ID KCTD1_HUMAN Reviewed; 257 AA. AC Q719H9; A8K1F5; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-FEB-2021, entry version 136. DE RecName: Full=BTB/POZ domain-containing protein KCTD1; DE AltName: Full=Potassium channel tetramerization domain-containing protein 1; GN Name=KCTD1; Synonyms=C18orf5; 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]. RA Zhang D.L., Cai J.J., Ma D.L.; RT "Cloning and characterization of a novel human gene, potassium channel RT tetramerization domain containing 1 (KCTD1)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Caudate nucleus; 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]. RC TISSUE=Skin; 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 [4] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [5] RP FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=18358072; DOI=10.1089/dna.2007.0662; RA Ding X.F., Luo C., Ren K.Q., Zhang J., Zhou J.L., Hu X., Liu R.S., Wang Y., RA Gao X., Zhang J.; RT "Characterization and expression of a human KCTD1 gene containing the BTB RT domain, which mediates transcriptional repression and homomeric RT interactions."; RL DNA Cell Biol. 27:257-265(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-12, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP FUNCTION, AND INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C. RX PubMed=19115315; DOI=10.1002/jcb.22002; RA Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A., RA Zhu J., Gao X., Zhang J.; RT "The interaction of KCTD1 with transcription factor AP-2alpha inhibits its RT transactivation."; RL J. Cell. Biochem. 106:285-295(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [9] RP VARIANTS SENS GLU-30; ARG-31; LEU-31; SER-31; GLN-33; PRO-33; ASP-62 AND RP PRO-74. RX PubMed=23541344; DOI=10.1016/j.ajhg.2013.03.002; RA Marneros A.G., Beck A.E., Turner E.H., McMillin M.J., Edwards M.J., RA Field M., de Macena Sobreira N.L., Perez A.B., Fortes J.A., Lampe A.K., RA Giovannucci Uzielli M.L., Gordon C.T., Plessis G., Le Merrer M., Amiel J., RA Reichenberger E., Shively K.M., Cerrato F., Labow B.I., Tabor H.K., RA Smith J.D., Shendure J., Nickerson D.A., Bamshad M.J.; RT "Mutations in KCTD1 cause scalp-ear-nipple syndrome."; RL Am. J. Hum. Genet. 92:621-626(2013). CC -!- FUNCTION: May repress the transcriptional activity of AP-2 family CC members, including TFAP2A, TFAP2B and TFAP2C to various extent. CC {ECO:0000269|PubMed:18358072, ECO:0000269|PubMed:19115315}. CC -!- SUBUNIT: Can form homodimers. Interacts with TFAP2A, TFAP2B and TFAP2C CC via the BTB domain. {ECO:0000269|PubMed:19115315}. CC -!- INTERACTION: CC Q719H9; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-9027502, EBI-6255981; CC Q719H9; Q9Y3B2: EXOSC1; NbExp=6; IntAct=EBI-9027502, EBI-371892; CC Q719H9; Q719H9: KCTD1; NbExp=6; IntAct=EBI-9027502, EBI-9027502; CC Q719H9; Q96SI1: KCTD15; NbExp=3; IntAct=EBI-9027502, EBI-715783; CC Q719H9; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-9027502, EBI-12382297; CC Q719H9; P25800: LMO1; NbExp=3; IntAct=EBI-9027502, EBI-8639312; CC Q719H9; Q8TAP4: LMO3; NbExp=3; IntAct=EBI-9027502, EBI-742259; CC Q719H9; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-9027502, EBI-11742507; CC Q719H9; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-9027502, EBI-739832; CC Q719H9; Q15014: MORF4L2; NbExp=3; IntAct=EBI-9027502, EBI-399257; CC Q719H9; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-9027502, EBI-741158; CC Q719H9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-9027502, EBI-79165; CC