KCTD5_HUMAN
ID KCTD5_HUMAN Reviewed; 234 AA.
AC Q9NXV2; D3DU96;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=BTB/POZ domain-containing protein KCTD5;
GN Name=KCTD5;
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], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP AAV-S REP (MICROBIAL INFECTION).
RX PubMed=17239418; DOI=10.1016/j.virol.2006.12.010;
RA Weger S., Hammer E., Goetz A., Heilbronn R.;
RT "Identification of a cytoplasmic interaction partner of the large
RT regulatory proteins Rep78/Rep68 of adeno-associated virus type 2 (AAV-2).";
RL Virology 362:192-206(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [5]
RP PROTEIN SEQUENCE OF 2-13 AND 48-59, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (OCT-2008) to UniProtKB.
RN [6]
RP POSSIBLE FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CUL3, AND
RP INDUCTION.
RX PubMed=18573101; DOI=10.1111/j.1742-4658.2008.06537.x;
RA Bayon Y., Trinidad A.G., de la Puerta M.L., Del Carmen Rodriguez M.,
RA Bogetz J., Rojas A., De Pereda J.M., Rahmouni S., Williams S.,
RA Matsuzawa S., Reed J.C., Crespo M.S., Mustelin T., Alonso A.;
RT "KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases.";
RL FEBS J. 275:3900-3910(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-234, SUBUNIT, DOMAIN BTB,
RP INTERACTION WITH GORASP2, AND FUNCTION.
RX PubMed=19361449; DOI=10.1016/j.jmb.2009.01.030;
RA Dementieva I.S., Tereshko V., McCrossan Z.A., Solomaha E., Araki D., Xu C.,
RA Grigorieff N., Goldstein S.A.;
RT "Pentameric assembly of potassium channel tetramerization domain-containing
RT protein 5.";
RL J. Mol. Biol. 387:175-191(2009).
CC -!- FUNCTION: Its interaction with CUL3 suggests that it may act as a
CC substrate adapter in some E3 ligase complex (PubMed:18573101). Does not
CC affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2
CC and Kv3.4/KCNC4 (PubMed:19361449). {ECO:0000269|PubMed:18573101,
CC ECO:0000269|PubMed:19361449}.
CC -!- SUBUNIT: Homopentamer (PubMed:19361449). Interacts (via C-terminus)
CC with GRASP55/GORASP2 (PubMed:19361449). Interacts with CUL3 and with
CC ubiquitinated proteins (PubMed:18573101). Interacts with CRY1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8VC57,
CC ECO:0000269|PubMed:18573101, ECO:0000269|PubMed:19361449}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adeno-associated virus 2
CC (AAV-2) REP proteins. {ECO:0000269|PubMed:17239418}.
CC -!- INTERACTION:
CC Q9NXV2; Q9NXV2: KCTD5; NbExp=2; IntAct=EBI-1056857, EBI-1056857;
CC Q9NXV2; P03132: Rep68; Xeno; NbExp=3; IntAct=EBI-1056857, EBI-7387242;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17239418}.
CC Cytoplasm {ECO:0000269|PubMed:18573101}. Nucleus. Note=Predominantly
CC cytoplasmic, translocated to the nucleus upon interaction with Rep
CC proteins. {ECO:0000269|PubMed:18573101}.
CC -!- INDUCTION: Up-regulated in peripheral blood lymphocytes stimulated
CC through the T-cell receptor. {ECO:0000269|PubMed:18573101}.
CC -!- DOMAIN: The BTB (POZ) domain is atypical and mediates the formation of
CC a homopentamer instead of a homotetramer (PubMed:19361449).
CC Homopentamerization is due to the presence of 4 residues in the BTB
CC (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118.
CC {ECO:0000269|PubMed:19361449}.
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DR EMBL; AK000047; BAA90906.1; -; mRNA.
DR EMBL; CH471112; EAW85489.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85491.1; -; Genomic_DNA.
DR EMBL; BC007314; AAH07314.1; -; mRNA.
DR CCDS; CCDS10475.1; -.
DR RefSeq; NP_061865.1; NM_018992.3.
DR PDB; 3DRX; X-ray; 3.11 A; A/B/C/D/E=34-234.
DR PDB; 3DRY; X-ray; 3.30 A; A/B/C/D/E=34-234.
