O43474 (KLF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Krueppel-like factor 4

Alternative name(s):
Epithelial zinc finger protein EZF
Gut-enriched krueppel-like factor

Gene names

Name:	KLF4
Synonyms:	EZF, GKLF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription. Ref.10 Ref.15
Subunit structure	Interacts with POU5F1/OCT4 and SOX2 By similarity. Interacts with MUC1 (via the C-terminal domain). Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a Ref.10 Ref.17
Subcellular location	Nucleus.
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.12
Biotechnological use	POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Ref.11
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers.
Sequence caution	The sequence AAB48399.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC03462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAD42165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH29923.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH30811.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence ABG25917.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAG36271.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence EAW59020.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAW59021.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to cycloheximide Inferred from electronic annotation. Source: Ensembl cellular response to growth factor stimulus Inferred from direct assay PubMed 20551324. Source: BHF-UCL cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Ensembl cellular response to peptide Inferred from electronic annotation. Source: Ensembl epidermal cell differentiation Inferred from electronic annotation. Source: Ensembl epidermis morphogenesis Inferred from electronic annotation. Source: Ensembl fat cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL mesodermal cell fate determination Traceable author statement PubMed 8940147. Source: ProtInc negative regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Ensembl negative regulation of NF-kappaB transcription factor activity Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of cell migration involved in sprouting angiogenesis Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of cell proliferation Traceable author statement PubMed 8702718. Source: ProtInc negative regulation of chemokine (C-X-C motif) ligand 2 production Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of heterotypic cell-cell adhesion Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of inflammatory response Traceable author statement PubMed 20551324. Source: BHF-UCL negative regulation of interleukin-8 biosynthetic process Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of muscle hyperplasia Inferred from electronic annotation. Source: Ensembl negative regulation of phosphatidylinositol 3-kinase signaling Inferred from electronic annotation. Source: Ensembl negative regulation of protein kinase B signaling Inferred from electronic annotation. Source: Ensembl negative regulation of response to cytokine stimulus Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Ensembl negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 20551324. Source: BHF-UCL negative regulation of transcription, DNA-templated Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of hemoglobin biosynthetic process Inferred from mutant phenotype PubMed 21539536. Source: BHF-UCL positive regulation of protein metabolic process Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: BHF-UCL positive regulation of transcription, DNA-templated Inferred from sequence or structural similarity. Source: UniProtKB post-embryonic camera-type eye development Inferred from electronic annotation. Source: Ensembl post-embryonic hemopoiesis Inferred from mutant phenotype PubMed 21539536. Source: BHF-UCL regulation of cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB response to retinoic acid Inferred from electronic annotation. Source: Ensembl stem cell maintenance Inferred from sequence or structural similarity. Source: UniProtKB transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	nuclear chromatin Inferred from direct assay PubMed 21539536. Source: BHF-UCL nucleus Inferred from direct assay. Source: HPA transcription factor complex Inferred from electronic annotation. Source: Ensembl
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from mutant phenotype PubMed 21539536. Source: BHF-UCL RNA polymerase II transcription factor binding Inferred from physical interaction PubMed 21539536. Source: BHF-UCL RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 21539536. Source: BHF-UCL core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 21539536. Source: BHF-UCL double-stranded DNA binding Inferred from electronic annotation. Source: Ensembl phosphatidylinositol 3-kinase regulator activity Inferred from electronic annotation. Source: Ensembl protein binding Inferred from physical interaction PubMed 19751731. Source: IntAct sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: UniProtKB sequence-specific DNA binding transcription factor recruiting transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL transcription regulatory region DNA binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTBP1	Q13363	4	EBI-7232405,EBI-908846

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43474-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O43474-1)

The sequence of this isoform differs from the canonical sequence as follows:
     367-400: Missing.

Isoform 3 (identifier: O43474-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
     367-400: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: O43474-5)

Also known as: 1a;

The sequence of this isoform differs from the canonical sequence as follows:
     43-118: RWREELSHMK...LSNSLTHPPE → SSCHPVPACQ...VDGNSPAQMN
     119-513: Missing.

