KLH13_HUMAN
ID KLH13_HUMAN Reviewed; 655 AA.
AC Q9P2N7; B3KV78; B3KWM7; B7Z3S9; B7Z5P2; B7Z802; D3DWH6; Q6P2E3; Q96QI7;
AC Q9UDN9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Kelch-like protein 13;
DE AltName: Full=BTB and kelch domain-containing protein 2;
GN Name=KLHL13; Synonyms=BKLHD2, KIAA1309;
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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Howell G.R., Huckle E., Ross M.T.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC TISSUE=Brain, Testis, and Thalamus;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH AURKB; CUL3 AND KLHL9.
RX PubMed=17543862; DOI=10.1016/j.devcel.2007.03.019;
RA Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.;
RT "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
RT regulating mitotic progression and completion of cytokinesis in human
RT cells.";
RL Dev. Cell 12:887-900(2007).
RN [9]
RP FUNCTION.
RX PubMed=19995937; DOI=10.1083/jcb.200906117;
RA Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M.,
RA Sumara I., Peter M.;
RT "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
RT microtubules in anaphase and is required for cytokinesis.";
RL J. Cell Biol. 187:791-800(2009).
RN [10]
RP VARIANT ILE-223.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [11]
RP VARIANT SER-261.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex required for mitotic progression and
CC cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates
CC the ubiquitination of AURKB and controls the dynamic behavior of AURKB
CC on mitotic chromosomes and thereby coordinates faithful mitotic
CC progression and completion of cytokinesis.
CC {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862,
CC ECO:0000269|PubMed:19995937}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase
CC complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1. Interacts
CC with AURKB. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862}.
CC -!- INTERACTION:
CC Q9P2N7; Q13618: CUL3; NbExp=7; IntAct=EBI-1996321, EBI-456129;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9P2N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2N7-2; Sequence=VSP_037530;
CC Name=3;
CC IsoId=Q9P2N7-3; Sequence=VSP_037531;
CC Name=4;
CC IsoId=Q9P2N7-4; Sequence=VSP_037532;
CC Name=5;
CC IsoId=Q9P2N7-5; Sequence=VSP_037533;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC41335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB037730; BAA92547.1; ALT_INIT; mRNA.
DR EMBL; AL591986; CAC41335.1; ALT_INIT; mRNA.
DR EMBL; AK122724; BAG53690.1; -; mRNA.
DR EMBL; AK125356; BAG54189.1; -; mRNA.
DR EMBL; AK296324; BAH12315.1; -; mRNA.
DR EMBL; AK299257; BAH12978.1; -; mRNA.
DR EMBL; AK302713; BAH13788.1; -; mRNA.
DR EMBL; AC006968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006963; AAF03529.1; -; Genomic_DNA.
DR EMBL; CH471161; EAW89898.1; -; Genomic_DNA.
DR EMBL; CH471161; EAW89900.1; -; Genomic_DNA.
DR EMBL; BC064576; AAH64576.2; -; mRNA.
DR CCDS; CCDS14571.1; -. [Q9P2N7-1]
DR CCDS; CCDS55480.1; -. [Q9P2N7-5]
DR CCDS; CCDS55481.1; -. [Q9P2N7-3]
DR RefSeq; NP_001161771.1; NM_001168299.1. [Q9P2N7-5]
DR RefSeq; NP_001161772.1; NM_001168300.1. [Q9P2N7-4]
DR RefSeq; NP_001161773.1; NM_001168301.1. [Q9P2N7-3]
DR RefSeq; NP_001161774.1; NM_001168302.1. [Q9P2N7-3]
DR RefSeq; NP_001161775.1; NM_001168303.1. [Q9P2N7-2]
DR RefSeq; NP_277030.2; NM_033495.3. [Q9P2N7-1]
DR RefSeq; XP_011529713.1; XM_011531411.1. [Q9P2N7-1]
DR RefSeq; XP_016885439.1; XM_017029950.1. [Q9P2N7-3]
DR AlphaFoldDB; Q9P2N7; -.
DR SMR; Q9P2N7; -.
DR BioGRID; 124688; 128.
DR CORUM; Q9P2N7; -.
DR IntAct; Q9P2N7; 36.
DR MINT; Q9P2N7; -.
DR STRING; 9606.ENSP00000443191; -.
DR iPTMnet; Q9P2N7; -.
DR PhosphoSitePlus; Q9P2N7; -.
DR BioMuta; KLHL13; -.
DR DMDM; 239938883; -.
DR EPD; Q9P2N7; -.
DR jPOST; Q9P2N7; -.
DR MassIVE; Q9P2N7; -.
DR MaxQB; Q9P2N7; -.
DR PaxDb; Q9P2N7; -.
DR PeptideAtlas; Q9P2N7; -.
DR PRIDE; Q9P2N7; -.
DR ProteomicsDB; 83867; -. [Q9P2N7-1]
DR ProteomicsDB; 83868; -. [Q9P2N7-2]
DR ProteomicsDB; 83869; -. [Q9P2N7-3]
DR ProteomicsDB; 83870; -. [Q9P2N7-4]
DR ProteomicsDB; 83871; -. [Q9P2N7-5]
DR Antibodypedia; 29658; 141 antibodies from 25 providers.
DR DNASU; 90293; -.
