Krueppel-like factor 1 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

P46099 (KLF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Krueppel-like factor 1

Alternative name(s):
Erythroid krueppel-like transcription factor
Short name=EKLF

Gene names

Name:	Klf1
Synonyms:	Elkf

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	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. Ref.6 Ref.7
Subcellular location	Nucleus. Note: Colocalizes with SUMO1 in nuclear speckles.
Tissue specificity	Erythroid-specific. Only expressed in bone marrow and spleen.
Post-translational modification	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. Sumoylated; sumoylation, promoted by PIAS1, leads to repression of megakaryocyte differentiation. Also promotes the interaction with the CDH4 subunit of the NuRD repression complex. Ref.7 Phosphorylated primarily on serine residues in the transactivation domain. Phosphorylation on Thr-23 is critical for the transactivation activity. Ref.4
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers.
Sequence caution	The sequence AAA37546.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from direct assay PubMed 15489291. Source: MGI embryonic hemopoiesis Inferred from mutant phenotype PubMed 19409822 PubMed 7753194. Source: MGI erythrocyte maturation Inferred from mutant phenotype PubMed 7753195. Source: MGI in utero embryonic development Inferred from mutant phenotype PubMed 7753194. Source: MGI liver development Inferred from mutant phenotype PubMed 7753194. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19251649. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from sequence or structural similarity PubMed 15820306. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Krueppel-like factor 1

PRO_0000047161

Regions

Zinc finger

275 – 299

C2H2-type 1

Zinc finger

305 – 329

C2H2-type 2

Zinc finger

335 – 357

C2H2-type 3

Compositional bias

58 – 76

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

Phosphothreonine; by CK2 Probable

Modified residue

270

N6-acetyllysine Ref.5

Modified residue

284

N6-acetyllysine Ref.5

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Experimental info

Mutagenesis

T → A: Greatly reduced transactivation activity. Ref.4

Mutagenesis

T → D: No change in transactivation activity. Ref.4

Mutagenesis

25 – 26

ED → AG: Abolishes most of transactivation activity.

Mutagenesis

K → 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. Ref.7

Mutagenesis

270

K → A or R: No effect on DNA binding. Transactivation activity reduced by 50%. Loss of superactivation by CBP of EP300. Ref.5

Mutagenesis

284

K → A or R: No effect on DNA binding. No change in transactivation activity. No loss of superactivation by CBP or EP300. Ref.5 Ref.6

Mutagenesis

295

H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. Ref.6

Mutagenesis

325

H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. Ref.6

Mutagenesis

353

H → N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity. Ref.6

Sequence conflict

C → Y in AAC24497. Ref.3

Sequence conflict

116

A → T in AAC24497. Ref.3

Sequence conflict

223

G → P in AAC24497. Ref.3

Sequence conflict

287

S → T in AAC24497. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P46099 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 6FD59F294DDA45D1
Show »

FASTA

358

37,757

        10         20         30         40         50         60 
MASAETVLPS ISTLTTLGQF LDTQEDFLKW WRSEETQDLG PGPPNPTGPS LHVSLKSEDP 

        70         80         90        100        110        120 
SGEDDERDVT CAWDPDLFLT NFPGSESPGT SRTCALAPSV GPVAQFEPPE SLGAYAGGPG 

       130        140        150        160        170        180 
LVTGPLGSEE HTSWAHPTPR PPAPEPFVAP ALAPGLAPKA QPSYSDSRAG SVGGFFPRAG 

       190        200        210        220        230        240 
LAVPAAPGAP YGLLSGYPAL YPAPQYQGHF QLFRGLAAPS AGGTAPPSFL NCLGPGTVAT 

       250        260        270        280        290        300 
ELGATAIAGD AGLSPGTAPP KRSRRTLAPK RQAAHTCGHE GCGKSYSKSS HLKAHLRTHT 

       310        320        330        340        350 
GEKPYACSWD GCDWRFARSD ELTRHYRKHT GHRPFCCGLC PRAFSRSDHL ALHMKRHL

« Hide

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97200 mRNA. Translation: AAA37546.1. Different initiation. AF019074 Genomic DNA. Translation: AAB87861.1. AF033102 Genomic DNA. Translation: AAC24497.1.
IPI	IPI00230364.
PIR	A48060.
UniGene	Mm.4847.
3D structure databases
ProteinModelPortal	P46099.
SMR	P46099. Positions 275-358.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48738N.
PTM databases
PhosphoSite	P46099.
Proteomic databases
PRIDE	P46099.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:1342771. Klf1.
Phylogenomic databases
eggNOG	COG5048.
HOVERGEN	HBG006220.
InParanoid	P46099.
OrthoDB	EOG48SGTT.
Gene expression databases
CleanEx	MM_KLF1.
Genevestigator	P46099.
GermOnline	ENSMUSG00000054191. Mus musculus.
Family and domain databases
Gene3D	3.30.160.60. 3 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
SMART	SM00355. ZnF_C2H2. 3 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 3 hits. PS50157. ZINC_FINGER_C2H2_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

KLF1_MOUSE

Accession

Primary (citable) accession number: P46099
Secondary accession number(s): O70261

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents