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O75461

- E2F6_HUMAN

UniProt

O75461 - E2F6_HUMAN

Protein

Transcription factor E2F6

Gene

E2F6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi50 – 12980Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. sequence-specific DNA binding transcription factor activity Source: Ensembl
    3. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    2. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Ensembl
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiO75461.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F6
    Short name:
    E2F-6
    Gene namesi
    Name:E2F6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3120. E2F6.

    Subcellular locationi

    GO - Cellular componenti

    1. MLL1 complex Source: UniProtKB
    2. nucleus Source: MGI
    3. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681L → E: Reduction in repressor activity, little effect on S-phase entry.

    Organism-specific databases

    PharmGKBiPA27578.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281Transcription factor E2F6PRO_0000219472Add
    BLAST

    Proteomic databases

    MaxQBiO75461.
    PaxDbiO75461.
    PRIDEiO75461.

    PTM databases

    PhosphoSiteiO75461.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined. Highest levels in placenta, skeletal muscle, heart, ovary, kidney, small intestine and spleen.

    Gene expression databases

    ArrayExpressiO75461.
    BgeeiO75461.
    CleanExiHS_E2F6.
    GenevestigatoriO75461.

    Interactioni

    Subunit structurei

    Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.2 Publications

    Protein-protein interaction databases

    BioGridi108208. 30 interactions.
    DIPiDIP-41699N.
    IntActiO75461. 4 interactions.
    MINTiMINT-158232.
    STRINGi9606.ENSP00000370936.

    Structurei

    3D structure databases

    ProteinModelPortaliO75461.
    SMRiO75461. Positions 63-126, 143-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 22293DimerizationSequence AnalysisAdd
    BLAST
    Regioni143 – 16422Leucine-zipperAdd
    BLAST
    Regioni173 – 281109Transcription repressionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi95 – 12935DEF boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi265 – 2684Poly-Glu

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG251536.
    HOGENOMiHOG000112309.
    HOVERGENiHBG002227.
    InParanoidiO75461.
    KOiK09390.
    OMAiMNASVMT.
    PhylomeDBiO75461.
    TreeFamiTF105566.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR015633. E2F.
    IPR003316. E2F_TDP.
    IPR015635. Transcription_factor_E2F6.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF19. PTHR12081:SF19. 1 hit.
    PfamiPF02319. E2F_TDP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75461-1) [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

    MSQQRPARKL PSLLLDPTEE TVRRRCRDPI NVEGLLPSKI RINLEDNVQY    50
    VSMRKALKVK RPRFDVSLVY LTRKFMDLVR SAPGGILDLN KVATKLGVRK 100
    RRVYDITNVL DGIDLVEKKS KNHIRWIGSD LSNFGAVPQQ KKLQEELSDL 150
    SAMEDALDEL IKDCAQQLFE LTDDKENERL AYVTYQDIHS IQAFHEQIVI 200
    AVKAPAETRL DVPAPREDSI TVHIRSTNGP IDVYLCEVEQ GQTSNKRSEG 250
    VGTSSSESTH PEGPEEEENP QQSEELLEVS N 281
    Length:281
    Mass (Da):31,844
    Last modified:November 1, 1998 - v1
    Checksum:i539E049C15AD3508
    GO
    Isoform 2 (identifier: O75461-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: Missing.

    Show »
    Length:206
    Mass (Da):22,982
    Checksum:i6C79669AFD6F42EC
    GO
    Isoform 3 (identifier: O75461-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLL → MNPS

