ID KCTD6_MOUSE Reviewed; 237 AA.
AC Q8BNL5; Q3TXX1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=BTB/POZ domain-containing protein KCTD6;
GN Name=Kctd6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=21472142; DOI=10.1593/neo.101630;
RA De Smaele E., Di Marcotullio L., Moretti M., Pelloni M., Occhione M.A.,
RA Infante P., Cucchi D., Greco A., Pietrosanti L., Todorovic J., Coni S.,
RA Canettieri G., Ferretti E., Bei R., Maroder M., Screpanti I., Gulino A.;
RT "Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3
RT adaptors suppressing histone deacetylase and Hedgehog activity in
RT medulloblastoma.";
RL Neoplasia 13:374-385(2011).
CC -!- FUNCTION: Probable substrate-specific adapter of a BCR (BTB-CUL3-RBX1)
CC E3 ubiquitin-protein ligase complex mediating the ubiquitination and
CC subsequent proteasomal degradation of target proteins. Promotes the
CC ubiquitination of HDAC1; the function seems to depend on KCTD11:KCTD6
CC oligomerization. Can function as antagonist of the Hedgehog pathway by
CC affecting the nuclear transfer of transcription factor GLI1; the
CC function probably occurs via HDAC1 down-regulation, keeping GLI1
CC acetylated and inactive. Inhibits cell growth and tumorigenicity of
CC medulloblastoma (MDB). Involved in regulating protein levels of ANK1
CC isoform Mu7 probably implicating CUL3-dependent proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q8NC69}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homopentamer. Interacts with KCTD11; KCTD6 and KCTD11 may
CC associate in heteropentameric assemblies. Interacts (via BTB domain)
CC with CUL3; initially a 4:4 stoichiometry has been reported, however,
CC electron microscopy revealed pentameric states with a five-pointed
CC pinwheel shape. The interaction with CUL3 is indicative for a
CC participation in a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase
CC complex. Interacts with HDAC1; probably indirect as the interaction
CC requires the presence of KCTD11. Interacts with USP21 (preferentially
CC catalytic inactive form). Interacts with ANK1 isoform Mu7; detected in
CC striated muscle. Interacts with USP11 (By similarity).
CC {ECO:0000250|UniProtKB:Q8NC69}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:Q8NC69}. Note=Colocalizes with ANK1 isoform Mu7
CC at the M line in differentiated skeletal muscle cells and heart.
CC {ECO:0000250|UniProtKB:Q8NC69}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum and brain.
CC {ECO:0000269|PubMed:21472142}.
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DR EMBL; AK082924; BAC38692.1; -; mRNA.
DR EMBL; AK159067; BAE34793.1; -; mRNA.
DR EMBL; BC096370; AAH96370.1; -; mRNA.
DR CCDS; CCDS26812.1; -.
DR RefSeq; NP_001292865.1; NM_001305936.1.
DR RefSeq; NP_001292866.1; NM_001305937.1.
DR RefSeq; NP_082058.1; NM_027782.3.
DR RefSeq; XP_006518168.1; XM_006518105.3.
DR AlphaFoldDB; Q8BNL5; -.
DR SMR; Q8BNL5; -.
DR IntAct; Q8BNL5; 1.
DR STRING; 10090.ENSMUSP00000129059; -.
DR PhosphoSitePlus; Q8BNL5; -.
DR MaxQB; Q8BNL5; -.
DR PaxDb; 10090-ENSMUSP00000129059; -.
DR ProteomicsDB; 263512; -.
DR Antibodypedia; 15221; 156 antibodies from 21 providers.
DR DNASU; 71393; -.
DR Ensembl; ENSMUST00000022272.14; ENSMUSP00000022272.7; ENSMUSG00000021752.15.
DR Ensembl; ENSMUST00000170111.3; ENSMUSP00000129059.2; ENSMUSG00000021752.15.
DR GeneID; 71393; -.
DR KEGG; mmu:71393; -.
DR UCSC; uc007sex.2; mouse.
DR AGR; MGI:1918643; -.
DR CTD; 200845; -.
DR MGI; MGI:1918643; Kctd6.
DR VEuPathDB; HostDB:ENSMUSG00000021752; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000157869; -.
DR HOGENOM; CLU_070345_1_0_1; -.
DR InParanoid; Q8BNL5; -.
DR OMA; WGYIMTE; -.
DR OrthoDB; 2912088at2759; -.
DR PhylomeDB; Q8BNL5; -.
DR TreeFam; TF315332; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71393; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Kctd6; mouse.
DR PRO; PR:Q8BNL5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BNL5; Protein.
DR Bgee; ENSMUSG00000021752; Expressed in otolith organ and 228 other cell types or tissues.
DR ExpressionAtlas; Q8BNL5; baseline and differential.
DR Genevisible; Q8BNL5; MM.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR14499:SF10; BTB_POZ DOMAIN-CONTAINING PROTEIN KCTD6; 1.
DR PANTHER; PTHR14499; POTASSIUM CHANNEL TETRAMERIZATION DOMAIN-CONTAINING; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Growth regulation; Reference proteome; Tumor suppressor;
KW Ubl conjugation pathway.
FT CHAIN 1..237
FT /note="BTB/POZ domain-containing protein KCTD6"
FT /id="PRO_0000251249"
FT DOMAIN 12..81
FT /note="BTB"
FT REGION 1..104
FT /note="Interaction with ANK1 isoform Mu7"
FT /evidence="ECO:0000250|UniProtKB:Q8NC69"
FT REGION 10..110
FT /note="Interaction with CUL3"
FT /evidence="ECO:0000250|UniProtKB:Q8NC69"
FT REGION 113..187
FT /note="Interaction with USP21"
FT /evidence="ECO:0000250|UniProtKB:Q8NC69"
FT CONFLICT 233
FT /note="R -> S (in Ref. 1; BAE34793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 27624 MW; 83B641919B0F4D9E CRC64;
MDNGDWGYMM SDPVTLNVGG HLYTTSLTTL TRYPDSMLGA MFGGDFPTAR DPQGNYFIDR
DGPLFRYVLN FLRTSELTLP LDFKEFDLLR KEADFYQIEP LIQCLNDPRP LYPMDTFEEV
VELSSTRKLS KYSNPVAVII TQLTITTKVH SLLEGISNYF TKWNKHMMDT RDCQVSFTFG
PCDYHQEVSL RVHLMEYITK QGFTIRNTRV HHMSERANEN TVEHNWTFCR LARKTDD
//
