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Krueppel-like factor 8 (Basic krueppel-like factor 3) (Zinc finger protein 741)

 KLF8_HUMAN              Reviewed;         359 AA.
O95600; B4DJN3; E7EQQ8; L0R3U8; L0R4U2; Q2M246; Q59GV5; Q5HYQ5;
Q5JXP7; Q6MZJ7; Q9UGC4;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
30-AUG-2017, entry version 149.
RecName: Full=Krueppel-like factor 8;
AltName: Full=Basic krueppel-like factor 3;
AltName: Full=Zinc finger protein 741;
Name=KLF8; Synonyms=BKLF3, ZNF741;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Gorski J.L., MacDonald M., Vananthwerp M., Burright E.N., Bialecki M.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND ALTERNATIVE
SPLICING.
PubMed=23134681; DOI=10.1096/fj.12-220319;
Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B.,
Camacho S.C., Martignetti J.A.;
"Shaking the family tree: Identification of novel and biologically
active alternatively spliced isoforms across the KLF family of
transcription factors.";
FASEB J. 27:432-436(2013).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=10756197; DOI=10.1093/nar/28.9.1955;
van Vliet J., Turner J., Crossley M.;
"Human Kruppel-like factor 8: a CACCC-box binding protein that
associates with CtBP and represses transcription.";
Nucleic Acids Res. 28:1955-1962(2000).
[9]
FUNCTION.
PubMed=12820964; DOI=10.1016/S1097-2765(03)00179-5;
Zhao J., Bian Z.C., Yee K., Chen B.P., Chien S., Guan J.L.;
"Identification of transcription factor KLF8 as a downstream target of
focal adhesion kinase in its regulation of cyclin D1 and cell cycle
progression.";
Mol. Cell 11:1503-1515(2003).
[10]
SUMOYLATION AT LYS-67, INTERACTION WITH PIAS1; PIAS2 AND PIAS4,
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-67 AND LYS-217.
PubMed=16617055; DOI=10.1074/jbc.M513135200;
Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L.,
Zhao J.;
"Sumoylation delimits KLF8 transcriptional activity associated with
the cell cycle regulation.";
J. Biol. Chem. 281:16664-16671(2006).
-!- FUNCTION: Transcriptional repressor and activator. Binds to CACCC-
boxes promoter elements. Also binds the GT-box of cyclin D1
promoter and mediates cell cycle progression at G(1) phase as a
downstream target of focal adhesion kinase (FAK).
{ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:12820964,
ECO:0000269|PubMed:16617055}.
-!- SUBUNIT: Interacts with corepressor CtBP2. Interacts with PIAS1,
PIAS2, AND PIAS4; the interaction with each ligase sumoylates
KLF8. {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:16617055}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617055}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95600-1; Sequence=Displayed;
Name=2;
IsoId=O95600-3; Sequence=VSP_045460;
Name=3;
IsoId=O95600-4; Sequence=VSP_047480, VSP_045460;
Name=4;
IsoId=O95600-5; Sequence=VSP_047481;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10756197}.
-!- PTM: Sumoylation at Lys-67 represses transcriptional activity and
reduces cell cycle progression into the G(1) phase. Has no effect
on subcellular location. {ECO:0000269|PubMed:16617055}.
-!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; U28282; AAC99849.1; -; mRNA.
EMBL; HF546207; CCO02793.1; -; mRNA.
EMBL; HF546208; CCO02794.1; -; mRNA.
EMBL; HF546209; CCO02795.1; -; mRNA.
EMBL; AK296156; BAG58895.1; -; mRNA.
EMBL; AB209004; BAD92241.1; ALT_SEQ; mRNA.
EMBL; BX641066; CAE46033.1; ALT_SEQ; mRNA.
EMBL; BX322609; CAI41397.1; -; Genomic_DNA.
EMBL; AL050309; CAI41397.1; JOINED; Genomic_DNA.
EMBL; AL050309; CAI42343.1; -; Genomic_DNA.
EMBL; BX322609; CAI42343.1; JOINED; Genomic_DNA.
EMBL; BC105130; AAI05131.1; -; mRNA.
EMBL; BC112109; AAI12110.1; -; mRNA.
CCDS; CCDS14373.1; -. [O95600-1]
CCDS; CCDS55428.1; -. [O95600-3]
RefSeq; NP_001152768.1; NM_001159296.2. [O95600-3]
RefSeq; NP_001311028.1; NM_001324099.1. [O95600-4]
RefSeq; NP_001311029.1; NM_001324100.1. [O95600-5]
RefSeq; NP_001311031.1; NM_001324102.1. [O95600-1]