    Show »
    Length:249
    Mass (Da):28,103
    Checksum:i49DE2FD637490D32
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 82AR → HE in AAC14694. (PubMed:9501179)Curated
    Sequence conflicti66 – 661V → A in AAT02637. (PubMed:15081404)Curated
    Sequence conflicti220 – 2201I → V in AAC14694. (PubMed:9501179)Curated
    Sequence conflicti229 – 2291G → E in AAC14694. (PubMed:9501179)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575Missing in isoform 2. 1 PublicationVSP_008771Add
    BLAST
    Alternative sequencei1 – 3636MSQQR…VEGLL → MNPS in isoform 3. 1 PublicationVSP_054754Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059292 mRNA. Translation: AAC31426.1.
    AY083996 mRNA. Translation: AAM10783.1.
    AY083997 Genomic DNA. Translation: AAM10784.1.
    AY083997 Genomic DNA. Translation: AAM10785.1.
    AY551347 mRNA. Translation: AAT02637.1.
    AJ493061 Genomic DNA. Translation: CAD37950.1.
    AK290413 mRNA. Translation: BAF83102.1.
    AC099344 Genomic DNA. Translation: AAY14826.1.
    CH471053 Genomic DNA. Translation: EAX00931.1.
    BC008348 mRNA. Translation: AAH08348.1.
    BC107740 mRNA. Translation: AAI07741.1.
    AF041381 mRNA. Translation: AAC14694.1.
    CCDSiCCDS1680.2. [O75461-1]
    CCDS62858.1. [O75461-2]
    CCDS62859.1. [O75461-3]
    RefSeqiNP_001265204.1. NM_001278275.1. [O75461-3]
    NP_001265205.1. NM_001278276.1. [O75461-2]
    NP_001265206.1. NM_001278277.1. [O75461-2]
    NP_001265207.1. NM_001278278.1. [O75461-2]
    NP_937987.2. NM_198256.3. [O75461-1]
    XP_005246211.1. XM_005246154.2. [O75461-2]
    XP_005246212.1. XM_005246155.2. [O75461-2]
    UniGeneiHs.603093.

    Genome annotation databases

    EnsembliENST00000307236; ENSP00000302159; ENSG00000169016. [O75461-3]
    ENST00000381525; ENSP00000370936; ENSG00000169016. [O75461-1]
    ENST00000542100; ENSP00000446315; ENSG00000169016. [O75461-2]
    ENST00000546212; ENSP00000438864; ENSG00000169016. [O75461-2]
    GeneIDi1876.
    KEGGihsa:1876.
    UCSCiuc002rbe.4. human. [O75461-1]
    uc002rbf.4. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059292 mRNA. Translation: AAC31426.1 .
    AY083996 mRNA. Translation: AAM10783.1 .
    AY083997 Genomic DNA. Translation: AAM10784.1 .
    AY083997 Genomic DNA. Translation: AAM10785.1 .
    AY551347 mRNA. Translation: AAT02637.1 .
    AJ493061 Genomic DNA. Translation: CAD37950.1 .
    AK290413 mRNA. Translation: BAF83102.1 .
    AC099344 Genomic DNA. Translation: AAY14826.1 .
    CH471053 Genomic DNA. Translation: EAX00931.1 .
    BC008348 mRNA. Translation: AAH08348.1 .
    BC107740 mRNA. Translation: AAI07741.1 .
    AF041381 mRNA. Translation: AAC14694.1 .
    CCDSi CCDS1680.2. [O75461-1 ]
    CCDS62858.1. [O75461-2 ]
    CCDS62859.1. [O75461-3 ]
    RefSeqi NP_001265204.1. NM_001278275.1. [O75461-3 ]
    NP_001265205.1. NM_001278276.1. [O75461-2 ]
    NP_001265206.1. NM_001278277.1. [O75461-2 ]
    NP_001265207.1. NM_001278278.1. [O75461-2 ]
    NP_937987.2. NM_198256.3. [O75461-1 ]
    XP_005246211.1. XM_005246154.2. [O75461-2 ]
    XP_005246212.1. XM_005246155.2. [O75461-2 ]
    UniGenei Hs.603093.

