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O08856 (ELL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Subcellular location

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

Sequence similarities

Belongs to the ELL/occludin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 602601RNA polymerase II elongation factor ELL
PRO_0000146734

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3001Phosphoserine By similarity
Modified residue5421Phosphoserine By similarity

Experimental info

Sequence conflict1031Y → H in AAC53150. Ref.1
Sequence conflict1031Y → H in AAH14816. Ref.4
Sequence conflict1031Y → H in AAH24894. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O08856 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DECAD56CF19ABF4B

FASTA60267,146
        10         20         30         40         50         60 
MAALKEARSY GLSCGRVSDG SRVSVFHVKL TDSALKAFES YRAHQDSVSL RPSIRFEGSQ 

        70         80         90        100        110        120 
GHISIPQPDC PEEVRAFSFY LSNIGRDSPQ GSFDCIQQYV SSYGDVHLDC LGSIQDKVTV 

       130        140        150        160        170        180 
CATDDSYQKA RQSMAQAEEE TRSRSAIVIK AGGRYMGKKV QFRKPAPGAA DAVPSRKRAT 

       190        200        210        220        230        240 
PINLASAIRK SSGSGASSVV QRPFRDRVLH LLALRPYRKA ELLLRLQKDG LTQADKDTLD 

       250        260        270        280        290        300 
SLLQQVASVN PKDGTCTLQD CMYKSLQKDW PGYSEGDRQL LKRMLMRKLC QPQNATTDSS 

       310        320        330        340        350        360 
PPREHGRSAS PSQKRPTDFI DPLASKKPRI SHFTQRAQPT LNGKLGAPNG HETLLPAPGP 

       370        380        390        400        410        420 
TPSDTLSSSH LPPRLEPPRT HDPLADVSND LGHSTQDYKH QEATPAPAPH LGLPLLTDFP 

       430        440        450        460        470        480 
QAEQPTSSSH THSRPKKKSK KHKDKERPPE ERPPAPQPDA PTAPALPPDA PGLNGACDNE 

       490        500        510        520        530        540 
PTSSSETPDY LLKYPAISSS EQRQSYKNDF NAEYSEYRSL HARIEQITRR FTQLDAQLRQ 

       550        560        570        580        590        600 
LSQGSDEYET TRGQILQEYR KIKKTNTNYS CEKRRCEYLH RKLAHIKRLI AEYDQRQLQA 


WP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22372.1.
RefSeqNP_031950.2. NM_007924.2.
UniGeneMm.271973.

3D structure databases

ProteinModelPortalO08856.
SMRO08856. Positions 201-295, 489-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199432. 3 interactions.
IntActO08856. 3 interactions.
STRING10090.ENSMUSP00000091163.

PTM databases

PhosphoSiteO08856.

Proteomic databases

PaxDbO08856.
PRIDEO08856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000093454; ENSMUSP00000091163; ENSMUSG00000070002.
GeneID13716.
KEGGmmu:13716.
UCSCuc009mau.1. mouse.

Organism-specific databases

CTD8178.
MGIMGI:109377. Ell.

Phylogenomic databases

eggNOGNOG321810.
GeneTreeENSGT00550000074378.
HOGENOMHOG000112356.
HOVERGENHBG005578.
InParanoidQ3TXY9.
KOK15183.
OMACIQQYVS.
OrthoDBEOG7P02HN.
TreeFamTF326161.

Gene expression databases

BgeeO08856.
CleanExMM_ELL.
GenevestigatorO08856.

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. mouse.
NextBio284496.
PROO08856.
SOURCESearch...

Entry information

Entry nameELL_MOUSE
AccessionPrimary (citable) accession number: O08856
Secondary accession number(s): Q3TXY9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot