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O95600

- KLF8_HUMAN

UniProt

O95600 - KLF8_HUMAN

Protein

Krueppel-like factor 8

Gene

KLF8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (02 Nov 2001)
      Previous versions | rss
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    Functioni

    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 G1 phase as a downstream target of focal adhesion kinase (FAK).3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri274 – 29825C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32825C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri334 – 35623C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Krueppel-like factor 8
    Alternative name(s):
    Basic krueppel-like factor 3
    Zinc finger protein 741
    Gene namesi
    Name:KLF8
    Synonyms:BKLF3, ZNF741
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6351. KLF8.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671K → R: Abolishes sumoylation. No change in nuclear location. Increases transcriptional activity and cell cycle progression. Abolishes sumoylation; when associated with R-217. 1 Publication
    Mutagenesisi217 – 2171K → R: No change in sumoylation. Abolishes sumoylation; when associated with R-67. 1 Publication

    Organism-specific databases

    PharmGKBiPA30141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Krueppel-like factor 8PRO_0000047176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki67 – 67Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylation at Lys-67 represses transcriptional activity and reduces cell cycle progression into the G1 phase. Has no effect on subcellular location.1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiO95600.
    PRIDEiO95600.

    PTM databases

    PhosphoSiteiO95600.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiO95600.
    BgeeiO95600.
    CleanExiHS_KLF8.
    GenevestigatoriO95600.

    Interactioni

    Subunit structurei

    Interacts with corepressor CtBP2. Interacts with PIAS1, PIAS2, AND PIAS4; the interaction with each ligase sumoylates KLF8.2 Publications

    Protein-protein interaction databases

    BioGridi116435. 9 interactions.
    IntActiO95600. 1 interaction.
    MINTiMINT-7969747.
    STRINGi9606.ENSP00000417303.

    Structurei

    3D structure databases

    ProteinModelPortaliO95600.
    SMRiO95600. Positions 274-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri274 – 29825C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32825C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri334 – 35623C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOVERGENiHBG003941.
    InParanoidiO95600.
    KOiK09205.
    OMAiPVQIRDP.
    OrthoDBiEOG7Z69CW.
    PhylomeDBiO95600.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95600-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MVDMDKLINN LEVQLNSEGG SMQVFKQVTA SVRNRDPPEI EYRSNMTSPT    50
    LLDANPMENP ALFNDIKIEP PEELLASDFS LPQVEPVDLS FHKPKAPLQP 100
    ASMLQAPIRP PKPQSSPQTL VVSTSTSDMS TSANIPTVLT PGSVLTSSQS 150
    TGSQQILHVI HTIPSVSLPN KMGGLKTIPV VVQSLPMVYT TLPADGGPAA 200
    ITVPLIGGDG KNAGSVKVDP TSMSPLEIPS DSEESTIESG SSALQSLQGL 250
    QQEPAAMAQM QGEESLDLKR RRIHQCDFAG CSKVYTKSSH LKAHRRIHTG 300
    EKPYKCTWDG CSWKFARSDE LTRHFRKHTG IKPFRCTDCN RSFSRSDHLS 350
    LHRRRHDTM 359
    Length:359
    Mass (Da):39,314
    Last modified:November 2, 2001 - v2
    Checksum:iF8FDCC1FD477C04F
    GO
    Isoform 2 (identifier: O95600-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         254-359: PAAMAQMQGE...SLHRRRHDTM → REAL

    Show »
    Length:257
    Mass (Da):27,242
    Checksum:i86CF13DBD7494270
    GO
    Isoform 3 (identifier: O95600-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MVDMDKLINNLEVQLNSEGGSMQVFKQ → MSLPEDGMSSGHFRSPQLVTWS
         254-359: PAAMAQMQGE...SLHRRRHDTM → REAL

    Show »
    Length:252
    Mass (Da):26,623
    Checksum:i0B68B09E33AC87A8
    GO
    Isoform 4 (identifier: O95600-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         216-299: Missing.

    Show »
    Length:275
    Mass (Da):30,050
    Checksum:i7CB5F2431F0E06D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671S → I in BAG58895. (PubMed:14702039)Curated
    Sequence conflicti263 – 2631E → G in AAC99849. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MVDMD…QVFKQ → MSLPEDGMSSGHFRSPQLVT WS in isoform 3. 1 PublicationVSP_047480Add
    BLAST
    Alternative sequencei216 – 29984Missing in isoform 4. 1 PublicationVSP_047481Add
    BLAST
    Alternative sequencei254 – 359106PAAMA…RHDTM → REAL in isoform 2 and isoform 3. 2 PublicationsVSP_045460Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28282 mRNA. Translation: AAC99849.1.
    HF546207 mRNA. Translation: CCO02793.1.
    HF546208 mRNA. Translation: CCO02794.1.
    HF546209 mRNA. Translation: CCO02795.1.
    AK296156 mRNA. Translation: BAG58895.1.
    AB209004 mRNA. Translation: BAD92241.1. Sequence problems.
    BX641066 mRNA. Translation: CAE46033.1. Sequence problems.
    BX322609, AL050309 Genomic DNA. Translation: CAI41397.1.
    AL050309, BX322609 Genomic DNA. Translation: CAI42343.1.
    BC105130 mRNA. Translation: AAI05131.1.
    BC112109 mRNA. Translation: AAI12110.1.
    CCDSiCCDS14373.1. [O95600-1]
    CCDS55428.1. [O95600-3]
    RefSeqiNP_001152768.1. NM_001159296.1. [O95600-3]
    NP_009181.2. NM_007250.4. [O95600-1]
    XP_005262034.1. XM_005261977.1. [O95600-1]
    XP_005262035.1. XM_005261978.1. [O95600-1]
    XP_005262036.1. XM_005261979.1. [O95600-1]
    XP_006724638.1. XM_006724575.1. [O95600-3]
    UniGeneiHs.646614.

