ID   KLDC2_HUMAN             Reviewed;         406 AA.
AC   Q9Y2U9; B3KPF9; Q6IAF0; Q86TY9;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=Kelch domain-containing protein 2 {ECO:0000305};
DE   AltName: Full=Hepatocellular carcinoma-associated antigen 33 {ECO:0000303|PubMed:12097419};
DE   AltName: Full=Host cell factor homolog LCP {ECO:0000303|PubMed:11384994};
DE   AltName: Full=Host cell factor-like protein 1 {ECO:0000303|PubMed:11384994};
DE            Short=HCLP-1 {ECO:0000303|PubMed:11384994};
GN   Name=KLHDC2 {ECO:0000303|PubMed:16964437,
GN   ECO:0000312|HGNC:HGNC:20231};
GN   Synonyms=HCA33 {ECO:0000303|PubMed:12097419};
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), FUNCTION, INTERACTION WITH CREB3,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11384994; DOI=10.1074/jbc.m103893200;
RA   Zhou H.-J., Wong C.-M., Chen J.-H., Qiang B.-Q., Yuan J.-G., Jin D.-Y.;
RT   "Inhibition of LZIP-mediated transcription through direct interaction with
RT   a novel host cell factor-like protein.";
RL   J. Biol. Chem. 276:28933-28938(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Hepatoma;
RX   PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA   Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA   Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA   Chen W.-F.;
RT   "Large scale identification of human hepatocellular carcinoma-associated
RT   antigens by autoantibodies.";
RL   J. Immunol. 169:1102-1109(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Ovarian carcinoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Kidney;
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   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16964437; DOI=10.1007/s11010-006-9304-6;
RA   Chin K.-T., Xu H.-T., Ching Y.-P., Jin D.-Y.;
RT   "Differential subcellular localization and activity of kelch repeat
RT   proteins KLHDC1 and KLHDC2.";
RL   Mol. Cell. Biochem. 296:109-119(2007).
RN   [9]
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).
RN   [10]
RP   FUNCTION.
RX   PubMed=26138980; DOI=10.1126/science.aab0515;
RA   Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT   "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT   by failed UGA/Sec decoding.";
RL   Science 349:91-95(2015).
RN   [11]
RP   FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP   COMPLEX.
RX   PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA   Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT   "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT   terminal degrons.";
RL   Cell 173:1622-1635(2018).
RN   [12]
RP   FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP   COMPLEX.
RX   PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006;
RA   Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y.,
RA   Elledge S.J., Zheng N., Yen H.S.;
RT   "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases.";
RL   Mol. Cell 70:602-613(2018).
RN   [13] {ECO:0007744|PDB:6DO3, ECO:0007744|PDB:6DO4, ECO:0007744|PDB:6DO5}
RP   X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-362 IN COMPLEX WITH SELENOK;
RP   SELENOS OR USP1, FUNCTION, PATHWAY, IDENTIFICATION IN A CRL2 E3
RP   UBIQUITIN-PROTEIN LIGASE COMPLEX, AND MUTAGENESIS OF LYS-147; ARG-189;
RP   ARG-236; ARG-241 AND SER-269.
RX   PubMed=30526872; DOI=10.1016/j.molcel.2018.10.021;
RA   Rusnac D.V., Lin H.C., Canzani D., Tien K.X., Hinds T.R., Tsue A.F.,
RA   Bush M.F., Yen H.S., Zheng N.;
RT   "Recognition of the diglycine C-end degron by CRL2(KLHDC2) ubiquitin
RT   ligase.";
RL   Mol. Cell 72:813-822(2018).
