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O08856

- ELL_MOUSE

UniProt

O08856 - ELL_MOUSE

Protein

RNA polymerase II elongation factor ELL

Gene

Ell

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription. ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription By similarity. Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968).By similarity1 Publication

    GO - Molecular functioni

    1. phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. in utero embryonic development Source: MGI
    2. negative regulation of phosphatase activity Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription elongation from RNA polymerase II promoter Source: InterPro

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_226490. RNA Polymerase II Transcription Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II elongation factor ELL
    Alternative name(s):
    Eleven-nineteen lysine-rich leukemia protein
    Gene namesi
    Name:Ell
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109377. Ell.

    Subcellular locationi

    Nucleus By similarity. Nucleus speckle By similarity. NucleusCajal body By similarity
    Note: Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes By similarity.By similarity

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB-SubCell
    2. nuclear speck Source: UniProtKB
    3. transcription elongation factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 602601RNA polymerase II elongation factor ELLPRO_0000146734Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei300 – 3001PhosphoserineBy similarity
    Modified residuei542 – 5421PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO08856.
    PRIDEiO08856.

    PTM databases

    PhosphoSiteiO08856.

    Expressioni

    Gene expression databases

    BgeeiO08856.
    CleanExiMM_ELL.
    GenevestigatoriO08856.

    Interactioni

    Subunit structurei

    Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts with ICE1 (via N-terminus domain). Interacts with ICE2. Interacts with AFF4; the interaction is direct. Interacts with EAF1 and EAF2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199432. 3 interactions.
    IntActiO08856. 3 interactions.
    STRINGi10090.ENSMUSP00000091163.

    Structurei

    3D structure databases

    ProteinModelPortaliO08856.
    SMRiO08856. Positions 201-295, 489-597.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ELL/occludin family.Curated

    Phylogenomic databases

    eggNOGiNOG321810.
    GeneTreeiENSGT00550000074378.
    HOGENOMiHOG000112356.
    HOVERGENiHBG005578.
    InParanoidiQ3TXY9.
    KOiK15183.
    OMAiCIQQYVS.
    OrthoDBiEOG7P02HN.
    TreeFamiTF326161.

    Family and domain databases

    InterProiIPR010844. Occludin_RNApol2_elong_fac_ELL.
    IPR019464. RNA_pol_II_elong_fac_ELL.
    [Graphical view]
    PfamiPF10390. ELL. 1 hit.
    PF07303. Occludin_ELL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O08856-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALKEARSY GLSCGRVSDG SRVSVFHVKL TDSALKAFES YRAHQDSVSL    50
    RPSIRFEGSQ GHISIPQPDC PEEVRAFSFY LSNIGRDSPQ GSFDCIQQYV 100
    SSYGDVHLDC LGSIQDKVTV CATDDSYQKA RQSMAQAEEE TRSRSAIVIK 150
    AGGRYMGKKV QFRKPAPGAA DAVPSRKRAT PINLASAIRK SSGSGASSVV 200
    QRPFRDRVLH LLALRPYRKA ELLLRLQKDG LTQADKDTLD SLLQQVASVN 250
    PKDGTCTLQD CMYKSLQKDW PGYSEGDRQL LKRMLMRKLC QPQNATTDSS 300
    PPREHGRSAS PSQKRPTDFI DPLASKKPRI SHFTQRAQPT LNGKLGAPNG 350
    HETLLPAPGP TPSDTLSSSH LPPRLEPPRT HDPLADVSND LGHSTQDYKH 400
    QEATPAPAPH LGLPLLTDFP QAEQPTSSSH THSRPKKKSK KHKDKERPPE 450
    ERPPAPQPDA PTAPALPPDA PGLNGACDNE PTSSSETPDY LLKYPAISSS 500
    EQRQSYKNDF NAEYSEYRSL HARIEQITRR FTQLDAQLRQ LSQGSDEYET 550
    TRGQILQEYR KIKKTNTNYS CEKRRCEYLH RKLAHIKRLI AEYDQRQLQA 600
    WP 602
    Length:602
    Mass (Da):67,146
    Last modified:July 27, 2011 - v2
    Checksum:iDECAD56CF19ABF4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031Y → H in AAC53150. (PubMed:9037066)Curated
    Sequence conflicti103 – 1031Y → H in AAH14816. (PubMed:15489334)Curated
    Sequence conflicti103 – 1031Y → H in AAH24894. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80227 mRNA. Translation: AAC53150.1.
    AK159027 mRNA. Translation: BAE34775.1.
    CH466569 Genomic DNA. Translation: EDL28843.1.
    BC014816 mRNA. Translation: AAH14816.1.
    BC024894 mRNA. Translation: AAH24894.1.
    CCDSiCCDS22372.1.
    RefSeqiNP_031950.2. NM_007924.2.
    UniGeneiMm.271973.

    Genome annotation databases

    EnsembliENSMUST00000093454; ENSMUSP00000091163; ENSMUSG00000070002.
    GeneIDi13716.
    KEGGimmu:13716.
    UCSCiuc009mau.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80227 mRNA. Translation: AAC53150.1 .
    AK159027 mRNA. Translation: BAE34775.1 .
    CH466569 Genomic DNA. Translation: EDL28843.1 .
    BC014816 mRNA. Translation: AAH14816.1 .
    BC024894 mRNA. Translation: AAH24894.1 .
    CCDSi CCDS22372.1.
    RefSeqi NP_031950.2. NM_007924.2.
    UniGenei Mm.271973.

    3D structure databases

    ProteinModelPortali O08856.
    SMRi O08856. Positions 201-295, 489-597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199432. 3 interactions.
    IntActi O08856. 3 interactions.
    STRINGi 10090.ENSMUSP00000091163.

    PTM databases

    PhosphoSitei O08856.

    Proteomic databases

    PaxDbi O08856.
    PRIDEi O08856.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000093454 ; ENSMUSP00000091163 ; ENSMUSG00000070002 .
    GeneIDi 13716.
    KEGGi mmu:13716.
    UCSCi uc009mau.1. mouse.

    Organism-specific databases

    CTDi 8178.
    MGIi MGI:109377. Ell.

    Phylogenomic databases

    eggNOGi NOG321810.
    GeneTreei ENSGT00550000074378.
    HOGENOMi HOG000112356.
    HOVERGENi HBG005578.
    InParanoidi Q3TXY9.
    KOi K15183.
    OMAi CIQQYVS.
    OrthoDBi EOG7P02HN.
    TreeFami TF326161.

    Enzyme and pathway databases

    Reactomei REACT_226490. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    ChiTaRSi ELL. mouse.
    NextBioi 284496.
    PROi O08856.
    SOURCEi Search...

    Gene expression databases

    Bgeei O08856.
    CleanExi MM_ELL.
    Genevestigatori O08856.

    Family and domain databases

    InterProi IPR010844. Occludin_RNApol2_elong_fac_ELL.
    IPR019464. RNA_pol_II_elong_fac_ELL.
    [Graphical view ]
    Pfami PF10390. ELL. 1 hit.
    PF07303. Occludin_ELL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Developmental analysis and subcellular localization of the murine homologue of ELL."
      Thirman M.J., Diskin E.B., Bin S.S., Ip H.S., Miller J.M., Simon M.C.
      Proc. Natl. Acad. Sci. U.S.A. 94:1408-1413(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Visual cortex.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Strain: FVB/N.
      Tissue: Liver and Mammary gland.
    5. Cited for: FUNCTION.

    Entry informationi

    Entry nameiELL_MOUSE
    AccessioniPrimary (citable) accession number: O08856
    Secondary accession number(s): Q3TXY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3