RefSeq; NP_009181.2; NM_007250.5. [O95600-1]
RefSeq; XP_005262034.1; XM_005261977.2. [O95600-1]
RefSeq; XP_005262036.1; XM_005261979.3. [O95600-1]
RefSeq; XP_006724638.1; XM_006724575.2. [O95600-3]
UniGene; Hs.646614; -.
ProteinModelPortal; O95600; -.
SMR; O95600; -.
BioGrid; 116435; 13.
ELM; O95600; -.
IntAct; O95600; 6.
MINT; MINT-7969747; -.
STRING; 9606.ENSP00000417303; -.
iPTMnet; O95600; -.
PhosphoSitePlus; O95600; -.
BioMuta; KLF8; -.
PaxDb; O95600; -.
PeptideAtlas; O95600; -.
PRIDE; O95600; -.
DNASU; 11279; -.
Ensembl; ENST00000374928; ENSP00000364063; ENSG00000102349. [O95600-3]
Ensembl; ENST00000468660; ENSP00000417303; ENSG00000102349. [O95600-1]
Ensembl; ENST00000640927; ENSP00000492126; ENSG00000102349. [O95600-4]
GeneID; 11279; -.
KEGG; hsa:11279; -.
UCSC; uc004dur.4; human. [O95600-1]
CTD; 11279; -.
DisGeNET; 11279; -.
GeneCards; KLF8; -.
HGNC; HGNC:6351; KLF8.
HPA; HPA071740; -.
MIM; 300286; gene.
neXtProt; NX_O95600; -.
OpenTargets; ENSG00000102349; -.
PharmGKB; PA30141; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118998; -.
HOVERGEN; HBG003941; -.
InParanoid; O95600; -.
KO; K09205; -.
OMA; PAAMTQM; -.
OrthoDB; EOG091G1BN0; -.
PhylomeDB; O95600; -.
TreeFam; TF350556; -.
SIGNOR; O95600; -.
GeneWiki; KLF8; -.
GenomeRNAi; 11279; -.
PRO; PR:O95600; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102349; -.
CleanEx; HS_KLF8; -.
ExpressionAtlas; O95600; baseline and differential.
Genevisible; O95600; HS.
GO; GO:0016235; C:aggresome; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:NTNU_SB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 359 Krueppel-like factor 8.
/FTId=PRO_0000047176.
ZN_FING 274 298 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 304 328 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 334 356 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
CROSSLNK 67 67 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
VAR_SEQ 1 27 MVDMDKLINNLEVQLNSEGGSMQVFKQ -> MSLPEDGMSS
GHFRSPQLVTWS (in isoform 3).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047480.
VAR_SEQ 216 299 Missing (in isoform 4).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047481.
VAR_SEQ 254 359 PAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAH
RRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFR
CTDCNRSFSRSDHLSLHRRRHDTM -> REAL (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:23134681}.
/FTId=VSP_045460.
MUTAGEN 67 67 K->R: Abolishes sumoylation. No change in
nuclear location. Increases
transcriptional activity and cell cycle
progression. Abolishes sumoylation; when
associated with R-217.
{ECO:0000269|PubMed:16617055}.
MUTAGEN 217 217 K->R: No change in sumoylation. Abolishes
sumoylation; when associated with R-67.
{ECO:0000269|PubMed:16617055}.
CONFLICT 167 167 S -> I (in Ref. 3; BAG58895).
{ECO:0000305}.
CONFLICT 263 263 E -> G (in Ref. 1; AAC99849).
{ECO:0000305}.
SEQUENCE 359 AA; 39314 MW; F8FDCC1FD477C04F CRC64;
MVDMDKLINN LEVQLNSEGG SMQVFKQVTA SVRNRDPPEI EYRSNMTSPT LLDANPMENP
ALFNDIKIEP PEELLASDFS LPQVEPVDLS FHKPKAPLQP ASMLQAPIRP PKPQSSPQTL
VVSTSTSDMS TSANIPTVLT PGSVLTSSQS TGSQQILHVI HTIPSVSLPN KMGGLKTIPV
VVQSLPMVYT TLPADGGPAA ITVPLIGGDG KNAGSVKVDP TSMSPLEIPS DSEESTIESG
SSALQSLQGL QQEPAAMAQM QGEESLDLKR RRIHQCDFAG CSKVYTKSSH LKAHRRIHTG
EKPYKCTWDG CSWKFARSDE LTRHFRKHTG IKPFRCTDCN RSFSRSDHLS LHRRRHDTM


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18-003-42295 Krueppel-like factor 1 - Erythroid krueppel-like transcription factor; EKLF; Erythroid transcription factor Polyclonal 0.1 mg Protein A
25-012 ZNF263 belongs to the krueppel C2H2-type zinc-finger protein family. It contains 9 C2H2-type zinc fingers, 1 KRAB domain and 1 SCAN box domain. ZNF263 might play an important role in basic cellular pr 0.05 mg
EIAAB46848 Hkr3,Krueppel-related zinc finger protein 3,Mouse,Mus musculus,Protein HKR3,Zbtb48,Zinc finger and BTB domain-containing protein 48


 

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