Isoform 5 (identifier: O43474-6)

The sequence of this isoform differs from the canonical sequence as follows:
     43-63: RWREELSHMKRLPPVLPGRPY → VRNLTTVTGTAVDGNSPAQMN
     64-513: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 513	513	Krueppel-like factor 4		PRO_0000047167
Regions
	Zinc finger	430 – 454	25	C2H2-type 1
	Zinc finger	460 – 484	25	C2H2-type 2
	Zinc finger	490 – 512	23	C2H2-type 3
	Region	473 – 504	32	Interaction with target DNA By similarity
	Motif	101 – 109	9	9aaTAD
	Compositional bias	125 – 149	25	Ser-rich
	Compositional bias	179 – 415	237	Pro-rich
Amino acid modifications
	Modified residue	254	1	Phosphoserine Ref.16
	Cross-link	32		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Natural variations
	Alternative sequence	1 – 50	50	Missing in isoform 3.		VSP_040569
	Alternative sequence	43 – 118	76	RWREE…THPPE → SSCHPVPACQRSPSQRGEDD RGPGKGPPPTLVITRAAAKP TQRVPISRHTCEPTQVRNLT TVTGTAVDGNSPAQMN in isoform 4.		VSP_047470
	Alternative sequence	43 – 63	21	RWREE…PGRPY → VRNLTTVTGTAVDGNSPAQM N in isoform 5.		VSP_047471
	Alternative sequence	64 – 513	450	Missing in isoform 5.		VSP_047472
	Alternative sequence	119 – 513	395	Missing in isoform 4.		VSP_047473
	Alternative sequence	367 – 400	34	Missing in isoform 2 and isoform 3.		VSP_036399
	Natural variant	315	1	T → S. Ref.4 Corresponds to variant rs1059913 [ dbSNP | Ensembl ].		VAR_059888
	Natural variant	321	1	L → F. Ref.4 Corresponds to variant rs1059914 [ dbSNP | Ensembl ].		VAR_059889
Experimental info
	Sequence conflict	60 – 61	2	GR → AG in AAC03462. Ref.1
	Sequence conflict	77	1	G → A in AAC03462. Ref.1
	Sequence conflict	251	1	S → T in AAC03462. Ref.1
	Sequence conflict	304	1	D → N in AAB48399. Ref.4
	Sequence conflict	329	1	D → E in AAB48399. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 3B6113A3EF333935	FASTA	513	54,671
	10 20 30 40 50 60 MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG 70 80 90 100 110 120 RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV 130 140 150 160 170 180 AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP 190 200 210 220 230 240 PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS 250 260 270 280 290 300 EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP 310 320 330 340 350 360 AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV 370 380 390 400 410 420 PPLHYQGQSR GFVARAGEPC VCWPHFGTHG MMLTPPSSPL ELMPPGSCMP EEPKPKRGRR 430 440 450 460 470 480 SWPRKRTATH TCDYAGCGKT YTKSSHLKAH LRTHTGEKPY HCDWDGCGWK FARSDELTRH 490 500 510 YRKHTGHRPF QCQKCDRAFS RSDHLALHMK RHF
	Isoform 2 [UniParc]. Checksum: 039095BBF3E3F78D	FASTA	479	51,076
	10 20 30 40 50 60 MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG 70 80 90 100 110 120 RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV 130 140 150 160 170 180 AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP 190 200 210 220 230 240 PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS 250 260 270 280 290 300 EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP 310 320 330 340 350 360 AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV 370 380 390 400 410 420 PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTATHTCDY AGCGKTYTKS SHLKAHLRTH 430 440 450 460 470 TGEKPYHCDW DGCGWKFARS DELTRHYRKH TGHRPFQCQK CDRAFSRSDH LALHMKRHF
	Isoform 3 [UniParc]. Checksum: 99B86BE95A31F23D	FASTA	429	45,639
	10 20 30 40 50 60 MKRLPPVLPG RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS 70 80 90 100 110 120 NSLTHPPESV AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG 130 140 150 160 170 180 LLYGRESAPP PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV 190 200 210 220 230 240 LKASLSAPGS EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA 250 260 270 280 290 300 GPPLSNGHRP AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS 310 320 330 340 350 360 FLPDQMQPQV PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTATHTCDY AGCGKTYTKS 370 380 390 400 410 420 SHLKAHLRTH TGEKPYHCDW DGCGWKFARS DELTRHYRKH TGHRPFQCQK CDRAFSRSDH LALHMKRHF
	Isoform 4 (1a) [UniParc]. Checksum: 9E900F0852665920	FASTA	118	12,329
	10 20 30 40 50 60 MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNSSCHPVPA CQRSPSQRGE 70 80 90 100 110 DDRGPGKGPP PTLVITRAAA KPTQRVPISR HTCEPTQVRN LTTVTGTAVD GNSPAQMN
	Isoform 5 [UniParc]. Checksum: 2A7B5BE789162A89	FASTA	63	6,489