CC   -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC       ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC       degrons) pathway, which recognizes a C-degron located at the extreme C
CC       terminus of target proteins, leading to their ubiquitination and
CC       degradation (PubMed:29779948, PubMed:29775578, PubMed:30526872). The C-
CC       degron recognized by the DesCEND pathway is usually a motif of less
CC       than ten residues and can be present in full-length proteins, truncated
CC       proteins or proteolytically cleaved forms (PubMed:29779948,
CC       PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2) complex
CC       specifically recognizes proteins with a diglycine (Gly-Gly) at the C-
CC       terminus, leading to their ubiquitination and degradation
CC       (PubMed:29779948, PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2)
CC       complex mediates ubiquitination and degradation of truncated SELENOK
CC       and SELENOS selenoproteins produced by failed UGA/Sec decoding, which
CC       end with a diglycine (PubMed:26138980, PubMed:30526872). The
CC       CRL2(KLHDC2) complex also recognizes proteolytically cleaved proteins
CC       ending with Gly-Gly, such as the N-terminal fragment of USP1, leading
CC       to their degradation (PubMed:29775578, PubMed:30526872). May also act
CC       as an indirect repressor of CREB3-mediated transcription by interfering
CC       with CREB3-DNA-binding (PubMed:11384994). {ECO:0000269|PubMed:11384994,
CC       ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578,
CC       ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30526872}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948,
CC       ECO:0000269|PubMed:30526872}.
CC   -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC       named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC       CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC       KLHDC2 (PubMed:29779948, PubMed:29775578, PubMed:30526872). Interacts
CC       with CREB3; interaction is direct and specific as it does not interact
CC       with CREB1, ATF4, ATF6, JUN, FOS, CEBPA or herpes simplex virus
CC       transactivator VP16 (PubMed:11384994). {ECO:0000269|PubMed:11384994,
CC       ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948,
CC       ECO:0000269|PubMed:30526872}.
CC   -!- INTERACTION:
CC       Q9Y2U9; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-715326, EBI-744342;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11384994,
CC       ECO:0000269|PubMed:16964437}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y2U9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2U9-2; Sequence=VSP_030165, VSP_030166;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with high levels in skeletal
CC       muscle, heart, pancreas and liver (PubMed:11384994, PubMed:16964437).
CC       Undetectable in peripheral blood leukocytes (PubMed:16964437).
CC       {ECO:0000269|PubMed:11384994, ECO:0000269|PubMed:16964437}.
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DR   EMBL; AF113131; AAD21038.1; -; mRNA.
DR   EMBL; AF244137; AAF66246.1; -; mRNA.
DR   EMBL; BX161429; CAD61901.1; -; mRNA.
DR   EMBL; AK001771; BAA91898.1; -; mRNA.
DR   EMBL; AK056298; BAG51671.1; -; mRNA.
DR   EMBL; CR457205; CAG33486.1; -; mRNA.
DR   EMBL; CH471078; EAW65749.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW65750.1; -; Genomic_DNA.
DR   EMBL; BC002335; AAH02335.1; -; mRNA.
DR   EMBL; BC024192; AAH24192.1; -; mRNA.
DR   CCDS; CCDS9693.1; -. [Q9Y2U9-1]
DR   RefSeq; NP_055130.1; NM_014315.2. [Q9Y2U9-1]
DR   PDB; 6DO3; X-ray; 2.17 A; A/B=1-362.
DR   PDB; 6DO4; X-ray; 2.20 A; A/B=1-362.
DR   PDB; 6DO5; X-ray; 2.50 A; A/B=1-362.
DR   PDB; 8EBL; X-ray; 1.37 A; A/B=15-361.
DR   PDB; 8EBM; X-ray; 1.58 A; A/B=15-361.
DR   PDB; 8EBN; X-ray; 2.60 A; A/B=1-406.
DR   PDB; 8PIF; X-ray; 1.78 A; A/B=1-362.
DR   PDBsum; 6DO3; -.
DR   PDBsum; 6DO4; -.
DR   PDBsum; 6DO5; -.
DR   PDBsum; 8EBL; -.
DR   PDBsum; 8EBM; -.
DR   PDBsum; 8EBN; -.
