KLF5_HUMAN
ID KLF5_HUMAN Reviewed; 457 AA.
AC Q13887; A2TJX0; L0R3U5; L0R4T9; Q9UHP8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Krueppel-like factor 5;
DE AltName: Full=Basic transcription element-binding protein 2;
DE Short=BTE-binding protein 2;
DE AltName: Full=Colon krueppel-like factor;
DE AltName: Full=GC-box-binding protein 2;
DE AltName: Full=Intestinal-enriched krueppel-like factor;
DE AltName: Full=Transcription factor BTEB2;
GN Name=KLF5; Synonyms=BTEB2, CKLF, IKLF;
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] (ISOFORM 1).
RX PubMed=10572182; DOI=10.1093/nar/27.24.4807;
RA Shi H., Zhang Z., Wang X., Liu S., Teng C.T.;
RT "Isolation and characterization of a gene encoding human Kruppel-like
RT factor 5 (IKLF): binding to the CAAT/GT box of the mouse lactoferrin gene
RT promoter.";
RL Nucleic Acids Res. 27:4807-4815(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING.
RX PubMed=23134681; DOI=10.1096/fj.12-220319;
RA Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B., Camacho S.C.,
RA Martignetti J.A.;
RT "Shaking the family tree: Identification of novel and biologically active
RT alternatively spliced isoforms across the KLF family of transcription
RT factors.";
RL FASEB J. 27:432-436(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ohnishi S., Yoshida T., Ramirez F., Terada M., Friedrich L.;
RT "Human basic transcription element binding protein 2.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sur I., Unden A.-B., Toftgard R.;
RT "Human Kruppel like factor5/KLF5: expression in human skin and hair
RT follicles.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Dong X., Guo P., Dong J.;
RT "Functional identification testis-specific transcript of Kruppel-like
RT factor 5 (tKLF5).";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 239-457 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8479902; DOI=10.1093/nar/21.7.1527;
RA Sogawa K., Imataka H., Yamasaki Y., Kusume H., Abe H., Fujii-Kuriyama Y.;
RT "cDNA cloning and transcriptional properties of a novel GC box-binding
RT protein, BTEB2.";
RL Nucleic Acids Res. 21:1527-1532(1993).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH WWP1, UBIQUITINATION, AND
RP MUTAGENESIS OF 324-PRO--TYR-328.
RX PubMed=15735697; DOI=10.1038/sj.onc.1208497;
RA Chen C., Sun X., Ran Q., Wilkinson K.D., Murphy T.J., Simons J.W.,
RA Dong J.T.;
RT "Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer
RT and untransformed epithelial cells.";
RL Oncogene 24:3319-3327(2005).
RN [12]
RP INTERACTION WITH ANP32B.
RX PubMed=18039846; DOI=10.1128/mcb.01396-07;
RA Munemasa Y., Suzuki T., Aizawa K., Miyamoto S., Imai Y., Matsumura T.,
RA Horikoshi M., Nagai R.;
RT "Promoter region-specific histone incorporation by the novel histone
RT chaperone ANP32B and DNA-binding factor KLF5.";
RL Mol. Cell. Biol. 28:1171-1181(2008).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-52; LYS-94 AND LYS-110,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
RN [15]
RP STRUCTURE BY NMR OF 363-457.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of three tandem repeats of ZF-C2H2 domains from human
RT kruppel-like factor 5.";
RL Submitted (FEB-2008) to the PDB data bank.
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] SER-301.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcription factor that binds to GC box promoter elements.
CC Activates the transcription of these genes.
CC -!- SUBUNIT: Interacts with WWP1. Interacts with ANP32B; this interaction
CC induces promoter region-specific histone incorporation and inhibition
CC of histone acetylation by ANP32B. {ECO:0000269|PubMed:15735697,
CC ECO:0000269|PubMed:18039846}.
