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Protein

Krueppel-like factor 1

Gene

Klf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator of erythrocyte development. Binds to the CACCC box in the beta-globin gene promoter and activates transcription. Probably serves as a general switch factor for erythroid development. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri275 – 29925C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri305 – 32925C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri335 – 35723C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • activating transcription factor binding Source: BHF-UCL
  • core promoter proximal region sequence-specific DNA binding Source: MGI
  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  • chromatin remodeling Source: MGI
  • embryonic hemopoiesis Source: MGI
  • erythrocyte development Source: MGI
  • erythrocyte differentiation Source: MGI
  • erythrocyte maturation Source: MGI
  • in utero embryonic development Source: MGI
  • liver development Source: MGI
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Krueppel-like factor 1
Alternative name(s):
Erythroid krueppel-like transcription factor
Short name:
EKLF
Gene namesi
Name:Klf1
Synonyms:Elkf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1342771. Klf1.

Subcellular locationi

  • Nucleus

  • Note: Colocalizes with SUMO1 in nuclear speckles.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231T → A: Greatly reduced transactivation activity. 1 Publication
Mutagenesisi23 – 231T → D: No change in transactivation activity. 1 Publication
Mutagenesisi25 – 262ED → AG: Abolishes most of transactivation activity. 1 Publication
Mutagenesisi56 – 561K → R: Abolishes sumoylation. No change in nuclear localization but no colocalization with SUMO1. Reduces inhibition of megakaryocytic differentiation. No decrease in bone marrow precursors to form megakaryocytic colonies. No effect on erythroid differentiation. 1 Publication
Mutagenesisi270 – 2701K → A or R: No effect on DNA binding. Transactivation activity reduced by 50%. Loss of superactivation by CBP of EP300. 1 Publication
Mutagenesisi284 – 2841K → A or R: No effect on DNA binding. No change in transactivation activity. No loss of superactivation by CBP or EP300. 2 Publications
Mutagenesisi295 – 2951H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. 1 Publication
Mutagenesisi325 – 3251H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. 1 Publication
Mutagenesisi353 – 3531H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Krueppel-like factor 1PRO_0000047161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphothreonine; by CK21 Publication
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei270 – 2701N6-acetyllysine1 Publication
Modified residuei284 – 2841N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated; can be acetylated on both Lys-270 and Lys-288. Acetylation on Lys-270 (by CBP) appears to be the major site affecting EKLF transactivation activity.1 Publication
Sumoylated; sumoylation, promoted by PIAS1, leads to repression of megakaryocyte differentiation. Also promotes the interaction with the CDH4 subunit of the NuRD repression complex.1 Publication
Phosphorylated primarily on serine residues in the transactivation domain. Phosphorylation on Thr-23 is critical for the transactivation activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP46099.
PRIDEiP46099.

PTM databases

iPTMnetiP46099.
PhosphoSiteiP46099.

Expressioni

Tissue specificityi

Erythroid-specific. Only expressed in bone marrow and spleen.

Gene expression databases

CleanExiMM_KLF1.

Interactioni

Subunit structurei

Interacts with CBP and EP300; the interactions enhance the transactivation activity. Interacts with PCAF; the interaction does not acetylate EKLF and inhibits its transactivation activity (By similarity). Interacts with CDH4; the interaction is SUMO-dependent and leads to transcriptional repression.By similarity2 Publications

GO - Molecular functioni

  • activating transcription factor binding Source: BHF-UCL
  • protein domain specific binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-48738N.
STRINGi10090.ENSMUSP00000064366.

Structurei

3D structure databases

ProteinModelPortaliP46099.
SMRiP46099. Positions 275-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi58 – 7619Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri275 – 29925C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri305 – 32925C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri335 – 35723C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
HOVERGENiHBG006220.
InParanoidiP46099.
PhylomeDBiP46099.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR031786. EKLF_TAD1.
IPR031784. EKLF_TAD2.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF16832. EKLF_TAD1. 1 hit.
PF16833. EKLF_TAD2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAETVLPS ISTLTTLGQF LDTQEDFLKW WRSEETQDLG PGPPNPTGPS
60 70 80 90 100
LHVSLKSEDP SGEDDERDVT CAWDPDLFLT NFPGSESPGT SRTCALAPSV
110 120 130 140 150
GPVAQFEPPE SLGAYAGGPG LVTGPLGSEE HTSWAHPTPR PPAPEPFVAP
160 170 180 190 200
ALAPGLAPKA QPSYSDSRAG SVGGFFPRAG LAVPAAPGAP YGLLSGYPAL
210 220 230 240 250
YPAPQYQGHF QLFRGLAAPS AGGTAPPSFL NCLGPGTVAT ELGATAIAGD
260 270 280 290 300
AGLSPGTAPP KRSRRTLAPK RQAAHTCGHE GCGKSYSKSS HLKAHLRTHT
310 320 330 340 350
GEKPYACSWD GCDWRFARSD ELTRHYRKHT GHRPFCCGLC PRAFSRSDHL

