KCTD1_HUMAN
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 03-AUG-2022, entry version 142.
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: TRAPPC2; NbExp=3; IntAct=EBI-9027502, EBI-5663373;
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 -!- 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.
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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 AlphaFoldDB; Q719H9; -.
DR SMR; Q719H9; -.
DR BioGRID; 129804; 35.
DR IntAct; Q719H9; 22.
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; 107 antibodies from 12 providers.
DR DNASU; 284252; -.
DR Ensembl; ENST00000317932.11; ENSP00000314831.7; ENSG00000134504.14.
DR Ensembl; ENST00000408011.7; ENSP00000384367.3; ENSG00000134504.14.
DR Ensembl; ENST00000417602.5; ENSP00000408405.2; ENSG00000134504.14.
DR Ensembl; ENST00000579973.5; ENSP00000464170.1; ENSG00000134504.14.
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; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000156453; -.
DR InParanoid; Q719H9; -.
DR OMA; YFDIVPM; -.
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 SignaLink; Q719H9; -.
DR BioGRID-ORCS; 284252; 22 hits in 1079 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 oviduct epithelium and 175 other tissues.
DR ExpressionAtlas; Q719H9; baseline and differential.
DR Genevisible; Q719H9; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR Gene3D; 3.30.710.10; -; 1.
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 REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:5BXD"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:5BXD"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5BXD"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:5BXD"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:5BXD"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5BXB"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5BXB"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:5BXB"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5BXD"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:5BXD"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5BXD"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:5BXD"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5BXB"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6S4L"
FT STRAND 141..160
FT /evidence="ECO:0007829|PDB:6S4L"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:6S4L"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6S4L"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6S4L"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:6S4L"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:6S4L"
FT STRAND 226..237
FT /evidence="ECO:0007829|PDB:6S4L"
FT STRAND 246..248
FT /evidence="ECO:0007829|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