DR   PDBsum; 8PIF; -.
DR   AlphaFoldDB; Q9Y2U9; -.
DR   SMR; Q9Y2U9; -.
DR   BioGRID; 117123; 79.
DR   ComplexPortal; CPX-2226; KLHDC2-Elongin C-Elongin B E3 ubiquitin ligase complex.
DR   IntAct; Q9Y2U9; 56.
DR   MINT; Q9Y2U9; -.
DR   STRING; 9606.ENSP00000298307; -.
DR   iPTMnet; Q9Y2U9; -.
DR   PhosphoSitePlus; Q9Y2U9; -.
DR   BioMuta; KLHDC2; -.
DR   DMDM; 28380093; -.
DR   EPD; Q9Y2U9; -.
DR   jPOST; Q9Y2U9; -.
DR   MassIVE; Q9Y2U9; -.
DR   MaxQB; Q9Y2U9; -.
DR   PaxDb; 9606-ENSP00000298307; -.
DR   PeptideAtlas; Q9Y2U9; -.
DR   ProteomicsDB; 85905; -. [Q9Y2U9-1]
DR   ProteomicsDB; 85906; -. [Q9Y2U9-2]
DR   Pumba; Q9Y2U9; -.
DR   Antibodypedia; 23574; 114 antibodies from 19 providers.
DR   DNASU; 23588; -.
DR   Ensembl; ENST00000298307.10; ENSP00000298307.5; ENSG00000165516.11. [Q9Y2U9-1]
DR   Ensembl; ENST00000555443.5; ENSP00000450944.1; ENSG00000165516.11. [Q9Y2U9-2]
DR   Ensembl; ENST00000555739.5; ENSP00000450539.1; ENSG00000165516.11. [Q9Y2U9-2]
DR   GeneID; 23588; -.
DR   KEGG; hsa:23588; -.
DR   MANE-Select; ENST00000298307.10; ENSP00000298307.5; NM_014315.3; NP_055130.1.
DR   UCSC; uc001wwx.4; human. [Q9Y2U9-1]
DR   AGR; HGNC:20231; -.
DR   CTD; 23588; -.
DR   DisGeNET; 23588; -.
DR   GeneCards; KLHDC2; -.
DR   HGNC; HGNC:20231; KLHDC2.
DR   HPA; ENSG00000165516; Low tissue specificity.
DR   MIM; 611280; gene.
DR   neXtProt; NX_Q9Y2U9; -.
DR   OpenTargets; ENSG00000165516; -.
DR   PharmGKB; PA134924955; -.
DR   VEuPathDB; HostDB:ENSG00000165516; -.
DR   eggNOG; KOG0379; Eukaryota.
DR   GeneTree; ENSGT00940000157150; -.
DR   HOGENOM; CLU_1151487_0_0_1; -.
DR   InParanoid; Q9Y2U9; -.
DR   OMA; MGKLLQF; -.
DR   OrthoDB; 2906516at2759; -.
DR   PhylomeDB; Q9Y2U9; -.
DR   TreeFam; TF314081; -.
DR   PathwayCommons; Q9Y2U9; -.
DR   SignaLink; Q9Y2U9; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 23588; 12 hits in 1162 CRISPR screens.
DR   ChiTaRS; KLHDC2; human.
DR   GenomeRNAi; 23588; -.
DR   Pharos; Q9Y2U9; Tbio.
DR   PRO; PR:Q9Y2U9; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y2U9; Protein.
DR   Bgee; ENSG00000165516; Expressed in parotid gland and 215 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2U9; baseline and differential.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   PANTHER; PTHR46228; KELCH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46228:SF3; KELCH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13418; Kelch_4; 3.
DR   SUPFAM; SSF117281; Kelch motif; 2.