CC -!- INTERACTION:
CC Q13887; P54253: ATXN1; NbExp=7; IntAct=EBI-2696013, EBI-930964;
CC Q13887; P46379-2: BAG6; NbExp=3; IntAct=EBI-2696013, EBI-10988864;
CC Q13887; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2696013, EBI-21553822;
CC Q13887; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2696013, EBI-12593112;
CC Q13887; O14645: DNALI1; NbExp=3; IntAct=EBI-2696013, EBI-395638;
CC Q13887; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-2696013, EBI-6398041;
CC Q13887; O14901: KLF11; NbExp=3; IntAct=EBI-2696013, EBI-948266;
CC Q13887; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-2696013, EBI-6190702;
CC Q13887; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2696013, EBI-2811583;
CC Q13887; P0CG48: UBC; NbExp=2; IntAct=EBI-2696013, EBI-3390054;
CC Q13887; P46937: YAP1; NbExp=2; IntAct=EBI-2696013, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15735697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13887-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13887-2; Sequence=VSP_047474;
CC Name=3;
CC IsoId=Q13887-3; Sequence=VSP_047475, VSP_047476;
CC Name=4;
CC IsoId=Q13887-4; Sequence=VSP_057567;
CC -!- TISSUE SPECIFICITY: Expressed only in testis and placenta.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
CC proteasomal degradation of this protein. {ECO:0000269|PubMed:15735697}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KLF5ID41074ch13q21.html";
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DR EMBL; AF132818; AAF18307.1; -; mRNA.
DR EMBL; HF546203; CCO02789.1; -; mRNA.
DR EMBL; HF546204; CCO02790.1; -; mRNA.
DR EMBL; AB030824; BAA96461.1; -; mRNA.
DR EMBL; AF287272; AAF88068.1; -; mRNA.
DR EMBL; EF208215; ABM97548.1; -; mRNA.
DR EMBL; AK302280; BAG63623.1; -; mRNA.
DR EMBL; AL354720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80526.1; -; Genomic_DNA.
DR EMBL; BC007695; AAH07695.1; -; mRNA.
DR EMBL; BC042131; AAH42131.1; -; mRNA.
DR EMBL; D14520; BAA03393.1; -; mRNA.
DR CCDS; CCDS66562.1; -. [Q13887-4]
DR CCDS; CCDS9448.1; -. [Q13887-1]
DR PIR; S35643; S35643.
DR RefSeq; NP_001273747.1; NM_001286818.1. [Q13887-4]
DR RefSeq; NP_001721.2; NM_001730.4. [Q13887-1]
DR PDB; 2EBT; NMR; -; A=365-457.
DR PDBsum; 2EBT; -.
DR AlphaFoldDB; Q13887; -.
DR SMR; Q13887; -.
DR BioGRID; 107153; 186.
DR IntAct; Q13887; 137.
DR MINT; Q13887; -.
DR STRING; 9606.ENSP00000366915; -.
DR BindingDB; Q13887; -.
DR ChEMBL; CHEMBL1293249; -.
DR GlyGen; Q13887; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13887; -.
DR PhosphoSitePlus; Q13887; -.
DR BioMuta; KLF5; -.
DR DMDM; 12644412; -.
DR EPD; Q13887; -.
DR jPOST; Q13887; -.
DR MassIVE; Q13887; -.
DR MaxQB; Q13887; -.
DR PaxDb; Q13887; -.
DR PeptideAtlas; Q13887; -.
DR PRIDE; Q13887; -.
DR ProteomicsDB; 527; -.
DR ProteomicsDB; 59715; -. [Q13887-1]
DR Antibodypedia; 24429; 373 antibodies from 35 providers.
DR DNASU; 688; -.
DR Ensembl; ENST00000377687.6; ENSP00000366915.4; ENSG00000102554.14. [Q13887-1]
DR Ensembl; ENST00000539231.5; ENSP00000440407.1; ENSG00000102554.14. [Q13887-4]
DR GeneID; 688; -.
DR KEGG; hsa:688; -.
DR MANE-Select; ENST00000377687.6; ENSP00000366915.4; NM_001730.5; NP_001721.2.
DR UCSC; uc001vjd.5; human.
DR CTD; 688; -.
