Reviewed, UniProtKB/Swiss-Prot P55199 (ELL_HUMAN)

Names and origin

Protein names

Recommended name:
    RNA polymerase II elongation factor ELL
Alternative name(s):
    Eleven-nineteen lysine-rich leukemia protein

Gene names

Name:	ELL
Synonyms:	C19orf17

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Ref.3 Ref.7
Subunit structure	Interacts with EAF1 and EAF2. Ref.4 Ref.5
Subcellular location	Nucleus speckle. Nucleus › Cajal 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10
Involvement in disease	A chromosomal translocation involving ELL is found in acute leukemias. Translocation t(11;19)(q23;p13.1) with MLL/HRX. The result is a rogue activator protein.
Sequence similarities	Belongs to the ELL/occludin family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Ref.3 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell transcription elongation factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	RNA polymerase II transcription elongation factor activity Inferred from electronic annotation. Source: InterPro positive transcription elongation factor activity Ref.3 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TFPT	P0C1Z6	1	EBI-1245868,EBI-1245626

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 621	621	RNA polymerase II elongation factor ELL		PRO_0000146733
Regions
	Motif	445 – 459	15	Nuclear localization signal Potential
Sites
	Site	46	1	MLL fusion point (in acute myeloid leukemia patient)
Amino acid modifications
	Modified residue	170	1	Phosphothreonine Ref.8
	Modified residue	309	1	Phosphoserine Ref.10
	Modified residue	561	1	Phosphoserine Ref.9
Natural variations
	Natural variant	297	1	S → N: dbSNP rs2303694.		VAR_053072
	Natural variant	387	1	R → W: dbSNP rs35245196.		VAR_053073

Sequences

	Sequence		Length	Mass (Da)
	P55199-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EB4A3F94CA8A411F	FASTA	621	68,265
	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

References

	« Hide 'large scale' referencesShow '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: 7991593] [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: 15489334] [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: 8596958] [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: 11418481] [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: 12446457] [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: 12686606] [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: 16006523] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION.
[8]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, MASS SPECTROMETRY.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, MASS SPECTROMETRY.
[11]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

U16282 mRNA. Translation: AAA57120.1.
BC049195 mRNA. Translation: AAH49195.1.

IPI

IPI00023467.

PIR

I38880.

RefSeq

NP_006523.1.

UniGene

Hs.515260

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DOA	NMR	-	A	200-292	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P55199. 1 interaction.

PTM databases

PhosphoSite

P55199.

Proteomic databases

PRIDE

P55199.

Genome annotation databases

Ensembl

ENSG00000105656. Homo sapiens. [Contig view]

GeneID

8178.

KEGG

hsa:8178.

Organism-specific databases

GeneCards

GC19M018416.

H-InvDB

HIX0014915.
HIX0038310.

HGNC

HGNC:23114. ELL.

MIM

600284. gene.

PharmGKB

PA134939610.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P55199.

HOVERGEN

P55199.

OMA

P55199. RYLGKKV.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_6143. Pausing and recovery of Tat-mediated HIV-1 elongation.
REACT_6185. HIV Infection.
REACT_6244. Pausing and recovery of HIV-1 elongation.
REACT_6259. HIV-1 elongation arrest and recovery.
REACT_6344. Tat-mediated HIV-1 elongation arrest and recovery.
REACT_71. Gene Expression.
REACT_769. Pausing and recovery of elongation.

Gene expression databases

ArrayExpress

P55199.

Bgee

P55199.

CleanEx

HS_ELL.

GermOnline

ENSG00000105656. Homo sapiens.

Family and domain databases

InterPro

IPR010844. Occludin_ELL_domain.
IPR019464. RNA_pol_II_elong_fac_ELL.
[Graphical view]

Pfam

PF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

30861.

SOURCE

Search...

Entry information

Entry name

ELL_HUMAN

Accession

Primary (citable) accession number: P55199

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)