Q719H9; O15160: POLR1C; NbExp=6; IntAct=EBI-9027502, EBI-1055079; CC Q719H9; P54646: PRKAA2; NbExp=3; IntAct=EBI-9027502, EBI-1383852; CC Q719H9; P25786: PSMA1; NbExp=3; IntAct=EBI-9027502, EBI-359352; CC Q719H9; O00560: SDCBP; NbExp=6; IntAct=EBI-9027502, EBI-727004; CC Q719H9; Q96PF1: TGM7; NbExp=3; IntAct=EBI-9027502, EBI-12029034; CC Q719H9; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-9027502, EBI-11961968; CC Q719H9; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-9027502, EBI-7353612; CC Q719H9; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-9027502, EBI-10180829; CC Q719H9; P24278: ZBTB25; NbExp=3; IntAct=EBI-9027502, EBI-739899; CC Q719H9; P0DI81; NbExp=3; IntAct=EBI-9027502, EBI-5663373; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18358072}. CC -!- TISSUE SPECIFICITY: Expressed in mammary gland, kidney, brain and CC ovary. {ECO:0000269|PubMed:18358072}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. CC -!- DISEASE: Scalp-ear-nipple syndrome (SENS) [MIM:181270]: A disease CC characterized by aplasia cutis congenita of the scalp, breast anomalies CC that range from hypothelia or athelia to amastia, and minor anomalies CC of the external ears. Less frequent clinical characteristics include CC nail dystrophy, dental anomalies, cutaneous syndactyly of the digits, CC and renal malformations. Penetrance appears to be high, although there CC is substantial variable expressivity within families. CC {ECO:0000269|PubMed:23541344}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF542549; AAQ09532.1; -; mRNA. DR EMBL; AK289870; BAF82559.1; -; mRNA. DR EMBL; BC063652; AAH63652.1; -; mRNA. DR CCDS; CCDS11888.1; -. DR RefSeq; NP_001129677.1; NM_001136205.2. DR RefSeq; NP_001136202.1; NM_001142730.2. DR RefSeq; NP_001245150.1; NM_001258221.1. DR RefSeq; NP_945342.1; NM_198991.3. DR RefSeq; XP_016881197.1; XM_017025708.1. DR PDB; 5BXB; X-ray; 2.17 A; A/B/C/D/E/F/G/H/I/J=29-132. DR PDB; 5BXD; X-ray; 1.80 A; A/B/C/D/E=29-132. DR PDB; 6S4L; X-ray; 2.42 A; A/B/C/D/E=28-257. DR PDBsum; 5BXB; -. DR PDBsum; 5BXD; -. DR PDBsum; 6S4L; -. DR SMR; Q719H9; -. DR BioGRID; 129804; 29. DR IntAct; Q719H9; 21. DR MINT; Q719H9; -. DR STRING; 9606.ENSP00000384367; -. DR iPTMnet; Q719H9; -. DR PhosphoSitePlus; Q719H9; -. DR BioMuta; KCTD1; -. DR DMDM; 74738338; -. DR EPD; Q719H9; -. DR jPOST; Q719H9; -. DR MassIVE; Q719H9; -. DR MaxQB; Q719H9; -. DR PaxDb; Q719H9; -. DR PeptideAtlas; Q719H9; -. DR PRIDE; Q719H9; -. DR ProteomicsDB; 68593; -. DR Antibodypedia; 54340; 102 antibodies. DR DNASU; 284252; -. DR Ensembl; ENST00000317932; ENSP00000314831; ENSG00000134504. DR Ensembl; ENST00000408011; ENSP00000384367; ENSG00000134504. DR Ensembl; ENST00000417602; ENSP00000408405; ENSG00000134504. DR Ensembl; ENST00000579973; ENSP00000464170; ENSG00000134504. DR GeneID; 284252; -. DR KEGG; hsa:284252; -. DR UCSC; uc002kvw.6; human. DR CTD; 284252; -. DR DisGeNET; 284252; -. DR GeneCards; KCTD1; -. DR HGNC; HGNC:18249; KCTD1. DR HPA; ENSG00000134504; Low tissue specificity. DR MalaCards; KCTD1; -. DR MIM; 181270; phenotype. DR MIM; 613420; gene. DR neXtProt; NX_Q719H9; -. DR OpenTargets; ENSG00000134504; -. DR Orphanet; 2036; Scalp-ear-nipple syndrome. DR PharmGKB; PA30082; -. DR VEuPathDB; HostDB:ENSG00000134504.12; -. DR eggNOG; KOG2723; Eukaryota. DR GeneTree; ENSGT00940000156453; -. DR InParanoid; Q719H9; -. DR OrthoDB; 626946at2759; -. DR PhylomeDB; Q719H9; -. DR PathwayCommons; Q719H9; -. DR Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors. DR BioGRID-ORCS; 284252; 5 hits in 877 CRISPR screens. DR ChiTaRS; KCTD1; human. DR GenomeRNAi; 284252; -. DR Pharos; Q719H9; Tbio. DR PRO; PR:Q719H9; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q719H9; protein. DR Bgee; ENSG00000134504; Expressed in vagina and 210 other tissues. DR ExpressionAtlas; Q719H9; baseline and differential. DR Genevisible; Q719H9; HS. