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Protein

Krueppel-like factor 3

Gene

Klf3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri259 – 283C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri289 – 313C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri319 – 341C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1342773. Klf3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10K → 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 Publication1
Mutagenesisi12E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. 1 Publication1
Mutagenesisi197K → 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 Publication1
Mutagenesisi199E → A: Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. 1 Publication1
Mutagenesisi341H → A, D, E, N, Q or R: Little change in DNA-binding ability. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000471661 – 344Krueppel-like factor 3Add BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei71PhosphoserineBy similarity1
Modified residuei91PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei107PhosphoserineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei215PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1
Modified residuei249PhosphoserineBy similarity1

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.
PaxDbiQ60980.
PRIDEiQ60980.

PTM databases

iPTMnetiQ60980.
PhosphoSitePlusiQ60980.

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

BgeeiENSMUSG00000029178.
CleanExiMM_KLF3.
ExpressionAtlasiQ60980. baseline and differential.
GenevisibleiQ60980. MM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi200965. 2 interactors.
STRINGi10090.ENSMUSP00000128429.

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi316 – 319Combined sources4
Turni322 – 324Combined sources3
Beta strandi328 – 330Combined sources3
Helixi331 – 338Combined sources8
Helixi339 – 341Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P7ANMR-A314-344[»]
1U85NMR-A314-344[»]
1U86NMR-A314-344[»]
ProteinModelPortaliQ60980.
SMRiQ60980.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60980.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 74Repressor domainAdd BLAST74

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi61 – 65CTBP-binding motif5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 250Pro-richAdd BLAST250

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri259 – 283C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri289 – 313C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri319 – 341C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118998.
HOGENOMiHOG000232138.
HOVERGENiHBG003941.
InParanoidiQ60980.
KOiK15605.
OrthoDBiEOG091G1BN0.
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]
PfamiPF00096. zf-C2H2. 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.

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:
EMBLi
GenBanki
DDBJi
Links Updated
U36340 mRNA. Translation: AAA93256.1.
CCDSiCCDS19301.1.
PIRiJC6100.
RefSeqiNP_032479.1. NM_008453.5.
XP_006503814.1. XM_006503751.3.
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:
EMBLi
GenBanki
DDBJi
Links Updated
U36340 mRNA. Translation: AAA93256.1.
CCDSiCCDS19301.1.
PIRiJC6100.
RefSeqiNP_032479.1. NM_008453.5.
XP_006503814.1. XM_006503751.3.
UniGeneiMm.392759.
Mm.439720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P7ANMR-A314-344[»]
1U85NMR-A314-344[»]
1U86NMR-A314-344[»]
ProteinModelPortaliQ60980.
SMRiQ60980.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200965. 2 interactors.
STRINGi10090.ENSMUSP00000128429.

PTM databases

iPTMnetiQ60980.
PhosphoSitePlusiQ60980.

Proteomic databases

MaxQBiQ60980.
PaxDbiQ60980.
PRIDEiQ60980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51274.
MGIiMGI:1342773. Klf3.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118998.
HOGENOMiHOG000232138.
HOVERGENiHBG003941.
InParanoidiQ60980.
KOiK15605.
OrthoDBiEOG091G1BN0.
PhylomeDBiQ60980.
TreeFamiTF350556.

Miscellaneous databases

ChiTaRSiKlf3. mouse.
EvolutionaryTraceiQ60980.
PROiQ60980.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029178.
CleanExiMM_KLF3.
ExpressionAtlasiQ60980. baseline and differential.
GenevisibleiQ60980. MM.

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]
PfamiPF00096. zf-C2H2. 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...

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: November 2, 2016
This is version 147 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

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.