DR DisGeNET; 688; -.
DR GeneCards; KLF5; -.
DR HGNC; HGNC:6349; KLF5.
DR HPA; ENSG00000102554; Tissue enhanced (esophagus, skin).
DR MalaCards; KLF5; -.
DR MIM; 602903; gene.
DR neXtProt; NX_Q13887; -.
DR OpenTargets; ENSG00000102554; -.
DR PharmGKB; PA30139; -.
DR VEuPathDB; HostDB:ENSG00000102554; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156711; -.
DR InParanoid; Q13887; -.
DR OMA; QEMPSQF; -.
DR PhylomeDB; Q13887; -.
DR TreeFam; TF350556; -.
DR PathwayCommons; Q13887; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q13887; -.
DR SIGNOR; Q13887; -.
DR BioGRID-ORCS; 688; 149 hits in 1113 CRISPR screens.
DR ChiTaRS; KLF5; human.
DR EvolutionaryTrace; Q13887; -.
DR GeneWiki; KLF5; -.
DR GenomeRNAi; 688; -.
DR Pharos; Q13887; Tchem.
DR PRO; PR:Q13887; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q13887; protein.
DR Bgee; ENSG00000102554; Expressed in lower esophagus mucosa and 172 other tissues.
DR ExpressionAtlas; Q13887; baseline and differential.
DR Genevisible; Q13887; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043426; F:MRF binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0099156; P:cell-cell signaling via exosome; IDA:BHF-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
DR GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0061586; P:positive regulation of transcription by transcription factor localization; IEA:Ensembl.
DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014901; P:satellite cell activation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR InterPro; IPR030401; KLF5.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF82; PTHR23235:SF82; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..457
FT /note="Krueppel-like factor 5"
FT /id="PRO_0000047169"
FT ZN_FING 373..397
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..427
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..328
FT /note="Interaction with WWP1"
FT /evidence="ECO:0000269|PubMed:15735697"
FT MOTIF 118..126
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 63..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 4)"
FT /id="VSP_057567"
FT VAR_SEQ 88..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047474"
FT VAR_SEQ 105..166
FT /note="IIPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITHLRTGLYKSQRP
FT CVTHIKTEPV -> MLLQLLLNWQFTIQIYPPPCQLTHKTSNLSDTIEGVTPIWRNDAS
FT TTAITLVAQKFIPSLLI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047475"
FT VAR_SEQ 167..457
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047476"
FT VARIANT 301
FT /note="P -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035555"
FT MUTAGEN 324..328
FT /note="Missing: Impairs ubiquitination and degradation."
FT /evidence="ECO:0000269|PubMed:15735697"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2EBT"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2EBT"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:2EBT"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:2EBT"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:2EBT"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:2EBT"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2EBT"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:2EBT"
SQ SEQUENCE 457 AA; 50792 MW; 3BF12BE272716E57 CRC64;
MATRVLSMSA RLGPVPQPPA PQDEPVFAQL KPVLGAANPA RDAALFPGEE LKHAHHRPQA
QPAPAQAPQP AQPPATGPRL PPEDLVQTRC EMEKYLTPQL PPVPIIPEHK KYRRDSASVV
DQFFTDTEGL PYSINMNVFL PDITHLRTGL YKSQRPCVTH IKTEPVAIFS HQSETTAPPP
APTQALPEFT SIFSSHQTAA PEVNNIFIKQ ELPTPDLHLS VPTQQGHLYQ LLNTPDLDMP
SSTNQTAAMD TLNVSMSAAM AGLNTHTSAV PQTAVKQFQG MPPCTYTMPS QFLPQQATYF
PPSPPSSEPG SPDRQAEMLQ NLTPPPSYAA TIASKLAIHN PNLPTTLPVN SQNIQPVRYN
RRSNPDLEKR RIHYCDYPGC TKVYTKSSHL KAHLRTHTGE KPYKCTWEGC DWRFARSDEL
TRHYRKHTGA KPFQCGVCNR SFSRSDHLAL HMKRHQN