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0045171; C:intercellular bridge; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR003131; T1-type_BTB. DR Pfam; PF02214; BTB_2; 1. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; SSF54695; 1. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..257 FT /note="BTB/POZ domain-containing protein KCTD1" FT /id="PRO_0000247144" FT DOMAIN 30..100 FT /note="BTB" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT VARIANT 30 FT /note="A -> E (in SENS; dbSNP:rs587776998)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069971" FT VARIANT 31 FT /note="P -> L (in SENS; dbSNP:rs587776999)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069972" FT VARIANT 31 FT /note="P -> R (in SENS; dbSNP:rs587776999)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069973" FT VARIANT 31 FT /note="P -> S (in SENS)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069974" FT VARIANT 33 FT /note="H -> P (in SENS; dbSNP:rs587777001)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069975" FT VARIANT 33 FT /note="H -> Q (in SENS; dbSNP:rs587777000)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069976" FT VARIANT 62 FT /note="G -> D (in SENS; dbSNP:rs587777003)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069977" FT VARIANT 74 FT /note="H -> P (in SENS; dbSNP:rs587777002)" FT /evidence="ECO:0000269|PubMed:23541344" FT /id="VAR_069978" FT VARIANT 107 FT /note="L -> W (in dbSNP:rs491684)" FT /id="VAR_049722" FT CONFLICT 141 FT /note="E -> K (in Ref. 2; BAF82559)" FT /evidence="ECO:0000305" FT STRAND 33..35 FT /evidence="ECO:0000244|PDB:5BXD" FT STRAND 37..39 FT /evidence="ECO:0000244|PDB:5BXD" FT STRAND 41..43 FT /evidence="ECO:0000244|PDB:5BXD" FT HELIX 45..48 FT /evidence="ECO:0000244|PDB:5BXD" FT HELIX 55..60 FT /evidence="ECO:0000244|PDB:5BXD" FT STRAND 61..64 FT /evidence="ECO:0000244|PDB:5BXB" FT STRAND 67..69 FT /evidence="ECO:0000244|PDB:5BXB" FT TURN 70..73 FT /evidence="ECO:0000244|PDB:5BXB" FT STRAND 74..76 FT /evidence="ECO:0000244|PDB:5BXD" FT HELIX 81..93 FT /evidence="ECO:0000244|PDB:5BXD" FT HELIX 105..114 FT /evidence="ECO:0000244|PDB:5BXD" FT HELIX 118..124 FT /evidence="ECO:0000244|PDB:5BXD" FT TURN 129..131 FT /evidence="ECO:0000244|PDB:5BXB" FT TURN 134..136 FT /evidence="ECO:0000244|PDB:6S4L" FT STRAND 141..160 FT /evidence="ECO:0000244|PDB:6S4L" FT HELIX 161..167 FT /evidence="ECO:0000244|PDB:6S4L" FT STRAND 189..194 FT /evidence="ECO:0000244|PDB:6S4L" FT HELIX 195..198 FT /evidence="ECO:0000244|PDB:6S4L" FT HELIX 203..212 FT /evidence="ECO:0000244|PDB:6S4L" FT STRAND 216..224 FT /evidence="ECO:0000244|PDB:6S4L" FT STRAND 226..237 FT /evidence="ECO:0000244|PDB:6S4L" FT STRAND 246..248 FT /evidence="ECO:0000244|PDB:6S4L" SQ SEQUENCE 257 AA; 29405 MW; 0513F3483A3C13A6 CRC64; MSRPLITRSP ASPLNNQGIP TPAQLTKSNA PVHIDVGGHM YTSSLATLTK YPESRIGRLF DGTEPIVLDS LKQHYFIDRD GQMFRYILNF LRTSKLLIPD DFKDYTLLYE EAKYFQLQPM LLEMERWKQD RETGRFSRPC ECLVVRVAPD LGERITLSGD KSLIEEVFPE IGDVMCNSVN AGWNHDSTHV IRFPLNGYCH LNSVQVLERL QQRGFEIVGS CGGGVDSSQF SEYVLRRELR RTPRVPSVIR IKQEPLD //