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O08856

- ELL_MOUSE

UniProt

O08856 - ELL_MOUSE

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Protein

RNA polymerase II elongation factor ELL

Gene
Ell
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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 By similarity.

GO - Molecular functioni

  1. phosphatase binding Source: UniProtKB

GO - Biological processi

  1. in utero embryonic development Source: MGI
  2. negative regulation of phosphatase activity Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription elongation from RNA polymerase II promoter Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_226490. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:109377. Ell.

Subcellular locationi

Nucleus speckle By similarity. NucleusCajal body By similarity
Note: Colocalizes with EAF2 to nuclear speckles. Also localized to Cajal (coiled) bodies By similarity.

GO - Cellular componenti

  1. Cajal body Source: UniProtKB-SubCell
  2. nuclear speck Source: UniProtKB
  3. transcription elongation factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 602601RNA polymerase II elongation factor ELLPRO_0000146734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei300 – 3001Phosphoserine By similarity
Modified residuei542 – 5421Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO08856.
PRIDEiO08856.

PTM databases

PhosphoSiteiO08856.

Expressioni

Gene expression databases

BgeeiO08856.
CleanExiMM_ELL.
GenevestigatoriO08856.

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 By similarity.

Protein-protein interaction databases

BioGridi199432. 3 interactions.
IntActiO08856. 3 interactions.
STRINGi10090.ENSMUSP00000091163.

Structurei

3D structure databases

ProteinModelPortaliO08856.
SMRiO08856. Positions 201-295, 489-597.

Family & Domainsi

Sequence similaritiesi

Belongs to the ELL/occludin family.

Phylogenomic databases

eggNOGiNOG321810.
GeneTreeiENSGT00550000074378.
HOGENOMiHOG000112356.
HOVERGENiHBG005578.
InParanoidiQ3TXY9.
KOiK15183.
OMAiCIQQYVS.
OrthoDBiEOG7P02HN.
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.

O08856-1 [UniParc]FASTAAdd to Basket

« Hide

MAALKEARSY GLSCGRVSDG SRVSVFHVKL TDSALKAFES YRAHQDSVSL    50
RPSIRFEGSQ GHISIPQPDC PEEVRAFSFY LSNIGRDSPQ GSFDCIQQYV 100
SSYGDVHLDC LGSIQDKVTV CATDDSYQKA RQSMAQAEEE TRSRSAIVIK 150
AGGRYMGKKV QFRKPAPGAA DAVPSRKRAT PINLASAIRK SSGSGASSVV 200
QRPFRDRVLH LLALRPYRKA ELLLRLQKDG LTQADKDTLD SLLQQVASVN 250
PKDGTCTLQD CMYKSLQKDW PGYSEGDRQL LKRMLMRKLC QPQNATTDSS 300
PPREHGRSAS PSQKRPTDFI DPLASKKPRI SHFTQRAQPT LNGKLGAPNG 350
HETLLPAPGP TPSDTLSSSH LPPRLEPPRT HDPLADVSND LGHSTQDYKH 400
QEATPAPAPH LGLPLLTDFP QAEQPTSSSH THSRPKKKSK KHKDKERPPE 450
ERPPAPQPDA PTAPALPPDA PGLNGACDNE PTSSSETPDY LLKYPAISSS 500
EQRQSYKNDF NAEYSEYRSL HARIEQITRR FTQLDAQLRQ LSQGSDEYET 550
TRGQILQEYR KIKKTNTNYS CEKRRCEYLH RKLAHIKRLI AEYDQRQLQA 600
WP 602
Length:602
Mass (Da):67,146
Last modified:July 27, 2011 - v2
Checksum:iDECAD56CF19ABF4B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031Y → H in AAC53150. 1 Publication
Sequence conflicti103 – 1031Y → H in AAH14816. 1 Publication
Sequence conflicti103 – 1031Y → H in AAH24894. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80227 mRNA. Translation: AAC53150.1.
AK159027 mRNA. Translation: BAE34775.1.
CH466569 Genomic DNA. Translation: EDL28843.1.
BC014816 mRNA. Translation: AAH14816.1.
BC024894 mRNA. Translation: AAH24894.1.
CCDSiCCDS22372.1.
RefSeqiNP_031950.2. NM_007924.2.
UniGeneiMm.271973.

Genome annotation databases

EnsembliENSMUST00000093454; ENSMUSP00000091163; ENSMUSG00000070002.
GeneIDi13716.
KEGGimmu:13716.
UCSCiuc009mau.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U80227 mRNA. Translation: AAC53150.1 .
AK159027 mRNA. Translation: BAE34775.1 .
CH466569 Genomic DNA. Translation: EDL28843.1 .
BC014816 mRNA. Translation: AAH14816.1 .
BC024894 mRNA. Translation: AAH24894.1 .
CCDSi CCDS22372.1.
RefSeqi NP_031950.2. NM_007924.2.
UniGenei Mm.271973.

3D structure databases

ProteinModelPortali O08856.
SMRi O08856. Positions 201-295, 489-597.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199432. 3 interactions.
IntActi O08856. 3 interactions.
STRINGi 10090.ENSMUSP00000091163.

PTM databases

PhosphoSitei O08856.

Proteomic databases

PaxDbi O08856.
PRIDEi O08856.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000093454 ; ENSMUSP00000091163 ; ENSMUSG00000070002 .
GeneIDi 13716.
KEGGi mmu:13716.
UCSCi uc009mau.1. mouse.

Organism-specific databases

CTDi 8178.
MGIi MGI:109377. Ell.

Phylogenomic databases

eggNOGi NOG321810.
GeneTreei ENSGT00550000074378.
HOGENOMi HOG000112356.
HOVERGENi HBG005578.
InParanoidi Q3TXY9.
KOi K15183.
OMAi CIQQYVS.
OrthoDBi EOG7P02HN.
TreeFami TF326161.

Enzyme and pathway databases

Reactomei REACT_226490. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSi ELL. mouse.
NextBioi 284496.
PROi O08856.
SOURCEi Search...

Gene expression databases

Bgeei O08856.
CleanExi MM_ELL.
Genevestigatori O08856.

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. "Developmental analysis and subcellular localization of the murine homologue of ELL."
    Thirman M.J., Diskin E.B., Bin S.S., Ip H.S., Miller J.M., Simon M.C.
    Proc. Natl. Acad. Sci. U.S.A. 94:1408-1413(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Visual cortex.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: FVB/N.
    Tissue: Liver and Mammary gland.

Entry informationi

Entry nameiELL_MOUSE
AccessioniPrimary (citable) accession number: O08856
Secondary accession number(s): Q3TXY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi