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Q60980 (KLF3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Krueppel-like factor 3
Alternative name(s):
Basic krueppel-like factor
CACCC-box-binding protein BKLF
TEF-2
Gene names
Name:Klf3
Synonyms:Bklf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the CACCC box of erythroid cell-expressed genes. May play a role in hematopoiesis. Ref.1 Ref.2

Subunit structure

Monomer. Ref.3

Subcellular location

Nucleus Probable.

Tissue specificity

In 8.5 day embryos, expressed in midbrain, anterior hindbrain and ventral forebrain. In 9 day embryos, expressed throughout ventral anterior half of embryo including midbrain-hindbrain junction, ventral midbrain, diencephalon and forebrain. At 10.5 days, distribution is more widespread with expression also found in developing limb buds. Widely expressed in the adult. Ref.1

Post-translational modification

Sumoylated with SUMO1. Sumoylation is enhanced by PIAS1, PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances transcriptional repression, but has no effect on DNA binding. Sumoylation on Lys-197 is the major site. Ref.2

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 3 C2H2-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Krueppel-like factor 3
PRO_0000047166

Regions

Zinc finger259 – 28325C2H2-type 1
Zinc finger289 – 31325C2H2-type 2
Zinc finger319 – 34123C2H2-type 3
Region1 – 7474Repressor domain
Motif61 – 655CTBP-binding motif
Compositional bias1 – 250250Pro-rich

Amino acid modifications

Modified residue911Phosphoserine By similarity
Modified residue1001Phosphoserine By similarity
Modified residue1101Phosphoserine By similarity
Modified residue2491Phosphoserine By similarity
Cross-link10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.2
Cross-link197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.2

Experimental info

Mutagenesis101K → A: Reduced sumoylation levels. No effect on DNA-binding and slight reduction of transcriptional repression. Abolishes sumoylation. No effect on DNA-binding but great reduction in transcriptional repression; when associated with A-197. Ref.2
Mutagenesis121E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. Ref.2
Mutagenesis1971K → A: Reduced sumoylation levels. No effect on DNA-binding and slight reduction of transcriptional repression. Abolishes sumoylation. No effect on DNA-binding but great reduction of transcriptional repression; when associated with A-10. Ref.2
Mutagenesis1991E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. Ref.2
Mutagenesis3411H → A, D, E, N, Q or R: Little change in DNA-binding ability. Ref.3

Secondary structure

......... 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60980 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2BB7E3B63A7C1D88

FASTA34438,561
        10         20         30         40         50         60 
MLMFDPVPVK QEAMDPVSVS FPSNYIESMK PNKYGVIYST PLPDKFFQTP EGLTHGIQVE 

        70         80         90        100        110        120 
PVDLTVNKRG SPPAAGGSPS SLKFPSHRRA SPGLSMPSSS PPIKKYSPPS PGVQPFGVPL 

       130        140        150        160        170        180 
SMPPVMAAAL SRHGIRSPGI LPVIQPVVVQ PVPFMYTSHL QQPLMVSLSE EMDNSNSGMP 

       190        200        210        220        230        240 
VPVIESYEKP LLQKKIKIEP GIEPQRTDYY PEEMSPPLMN PVSPPQALLQ ENHPSVIVQP 

       250        260        270        280        290        300 
GKRPLPVESP DTQRKRRIHR CDYDGCNKVY TKSSHLKAHR RTHTGEKPYK CTWEGCTWKF 

       310        320        330        340 
ARSDELTRHF RKHTGIKPFQ CPDCDRSFSR SDHLALHRKR HMLV 

« Hide

References

[1]"Isolation and characterization of the cDNA encoding BKLF/TEF-2, a major CACCC-box-binding protein in erythroid cells and selected other cells."
Crossley M., Whitelaw E., Perkins A., Williams G., Fujiwara Y., Orkin S.H.
Mol. Cell. Biol. 16:1695-1705(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: DBA.
Tissue: Leukemia.
[2]"Role for SUMO modification in facilitating transcriptional repression by BKLF."
Perdomo J., Verger A., Turner J., Crossley M.
Mol. Cell. Biol. 25:1549-1559(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-10 AND LYS-197, FUNCTION, MUTAGENESIS OF LYS-10; GLU-12; LYS-197 AND GLU-199.
[3]"CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions."
Simpson R.J.Y., Cram E.D., Czolij R., Matthews J.M., Crossley M., Mackay J.P.
J. Biol. Chem. 278:28011-28018(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 314-344 OF WILD TYPE AND MUTANT FORMS, SUBUNIT, DNA-BINDING, MUTAGENESIS OF HIS-341.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36340 mRNA. Translation: AAA93256.1.
CCDSCCDS19301.1.
PIRJC6100.
RefSeqNP_032479.1. NM_008453.5.
XP_006503814.1. XM_006503751.1.
UniGeneMm.392759.
Mm.439720.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P7ANMR-A314-344[»]
1U85NMR-A314-344[»]
1U86NMR-A314-344[»]
ProteinModelPortalQ60980.
SMRQ60980. Positions 216-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200965. 1 interaction.

PTM databases

PhosphoSiteQ60980.

Proteomic databases

MaxQBQ60980.
PRIDEQ60980.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165536; ENSMUSP00000129363; ENSMUSG00000029178.
ENSMUST00000166409; ENSMUSP00000128429; ENSMUSG00000029178.
GeneID16599.
KEGGmmu:16599.
UCSCuc008xmr.1. mouse.

Organism-specific databases

CTD51274.
MGIMGI:1342773. Klf3.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00750000117621.
HOGENOMHOG000232138.
HOVERGENHBG003941.
InParanoidQ60980.
KOK15605.
OMANSSMQVP.
OrthoDBEOG747PJ4.
PhylomeDBQ60980.
TreeFamTF350556.

Gene expression databases

ArrayExpressQ60980.
BgeeQ60980.
CleanExMM_KLF3.
GenevestigatorQ60980.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKLF3. mouse.
EvolutionaryTraceQ60980.
NextBio290173.
PROQ60980.
SOURCESearch...

Entry information

Entry nameKLF3_MOUSE
AccessionPrimary (citable) accession number: Q60980
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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