ALHMKRHL
Length:358
Mass (Da):37,757
Last modified:November 1, 1997 - v2
Checksum:i6FD59F294DDA45D1
GO

Sequence cautioni

The sequence AAA37546.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941C → Y in AAC24497 (PubMed:7565748).Curated
Sequence conflicti116 – 1161A → T in AAC24497 (PubMed:7565748).Curated
Sequence conflicti223 – 2231G → P in AAC24497 (PubMed:7565748).Curated
Sequence conflicti287 – 2871S → T in AAC24497 (PubMed:7565748).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97200 mRNA. Translation: AAA37546.1. Different initiation.
AF019074 Genomic DNA. Translation: AAB87861.1.
AF033102 Genomic DNA. Translation: AAC24497.1.
PIRiA48060.
UniGeneiMm.4847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97200 mRNA. Translation: AAA37546.1. Different initiation.
AF019074 Genomic DNA. Translation: AAB87861.1.
AF033102 Genomic DNA. Translation: AAC24497.1.
PIRiA48060.
UniGeneiMm.4847.

3D structure databases

ProteinModelPortaliP46099.
SMRiP46099. Positions 275-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48738N.
STRINGi10090.ENSMUSP00000064366.

PTM databases

iPTMnetiP46099.
PhosphoSiteiP46099.

Proteomic databases

PaxDbiP46099.
PRIDEiP46099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1342771. Klf1.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
HOVERGENiHBG006220.
InParanoidiP46099.
PhylomeDBiP46099.

Miscellaneous databases

PROiP46099.
SOURCEiSearch...

Gene expression databases

CleanExiMM_KLF1.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR031786. EKLF_TAD1.
IPR031784. EKLF_TAD2.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF16832. EKLF_TAD1. 1 hit.
PF16833. EKLF_TAD2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Kruppel family of nuclear proteins."
    Miller I.J., Bieker J.J.
    Mol. Cell. Biol. 13:2776-2786(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Jenkins N.A., Gilbert D.J., Copeland N.G., Gruzglin E., Bieker J.J.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  3. "Isolation of a gene encoding a functional zinc finger protein homologous to erythroid Kruppel-like factor: identification of a new multigene family."
    Anderson K.P., Kern C.B., Crable S.C., Lingrel J.B.
    Mol. Cell. Biol. 15:5957-5965(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  4. "Regulation of erythroid Krueppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain."
    Ouyang L., Chen X., Bieker J.J.
    J. Biol. Chem. 273:23019-23025(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-23, FUNCTION, MUTAGENESIS OF THR-23 AND 25-GLU-ASP-26.
  5. "Site-specific acetylation by p300 or CREB binding protein regulates erythroid Krueppel-like factor transcriptional activity via its interaction with the SWI-SNF complex."
    Zhang W., Kadam S., Emerson B.M., Bieker J.J.
    Mol. Cell. Biol. 21:2413-2422(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-270 AND LYS-284, FUNCTION, MUTAGENESIS OF LYS-270 AND LYS-284.
  6. "Stage-specific repression by the EKLF transcriptional activator."
    Chen X., Bieker J.J.
    Mol. Cell. Biol. 24:10416-10424(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIN3A AND HDAC1, MUTAGENESIS OF LYS-284; HIS-295; HIS-325 AND HIS-353.
  7. "Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis."
    Siatecka M., Xue L., Bieker J.J.
    Mol. Cell. Biol. 27:8547-8560(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-56, INTERACTION WITH CHD4, FUNCTION, MUTAGENESIS OF LYS-56.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiKLF1_MOUSE
AccessioniPrimary (citable) accession number: P46099
Secondary accession number(s): O70261
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.