DR PDB; 3DRZ; X-ray; 1.90 A; A/B/C/D/E=40-145.
DR PDBsum; 3DRX; -.
DR PDBsum; 3DRY; -.
DR PDBsum; 3DRZ; -.
DR AlphaFoldDB; Q9NXV2; -.
DR SMR; Q9NXV2; -.
DR BioGRID; 119958; 113.
DR IntAct; Q9NXV2; 28.
DR MINT; Q9NXV2; -.
DR STRING; 9606.ENSP00000301738; -.
DR GlyGen; Q9NXV2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NXV2; -.
DR PhosphoSitePlus; Q9NXV2; -.
DR BioMuta; KCTD5; -.
DR DMDM; 50401182; -.
DR EPD; Q9NXV2; -.
DR jPOST; Q9NXV2; -.
DR MassIVE; Q9NXV2; -.
DR MaxQB; Q9NXV2; -.
DR PaxDb; Q9NXV2; -.
DR PeptideAtlas; Q9NXV2; -.
DR PRIDE; Q9NXV2; -.
DR ProteomicsDB; 83137; -.
DR Antibodypedia; 42594; 98 antibodies from 20 providers.
DR DNASU; 54442; -.
DR Ensembl; ENST00000301738.9; ENSP00000301738.4; ENSG00000167977.9.
DR GeneID; 54442; -.
DR KEGG; hsa:54442; -.
DR MANE-Select; ENST00000301738.9; ENSP00000301738.4; NM_018992.4; NP_061865.1.
DR UCSC; uc002crd.5; human.
DR CTD; 54442; -.
DR DisGeNET; 54442; -.
DR GeneCards; KCTD5; -.
DR HGNC; HGNC:21423; KCTD5.
DR HPA; ENSG00000167977; Low tissue specificity.
DR MIM; 611285; gene.
DR neXtProt; NX_Q9NXV2; -.
DR OpenTargets; ENSG00000167977; -.
DR PharmGKB; PA134923177; -.
DR VEuPathDB; HostDB:ENSG00000167977; -.
DR eggNOG; KOG2715; Eukaryota.
DR GeneTree; ENSGT00940000160374; -.
DR HOGENOM; CLU_070830_1_0_1; -.
DR InParanoid; Q9NXV2; -.
DR OMA; ISVGMQY; -.
DR OrthoDB; 1333587at2759; -.
DR PhylomeDB; Q9NXV2; -.
DR TreeFam; TF313754; -.
DR PathwayCommons; Q9NXV2; -.
DR SignaLink; Q9NXV2; -.
DR BioGRID-ORCS; 54442; 60 hits in 1098 CRISPR screens.
DR ChiTaRS; KCTD5; human.
DR EvolutionaryTrace; Q9NXV2; -.
DR GenomeRNAi; 54442; -.
DR Pharos; Q9NXV2; Tbio.
DR PRO; PR:Q9NXV2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NXV2; protein.
DR Bgee; ENSG00000167977; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q9NXV2; baseline and differential.
DR Genevisible; Q9NXV2; 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:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 DisProt; DP02706; -.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:20068231"
FT CHAIN 2..234
FT /note="BTB/POZ domain-containing protein KCTD5"
FT /id="PRO_0000191291"
FT DOMAIN 44..146
FT /note="BTB"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:20068231"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 178
FT /note="G -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3DRZ"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3DRZ"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:3DRZ"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:3DRZ"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:3DRZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3DRZ"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3DRZ"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3DRY"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:3DRZ"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:3DRZ"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3DRY"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3DRX"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3DRX"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3DRX"
FT TURN 190..194
FT /evidence="ECO:0007829|PDB:3DRX"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3DRX"
SQ SEQUENCE 234 AA; 26093 MW; 22097CF5F41CD43D CRC64;
MAENHCELLS PARGGIGAGL GGGLCRRCSA GLGALAQRPG SVSKWVRLNV GGTYFLTTRQ
TLCRDPKSFL YRLCQADPDL DSDKDETGAY LIDRDPTYFG PVLNYLRHGK LVINKDLAEE
GVLEEAEFYN ITSLIKLVKD KIRERDSKTS QVPVKHVYRV LQCQEEELTQ MVSTMSDGWK
FEQLVSIGSS YNYGNEDQAE FLCVVSKELH NTPYGTASEP SEKAKILQER GSRM
