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KLF2_RAT
ID   KLF2_RAT                Reviewed;         351 AA.
AC   Q9ET58;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Krueppel-like factor 2;
DE   AltName: Full=Lung krueppel-like factor;
GN   Name=Klf2; Synonyms=Lklf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Brown Norway/SsNHsd;
RA   Haag F., Bartels K., Rothenburg S., Stahmer I., Thiele H.-G.,
RA   Koch-Nolte F.;
RT   "The gene for the transcription factor LKLF is developmentally expressed in
RT   rat T cells and is not defective in lymphopenic diabetes-prone BB rats.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171 AND THR-240, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transcription factor that binds to the CACCC box in the
CC       promoter of target genes such as HBB/beta globin or NOV and activates
CC       their transcription. Might be involved in transcriptional regulation by
CC       modulating the binding of the RARA nuclear receptor to RARE DNA
CC       elements (By similarity). {ECO:0000250|UniProtKB:Q9Y5W3}.
CC   -!- SUBUNIT: Interacts with WWP1. {ECO:0000250|UniProtKB:Q60843,
CC       ECO:0000250|UniProtKB:Q9Y5W3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:Q9Y5W3}.
CC   -!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
CC       proteasomal degradation of this protein (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF181251; AAG02141.1; -; Genomic_DNA.
DR   RefSeq; NP_001007685.1; NM_001007684.1.
DR   AlphaFoldDB; Q9ET58; -.
DR   SMR; Q9ET58; -.
DR   STRING; 10116.ENSRNOP00000019052; -.
DR   iPTMnet; Q9ET58; -.
DR   PhosphoSitePlus; Q9ET58; -.
DR   PaxDb; Q9ET58; -.
DR   Ensembl; ENSRNOT00000112398; ENSRNOP00000083422; ENSRNOG00000067705.
DR   GeneID; 306330; -.
DR   KEGG; rno:306330; -.
DR   UCSC; RGD:1359220; rat.
DR   CTD; 10365; -.
DR   RGD; 1359220; Klf2.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163163; -.
DR   HOGENOM; CLU_002678_33_1_1; -.
DR   InParanoid; Q9ET58; -.
DR   OMA; LHERWKC; -.
DR   OrthoDB; 1273088at2759; -.
DR   PhylomeDB; Q9ET58; -.
DR   TreeFam; TF350556; -.
DR   PRO; PR:Q9ET58; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000014205; Expressed in lung and 19 other tissues.
DR   Genevisible; Q9ET58; RN.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR   GO; GO:0071409; P:cellular response to cycloheximide; IEP:RGD.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR   GO; GO:0071499; P:cellular response to laminar fluid shear stress; ISO:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR   GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0097533; P:cellular stress response to acid chemical; ISO:RGD.
DR   GO; GO:0034101; P:erythrocyte homeostasis; ISO:RGD.
DR   GO; GO:0043249; P:erythrocyte maturation; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:RGD.
DR   GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:RGD.
DR   GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
DR   GO; GO:0060509; P:type I pneumocyte differentiation; ISO:RGD.
DR   GO; GO:0042311; P:vasodilation; ISO:RGD.
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; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..351
FT                   /note="Krueppel-like factor 2"
FT                   /id="PRO_0000047164"
FT   ZN_FING         268..292
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         298..322
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         328..350
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          20..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..264
FT                   /note="Interaction with WWP1"
FT                   /evidence="ECO:0000250"
FT   REGION          156..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..50
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5W3"
FT   COMPBIAS        58..84
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..209
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         171
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         240
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60843"
SQ   SEQUENCE   351 AA;  37313 MW;  2E4EB6B0577A53A4 CRC64;
     MALSEPILPS FATFASPCER GLQERWPRNE PEAGSTDEDL NSVLDFILSM GLDGLGAENP
     PEPPPQPPPP AFYYPEPGAP PPYGTPAAGL GTELLRPDLD APQGPALHGR FLLAPPGRLV
     KAEPPEVDGG GYGCAAGLAR GPRGLKLEGA LGATGACMRG PAGRPPPPSD TPPLSPDGPP
     RLPAPGPRNP FPPPFGPGPS FGGPGPALHY GPPAPGAFGL FDDAAAALGL APPATRGLLT
     PPSSPLELLE AKPKRGRRSW PRKRAATHTC SYTNCGKTYT KSSHLKAHLR THTGEKPYHC
     NWDGCGWKFA RSDELTRHYR KHTGHRPFQC HLCDRAFSRS DHLALHMKRH M
 
 
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