ID KLF3_HUMAN Reviewed; 345 AA. AC P57682; Q6PIR1; Q86TN0; Q9P2X6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 08-NOV-2023, entry version 195. DE RecName: Full=Krueppel-like factor 3; DE AltName: Full=Basic krueppel-like factor; DE AltName: Full=CACCC-box-binding protein BKLF; DE AltName: Full=TEF-2; GN Name=KLF3; Synonyms=BKLF; 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). RA Matsumoto N., Yoshida T., Terada M.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=12812068; RA Wang M.J., Qu X.H., Wang L.S., Zhai Y., Wu S.L., He F.C.; RT "cDNA cloning, subcellular localization and tissue expression of a new RT human Kruppel-like transcription factor: human basic Kruppel-like factor RT (hBKLF)."; RL Yi Chuan Xue Bao 30:1-9(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Hippocampus; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-101, 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-111, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-92; SER-101 AND RP SER-250, AND IDENTIFICATION BY 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-196 AND LYS-198, AND RP 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 [11] RP INACTIVATION OF 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). CC -!- FUNCTION: Binds to the CACCC box of erythroid cell-expressed genes. May CC play a role in hematopoiesis (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- INTERACTION: CC P57682; Q86V38: ATN1; NbExp=3; IntAct=EBI-8472267, EBI-11954292; CC P57682; P54253: ATXN1; NbExp=4; IntAct=EBI-8472267, EBI-930964; CC P57682; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-8472267, EBI-11282723; CC P57682; P46379-2: BAG6; NbExp=3; IntAct=EBI-8472267, EBI-10988864; CC P57682; P02489: CRYAA; NbExp=3; IntAct=EBI-8472267, EBI-6875961; CC P57682; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-8472267, EBI-10171858; CC P57682; P56545-3: CTBP2; NbExp=3; IntAct=EBI-8472267, EBI-10171902; CC P57682; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-8472267, EBI-715104; CC P57682; Q92997: DVL3; NbExp=3; IntAct=EBI-8472267, EBI-739789; CC P57682; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-8472267, EBI-10174566; CC P57682; Q96KQ7: EHMT2; NbExp=4; IntAct=EBI-8472267, EBI-744366; CC P57682; P22607: FGFR3; NbExp=3; IntAct=EBI-8472267, EBI-348399; CC P57682; Q13643: FHL3; NbExp=11; IntAct=EBI-8472267, EBI-741101; CC P57682; O14908-2: GIPC1; NbExp=3; IntAct=EBI-8472267, EBI-25913156; CC P57682; P28799: GRN; NbExp=4; IntAct=EBI-8472267, EBI-747754; CC P57682; P01112: HRAS; NbExp=3; IntAct=EBI-8472267, EBI-350145; CC P57682; P04792: HSPB1; NbExp=3; IntAct=EBI-8472267, EBI-352682; CC P57682; O43464: HTRA2; NbExp=3; IntAct=EBI-8472267, EBI-517086; CC P57682; P42858: HTT; NbExp=6; IntAct=EBI-8472267, EBI-466029; CC P57682; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-8472267, EBI-751501; CC P57682; O60333-2: KIF1B; NbExp=3; IntAct=EBI-8472267, EBI-10975473; CC P57682; O14901: KLF11; NbExp=3; IntAct=EBI-8472267, EBI-948266; CC P57682; Q92876: KLK6; NbExp=3; IntAct=EBI-8472267, EBI-2432309; CC P57682; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-8472267, EBI-10258746; CC P57682; Q68G74: LHX8; NbExp=3; IntAct=EBI-8472267, EBI-8474075; CC P57682; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-8472267, EBI-473196; CC P57682; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-8472267, EBI-2811583; CC P57682; P32243-2: OTX2; NbExp=3; IntAct=EBI-8472267, EBI-9087860; CC P57682; O43933: PEX1; NbExp=3; IntAct=EBI-8472267, EBI-988601; CC P57682; P60891: PRPS1; NbExp=3; IntAct=EBI-8472267, EBI-749195; CC P57682; Q12933: TRAF2; NbExp=6; IntAct=EBI-8472267, EBI-355744; CC P57682; O76024: WFS1; NbExp=3; IntAct=EBI-8472267, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P57682-1; Sequence=Displayed; CC Name=2; CC IsoId=P57682-2; Sequence=VSP_014532; CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. In KLF3, the motif is CC inactive. {ECO:0000269|PubMed:31375868}. CC -!