KLH22_HUMAN
ID KLH22_HUMAN Reviewed; 634 AA.
AC Q53GT1; A8K3Q4; A8MTV3; B7Z2G1; D3DX30; Q96B68; Q96KC6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Kelch-like protein 22 {ECO:0000305};
GN Name=KLHL22 {ECO:0000312|HGNC:HGNC:25888};
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 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Embryo;
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] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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=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 [7]
RP FUNCTION, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE
RP COMPLEX.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-605, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP INTERACTION WITH PLK1.
RX PubMed=24067371; DOI=10.4161/cc.25369;
RA Metzger T., Kleiss C., Sumara I.;
RT "CUL3 and protein kinases: insights from PLK1/KLHL22 interaction.";
RL Cell Cycle 12:2291-2296(2013).
RN [11]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK1.
RX PubMed=23455478; DOI=10.1038/ncb2695;
RA Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H.,
RA Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.;
RT "Ubiquitylation-dependent localization of PLK1 in mitosis.";
RL Nat. Cell Biol. 15:430-439(2013).
RN [12]
RP FUNCTION, PATHWAY, INTERACTION WITH DEPDC5 AND YWHAE, SUBCELLULAR LOCATION,
RP MISCELLANEOUS, AND MUTAGENESIS OF SER-18.
RX PubMed=29769719; DOI=10.1038/s41586-018-0128-9;
RA Chen J., Ou Y., Yang Y., Li W., Xu Y., Xie Y., Liu Y.;
RT "KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
RT tumorigenesis and ageing.";
RL Nature 557:585-589(2018).
RN [13]
RP VARIANT GLN-20.
RX PubMed=28493397; DOI=10.1002/humu.23246;
RG UK10K;
RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
RA FitzPatrick D.R.;
RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma.";
RL Hum. Mutat. 38:942-946(2017).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex required for chromosome alignment and
CC localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase
CC complex mediates monoubiquitination of PLK1, leading to PLK1
CC dissociation from phosphoreceptor proteins and subsequent removal from
CC kinetochores, allowing silencing of the spindle assembly checkpoint
CC (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not
CC lead to PLK1 degradation (PubMed:19995937, PubMed:23455478). The
CC BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino
CC acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation
CC of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1
CC complex-mediated inhibition of the TORC1 pathway. It is therefore an
CC amino acid-dependent activator within the amino acid-sensing branch of
CC the TORC1 pathway, indirectly regulating different cellular processes
CC including cell growth and autophagy (PubMed:29769719).
CC {ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:23455478,
CC ECO:0000269|PubMed:29769719}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:29769719}.
CC -!- SUBUNIT: Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KLHL22 and RBX1 (PubMed:19995937). Interacts
CC with PLK1 (PubMed:24067371, PubMed:23455478). Interacts with DEPDC5
CC (via DEP domain); the interaction depends on amino acid availability
CC (PubMed:29769719). Interacts with YWHAE; required for the nuclear
CC localization of KLHL22 upon amino acid starvation (PubMed:29769719).
CC {ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:23455478,
CC ECO:0000269|PubMed:24067371, ECO:0000269|PubMed:29769719}.
CC -!- INTERACTION:
CC Q53GT1; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-1996072, EBI-744342;
CC Q53GT1; Q13148: TARDBP; NbExp=3; IntAct=EBI-1996072, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23455478,
CC ECO:0000269|PubMed:29769719}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:23455478}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:23455478}. Nucleus
CC {ECO:0000269|PubMed:29769719}. Lysosome {ECO:0000269|PubMed:29769719}.
CC Note=Mainly cytoplasmic in prophase and prometaphase. Associates with
CC the mitotic spindle as the cells reach chromosome bi-orientation.
CC Localizes to the centrosomes shortly before cells enter anaphase After
CC anaphase onset, predominantly associates with the polar microtubules
CC connecting the 2 opposing centrosomes and gradually diffuses into the
CC cytoplasm during telophase (PubMed:23455478). Localizes to the nucleus
CC upon amino acid starvation (PubMed:29769719). Relocalizes to the
CC cytosol and associates with lysosomes when amino acids are available
CC (PubMed:29769719). {ECO:0000269|PubMed:23455478,
CC ECO:0000269|PubMed:29769719}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53GT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53GT1-3; Sequence=VSP_057028;
CC -!- DISEASE: Note=Defects in KLHL22 has been found in a patient with
CC isolated coloboma, a defect of the eye characterized by the absence of
CC ocular structures due to abnormal morphogenesis of the optic cup and
CC stalk, and the fusion of the fetal fissure (optic fissure). Isolated
CC colobomas may be associated with an abnormally small eye
CC (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}.
CC -!- MISCELLANEOUS: Potential oncogene that is up-regulated in breast cancer
CC cells and promotes tumor growth. {ECO:0000269|PubMed:29769719}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55007.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; CR456352; CAG30238.1; -; mRNA.
DR EMBL; AK027266; BAB55007.1; ALT_SEQ; mRNA.
DR EMBL; AK290669; BAF83358.1; -; mRNA.
DR EMBL; AK294682; BAH11847.1; -; mRNA.
DR EMBL; AK222850; BAD96570.1; -; mRNA.
DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471176; EAX02961.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02962.1; -; Genomic_DNA.
DR EMBL; CH471176; EAX02963.1; -; Genomic_DNA.
DR EMBL; BC015923; AAH15923.1; -; mRNA.
DR CCDS; CCDS13780.1; -. [Q53GT1-1]
DR RefSeq; NP_116164.2; NM_032775.3. [Q53GT1-1]
DR RefSeq; XP_016884510.1; XM_017029021.1. [Q53GT1-1]
DR AlphaFoldDB; Q53GT1; -.
