KLF13_HUMAN
ID KLF13_HUMAN Reviewed; 288 AA.
AC Q9Y2Y9; Q9Y356;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Krueppel-like factor 13;
DE AltName: Full=Basic transcription element-binding protein 3;
DE Short=BTE-binding protein 3;
DE AltName: Full=Novel Sp1-like zinc finger transcription factor 1;
DE AltName: Full=RANTES factor of late activated T-lymphocytes 1;
DE Short=RFLAT-1;
DE AltName: Full=Transcription factor BTEB3;
DE AltName: Full=Transcription factor NSLP1;
GN Name=KLF13; Synonyms=BTEB3, NSLP1;
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].
RX PubMed=10023774; DOI=10.1016/s1074-7613(00)80010-2;
RA Song A., Chen Y.F., Thamatrakoln K., Storm T.A., Krensky A.M.;
RT "RFLAT-1: a new zinc finger transcription factor that activates RANTES gene
RT expression in T lymphocytes.";
RL Immunity 10:93-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10415854; DOI=10.1111/j.1749-6632.1999.tb09513.x;
RA Cook T., Gebelein B., Urrutia R.;
RT "Sp1 and its likes: biochemical and functional predictions for a growing
RT family of zinc finger transcription factors.";
RL Ann. N. Y. Acad. Sci. 880:94-102(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 FUNCTION.
RX PubMed=11477107; DOI=10.1074/jbc.m105831200;
RA Kaczynski J., Zhang J.S., Ellenrieder V., Conley A., Duenes T., Kester H.,
RA van Der Burg B., Urrutia R.;
RT "The Sp1-like protein BTEB3 inhibits transcription via the basic
RT transcription element box by interacting with mSin3A and HDAC-1 co-
RT repressors and competing with Sp1.";
RL J. Biol. Chem. 276:36749-36756(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-270, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Represses transcription by binding to the BTE site, a GC-rich
CC DNA element, in competition with the activator SP1. It also represses
CC transcription by interacting with the corepressor Sin3A and HDAC1.
CC Activates RANTES expression in T-cells. {ECO:0000269|PubMed:11477107}.
CC -!- INTERACTION:
CC Q9Y2Y9; P43694: GATA4; NbExp=3; IntAct=EBI-1255893, EBI-7049352;
CC Q9Y2Y9; Q13523: PRPF4B; NbExp=5; IntAct=EBI-1255893, EBI-395940;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The Ala/Pro-rich domain may contain discrete activation and
CC repression subdomains and also can mediate protein-protein
CC interactions.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF132599; AAD26864.1; -; mRNA.
DR EMBL; AF150628; AAD34020.1; -; mRNA.
DR EMBL; BC013946; AAH13946.1; -; mRNA.
DR EMBL; BC010438; AAH10438.1; -; mRNA.
DR EMBL; BC012741; AAH12741.1; -; mRNA.
DR CCDS; CCDS10025.1; -.
DR RefSeq; NP_001289390.1; NM_001302461.1.
DR RefSeq; NP_057079.2; NM_015995.3.
DR AlphaFoldDB; Q9Y2Y9; -.
DR SMR; Q9Y2Y9; -.
DR BioGRID; 119642; 16.
DR ELM; Q9Y2Y9; -.
DR IntAct; Q9Y2Y9; 6.
DR MINT; Q9Y2Y9; -.
DR STRING; 9606.ENSP00000302456; -.
DR iPTMnet; Q9Y2Y9; -.
DR PhosphoSitePlus; Q9Y2Y9; -.
DR BioMuta; KLF13; -.
DR DMDM; 17369913; -.
DR EPD; Q9Y2Y9; -.
DR jPOST; Q9Y2Y9; -.
DR MassIVE; Q9Y2Y9; -.
DR PaxDb; Q9Y2Y9; -.
DR PeptideAtlas; Q9Y2Y9; -.
DR PRIDE; Q9Y2Y9; -.
DR ProteomicsDB; 85939; -.
DR Antibodypedia; 9456; 185 antibodies from 32 providers.
DR DNASU; 51621; -.
DR Ensembl; ENST00000307145.4; ENSP00000302456.3; ENSG00000169926.11.
DR Ensembl; ENST00000621843.1; ENSP00000484904.1; ENSG00000275746.1.
DR GeneID; 51621; -.
DR KEGG; hsa:51621; -.
DR MANE-Select; ENST00000307145.4; ENSP00000302456.3; NM_015995.4; NP_057079.2.
DR CTD; 51621; -.
DR DisGeNET; 51621; -.
DR GeneCards; KLF13; -.
DR GeneReviews; KLF13; -.
DR HGNC; HGNC:13672; KLF13.
DR HPA; ENSG00000169926; Low tissue specificity.
DR MalaCards; KLF13; -.
DR MIM; 605328; gene.
DR neXtProt; NX_Q9Y2Y9; -.
DR OpenTargets; ENSG00000169926; -.
DR PharmGKB; PA30133; -.
DR VEuPathDB; HostDB:ENSG00000169926; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161911; -.
DR HOGENOM; CLU_002678_33_2_1; -.
DR InParanoid; Q9Y2Y9; -.
DR OMA; NQHVPNS; -.
DR OrthoDB; 1308225at2759; -.
DR PhylomeDB; Q9Y2Y9; -.
DR TreeFam; TF351003; -.
DR PathwayCommons; Q9Y2Y9; -.
DR SignaLink; Q9Y2Y9; -.
DR SIGNOR; Q9Y2Y9; -.
DR BioGRID-ORCS; 51621; 18 hits in 1099 CRISPR screens.
DR ChiTaRS; KLF13; human.
DR GeneWiki; KLF13; -.
DR GenomeRNAi; 51621; -.
DR Pharos; Q9Y2Y9; Tbio.
DR PRO; PR:Q9Y2Y9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y2Y9; protein.
DR Bgee; ENSG00000169926; Expressed in right hemisphere of cerebellum and 97 other tissues.
DR ExpressionAtlas; Q9Y2Y9; baseline and differential.
DR Genevisible; Q9Y2Y9; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..288
FT /note="Krueppel-like factor 13"
FT /id="PRO_0000047184"
FT ZN_FING 167..191
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 197..221
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 227..249
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 23..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJZ6"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJZ6"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJZ6"
FT CONFLICT 39
FT /note="A -> S (in Ref. 2; AAD34020)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..114
FT /note="EPTSPGAEGAA -> MSPPPPALKARR (in Ref. 2; AAD34020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 31180 MW; DD2765EE00E9C049 CRC64;
MAAAAYVDHF AAECLVSMSS RAVVHGPREG PESRPEGAAV AATPTLPRVE ERRDGKDSAS
LFVVARILAD LNQQAPAPAP AERREGAAAR KARTPCRLPP PAPEPTSPGA EGAAAAPPSP
AWSEPEPEAG LEPEREPGPA GSGEPGLRQR VRRGRSRADL ESPQRKHKCH YAGCEKVYGK
SSHLKAHLRT HTGERPFACS WQDCNKKFAR SDELARHYRT HTGEKKFSCP ICEKRFMRSD
HLTKHARRHA NFHPGMLQRR GGGSRTGSLS DYSRSDASSP TISPASSP
