KCD15_HUMAN
ID KCD15_HUMAN Reviewed; 283 AA.
AC Q96SI1; A8K600; Q9BVI6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=BTB/POZ domain-containing protein KCTD15;
DE AltName: Full=Potassium channel tetramerization domain-containing protein 15;
GN Name=KCTD15;
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).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-64.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND SER-38, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, AND INTERACTION WITH TFAP2A.
RX PubMed=23382213; DOI=10.1073/pnas.1300203110;
RA Zarelli V.E., Dawid I.B.;
RT "Inhibition of neural crest formation by Kctd15 involves regulation of
RT transcription factor AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2870-2875(2013).
CC -!- FUNCTION: During embryonic development, interferes with neural crest
CC formation (By similarity). Inhibits AP2 transcriptional activity by
CC interaction with its activation domain. {ECO:0000250,
CC ECO:0000269|PubMed:23382213}.
CC -!- SUBUNIT: Interacts with TFAP2A; this interaction inhibits TFAP2A
CC transcriptional activation. {ECO:0000269|PubMed:23382213}.
CC -!- INTERACTION:
CC Q96SI1; Q719H9: KCTD1; NbExp=3; IntAct=EBI-715783, EBI-9027502;
CC Q96SI1; Q96SI1: KCTD15; NbExp=2; IntAct=EBI-715783, EBI-715783;
CC Q96SI1; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-715783, EBI-945833;
CC Q96SI1-2; Q92870-2: APBB2; NbExp=3; IntAct=EBI-12382297, EBI-21535880;
CC Q96SI1-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12382297, EBI-930964;
CC Q96SI1-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12382297, EBI-3867333;
CC Q96SI1-2; P04792: HSPB1; NbExp=3; IntAct=EBI-12382297, EBI-352682;
CC Q96SI1-2; P42858: HTT; NbExp=6; IntAct=EBI-12382297, EBI-466029;
CC Q96SI1-2; Q719H9: KCTD1; NbExp=6; IntAct=EBI-12382297, EBI-9027502;
CC Q96SI1-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12382297, EBI-10975473;
CC Q96SI1-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12382297, EBI-22310682;
CC Q96SI1-2; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-12382297, EBI-12025760;
CC Q96SI1-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12382297, EBI-741158;
CC Q96SI1-2; Q7Z412: PEX26; NbExp=3; IntAct=EBI-12382297, EBI-752057;
CC Q96SI1-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-12382297, EBI-25882629;
CC Q96SI1-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12382297, EBI-749195;
CC Q96SI1-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-12382297, EBI-372899;
CC Q96SI1-2; P02766: TTR; NbExp=3; IntAct=EBI-12382297, EBI-711909;
CC Q96SI1-2; O76024: WFS1; NbExp=3; IntAct=EBI-12382297, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8K0E1}. Note=In
CC the brain, localizes to the arcuate hypothalamic nucleus, the
CC ventromedial hypothalamic nucleus and the accumbens nucleus of the
CC ventral striatum. {ECO:0000250|UniProtKB:Q8K0E1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96SI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SI1-2; Sequence=VSP_019958, VSP_019959;
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DR EMBL; AK027901; BAB55443.1; -; mRNA.
DR EMBL; AK291465; BAF84154.1; -; mRNA.
DR EMBL; BC001185; AAH01185.1; -; mRNA.
DR EMBL; BC009335; AAH09335.1; -; mRNA.
DR CCDS; CCDS12434.1; -. [Q96SI1-2]
DR CCDS; CCDS46039.1; -. [Q96SI1-1]
DR RefSeq; NP_001123466.1; NM_001129994.1. [Q96SI1-1]
DR RefSeq; NP_001123467.1; NM_001129995.1. [Q96SI1-1]
DR RefSeq; NP_076981.2; NM_024076.2. [Q96SI1-2]
DR RefSeq; XP_011525598.1; XM_011527296.1. [Q96SI1-1]
DR RefSeq; XP_011525599.1; XM_011527297.2. [Q96SI1-1]
DR RefSeq; XP_011525600.1; XM_011527298.2. [Q96SI1-1]
DR RefSeq; XP_016882772.1; XM_017027283.1. [Q96SI1-1]
DR AlphaFoldDB; Q96SI1; -.
DR SMR; Q96SI1; -.
DR BioGRID; 122506; 60.
DR IntAct; Q96SI1; 32.
DR MINT; Q96SI1; -.