	10 20 30 40 50 60 MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNVRNLTTVT GTAVDGNSPA QMN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human EZF, a Kruppel-like zinc finger protein, is expressed in vascular endothelial cells and contains transcriptional activation and repression domains." Yet S.-F., McA'Nulty M.M., Folta S.C., Yen H.-W., Yoshizumi M., Hsieh C.-M., Layne M.D., Chin M.T., Wang H., Perrella M.A., Jain M.K., Lee M.-E. J. Biol. Chem. 273:1026-1031(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Oncogene expression cloning by retroviral transduction of adenovirus E1A-immortalized rat kidney RK3E cells: transformation of a host with epithelial features by c-MYC and the zinc finger protein GKLF." Foster K.W., Ren S., Louro I.D., Lobo-Ruppert S.M., McKie-Bell P., Grizzle W., Hayes M.R., Broker T.R., Chow L.T., Ruppert J.M. Cell Growth Differ. 10:423-434(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Shaking the family tree: Identification of novel and biologically active alternatively spliced isoforms across the KLF family of transcription factors." Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B., Camacho S.C., Martignetti J.A. FASEB J. 27:432-436(2013) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), ALTERNATIVE SPLICING.
[4]	Garrett-Sinha L.A., de Crombrugghe B. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS SER-315 AND PHE-321. Tissue: Placenta.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Substantia nigra and Tongue.
[6]	SeattleSNPs variation discovery resource Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Cervix and Lung.
[10]	"Human mucin 1 oncoprotein represses transcription of the p53 tumor suppressor gene." Wei X., Xu H., Kufe D. Cancer Res. 67:1853-1858(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MUC1, FUNCTION.
[11]	"Induction of pluripotent stem cells from adult human fibroblasts by defined factors." Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K., Yamanaka S. Cell 131:861-872(2007) [PubMed] [Europe PMC] [Abstract] Cited for: BIOTECHNOLOGY.
[12]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells." Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X. Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32. Tissue: Cervix carcinoma.
[15]	"Kruppel-like factor 4 (Klf4) prevents embryonic stem (ES) cell differentiation by regulating Nanog gene expression." Zhang P., Andrianakos R., Yang Y., Liu C., Lu W. J. Biol. Chem. 285:9180-9189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1." Bjerke G.A., Hyman-Walsh C., Wotton D. Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PBX1 AND MEIS2.
[18]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF022184 mRNA. Translation: AAC03462.1. Different initiation. AF105036 mRNA. Translation: AAD42165.1. Different initiation. HF546201 mRNA. Translation: CCO02787.1. HF546202 mRNA. Translation: CCO02788.1. U70663 mRNA. Translation: AAB48399.1. Different initiation. AK095134 mRNA. Translation: BAG52991.1. AK313489 mRNA. Translation: BAG36271.1. Different initiation. DQ658241 Genomic DNA. Translation: ABG25917.1. Sequence problems. AL360218 Genomic DNA. Translation: CAI12254.2. CH471105 Genomic DNA. Translation: EAW59020.1. Sequence problems. CH471105 Genomic DNA. Translation: EAW59021.1. Sequence problems. BC029923 mRNA. Translation: AAH29923.1. Different initiation. BC030811 mRNA. Translation: AAH30811.1. Different initiation.
CCDS	CCDS6770.2. [O43474-1]
RefSeq	NP_004226.3. NM_004235.4. [O43474-1] XP_005252362.1. XM_005252305.1. [O43474-3]
UniGene	Hs.376206.
3D structure databases
ProteinModelPortal	O43474.
SMR	O43474. Positions 427-513.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	114726. 21 interactions.
DIP	DIP-57667N.
IntAct	O43474. 2 interactions.
MINT	MINT-7261942.
STRING	9606.ENSP00000363804.
PTM databases
PhosphoSite	O43474.
Proteomic databases
MaxQB	O43474.
PaxDb	O43474.
PRIDE	O43474.
Protocols and materials databases
DNASU	9314.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374672; ENSP00000363804; ENSG00000136826. [O43474-1]
GeneID	9314.
KEGG	hsa:9314.
UCSC	uc004bdf.2. human. [O43474-4] uc004bdg.3. human. [O43474-1] uc004bdh.3. human. [O43474-3]
Organism-specific databases
CTD	9314.
GeneCards	GC09M110247.
HGNC	HGNC:6348. KLF4.
HPA	HPA002926.
MIM	602253. gene.
neXtProt	NX_O43474.
PharmGKB	PA30138.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOVERGEN	HBG006220.
KO	K17846.
OMA	CTVGRPL.
PhylomeDB	O43474.
TreeFam	TF350556.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
SignaLink	O43474.
Gene expression databases
ArrayExpress	O43474.
Bgee	O43474.
CleanEx	HS_KLF4.
Genevestigator	O43474.
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
GeneWiki	KLF4.
GenomeRNAi	9314.
NextBio	34891.
PRO	O43474.
SOURCE	Search...

Entry information

Entry name

KLF4_HUMAN

Accession

Primary (citable) accession number: O43474
Secondary accession number(s): B2R8S4 , B3KT79, L0R3I6, L0R4N5, P78338, Q5T3J8, Q5T3J9, Q8N717, Q9UNP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 10, 2009
Last modified:	July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.