Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P55199

- ELL_HUMAN

UniProt

P55199 - ELL_HUMAN

Protein

RNA polymerase II elongation factor ELL

Gene

ELL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. 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, PubMed:23932780). Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (PubMed:23932780). 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.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei46 – 461KMT2A/MLL1 fusion point (in acute myeloid leukemia patient)

    GO - Molecular functioni

    1. phosphatase binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. gene expression Source: Reactome
    2. in utero embryonic development Source: Ensembl
    3. negative regulation of phosphatase activity Source: UniProtKB
    4. positive regulation of DNA-templated transcription, elongation Source: ProtInc
    5. positive regulation of viral transcription Source: Reactome
    6. transcription elongation from RNA polymerase II promoter Source: Reactome
    7. transcription from RNA polymerase II promoter Source: Reactome
    8. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. 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
    Synonyms:C19orf17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:23114. ELL.

    Subcellular locationi

    Nucleus. Nucleus speckle. NucleusCajal body
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving ELL is found in acute leukemias. Translocation t(11;19)(q23;p13.1) with KMT2A/MLL1. The result is a rogue activator protein.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA134939610.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 621620RNA polymerase II elongation factor ELLPRO_0000146733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei309 – 3091Phosphoserine2 Publications
    Modified residuei561 – 5611Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP55199.
    PaxDbiP55199.
    PRIDEiP55199.

    PTM databases

    PhosphoSiteiP55199.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested. Highest levels found in placenta, skeletal muscle, testis and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiP55199.
    BgeeiP55199.
    CleanExiHS_ELL.
    GenevestigatoriP55199.

    Organism-specific databases

    HPAiHPA046076.

    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 AFF4; the interaction is direct. Interacts with EAF1 and EAF2. Interacts with ICE1 (via N-terminus domain). Interacts with ICE2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP1CAP621362EBI-1245868,EBI-357253
    SNF8Q96H203EBI-1245868,EBI-747719

    Protein-protein interaction databases

    BioGridi113828. 32 interactions.
    IntActiP55199. 17 interactions.
    MINTiMINT-1511207.
    STRINGi9606.ENSP00000262809.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi207 – 21711
    Helixi222 – 23211
    Helixi236 – 24813
    Beta strandi249 – 2524
    Beta strandi254 – 2563
    Beta strandi258 – 2603
    Helixi265 – 2684
    Helixi279 – 29113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DOANMR-A200-292[»]
    ProteinModelPortaliP55199.
    SMRiP55199. Positions 204-297, 508-616.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55199.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi445 – 45915Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ELL/occludin family.Curated

    Phylogenomic databases

    eggNOGiNOG321810.
    HOGENOMiHOG000112356.
    HOVERGENiHBG005578.
    InParanoidiP55199.
    KOiK15183.
    OMAiCIQQYVS.
    OrthoDBiEOG7P02HN.
    PhylomeDBiP55199.
    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.

    P55199-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALKEDRSY GLSCGRVSDG SKVSVFHVKL TDSALRAFES YRARQDSVSL    50
    RPSIRFQGSQ GHISIPQPDC PAEARTFSFY LSNIGRDNPQ GSFDCIQQYV 100
    SSHGEVHLDC LGSIQDKITV CATDDSYQKA RQSMAQAEEE TRSRSAIVIK 150
    AGGRYLGKKV QFRKPAPGAT DAVPSRKRAT PINLASAIRK SGASAVSGGS 200
    GVSQRPFRDR VLHLLALRPY RKAELLLRLQ KDGLTQADKD ALDGLLQQVA 250
    NMSAKDGTCT LQDCMYKDVQ KDWPGYSEGD QQLLKRVLVR KLCQPQSTGS 300
    LLGDPAASSP PGERGRSASP PQKRLQPPDF IDPLANKKPR ISHFTQRAQP 350
    AVNGKLGVPN GREALLPTPG PPASTDTLSS STHLPPRLEP PRAHDPLADV 400
    SNDLGHSGRD CEHGEAAAPA PTVRLGLPLL TDCAQPSRPH GSPSRSKPKK 450
    KSKKHKDKER AAEDKPRAQL PDCAPATHAT PGAPADTPGL NGTCSVSSVP 500
    TSTSETPDYL LKYAAISSSE QRQSYKNDFN AEYSEYRDLH ARIERITRRF 550
    TQLDAQLRQL SQGSEEYETT RGQILQEYRK IKKTNTNYSQ EKHRCEYLHS 600
    KLAHIKRLIA EYDQRQLQAW P 621
    Length:621
    Mass (Da):68,265
    Last modified:October 1, 1996 - v1
    Checksum:iEB4A3F94CA8A411F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti297 – 2971S → N.
    Corresponds to variant rs2303694 [ dbSNP | Ensembl ].
    VAR_053072
    Natural varianti387 – 3871R → W.
    Corresponds to variant rs35245196 [ dbSNP | Ensembl ].
    VAR_053073

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16282 mRNA. Translation: AAA57120.1.
    BC049195 mRNA. Translation: AAH49195.1.
    CCDSiCCDS12380.1.
    PIRiI38880.
    RefSeqiNP_006523.1. NM_006532.3.
    UniGeneiHs.515260.