DR STRING; 9606.ENSP00000394390; -.
DR iPTMnet; Q96SI1; -.
DR PhosphoSitePlus; Q96SI1; -.
DR BioMuta; KCTD15; -.
DR DMDM; 74732704; -.
DR EPD; Q96SI1; -.
DR jPOST; Q96SI1; -.
DR MassIVE; Q96SI1; -.
DR MaxQB; Q96SI1; -.
DR PaxDb; Q96SI1; -.
DR PeptideAtlas; Q96SI1; -.
DR PRIDE; Q96SI1; -.
DR ProteomicsDB; 78113; -. [Q96SI1-1]
DR ProteomicsDB; 78114; -. [Q96SI1-2]
DR Antibodypedia; 29083; 256 antibodies from 29 providers.
DR DNASU; 79047; -.
DR Ensembl; ENST00000284006.10; ENSP00000284006.4; ENSG00000153885.15. [Q96SI1-2]
DR Ensembl; ENST00000430256.3; ENSP00000394390.1; ENSG00000153885.15. [Q96SI1-1]
DR Ensembl; ENST00000588881.5; ENSP00000464812.1; ENSG00000153885.15. [Q96SI1-1]
DR Ensembl; ENST00000589786.5; ENSP00000467612.1; ENSG00000153885.15. [Q96SI1-1]
DR Ensembl; ENST00000683859.1; ENSP00000508199.1; ENSG00000153885.15. [Q96SI1-1]
DR GeneID; 79047; -.
DR KEGG; hsa:79047; -.
DR MANE-Select; ENST00000683859.1; ENSP00000508199.1; NM_001129994.2; NP_001123466.1.
DR UCSC; uc002nuv.4; human. [Q96SI1-1]
DR CTD; 79047; -.
DR DisGeNET; 79047; -.
DR GeneCards; KCTD15; -.
DR HGNC; HGNC:23297; KCTD15.
DR HPA; ENSG00000153885; Low tissue specificity.
DR MIM; 615240; gene.
DR neXtProt; NX_Q96SI1; -.
DR OpenTargets; ENSG00000153885; -.
DR PharmGKB; PA134916319; -.
DR VEuPathDB; HostDB:ENSG00000153885; -.
DR eggNOG; KOG2723; Eukaryota.
DR GeneTree; ENSGT00940000159496; -.
DR HOGENOM; CLU_061268_1_0_1; -.
DR InParanoid; Q96SI1; -.
DR OMA; CREDRRM; -.
DR OrthoDB; 971350at2759; -.
DR PhylomeDB; Q96SI1; -.
DR PathwayCommons; Q96SI1; -.
DR Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR SignaLink; Q96SI1; -.
DR BioGRID-ORCS; 79047; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; KCTD15; human.
DR GeneWiki; KCTD15; -.
DR GenomeRNAi; 79047; -.
DR Pharos; Q96SI1; Tbio.
DR PRO; PR:Q96SI1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96SI1; protein.
DR Bgee; ENSG00000153885; Expressed in ventricular zone and 179 other tissues.
DR ExpressionAtlas; Q96SI1; baseline and differential.
DR Genevisible; Q96SI1; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR CDD; cd18388; BTB_POZ_KCTD15; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR045904; KCTD15_T1-type_BTB.
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 Alternative splicing; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..283
FT /note="BTB/POZ domain-containing protein KCTD15"
FT /id="PRO_0000247251"
FT DOMAIN 56..126
FT /note="BTB"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 232..234
FT /note="VLE -> DVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019958"
FT VAR_SEQ 235..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019959"
FT VARIANT 64
FT /note="G -> S (in dbSNP:rs17849437)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027090"
SQ SEQUENCE 283 AA; 31942 MW; 29E2ED079DB4E5CC CRC64;
MPHRKERPSG SSLHTHGSTG TAEGGNMSRL SLTRSPVSPL AAQGIPLPAQ LTKSNAPVHI
DVGGHMYTSS LATLTKYPDS RISRLFNGTE PIVLDSLKQH YFIDRDGEIF RYVLSFLRTS
KLLLPDDFKD FSLLYEEARY YQLQPMVREL ERWQQEQEQR RRSRACDCLV VRVTPDLGER
IALSGEKALI EEVFPETGDV MCNSVNAGWN QDPTHVIRFP LNGYCRLNSV QVLERLFQRG
FSVAASCGGG VDSSQFSEYV LCREERRPQP TPTAVRIKQE PLD