- PTM: Sumoylated with SUMO1. Sumoylation is enhanced by PIAS1, CC PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances CC transcriptional repression, but has no effect on DNA binding. CC Sumoylation on Lys-198 is the major site (By similarity). CC {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {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; AB024523; BAA92271.1; -; mRNA. DR EMBL; AF285837; AAK27329.1; -; mRNA. DR EMBL; BC030662; AAH30662.1; -; mRNA. DR EMBL; BC051687; AAH51687.1; -; mRNA. DR CCDS; CCDS3444.1; -. [P57682-1] DR RefSeq; NP_057615.3; NM_016531.5. [P57682-1] DR AlphaFoldDB; P57682; -. DR SMR; P57682; -. DR BioGRID; 119426; 160. DR IntAct; P57682; 175. DR STRING; 9606.ENSP00000261438; -. DR GlyGen; P57682; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P57682; -. DR PhosphoSitePlus; P57682; -. DR BioMuta; KLF3; -. DR DMDM; 12644533; -. DR EPD; P57682; -. DR jPOST; P57682; -. DR MassIVE; P57682; -. DR MaxQB; P57682; -. DR PaxDb; 9606-ENSP00000261438; -. DR PeptideAtlas; P57682; -. DR ProteomicsDB; 57007; -. [P57682-1] DR ProteomicsDB; 57008; -. [P57682-2] DR Pumba; P57682; -. DR Antibodypedia; 10444; 199 antibodies from 29 providers. DR DNASU; 51274; -. DR Ensembl; ENST00000261438.10; ENSP00000261438.5; ENSG00000109787.13. [P57682-1] DR Ensembl; ENST00000514033.1; ENSP00000421252.1; ENSG00000109787.13. [P57682-2] DR GeneID; 51274; -. DR KEGG; hsa:51274; -. DR MANE-Select; ENST00000261438.10; ENSP00000261438.5; NM_016531.6; NP_057615.3. DR UCSC; uc003gtg.3; human. [P57682-1] DR AGR; HGNC:16516; -. DR CTD; 51274; -. DR DisGeNET; 51274; -. DR GeneCards; KLF3; -. DR HGNC; HGNC:16516; KLF3. DR HPA; ENSG00000109787; Low tissue specificity. DR MIM; 609392; gene. DR neXtProt; NX_P57682; -. DR OpenTargets; ENSG00000109787; -. DR PharmGKB; PA30137; -. DR VEuPathDB; HostDB:ENSG00000109787; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000157456; -. DR HOGENOM; CLU_002678_33_0_1; -. DR InParanoid; P57682; -. DR OMA; PMKKFTP; -. DR OrthoDB; 3168417at2759; -. DR PhylomeDB; P57682; -. DR TreeFam; TF350556; -. DR PathwayCommons; P57682; -. DR SignaLink; P57682; -. DR SIGNOR; P57682; -. DR BioGRID-ORCS; 51274; 29 hits in 1176 CRISPR screens. DR ChiTaRS; KLF3; human. DR GeneWiki; KLF3; -. DR GenomeRNAi; 51274; -. DR Pharos; P57682; Tbio. DR PRO; PR:P57682; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P57682; Protein. DR Bgee; ENSG00000109787; Expressed in upper leg skin and 195 other tissues. DR Genevisible; P57682; HS. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc. 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl. DR GO; GO:0030097; P:hemopoiesis; TAS:ProtInc. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd21577; KLF3_N; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235:SF48; KRUEPPEL-LIKE FACTOR 3; 1. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. DR Pfam; PF00096; zf-C2H2; 3. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..345 FT /note="Krueppel-like factor 3" FT /id="PRO_0000047165" FT ZN_FING 260..284 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 290..314 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 320..342 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..74 FT /note="Repressor domain" FT REGION 66..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 60..68 FT /note="9aaTAD; inactive" FT /evidence="ECO:0000269|PubMed:31375868" FT MOTIF 61..65 FT /note="CTBP-binding motif" FT COMPBIAS 66..102 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60980" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60980" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60980" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 10 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 68 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 196 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 198 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 233..345 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014532" FT VARIANT 207 FT /note="R -> S (in dbSNP:rs17616226)" FT /id="VAR_052715" FT CONFLICT 85 FT /note="P -> R (in Ref. 3; AAH51687)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="P -> H (in Ref. 3; AAH51687)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="D -> G (in Ref. 3; AAH30662)" FT /evidence="ECO:0000305" SQ SEQUENCE 345 AA; 38829 MW; A490D642AB8F1FDC CRC64; MLMFDPVPVK QEAMDPVSVS YPSNYMESMK PNKYGVIYST PLPEKFFQTP EGLSHGIQME PVDLTVNKRS SPPSAGNSPS SLKFPSSHRR ASPGLSMPSS SPPIKKYSPP SPGVQPFGVP LSMPPVMAAA LSRHGIRSPG ILPVIQPVVV QPVPFMYTSH LQQPLMVSLS EEMENSSSSM QVPVIESYEK PISQKKIKIE PGIEPQRTDY YPEEMSPPLM NSVSPPQALL QENHPSVIVQ PGKRPLPVES PDTQRKRRIH RCDYDGCNKV YTKSSHLKAH RRTHTGEKPY KCTWEGCTWK FARSDELTRH FRKHTGIKPF QCPDCDRSFS RSDHLALHRK RHMLV //