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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)DescriptionActionsGraphical viewLength
Sitei46KMT2A/MLL1 fusion point (in acute myeloid leukemia patient)1 Publication1

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

GO - Biological processi

  • in utero embryonic development Source: Ensembl
  • negative regulation of phosphatase activity Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: ProtInc
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • snRNA transcription from RNA polymerase III promoter Source: UniProtKB
  • snRNA transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: Reactome
  • transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105656-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
SIGNORiP55199.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:23114. ELL.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • Cajal body Source: UniProtKB
  • cytoplasm Source: HPA
  • histone locus body Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • plasma membrane Source: HPA
  • transcriptionally active chromatin Source: UniProtKB
  • 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

DisGeNETi8178.
OpenTargetsiENSG00000105656.
PharmGKBiPA134939610.

Polymorphism and mutation databases

BioMutaiELL.
DMDMi1706635.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001467332 – 621RNA polymerase II elongation factor ELLAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei180PhosphothreonineCombined sources1
Modified residuei309PhosphoserineCombined sources1
Modified residuei561PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP55199.
MaxQBiP55199.
PaxDbiP55199.
PeptideAtlasiP55199.
PRIDEiP55199.

PTM databases

iPTMnetiP55199.
PhosphoSitePlusiP55199.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000105656.
CleanExiHS_ELL.
ExpressionAtlasiP55199. baseline and differential.
GenevisibleiP55199. HS.

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

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113828. 48 interactors.
IntActiP55199. 29 interactors.
MINTiMINT-1511207.
STRINGi9606.ENSP00000262809.

Structurei

Secondary structure

1621
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi207 – 217Combined sources11
Helixi222 – 232Combined sources11
Helixi236 – 248Combined sources13
Beta strandi249 – 252Combined sources4
Beta strandi254 – 256Combined sources3
Beta strandi258 – 260Combined sources3
Helixi265 – 268Combined sources4
Helixi279 – 291Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DOANMR-A200-292[»]
ProteinModelPortaliP55199.
SMRiP55199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55199.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi445 – 459Nuclear localization signalSequence analysisAdd BLAST15

Sequence similaritiesi

Belongs to the ELL/occludin family.Curated

Phylogenomic databases

eggNOGiKOG4796. Eukaryota.
ENOG410ZNGU. LUCA.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiP55199.
KOiK15183.
OMAiCIQQYVS.
OrthoDBiEOG091G043D.
PhylomeDBiP55199.
TreeFamiTF326161.

Family and domain databases

InterProiIPR031184. ELL.
IPR031176. ELL/occludin.
IPR019464. ELL_N.
IPR010844. Occludin_ELL.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR23288. PTHR23288. 1 hit.
PTHR23288:SF9. PTHR23288:SF9. 1 hit.
PfamiPF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_053072297S → N.Corresponds to variant rs2303694dbSNPEnsembl.1
Natural variantiVAR_053073387R → W.Corresponds to variant rs35245196dbSNPEnsembl.1

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.
UCSCiuc002njh.3. human.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DOANMR-A200-292[»]
ProteinModelPortaliP55199.
SMRiP55199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113828. 48 interactors.
IntActiP55199. 29 interactors.
MINTiMINT-1511207.
STRINGi9606.ENSP00000262809.

PTM databases

iPTMnetiP55199.
PhosphoSitePlusiP55199.

Polymorphism and mutation databases

BioMutaiELL.
DMDMi1706635.

Proteomic databases

EPDiP55199.
MaxQBiP55199.
PaxDbiP55199.
PeptideAtlasiP55199.
PRIDEiP55199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262809; ENSP00000262809; ENSG00000105656.
GeneIDi8178.
KEGGihsa:8178.
UCSCiuc002njh.3. human.

Organism-specific databases

CTDi8178.
DisGeNETi8178.
GeneCardsiELL.
H-InvDBHIX0038310.
HGNCiHGNC:23114. ELL.
HPAiHPA046076.
MIMi600284. gene.
neXtProtiNX_P55199.
OpenTargetsiENSG00000105656.
PharmGKBiPA134939610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4796. Eukaryota.
ENOG410ZNGU. LUCA.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiP55199.
KOiK15183.
OMAiCIQQYVS.
OrthoDBiEOG091G043D.
PhylomeDBiP55199.
TreeFamiTF326161.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105656-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-112387. Elongation arrest and recovery.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
SIGNORiP55199.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000105656.
CleanExiHS_ELL.
ExpressionAtlasiP55199. baseline and differential.
GenevisibleiP55199. HS.

Family and domain databases

InterProiIPR031184. ELL.
IPR031176. ELL/occludin.
IPR019464. ELL_N.
IPR010844. Occludin_ELL.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR23288. PTHR23288. 1 hit.
PTHR23288:SF9. PTHR23288:SF9. 1 hit.
PfamiPF10390. ELL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 149 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

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 one 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.