    3D structure databases

    ProteinModelPortali O75461.
    SMRi O75461. Positions 63-126, 143-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108208. 30 interactions.
    DIPi DIP-41699N.
    IntActi O75461. 4 interactions.
    MINTi MINT-158232.
    STRINGi 9606.ENSP00000370936.

    PTM databases

    PhosphoSitei O75461.

    Proteomic databases

    MaxQBi O75461.
    PaxDbi O75461.
    PRIDEi O75461.

    Protocols and materials databases

    DNASUi 1876.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307236 ; ENSP00000302159 ; ENSG00000169016 . [O75461-3 ]
    ENST00000381525 ; ENSP00000370936 ; ENSG00000169016 . [O75461-1 ]
    ENST00000542100 ; ENSP00000446315 ; ENSG00000169016 . [O75461-2 ]
    ENST00000546212 ; ENSP00000438864 ; ENSG00000169016 . [O75461-2 ]
    GeneIDi 1876.
    KEGGi hsa:1876.
    UCSCi uc002rbe.4. human. [O75461-1 ]
    uc002rbf.4. human.

    Organism-specific databases

    CTDi 1876.
    GeneCardsi GC02M011584.
    H-InvDB HIX0060106.
    HGNCi HGNC:3120. E2F6.
    MIMi 602944. gene.
    neXtProti NX_O75461.
    PharmGKBi PA27578.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251536.
    HOGENOMi HOG000112309.
    HOVERGENi HBG002227.
    InParanoidi O75461.
    KOi K09390.
    OMAi MNASVMT.
    PhylomeDBi O75461.
    TreeFami TF105566.

    Enzyme and pathway databases

    SignaLinki O75461.

    Miscellaneous databases

    GenomeRNAii 1876.
    NextBioi 7671.
    PROi O75461.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75461.
    Bgeei O75461.
    CleanExi HS_E2F6.
    Genevestigatori O75461.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR015633. E2F.
    IPR003316. E2F_TDP.
    IPR015635. Transcription_factor_E2F6.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF19. PTHR12081:SF19. 1 hit.
    Pfami PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Unusual proliferation arrest and transcriptional control properties of a newly discovered E2F family member, E2F-6."
      Gaubatz S., Wood J.G., Livingston D.M.
      Proc. Natl. Acad. Sci. U.S.A. 95:9190-9195(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "E2F-6: a novel member of the E2F family is an inhibitor of E2F-dependent transcription."
      Cartwright P., Mueller H., Wagener C., Holm K., Helin K.
      Oncogene 17:611-623(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    3. "Sequence for human E2F-6 alternative transcript."
      Salih M., Tuana B.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
      Tissue: Heart.
    4. "Human E2F6 is alternatively spliced to generate multiple protein isoforms."
      Kherrouche Z., De Launoit Y., Monte D.
      Biochem. Biophys. Res. Commun. 317:749-760(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "Cloning, genomic organisation and chromosomal mapping of the human E2F6/EMA gene."
      Schwertfeger N., Taudien S., Truss M., Morkel M., Pohlers M., Gruska I., Haaf T., Rosenthal A., Hagemeier C.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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 1).
      Tissue: Umbilical cord blood.
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. 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] (ISOFORM 1).
      Tissue: Lung.
    10. "E2F-6, a member of the E2F family that can behave as a transcriptional repressor."
      Trimarchi J.M., Fairchild B., Verona R., Moberg K., Andon N., Lees J.A.
      Proc. Natl. Acad. Sci. U.S.A. 95:2850-2855(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-281 (ISOFORM 1).
      Tissue: Fetal brain.
    11. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
      Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
      Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH TFDP1; MAX; MGA; EUHMTASE1; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
    12. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.

    Entry informationi

    Entry nameiE2F6_HUMAN
    AccessioniPrimary (citable) accession number: O75461
    Secondary accession number(s): A8K2Z8
    , G5E936, O60544, Q53QY9, Q6Q9Z6, Q7Z2H6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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 2
      Human chromosome 2: 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

    Dasty 3