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P55199

- ELL_HUMAN

UniProt

P55199 - ELL_HUMAN

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Protein
RNA polymerase II elongation factor ELL
Gene
ELL, C19orf17
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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.5 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
Complete GO annotation...

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 speckle. NucleusCajal body
Note: Colocalizes with EAF2 to nuclear speckles. Also localized to Cajal (coiled) bodies.3 Publications

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
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 621620RNA polymerase II elongation factor ELL
PRO_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, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with AFF4; the interaction is direct. Interacts with EAF1 and EAF2.4 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

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.

Miscellaneous databases

EvolutionaryTraceiP55199.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi445 – 45915Nuclear localization signal Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the ELL/occludin family.

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

« 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. "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.
  14. "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.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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: September 3, 2014
This is version 128 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

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