[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. TISSUE=Pancreas; DOI=10.1074/jbc.273.40.25929; PubMed=9748269 [NCBI, ExPASy, EBI, Israel, Japan] Cook T., Gebelein B., Mesa K., Mladek A., Urrutia R.; "Molecular cloning and characterization of TIEG2 reveals a new subfamily of transforming growth factor-beta-inducible Sp1-like zinc finger-encoding genes involved in the regulation of cell growth."; J. Biol. Chem. 273:25929-25936(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. TISSUE=Erythroid cell; PubMed=10207080 [NCBI, ExPASy, EBI, Israel, Japan] Asano H., Li X.S., Stamatoyannopoulos G.; "FKLF, a novel Kruppel-like factor that activates human embryonic and fetal beta-like globin genes."; Mol. Cell. Biol. 19:3571-3579(1999).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Hepatoma; DOI=10.1006/geno.2000.6362; PubMed=11087666 [NCBI, ExPASy, EBI, Israel, Japan] Scohy S., Gabant P., Van Reeth T., Hertveldt V., Dreze P.-L., Van Vooren P., Riviere M., Szpirer J., Szpirer C.; "Identification of KLF13 and KLF14 (SP6), novel members of the SP/XKLF transcription factor family."; Genomics 70:93-101(2000).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	VARIANTS MODY7 MET-220 AND SER-347, VARIANT ARG-62, CHARACTERIZATION OF VARIANTS MODY7 MET-220 AND SER-347, AND CHARACTERIZATION OF VARIANT ARG-62. DOI=10.1073/pnas.0409177102; PubMed=15774581 [NCBI, ExPASy, EBI, Israel, Japan] Neve B., Fernandez-Zapico M.E., Ashkenazi-Katalan V., Dina C., Hamid Y.H., Joly E., Vaillant E., Benmezroua Y., Durand E., Bakaher N., Delannoy V., Vaxillaire M., Cook T., Dallinga-Thie G.M., Jansen H., Charles M.-A., Clement K., Galan P., Hercberg S., Helbecque N., Charpentier G., Prentki M., Hansen T., Pedersen O., Urrutia R., Melloul D., Froguel P.; "Role of transcription factor KLF11 and its diabetes-associated gene variants in pancreatic beta cell function."; Proc. Natl. Acad. Sci. U.S.A. 102:4807-4812(2005).

Comments

FUNCTION: Transcription factor. Activates the epsilon- and gamma-globin gene promoters and, to a much lower degree, the beta-globin gene and represses promoters containing SP1-like binding inhibiting cell growth. Represses transcription of SMAD7 which enhances TGF-beta signaling. Induces apoptosis.
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Ubiquitous. Higher expression in erythroid cells.
INDUCTION: By TGF-beta.
DISEASE: Defects in KLF11 are the cause of maturity-onset diabetes of the young type 7 (MODY7) [MIM:610508]. MODY [MIM:606391] has an autosomal dominant inheritance, onset at age less than 25 years and a primary defect in insulin secretion. MODY pedigrees are usually multigenerational families with penetrance of 80 to 95%. Patients have a nonobese body habitus and the so-called metabolic syndrome characterized by diabetes, insulin resistance, hypertension, and hypertriglyceridemia is absent.
SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
SIMILARITY: Contains 3 C2H2-type zinc fingers.
CAUTION: PubMed:11087666 sequence was originally thought to originate from mouse.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF028008; AAC61880.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF272830; AAF75793.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063286; AAH63286.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069383; AAH69383.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074922; AAH74922.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00024692; -.

NP_003588.1; -.

3D structure databases

PDB

1PO4; Model; -; A=40-52.

[ExPASy / RCSB / EBI]

PDBsum

1PO4; -.

ModBase

O14901.

Protein-protein interaction databases

IntAct

O14901; 1.

PTM databases

PhosphoSite

O14901; -.

Organism-specific databases

GC02P010100; -.

HIX0001814; -.

HGNC:11811; KLF11.

603301; gene. [NCBI / EBI]
606391; phenotype. [NCBI / EBI]
610508; phenotype. [NCBI / EBI]

Orphanet

552; MODY syndrome.
101057; MODY7.

PharmGKB

PA36518; -.

Gene expression databases

O14901; -.

O14901; -.

