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   27-MAR-2024, entry version 177.
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; Q96GD4: AURKB; NbExp=2; IntAct=EBI-1996321, EBI-624291;
CC       Q9P2N7; Q13618: CUL3; NbExp=15; 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   CCDS; CCDS94657.1; -. [Q9P2N7-4]
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.
DR   RefSeq; NP_277030.2; NM_033495.3. [Q9P2N7-1]
DR   RefSeq; XP_011529713.1; XM_011531411.1.
DR   RefSeq; XP_016885439.1; XM_017029950.1.
DR   AlphaFoldDB; Q9P2N7; -.
DR   SMR; Q9P2N7; -.
DR   BioGRID; 124688; 130.
DR   ComplexPortal; CPX-8090; CRL3 E3 ubiquitin ligase complex, KLHL13 variant.
DR   CORUM; Q9P2N7; -.
DR   IntAct; Q9P2N7; 46.
DR   MINT; Q9P2N7; -.
DR   STRING; 9606.ENSP00000419803; -.
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; 9606-ENSP00000443191; -.
DR   PeptideAtlas; 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   Pumba; Q9P2N7; -.
DR   Antibodypedia; 29658; 156 antibodies from 25 providers.
DR   DNASU; 90293; -.
DR   Ensembl; ENST00000262820.7; ENSP00000262820.3; ENSG00000003096.15. [Q9P2N7-1]
DR   Ensembl; ENST00000371878.5; ENSP00000360945.2; ENSG00000003096.15. [Q9P2N7-4]
DR   Ensembl; ENST00000371882.5; ENSP00000360949.2; ENSG00000003096.15. [Q9P2N7-2]
DR   Ensembl; ENST00000469946.5; ENSP00000419803.2; ENSG00000003096.15. [Q9P2N7-5]
DR   Ensembl; ENST00000540167.6; ENSP00000441029.1; ENSG00000003096.15. [Q9P2N7-3]
DR   Ensembl; ENST00000541812.5; ENSP00000444450.1; ENSG00000003096.15. [Q9P2N7-3]
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   AGR; HGNC:22931; -.
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; 5472491at2759; -.
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   SIGNOR; Q9P2N7; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 90293; 8 hits in 793 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 166 other cell types or tissues.
DR   ExpressionAtlas; Q9P2N7; baseline and differential.
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; IBA:GO_Central.
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   CDD; cd18449; BACK_KLHL9_13; 1.
DR   CDD; cd18239; BTB_POZ_KLHL9_13; 1.
DR   Gene3D; 1.25.40.420; -; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 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   PANTHER; PTHR45632:SF7; KELCH-LIKE PROTEIN 13; 1.
DR   PANTHER; PTHR45632; LD33804P; 1.
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; Kelch motif; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   Genevisible; Q9P2N7; HS.
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
//