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Protein

RNA polymerase II elongation factor ELL

Gene

ELL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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 transcription elongation from RNA polymerase II promoter Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  7. positive regulation of viral transcription Source: Reactome
  8. snRNA transcription from RNA polymerase III promoter Source: UniProtKB
  9. snRNA transcription from RNA polymerase II promoter Source: UniProtKB
  10. transcription elongation from RNA polymerase II promoter Source: Reactome
  11. transcription from RNA polymerase II promoter Source: Reactome
  12. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
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.

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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:23114. ELL.

Subcellular locationi

  1. Nucleus
  2. Nucleus speckle
  3. NucleusCajal body

  4. 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
  2. histone locus body Source: UniProtKB
  3. nuclear speck Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. transcriptionally active chromatin Source: UniProtKB
  6. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiELL.
DMDMi1706635.

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

BgeeiP55199.
CleanExiHS_ELL.
ExpressionAtlasiP55199. baseline and differential.
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. 35 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 – 21711Combined sources
Helixi222 – 23211Combined sources
Helixi236 – 24813Combined sources
Beta strandi249 – 2524Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2603Combined sources
Helixi265 – 2684Combined sources
Helixi279 – 29113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074378.
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

        10         20         30         40         50
MAALKEDRSY GLSCGRVSDG SKVSVFHVKL TDSALRAFES YRARQDSVSL
60 70 80 90 100
RPSIRFQGSQ GHISIPQPDC PAEARTFSFY LSNIGRDNPQ GSFDCIQQYV
110 120 130 140 150
SSHGEVHLDC LGSIQDKITV CATDDSYQKA RQSMAQAEEE TRSRSAIVIK
160 170 180 190 200
AGGRYLGKKV QFRKPAPGAT DAVPSRKRAT PINLASAIRK SGASAVSGGS
210 220 230 240 250
GVSQRPFRDR VLHLLALRPY RKAELLLRLQ KDGLTQADKD ALDGLLQQVA
260 270 280 290 300
NMSAKDGTCT LQDCMYKDVQ KDWPGYSEGD QQLLKRVLVR KLCQPQSTGS
310 320 330 340 350
LLGDPAASSP PGERGRSASP PQKRLQPPDF IDPLANKKPR ISHFTQRAQP
360 370 380 390 400
AVNGKLGVPN GREALLPTPG PPASTDTLSS STHLPPRLEP PRAHDPLADV
410 420 430 440 450
SNDLGHSGRD CEHGEAAAPA PTVRLGLPLL TDCAQPSRPH GSPSRSKPKK
460 470 480 490 500
KSKKHKDKER AAEDKPRAQL PDCAPATHAT PGAPADTPGL NGTCSVSSVP
510 520 530 540 550
TSTSETPDYL LKYAAISSSE QRQSYKNDFN AEYSEYRDLH ARIERITRRF
560 570 580 590 600
TQLDAQLRQL SQGSEEYETT RGQILQEYRK IKKTNTNYSQ EKHRCEYLHS
610 620
KLAHIKRLIA EYDQRQLQAW P
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiELL.

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:
EMBLi
GenBanki
DDBJi
Links Updated
U16282 mRNA. Translation: AAA57120.1.
BC049195 mRNA. Translation: AAH49195.1.
CCDSiCCDS12380.1.
PIRiI38880.
RefSeqiNP_006523.1. NM_006532.3.
UniGeneiHs.515260.

3D structure databases

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

Protein-protein interaction databases

BioGridi113828. 35 interactions.
IntActiP55199. 17 interactions.
MINTiMINT-1511207.
STRINGi9606.ENSP00000262809.

PTM databases

PhosphoSiteiP55199.

Polymorphism and mutation databases

BioMutaiELL.
DMDMi1706635.

Proteomic databases

MaxQBiP55199.
PaxDbiP55199.
PRIDEiP55199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8178.
GeneCardsiGC19M018553.
H-InvDBHIX0038310.
HGNCiHGNC:23114. ELL.
HPAiHPA046076.
MIMi600284. gene.
neXtProtiNX_P55199.
PharmGKBiPA134939610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321810.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiP55199.
KOiK15183.
OMAiCIQQYVS.
OrthoDBiEOG7P02HN.
PhylomeDBiP55199.
TreeFamiTF326161.

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
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

ChiTaRSiELL. human.
EvolutionaryTraceiP55199.
GeneWikiiELL_(gene).
GenomeRNAii8178.
NextBioi30861.
PROiP55199.
SOURCEiSearch...

Gene expression databases

BgeeiP55199.
CleanExiHS_ELL.
ExpressionAtlasiP55199. baseline and differential.
GenevestigatoriP55199.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 134 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.