    Genome annotation databases

    EnsembliENST00000374928; ENSP00000364063; ENSG00000102349. [O95600-3]
    ENST00000468660; ENSP00000417303; ENSG00000102349. [O95600-1]
    GeneIDi11279.
    KEGGihsa:11279.
    UCSCiuc004dur.3. human. [O95600-1]
    uc011mop.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28282 mRNA. Translation: AAC99849.1 .
    HF546207 mRNA. Translation: CCO02793.1 .
    HF546208 mRNA. Translation: CCO02794.1 .
    HF546209 mRNA. Translation: CCO02795.1 .
    AK296156 mRNA. Translation: BAG58895.1 .
    AB209004 mRNA. Translation: BAD92241.1 . Sequence problems.
    BX641066 mRNA. Translation: CAE46033.1 . Sequence problems.
    BX322609 , AL050309 Genomic DNA. Translation: CAI41397.1 .
    AL050309 , BX322609 Genomic DNA. Translation: CAI42343.1 .
    BC105130 mRNA. Translation: AAI05131.1 .
    BC112109 mRNA. Translation: AAI12110.1 .
    CCDSi CCDS14373.1. [O95600-1 ]
    CCDS55428.1. [O95600-3 ]
    RefSeqi NP_001152768.1. NM_001159296.1. [O95600-3 ]
    NP_009181.2. NM_007250.4. [O95600-1 ]
    XP_005262034.1. XM_005261977.1. [O95600-1 ]
    XP_005262035.1. XM_005261978.1. [O95600-1 ]
    XP_005262036.1. XM_005261979.1. [O95600-1 ]
    XP_006724638.1. XM_006724575.1. [O95600-3 ]
    UniGenei Hs.646614.

    3D structure databases

    ProteinModelPortali O95600.
    SMRi O95600. Positions 274-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116435. 9 interactions.
    IntActi O95600. 1 interaction.
    MINTi MINT-7969747.
    STRINGi 9606.ENSP00000417303.

    PTM databases

    PhosphoSitei O95600.

    Proteomic databases

    PaxDbi O95600.
    PRIDEi O95600.

    Protocols and materials databases

    DNASUi 11279.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374928 ; ENSP00000364063 ; ENSG00000102349 . [O95600-3 ]
    ENST00000468660 ; ENSP00000417303 ; ENSG00000102349 . [O95600-1 ]
    GeneIDi 11279.
    KEGGi hsa:11279.
    UCSCi uc004dur.3. human. [O95600-1 ]
    uc011mop.2. human.

    Organism-specific databases

    CTDi 11279.
    GeneCardsi GC0XP056275.
    HGNCi HGNC:6351. KLF8.
    MIMi 300286. gene.
    neXtProti NX_O95600.
    PharmGKBi PA30141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOVERGENi HBG003941.
    InParanoidi O95600.
    KOi K09205.
    OMAi PVQIRDP.
    OrthoDBi EOG7Z69CW.
    PhylomeDBi O95600.
    TreeFami TF350556.

    Miscellaneous databases

    GeneWikii KLF8.
    GenomeRNAii 11279.
    NextBioi 42937.
    PROi O95600.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95600.
    Bgeei O95600.
    CleanExi HS_KLF8.
    Genevestigatori O95600.

    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. Gorski J.L., MacDonald M., Vananthwerp M., Burright E.N., Bialecki M.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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 2; 3 AND 4), ALTERNATIVE SPLICING.
    3. "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] (ISOFORM 2).
      Tissue: Thalamus.
    4. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    6. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain.
    8. "Human Kruppel-like factor 8: a CACCC-box binding protein that associates with CtBP and represses transcription."
      van Vliet J., Turner J., Crossley M.
      Nucleic Acids Res. 28:1955-1962(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    9. "Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression."
      Zhao J., Bian Z.C., Yee K., Chen B.P., Chien S., Guan J.L.
      Mol. Cell 11:1503-1515(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation."
      Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L., Zhao J.
      J. Biol. Chem. 281:16664-16671(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-67, INTERACTION WITH PIAS1; PIAS2 AND PIAS4, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-67 AND LYS-217.

    Entry informationi

    Entry nameiKLF8_HUMAN
    AccessioniPrimary (citable) accession number: O95600
    Secondary accession number(s): B4DJN3
    , E7EQQ8, L0R3U8, L0R4U2, Q2M246, Q59GV5, Q5HYQ5, Q5JXP7, Q6MZJ7, Q9UGC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: November 2, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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