 2; BAA77027)"
FT /evidence="ECO:0000305"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 529..532
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 555..562
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 567..575
FT /evidence="ECO:0007829|PDB:6GY5"
FT TURN 576..579
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:6GY5"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:6GY5"
SQ SEQUENCE 609 AA; 67955 MW; FA05E3FE8341B422 CRC64;
MEGKPMRRCT NIRPGETGMD VTSRCTLGDP NKLPEGVPQP ARMPYISDKH PRQTLEVINL
LRKHRELCDV VLVVGAKKIY AHRVILSACS PYFRAMFTGE LAESRQTEVV IRDIDERAME
LLIDFAYTSQ ITVEEGNVQT LLPAACLLQL AEIQEACCEF LKRQLDPSNC LGIRAFADTH
SCRELLRIAD KFTQHNFQEV MESEEFMLLP ANQLIDIISS DELNVRSEEQ VFNAVMAWVK
YSIQERRPQL PQVLQHVRLP LLSPKFLVGT VGSDPLIKSD EECRDLVDEA KNYLLLPQER
PLMQGPRTRP RKPIRCGEVL FAVGGWCSGD AISSVERYDP QTNEWRMVAS MSKRRCGVGV
SVLDDLLYAV GGHDGSSYLN SVERYDPKTN QWSSDVAPTS TCRTSVGVAV LGGFLYAVGG
QDGVSCLNIV ERYDPKENKW TRVASMSTRR LGVAVAVLGG FLYAVGGSDG TSPLNTVERY
NPQENRWHTI APMGTRRKHL GCAVYQDMIY AVGGRDDTTE LSSAERYNPR TNQWSPVVAM
TSRRSGVGLA VVNGQLMAVG GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK
MTHCESHIW