DR   Genevisible; Q9Y2U9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Kelch repeat; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..406
FT                   /note="Kelch domain-containing protein 2"
FT                   /id="PRO_0000119127"
FT   REPEAT          43..89
FT                   /note="Kelch 1"
FT   REPEAT          102..155
FT                   /note="Kelch 2"
FT   REPEAT          157..202
FT                   /note="Kelch 3"
FT   REPEAT          229..278
FT                   /note="Kelch 4"
FT   REPEAT          280..329
FT                   /note="Kelch 5"
FT   REPEAT          331..377
FT                   /note="Kelch 6"
FT   VAR_SEQ         239..249
FT                   /note="DARMNDLHYLN -> VSIQTTSMTCF (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030165"
FT   VAR_SEQ         250..406
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030166"
FT   MUTAGEN         147
FT                   /note="K->A: Strongly impaired ability to recognize
FT                   truncated SELENOK or cleaved USP1 with a diglycine
FT                   (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         189
FT                   /note="R->A: Does not affect ability to recognize truncated
FT                   SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the
FT                   C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         236
FT                   /note="R->A: Does not affect ability to recognize truncated
FT                   SELENOK with a diglycine (Gly-Gly) at the C-terminus.
FT                   Abolished ability to recognize cleaved USP1 with a
FT                   diglycine (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         236
FT                   /note="R->E: Abolished ability to recognize truncated
FT                   SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         241
FT                   /note="R->A,L,E: Abolished ability to recognize truncated
FT                   SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the
FT                   C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         241
FT                   /note="R->K: Does not affect ability to recognize truncated
FT                   SELENOK with a diglycine (Gly-Gly) at the C-terminus.
FT                   Abolished ability to recognize cleaved USP1 with a
FT                   diglycine (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         269
FT                   /note="S->A: Does not affect ability to recognize truncated
FT                   SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   MUTAGEN         269
FT                   /note="S->E,L: Abolished ability to recognize truncated
FT                   SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT                   /evidence="ECO:0000269|PubMed:30526872"
FT   CONFLICT        25
FT                   /note="E -> D (in Ref. 5; CAG33486)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:6DO3"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:8EBM"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   HELIX           181..184
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          195..199
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            200..203
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          222..226
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          229..237
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          240..249
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          268..270
FT                   /evidence="ECO:0007829|PDB:8EBN"
FT   STRAND          272..277
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          280..284
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          297..301
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            302..305
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          306..310
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   TURN            313..316
FT                   /evidence="ECO:0007829|PDB:6DO4"
FT   STRAND          323..326
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:8EBL"
FT   HELIX           364..374
FT                   /evidence="ECO:0007829|PDB:8EBN"
FT   HELIX           388..391
FT                   /evidence="ECO:0007829|PDB:8EBN"
FT   HELIX           393..396
FT                   /evidence="ECO:0007829|PDB:8EBN"
SQ   SEQUENCE   406 AA;  46099 MW;  07486B06AC4E97FF CRC64;
     MADGNEDLRA DDLPGPAFES YESMELACPA ERSGHVAVSD GRHMFVWGGY KSNQVRGLYD
     FYLPREELWI YNMETGRWKK INTEGDVPPS MSGSCAVCVD RVLYLFGGHH SRGNTNKFYM
     LDSRSTDRVL QWERIDCQGI PPSSKDKLGV WVYKNKLIFF GGYGYLPEDK VLGTFEFDET
     SFWNSSHPRG WNDHVHILDT ETFTWSQPIT TGKAPSPRAA HACATVGNRG FVFGGRYRDA
     RMNDLHYLNL DTWEWNELIP QGICPVGRSW HSLTPVSSDH LFLFGGFTTD KQPLSDAWTY
     CISKNEWIQF NHPYTEKPRL WHTACASDEG EVIVFGGCAN NLLVHHRAAH SNEILIFSVQ
     PKSLVRLSLE AVICFKEMLA NSWNCLPKHL LHSVNQRFGS NNTSGS
//