DR Ensembl; ENST00000262820.7; ENSP00000262820.3; ENSG00000003096.14. [Q9P2N7-1]
DR Ensembl; ENST00000469946.5; ENSP00000419803.2; ENSG00000003096.14. [Q9P2N7-5]
DR Ensembl; ENST00000540167.5; ENSP00000441029.1; ENSG00000003096.14. [Q9P2N7-3]
DR Ensembl; ENST00000541812.5; ENSP00000444450.1; ENSG00000003096.14. [Q9P2N7-3]
DR Ensembl; ENST00000545703.5; ENSP00000440707.1; ENSG00000003096.14. [Q9P2N7-2]
DR GeneID; 90293; -.
DR KEGG; hsa:90293; -.
DR MANE-Select; ENST00000540167.6; ENSP00000441029.1; NM_001168302.2; NP_001161774.1. [Q9P2N7-3]
DR UCSC; uc004eqk.4; human. [Q9P2N7-1]
DR CTD; 90293; -.
DR DisGeNET; 90293; -.
DR GeneCards; KLHL13; -.
DR HGNC; HGNC:22931; KLHL13.
DR HPA; ENSG00000003096; Tissue enhanced (endometrium).
DR MIM; 300655; gene.
DR neXtProt; NX_Q9P2N7; -.
DR OpenTargets; ENSG00000003096; -.
DR PharmGKB; PA134959204; -.
DR VEuPathDB; HostDB:ENSG00000003096; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000154359; -.
DR InParanoid; Q9P2N7; -.
DR OMA; XGITHDT; -.
DR OrthoDB; 250404at2759; -.
DR PhylomeDB; Q9P2N7; -.
DR TreeFam; TF328485; -.
DR PathwayCommons; Q9P2N7; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9P2N7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 90293; 8 hits in 715 CRISPR screens.
DR ChiTaRS; KLHL13; human.
DR GenomeRNAi; 90293; -.
DR Pharos; Q9P2N7; Tdark.
DR PRO; PR:Q9P2N7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9P2N7; protein.
DR Bgee; ENSG00000003096; Expressed in smooth muscle tissue and 164 other tissues.
DR ExpressionAtlas; Q9P2N7; baseline and differential.
DR Genevisible; Q9P2N7; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097602; F:cullin family protein binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP: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; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 5.
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 Alternative splicing; Cell cycle; Cell division; Kelch repeat; Mitosis;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..655
FT /note="Kelch-like protein 13"
FT /id="PRO_0000119115"
FT DOMAIN 92..161
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 196..297
FT /note="BACK"
FT REPEAT 341..389
FT /note="Kelch 1"
FT REPEAT 390..441
FT /note="Kelch 2"
FT REPEAT 442..488
FT /note="Kelch 3"
FT REPEAT 490..535
FT /note="Kelch 4"
FT REPEAT 537..587
FT /note="Kelch 5"
FT REPEAT 588..636
FT /note="Kelch 6"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_037530"
FT VAR_SEQ 1..33
FT /note="MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI -> MDHLHRGELVAAILR
FT NR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037531"
FT VAR_SEQ 1..33
FT /note="MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI -> MLRFISHLYCCSSKE
FT DCSEDDKCILSR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037532"
FT VAR_SEQ 1..33
FT /note="MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI -> MMRVQTLREKWAYWR
FT RRQLSLKQADFKDIFKKSTSG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037533"
FT VARIANT 223
FT /note="F -> I (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064725"
FT VARIANT 261
FT /note="T -> S (in dbSNP:rs141912385)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069423"
FT CONFLICT 14
FT /note="K -> R (in Ref. 3; BAG54189)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="L -> P (in Ref. 3; BAG54189)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="Q -> R (in Ref. 3; BAG54189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 73868 MW; 0916420562F0B093 CRC64;
MPLKWKTSSP AIWKFPVPVL KTSRSTPLSP AYISLVEEED QHMKLSLGGS EMGLSSHLQS
SKAGPTRIFT SNTHSSVVLQ GFDQLRLEGL LCDVTLMPGD TDDAFPVHRV MMASASDYFK
AMFTGGMKEQ DLMCIKLHGV SKVGLRKIID FIYTAKLSLN MDNLQDTLEA ASFLQILPVL
DFCKVFLISG VTLDNCVEVG RIANTYNLTE VDKYVNSFVL KNFPALLSTG EFLKLPFERL
AFVLSSNSLK HCTELELFKA TCRWLRLEEP RMDFAAKLMK NIRFPLMTPQ ELINYVQTVD
FMRTDNTCVN LLLEASNYQM MPYMQPVMQS DRTAIRSDTT HLVTLGGVLR QQLVVSKELR
MYDEKAHEWK SLAPMDAPRY QHGIAVIGNF LYVVGGQSNY DTKGKTAVDT VFRFDPRYNK
WMQVASLNEK RTFFHLSALK GYLYAVGGRN AAGELPTVEC YNPRTNEWTY VAKMSEPHYG
HAGTVYGGVM YISGGITHDT FQKELMCFDP DTDKWIQKAP MTTVRGLHCM CTVGERLYVI
GGNHFRGTSD YDDVLSCEYY SPILDQWTPI AAMLRGQSDV GVAVFENKIY VVGGYSWNNR
CMVEIVQKYD PDKDEWHKVF DLPESLGGIR ACTLTVFPPE ETTPSPSRES PLSAP