HS_KLF11; -.

ENSG00000172059; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (traceable author statement from ProtInc).
GO:0003700;	Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0008285;	Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
GO:0006366;	Biological process: transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
IPR013087; Znf_C2H2/integrase_DNA-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.

Pfam

PF00096; zf-C2H2; 3.
Pfam graphical view of domain structure.

ProDom

PD000003; Znf_C2H2; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00355; ZnF_C2H2; 3.
SMART graphical view of domain structure.

PROSITE

PS00028; ZINC_FINGER_C2H2_1; 3.
PS50157; ZINC_FINGER_C2H2_2; 3.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O14901; -.

Genome annotation databases

Ensembl

ENSG00000172059; Homo sapiens. [Contig view]

GeneID

8462; -.

KEGG

hsa:8462; -.

Phylogenomic databases

HOGENOM

O14901; -.

HOVERGEN

O14901; -.

OMA

O14901; CSPKNYE.

Other

31670; -.

KLF11; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Apoptosis; Diabetes mellitus; Disease mutation; DNA-binding; Metal-binding; Nucleus; Polymorphism; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Krueppel-like factor 11.`	`PRO_0000047180`
`ZN_FING`	`394 418`	`25`	`C2H2-type 1.`
`ZN_FING`	`424 448`	`25`	`C2H2-type 2.`
`ZN_FING`	`454 476`	`23`	`C2H2-type 3.`
`VARIANT`	`62 62`	`1`	`Q -> R (high frequency in individuals with diabetes mellitus type 2; increased repression activity; increased binding to mSin3A; impairs activation of insulin promoter; dbSNP:rs35927125 [NCBI]).`	`VAR_031522`
`VARIANT`	`220 220`	`1`	`T -> M (in MODY7; absent in one family member with diabetes; increased repression activity; no alteration in binding affinity to mSin3A; dbSNP:rs34336420 [NCBI]).`	`VAR_031523`
`VARIANT`	`347 347`	`1`	`A -> S (in MODY7; increased repression activity; no alteration in binding affinity to mSin3A).`	`VAR_031524`
`VARIANT`	`378 378`	`1`	`S -> F (in dbSNP:rs35476458 [NCBI]).`	`VAR_052717`
`CONFLICT`	`125 125`		`P -> S (in Ref. 3).`
`CONFLICT`	`144 150`		`VVARALS -> QWPDSD (in Ref. 3).`
`CONFLICT`	`371 371`		`P -> L (in Ref. 3).`
`CONFLICT`	`415 415`		`L -> V (in Ref. 3).`
`HELIX`	`43 49`	`7`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 55139 Da [This is the MW of the unprocessed precursor]

CRC64: A69863B5467FB068 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHTPDFAGPD DARAVDIMDI CESILERKRH DSERSTCSIL EQTDMEAVEA LVCMSSWGQR 

        70         80         90        100        110        120 
SQKGDLLRIR PLTPVSDSGD VTTTVHMDAA TPELPKDFHS LSTLCITPPQ SPDLVEPSTR 

       130        140        150        160        170        180 
TPVSPQVTDS KACTATDVLQ SSAVVARALS GGAERGLLGL EPVPSSPCRA KGTSVIRHTG 

       190        200        210        220        230        240 
ESPAACFPTI QTPDCRLSDS REGEEQLLGH FETLQDTHLT DSLLSTNLVS CQPCLHKSGG 

       250        260        270        280        290        300 
LLLTDKGQQA GWPGAVQTCS PKNYENDLPR KTTPLISVSV PAPPVLCQMI PVTGQSSMLP 

       310        320        330        340        350        360 
AFLKPPPQLS VGTVRPILAQ AAPAPQPVFV GPAVPQGAVM LVLPQGALPP PAPCAANVMA 

       370        380        390        400        410        420 
AGNTKLLPLA PAPVFITSSQ NCVPQVDFSR RRNYVCSFPG CRKTYFKSSH LKAHLRTHTG 

       430        440        450        460        470        480 
EKPFNCSWDG CDKKFARSDE LSRHRRTHTG EKKFVCPVCD RRFMRSDHLT KHARRHMTTK 

       490        500        510 
KIPGWQAEVG KLNRIASAES PGSPLVSMPA SA

O14901 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools