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Q60980

- KLF3_MOUSE

UniProt

Q60980 - KLF3_MOUSE

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Protein

Krueppel-like factor 3

Gene

Klf3

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

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri259 – 28325C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri289 – 31325C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri319 – 34123C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to peptide Source: Ensembl
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Krueppel-like factor 3
Alternative name(s):
Basic krueppel-like factor
CACCC-box-binding protein BKLF
TEF-2
Gene namesi
Name:Klf3
Synonyms:Bklf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1342773. Klf3.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101K → 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. 1 Publication
Mutagenesisi12 – 121E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. 1 Publication
Mutagenesisi197 – 1971K → 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. 1 Publication
Mutagenesisi199 – 1991E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. 1 Publication
Mutagenesisi341 – 3411H → A, D, E, N, Q or R: Little change in DNA-binding ability. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Krueppel-like factor 3PRO_0000047166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki10 – 10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity
Cross-linki197 – 197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei249 – 2491PhosphoserineBy similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ60980.
PRIDEiQ60980.

PTM databases

PhosphoSiteiQ60980.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ60980.
CleanExiMM_KLF3.
ExpressionAtlasiQ60980. baseline and differential.
GenevestigatoriQ60980.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi200965. 1 interaction.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi316 – 3194
Turni322 – 3243
Beta strandi328 – 3303
Helixi331 – 3388
Helixi339 – 3413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P7ANMR-A314-344[»]
1U85NMR-A314-344[»]
1U86NMR-A314-344[»]
ProteinModelPortaliQ60980.
SMRiQ60980. Positions 250-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60980.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7474Repressor domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi61 – 655CTBP-binding motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 250250Pro-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri259 – 28325C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri289 – 31325C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri319 – 34123C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118998.
HOGENOMiHOG000232138.
HOVERGENiHBG003941.
InParanoidiQ60980.
KOiK15605.
OMAiNSSMQVP.
OrthoDBiEOG747PJ4.
PhylomeDBiQ60980.
TreeFamiTF350556.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[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.

Q60980-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLMFDPVPVK QEAMDPVSVS FPSNYIESMK PNKYGVIYST PLPDKFFQTP
60 70 80 90 100
EGLTHGIQVE PVDLTVNKRG SPPAAGGSPS SLKFPSHRRA SPGLSMPSSS
110 120 130 140 150
PPIKKYSPPS PGVQPFGVPL SMPPVMAAAL SRHGIRSPGI LPVIQPVVVQ
160 170 180 190 200
PVPFMYTSHL QQPLMVSLSE EMDNSNSGMP VPVIESYEKP LLQKKIKIEP
210 220 230 240 250
GIEPQRTDYY PEEMSPPLMN PVSPPQALLQ ENHPSVIVQP GKRPLPVESP
260 270 280 290 300
DTQRKRRIHR CDYDGCNKVY TKSSHLKAHR RTHTGEKPYK CTWEGCTWKF
310 320 330 340
ARSDELTRHF RKHTGIKPFQ CPDCDRSFSR SDHLALHRKR HMLV
Length:344
Mass (Da):38,561
Last modified:November 1, 1996 - v1
Checksum:i2BB7E3B63A7C1D88
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U36340 mRNA. Translation: AAA93256.1.
CCDSiCCDS19301.1.
PIRiJC6100.
RefSeqiNP_032479.1. NM_008453.5.
XP_006503814.1. XM_006503751.1.
UniGeneiMm.392759.
Mm.439720.

Genome annotation databases

EnsembliENSMUST00000165536; ENSMUSP00000129363; ENSMUSG00000029178.
ENSMUST00000166409; ENSMUSP00000128429; ENSMUSG00000029178.
GeneIDi16599.
KEGGimmu:16599.
UCSCiuc008xmr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U36340 mRNA. Translation: AAA93256.1 .
CCDSi CCDS19301.1.
PIRi JC6100.
RefSeqi NP_032479.1. NM_008453.5.
XP_006503814.1. XM_006503751.1.
UniGenei Mm.392759.
Mm.439720.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P7A NMR - A 314-344 [» ]
1U85 NMR - A 314-344 [» ]
1U86 NMR - A 314-344 [» ]
ProteinModelPortali Q60980.
SMRi Q60980. Positions 250-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200965. 1 interaction.

PTM databases

PhosphoSitei Q60980.

Proteomic databases

MaxQBi Q60980.
PRIDEi Q60980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000165536 ; ENSMUSP00000129363 ; ENSMUSG00000029178 .
ENSMUST00000166409 ; ENSMUSP00000128429 ; ENSMUSG00000029178 .
GeneIDi 16599.
KEGGi mmu:16599.
UCSCi uc008xmr.1. mouse.

Organism-specific databases

CTDi 51274.
MGIi MGI:1342773. Klf3.

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000118998.
HOGENOMi HOG000232138.
HOVERGENi HBG003941.
InParanoidi Q60980.
KOi K15605.
OMAi NSSMQVP.
OrthoDBi EOG747PJ4.
PhylomeDBi Q60980.
TreeFami TF350556.

Miscellaneous databases

ChiTaRSi KLF3. mouse.
EvolutionaryTracei Q60980.
NextBioi 290173.
PROi Q60980.
SOURCEi Search...

Gene expression databases

Bgeei Q60980.
CleanExi MM_KLF3.
ExpressionAtlasi Q60980. baseline and differential.
Genevestigatori Q60980.

Family and domain databases

Gene3Di 3.30.160.60. 3 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 3 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiKLF3_MOUSE
AccessioniPrimary (citable) accession number: Q60980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3