DR SMR; Q53GT1; -.
DR BioGRID; 124308; 163.
DR IntAct; Q53GT1; 53.
DR MINT; Q53GT1; -.
DR STRING; 9606.ENSP00000331682; -.
DR iPTMnet; Q53GT1; -.
DR PhosphoSitePlus; Q53GT1; -.
DR BioMuta; KLHL22; -.
DR DMDM; 109892504; -.
DR EPD; Q53GT1; -.
DR jPOST; Q53GT1; -.
DR MassIVE; Q53GT1; -.
DR MaxQB; Q53GT1; -.
DR PaxDb; Q53GT1; -.
DR PeptideAtlas; Q53GT1; -.
DR PRIDE; Q53GT1; -.
DR ProteomicsDB; 62490; -. [Q53GT1-1]
DR Antibodypedia; 34893; 188 antibodies from 28 providers.
DR DNASU; 84861; -.
DR Ensembl; ENST00000328879.9; ENSP00000331682.4; ENSG00000099910.17. [Q53GT1-1]
DR GeneID; 84861; -.
DR KEGG; hsa:84861; -.
DR MANE-Select; ENST00000328879.9; ENSP00000331682.4; NM_032775.4; NP_116164.2.
DR UCSC; uc002zsl.2; human. [Q53GT1-1]
DR CTD; 84861; -.
DR DisGeNET; 84861; -.
DR GeneCards; KLHL22; -.
DR HGNC; HGNC:25888; KLHL22.
DR HPA; ENSG00000099910; Low tissue specificity.
DR MIM; 618020; gene.
DR neXtProt; NX_Q53GT1; -.
DR OpenTargets; ENSG00000099910; -.
DR PharmGKB; PA142671574; -.
DR VEuPathDB; HostDB:ENSG00000099910; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000159598; -.
DR HOGENOM; CLU_004253_14_3_1; -.
DR InParanoid; Q53GT1; -.
DR OMA; ERDCWEE; -.
DR OrthoDB; 250404at2759; -.
DR PhylomeDB; Q53GT1; -.
DR TreeFam; TF328485; -.
DR PathwayCommons; Q53GT1; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q53GT1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84861; 26 hits in 1121 CRISPR screens.
DR ChiTaRS; KLHL22; human.
DR GenomeRNAi; 84861; -.
DR Pharos; Q53GT1; Tbio.
DR PRO; PR:Q53GT1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q53GT1; protein.
DR Bgee; ENSG00000099910; Expressed in right hemisphere of cerebellum and 166 other tissues.
DR ExpressionAtlas; Q53GT1; baseline and differential.
DR Genevisible; Q53GT1; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005827; C:polar microtubule; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0071233; P:cellular response to leucine; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA: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; IPR030575; KLHL22.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR45632:SF5; PTHR45632:SF5; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 2.
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 Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Disease variant; Kelch repeat; Lysosome; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..634
FT /note="Kelch-like protein 22"
FT /id="PRO_0000242155"
FT DOMAIN 50..117
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 299..349
FT /note="Kelch 1"
FT REPEAT 350..399
FT /note="Kelch 2"
FT REPEAT 400..446
FT /note="Kelch 3"
FT REPEAT 448..493
FT /note="Kelch 4"
FT REPEAT 494..544
FT /note="Kelch 5"
FT REPEAT 545..593
FT /note="Kelch 6"
FT REGION 600..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZC3"
FT MOD_RES 466
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZC3"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZC3"
FT MOD_RES 605
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057028"
FT VARIANT 20
FT /note="P -> Q (found in a patient with isolated coloboma;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28493397"
FT /id="VAR_079854"
FT MUTAGEN 18
FT /note="S->A: Loss of interaction with YWHAE. Loss of
FT nuclear localization upon amino acid starvation."
FT /evidence="ECO:0000269|PubMed:29769719"
FT CONFLICT 352
FT /note="Y -> H (in Ref. 3; BAD96570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 71667 MW; 63A7AF7AAE0F56D7 CRC64;
MAEEQEFTQL CKLPAQPSHP HCVNNTYRSA QHSQALLRGL LALRDSGILF DVVLVVEGRH
IEAHRILLAA SCDYFRGMFA GGLKEMEQEE VLIHGVSYNA MCQILHFIYT SELELSLSNV
QETLVAACQL QIPEIIHFCC DFLMSWVDEE NILDVYRLAE LFDLSRLTEQ LDTYILKNFV
AFSRTDKYRQ LPLEKVYSLL SSNRLEVSCE TEVYEGALLY HYSLEQVQAD QISLHEPPKL
LETVRFPLME AEVLQRLHDK LDPSPLRDTV ASALMYHRNE SLQPSLQSPQ TELRSDFQCV
VGFGGIHSTP STVLSDQAKY LNPLLGEWKH FTASLAPRMS NQGIAVLNNF VYLIGGDNNV
QGFRAESRCW RYDPRHNRWF QIQSLQQEHA DLSVCVVGRY IYAVAGRDYH NDLNAVERYD
PATNSWAYVA PLKREVYAHA GATLEGKMYI TCGRRGEDYL KETHCYDPGS NTWHTLADGP
VRRAWHGMAT LLNKLYVIGG SNNDAGYRRD VHQVACYSCT SGQWSSVCPL PAGHGEPGIA
VLDNRIYVLG GRSHNRGSRT GYVHIYDVEK DCWEEGPQLD NSISGLAACV LTLPRSLLLE
PPRGTPDRSQ ADPDFASEVM SVSDWEEFDN SSED
