KCTD2_HUMAN
ID KCTD2_HUMAN Reviewed; 263 AA.
AC Q14681;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=BTB/POZ domain-containing protein KCTD2;
DE AltName: Full=Potassium channel tetramerization domain-containing protein 2;
GN Name=KCTD2; Synonyms=KIAA0176;
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].
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-29; 76-87; 124-136; 145-165; 189-209 AND 237-252,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11493.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; D79998; BAA11493.1; ALT_INIT; mRNA.
DR EMBL; AC087651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32728.1; -.
DR RefSeq; NP_056168.1; NM_015353.2.
DR AlphaFoldDB; Q14681; -.
DR SMR; Q14681; -.
DR BioGRID; 117057; 46.
DR IntAct; Q14681; 22.
DR STRING; 9606.ENSP00000312814; -.
DR iPTMnet; Q14681; -.
DR PhosphoSitePlus; Q14681; -.
DR BioMuta; KCTD2; -.
DR DMDM; 296439316; -.
DR EPD; Q14681; -.
DR jPOST; Q14681; -.
DR MassIVE; Q14681; -.
DR MaxQB; Q14681; -.
DR PaxDb; Q14681; -.
DR PeptideAtlas; Q14681; -.
DR PRIDE; Q14681; -.
DR ProteomicsDB; 60116; -.
DR Antibodypedia; 64770; 65 antibodies from 11 providers.
DR DNASU; 23510; -.
DR Ensembl; ENST00000322444.7; ENSP00000312814.6; ENSG00000180901.11.
DR GeneID; 23510; -.
DR KEGG; hsa:23510; -.
DR MANE-Select; ENST00000322444.7; ENSP00000312814.6; NM_015353.3; NP_056168.1.
DR UCSC; uc002jmp.4; human.
DR CTD; 23510; -.
DR DisGeNET; 23510; -.
DR GeneCards; KCTD2; -.
DR HGNC; HGNC:21294; KCTD2.
DR HPA; ENSG00000180901; Tissue enriched (brain).
DR MIM; 613422; gene.
DR neXtProt; NX_Q14681; -.
DR OpenTargets; ENSG00000180901; -.
DR PharmGKB; PA134890451; -.
DR VEuPathDB; HostDB:ENSG00000180901; -.
DR eggNOG; KOG2715; Eukaryota.
DR GeneTree; ENSGT00940000158336; -.
DR HOGENOM; CLU_070830_0_1_1; -.
DR InParanoid; Q14681; -.
DR OMA; PMPRGHG; -.
DR OrthoDB; 1333587at2759; -.
DR PhylomeDB; Q14681; -.
DR TreeFam; TF313754; -.
DR PathwayCommons; Q14681; -.
DR SignaLink; Q14681; -.
DR BioGRID-ORCS; 23510; 19 hits in 1081 CRISPR screens.
DR ChiTaRS; KCTD2; human.
DR GenomeRNAi; 23510; -.
DR Pharos; Q14681; Tdark.
DR PRO; PR:Q14681; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14681; protein.
DR Bgee; ENSG00000180901; Expressed in cerebellar hemisphere and 199 other tissues.
DR ExpressionAtlas; Q14681; baseline and differential.
DR Genevisible; Q14681; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 Acetylation; Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..263
FT /note="BTB/POZ domain-containing protein KCTD2"
FT /id="PRO_0000191287"
FT DOMAIN 72..172
FT /note="BTB"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 54
FT /note="P -> R (in Ref. 1; BAA11493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28527 MW; EF44819B2DC4AE49 CRC64;
MAELQLDPAM AGLGGGGGSG VGDGGGPVRG PPSPRPAGPT PRGHGRPAAA VAQPLEPGPG
PPERAGGGGA ARWVRLNVGG TYFVTTRQTL GREPKSFLCR LCCQEDPELD SDKDETGAYL
IDRDPTYFGP ILNYLRHGKL IITKELAEEG VLEEAEFYNI ASLVRLVKER IRDNENRTSQ
GPVKHVYRVL QCQEEELTQM VSTMSDGWKF EQLISIGSSY NYGNEDQAEF LCVVSRELNN
STNGIVIEPS EKAKILQERG SRM