    Genome annotation databases

    EnsembliENST00000262809; ENSP00000262809; ENSG00000105656.
    GeneIDi8178.
    KEGGihsa:8178.
    UCSCiuc002njg.3. human.

    Polymorphism databases

    DMDMi1706635.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16282 mRNA. Translation: AAA57120.1 .
    BC049195 mRNA. Translation: AAH49195.1 .
    CCDSi CCDS12380.1.
    PIRi I38880.
    RefSeqi NP_006523.1. NM_006532.3.
    UniGenei Hs.515260.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DOA NMR - A 200-292 [» ]
    ProteinModelPortali P55199.
    SMRi P55199. Positions 204-297, 508-616.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113828. 32 interactions.
    IntActi P55199. 17 interactions.
    MINTi MINT-1511207.
    STRINGi 9606.ENSP00000262809.

    PTM databases

    PhosphoSitei P55199.

    Polymorphism databases

    DMDMi 1706635.

    Proteomic databases

    MaxQBi P55199.
    PaxDbi P55199.
    PRIDEi P55199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262809 ; ENSP00000262809 ; ENSG00000105656 .
    GeneIDi 8178.
    KEGGi hsa:8178.
    UCSCi uc002njg.3. human.

    Organism-specific databases

    CTDi 8178.
    GeneCardsi GC19M018553.
    H-InvDB HIX0038310.
    HGNCi HGNC:23114. ELL.
    HPAi HPA046076.
    MIMi 600284. gene.
    neXtProti NX_P55199.
    PharmGKBi PA134939610.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321810.
    HOGENOMi HOG000112356.
    HOVERGENi HBG005578.
    InParanoidi P55199.
    KOi K15183.
    OMAi CIQQYVS.
    OrthoDBi EOG7P02HN.
    PhylomeDBi P55199.
    TreeFami TF326161.

    Enzyme and pathway databases

    Reactomei REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    ChiTaRSi ELL. human.
    EvolutionaryTracei P55199.
    GeneWikii ELL_(gene).
    GenomeRNAii 8178.
    NextBioi 30861.
    PROi P55199.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55199.
    Bgeei P55199.
    CleanExi HS_ELL.
    Genevestigatori P55199.

    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. "Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia."
      Thirman M.J., Levitan D.A., Kobayashi H., Simon M.C., Rowley J.D.
      Proc. Natl. Acad. Sci. U.S.A. 91:12110-12114(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "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].
      Tissue: Brain.
    3. "An RNA polymerase II elongation factor encoded by the human ELL gene."
      Shilatifard A., Lane W.S., Jackson K.W., Conaway R.C., Conaway J.W.
      Science 271:1873-1876(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION ELONGATION.
    4. "EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein."
      Simone F., Polak P.E., Kaberlein J.J., Luo R.T., Levitan D.A., Thirman M.J.
      Blood 98:201-209(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EAF1, SUBCELLULAR LOCATION.
    5. "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties."
      Simone F., Luo R.T., Polak P.E., Kaberlein J.J., Thirman M.J.
      Blood 101:2355-2362(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EAF2, SUBCELLULAR LOCATION.
    6. "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia."
      Polak P.E., Simone F., Kaberlein J.J., Luo R.T., Thirman M.J.
      Mol. Biol. Cell 14:1517-1528(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL."
      Kong S.E., Banks C.A., Shilatifard A., Conaway J.W., Conaway R.C.
      Proc. Natl. Acad. Sci. U.S.A. 102:10094-10098(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription."
      He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q.
      Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
    11. "AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia."
      Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.
      Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
    12. "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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEC COMPLEX, IDENTIFICATION IN THE LEC COMPLEX, INTERACTION WITH ICE1 AND ICE2.
    14. "ELL facilitates RNA polymerase II pause site entry and release."
      Byun J.S., Fufa T.D., Wakano C., Fernandez A., Haggerty C.M., Sung M.H., Gardner K.
      Nat. Commun. 3:633-633(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The super elongation complex (SEC) family in transcriptional control."
      Luo Z., Lin C., Shilatifard A.
      Nat. Rev. Mol. Cell Biol. 13:543-547(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON THE SUPER ELONGATION COMPLEX.
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. "The little elongation complex functions at initiation and elongation phases of snRNA gene transcription."
      Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C., Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C., Shilatifard A.
      Mol. Cell 51:493-505(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, INTERACTION WITH ICE1.
    18. "Solution structure of the helical domain in human eleven-nineteen lysine-rich leukemia protein ELL."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAY-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 197-297.

    Entry informationi

    Entry nameiELL_HUMAN
    AccessioniPrimary (citable) accession number: P55199
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 129 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3