KLF16_HUMAN
ID KLF16_HUMAN Reviewed; 252 AA.
AC Q9BXK1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Krueppel-like factor 16;
DE AltName: Full=Basic transcription element-binding protein 4;
DE Short=BTE-binding protein 4;
DE AltName: Full=Novel Sp1-like zinc finger transcription factor 2;
DE AltName: Full=Transcription factor BTEB4;
DE AltName: Full=Transcription factor NSLP2;
GN Name=KLF16; Synonyms=BTEB4, NSLP2;
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].
RC TISSUE=Pancreas;
RA Conley A., Urrutia R.;
RT "Isolation of a novel zinc finger transcription factor from the pancreas
RT extends the repertoire of Sp1-like proteins present in this organ (Abstract
RT #153).";
RL Pancreas 21:437-437(2000).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-152, 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
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-99, 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).
CC -!- FUNCTION: Transcription factor that binds GC and GT boxes and displaces
CC Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission
CC in the brain (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BXK1; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-5457991, EBI-12094670;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF327440; AAK15698.1; -; mRNA.
DR CCDS; CCDS12075.1; -.
DR RefSeq; NP_114124.1; NM_031918.3.
DR AlphaFoldDB; Q9BXK1; -.
DR SMR; Q9BXK1; -.
DR BioGRID; 123771; 426.
DR ELM; Q9BXK1; -.
DR IntAct; Q9BXK1; 406.
DR MINT; Q9BXK1; -.
DR STRING; 9606.ENSP00000250916; -.
DR iPTMnet; Q9BXK1; -.
DR PhosphoSitePlus; Q9BXK1; -.
DR SwissPalm; Q9BXK1; -.
DR BioMuta; KLF16; -.
DR DMDM; 17366682; -.
DR EPD; Q9BXK1; -.
DR jPOST; Q9BXK1; -.
DR MassIVE; Q9BXK1; -.
DR MaxQB; Q9BXK1; -.
DR PaxDb; Q9BXK1; -.
DR PeptideAtlas; Q9BXK1; -.
DR PRIDE; Q9BXK1; -.
DR ProteomicsDB; 79445; -.
DR Antibodypedia; 22829; 195 antibodies from 28 providers.
DR DNASU; 83855; -.
DR Ensembl; ENST00000250916.6; ENSP00000250916.3; ENSG00000129911.9.
DR Ensembl; ENST00000541015.5; ENSP00000439973.1; ENSG00000129911.9.
DR Ensembl; ENST00000617223.1; ENSP00000483701.1; ENSG00000129911.9.
DR GeneID; 83855; -.
DR KEGG; hsa:83855; -.
DR MANE-Select; ENST00000250916.6; ENSP00000250916.3; NM_031918.4; NP_114124.1.
DR UCSC; uc002luc.4; human.
DR CTD; 83855; -.
DR DisGeNET; 83855; -.
DR GeneCards; KLF16; -.
DR HGNC; HGNC:16857; KLF16.
DR HPA; ENSG00000129911; Tissue enhanced (brain).
DR MIM; 606139; gene.
DR neXtProt; NX_Q9BXK1; -.
DR OpenTargets; ENSG00000129911; -.
DR PharmGKB; PA30135; -.
DR VEuPathDB; HostDB:ENSG00000129911; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163280; -.
DR HOGENOM; CLU_002678_33_2_1; -.
DR InParanoid; Q9BXK1; -.
DR OMA; HRCTFNG; -.
DR OrthoDB; 1308225at2759; -.
DR PhylomeDB; Q9BXK1; -.
DR TreeFam; TF351003; -.
DR PathwayCommons; Q9BXK1; -.
DR SignaLink; Q9BXK1; -.
DR SIGNOR; Q9BXK1; -.
DR BioGRID-ORCS; 83855; 173 hits in 1107 CRISPR screens.
DR GenomeRNAi; 83855; -.
DR Pharos; Q9BXK1; Tbio.
DR PRO; PR:Q9BXK1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BXK1; protein.
DR Bgee; ENSG00000129911; Expressed in nucleus accumbens and 138 other tissues.
DR ExpressionAtlas; Q9BXK1; baseline and differential.
DR Genevisible; Q9BXK1; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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:0007212; P:dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..252
FT /note="Krueppel-like factor 16"
FT /id="PRO_0000047158"
FT ZN_FING 127..150
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 157..181
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..209
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 252 AA; 25431 MW; 9A0CB4B1A585A118 CRC64;
MSAAVACVDY FAADVLMAIS SGAVVHRGRP GPEGAGPAAG LDVRAARREA ASPGTPGPPP
PPPAASGPGP GAAAAPHLLA ASILADLRGG PGAAPGGASP ASSSSAASSP SSGRAPGAAP
SAAAKSHRCP FPDCAKAYYK SSHLKSHLRT HTGERPFACD WQGCDKKFAR SDELARHHRT
HTGEKRFSCP LCSKRFTRSD HLAKHARRHP GFHPDLLRRP GARSTSPSDS LPCSLAGSPA
PSPAPSPAPA GL
