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P55199 (ELL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II elongation factor ELL
Alternative name(s):
Eleven-nineteen lysine-rich leukemia protein
Gene names
Name:ELL
Synonyms:C19orf17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.7 Ref.10 Ref.11 Ref.13

Subunit structure

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. Ref.4 Ref.5 Ref.10 Ref.11

Subcellular location

Nucleus speckle. NucleusCajal body. Note: Colocalizes with EAF2 to nuclear speckles. Also localized to Cajal (coiled) bodies. Ref.4 Ref.5 Ref.6

Tissue specificity

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

Involvement in disease

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.

Sequence similarities

Belongs to the ELL/occludin family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 621620RNA polymerase II elongation factor ELL
PRO_0000146733

Regions

Motif445 – 45915Nuclear localization signal Potential

Sites

Site461KMT2A/MLL1 fusion point (in acute myeloid leukemia patient)

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue3091Phosphoserine Ref.9 Ref.12
Modified residue5611Phosphoserine Ref.8

Natural variations

Natural variant2971S → N.
Corresponds to variant rs2303694 [ dbSNP | Ensembl ].
VAR_053072
Natural variant3871R → W.
Corresponds to variant rs35245196 [ dbSNP | Ensembl ].
VAR_053073

Secondary structure

................ 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55199 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EB4A3F94CA8A411F

FASTA62168,265
        10         20         30         40         50         60 
MAALKEDRSY GLSCGRVSDG SKVSVFHVKL TDSALRAFES YRARQDSVSL RPSIRFQGSQ 

        70         80         90        100        110        120 
GHISIPQPDC PAEARTFSFY LSNIGRDNPQ GSFDCIQQYV SSHGEVHLDC LGSIQDKITV 

       130        140        150        160        170        180 
CATDDSYQKA RQSMAQAEEE TRSRSAIVIK AGGRYLGKKV QFRKPAPGAT DAVPSRKRAT 

       190        200        210        220        230        240 
PINLASAIRK SGASAVSGGS GVSQRPFRDR VLHLLALRPY RKAELLLRLQ KDGLTQADKD 

       250        260        270        280        290        300 
ALDGLLQQVA NMSAKDGTCT LQDCMYKDVQ KDWPGYSEGD QQLLKRVLVR KLCQPQSTGS 

       310        320        330        340        350        360 
LLGDPAASSP PGERGRSASP PQKRLQPPDF IDPLANKKPR ISHFTQRAQP AVNGKLGVPN 

       370        380        390        400        410        420 
GREALLPTPG PPASTDTLSS STHLPPRLEP PRAHDPLADV SNDLGHSGRD CEHGEAAAPA 

       430        440        450        460        470        480 
PTVRLGLPLL TDCAQPSRPH GSPSRSKPKK KSKKHKDKER AAEDKPRAQL PDCAPATHAT 

       490        500        510        520        530        540 
PGAPADTPGL NGTCSVSSVP TSTSETPDYL LKYAAISSSE QRQSYKNDFN AEYSEYRDLH 

       550        560        570        580        590        600 
ARIERITRRF TQLDAQLRQL SQGSEEYETT RGQILQEYRK IKKTNTNYSQ EKHRCEYLHS 

       610        620 
KLAHIKRLIA EYDQRQLQAW P 

« Hide

References

« Hide 'large scale' references
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16282 mRNA. Translation: AAA57120.1.
BC049195 mRNA. Translation: AAH49195.1.
PIRI38880.
RefSeqNP_006523.1. NM_006532.3.
UniGeneHs.515260.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DOANMR-A200-292[»]
ProteinModelPortalP55199.
SMRP55199. Positions 204-297, 508-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113828. 32 interactions.
IntActP55199. 17 interactions.
MINTMINT-1511207.
STRING9606.ENSP00000262809.

PTM databases

PhosphoSiteP55199.

Polymorphism databases

DMDM1706635.

Proteomic databases

PaxDbP55199.
PRIDEP55199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262809; ENSP00000262809; ENSG00000105656.
GeneID8178.
KEGGhsa:8178.
UCSCuc002njg.3. human.

Organism-specific databases

CTD8178.
GeneCardsGC19M018553.
H-InvDBHIX0038310.
HGNCHGNC:23114. ELL.
HPAHPA046076.
MIM600284. gene.
neXtProtNX_P55199.
PharmGKBPA134939610.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321810.
HOGENOMHOG000112356.
HOVERGENHBG005578.
InParanoidP55199.
KOK15183.
OMACIQQYVS.
OrthoDBEOG7P02HN.
PhylomeDBP55199.
TreeFamTF326161.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55199.
BgeeP55199.
CleanExHS_ELL.
GenevestigatorP55199.

Family and domain databases

InterProIPR010844. Occludin_RNApol2_elong_fac_ELL.
IPR019464. RNA_pol_II_elong_fac_ELL.
[Graphical view]
PfamPF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSELL. human.
EvolutionaryTraceP55199.
GeneWikiELL_(gene).
GenomeRNAi8178.
NextBio30861.
PROP55199.
SOURCESearch...

Entry information

Entry nameELL_HUMAN
AccessionPrimary (citable) accession number: P55199
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM