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Protein

ELL-associated factor 1

Gene

Eaf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a transcriptional transactivator of ELL and ELL2 elongation activities.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
ELL-associated factor 1
Gene namesi
Name:Eaf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1921677. Eaf1.

Subcellular locationi

  • Nucleus speckle By similarity
  • NucleusCajal body By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268ELL-associated factor 1PRO_0000130335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D4C5.
MaxQBiQ9D4C5.
PaxDbiQ9D4C5.
PRIDEiQ9D4C5.

PTM databases

iPTMnetiQ9D4C5.
PhosphoSiteiQ9D4C5.

Expressioni

Gene expression databases

BgeeiQ9D4C5.
CleanExiMM_EAF1.
GenevisibleiQ9D4C5. MM.

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). Interacts with ELL and ELL2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022446.

Structurei

3D structure databases

ProteinModelPortaliQ9D4C5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni182 – 26281Necessary for transactivation activityBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi127 – 16842Pro-richAdd
BLAST
Compositional biasi188 – 21124Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the EAF family.Curated

Phylogenomic databases

eggNOGiKOG4795. Eukaryota.
ENOG4111KQJ. LUCA.
GeneTreeiENSGT00390000017724.
HOGENOMiHOG000070137.
HOVERGENiHBG054898.
InParanoidiQ9D4C5.
KOiK15186.
OMAiSHQQPYS.
OrthoDBiEOG7ZPNNJ.
PhylomeDBiQ9D4C5.
TreeFamiTF320864.

Family and domain databases

InterProiIPR027093. EAF_fam.
IPR019194. Tscrpt_elong_fac_Eaf_N.
[Graphical view]
PANTHERiPTHR15970. PTHR15970. 1 hit.
PfamiPF09816. EAF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D4C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGTANPLLD REEHCLRLGE SFEKRPRASF HTIRYDFKPA SIDTSCEGEL
60 70 80 90 100
QVGKGDEVTI TLPHIPGSTP PMTVFKGNKR PYQKDCVLII NHDTGEYVLE
110 120 130 140 150
KLSSSIQVKK TRAEGSSKIQ ARMEQQPARP PQPSQPPPPP PPMPFRAPTK
160 170 180 190 200
PPAGPKTSPL KDNPSPEPQL DDIKRELRAE VDIIEQMSSS SGSSSSDSES
210 220 230 240 250
SSGSDDDSSS SAGEDNGPAS PPQPSHQQPY NSRPAVANGT SRPQGSSQLM
260
NTLRNDLQLS ESGSDSDD
Length:268
Mass (Da):28,967
Last modified:March 1, 2003 - v2
Checksum:i02ACBA8F33200C20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016628 mRNA. Translation: BAB30346.2.
AK044181 mRNA. Translation: BAC31806.1.
AK044737 mRNA. Translation: BAC32058.1.
BC079658 mRNA. Translation: AAH79658.1.
CCDSiCCDS26914.1.
RefSeqiNP_083208.1. NM_028932.4.
UniGeneiMm.491208.

Genome annotation databases

EnsembliENSMUST00000022446; ENSMUSP00000022446; ENSMUSG00000021890.
GeneIDi74427.
KEGGimmu:74427.
UCSCiuc007sxt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016628 mRNA. Translation: BAB30346.2.
AK044181 mRNA. Translation: BAC31806.1.
AK044737 mRNA. Translation: BAC32058.1.
BC079658 mRNA. Translation: AAH79658.1.
CCDSiCCDS26914.1.
RefSeqiNP_083208.1. NM_028932.4.
UniGeneiMm.491208.

3D structure databases

ProteinModelPortaliQ9D4C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022446.

PTM databases

iPTMnetiQ9D4C5.
PhosphoSiteiQ9D4C5.

Proteomic databases

EPDiQ9D4C5.
MaxQBiQ9D4C5.
PaxDbiQ9D4C5.
PRIDEiQ9D4C5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022446; ENSMUSP00000022446; ENSMUSG00000021890.
GeneIDi74427.
KEGGimmu:74427.
UCSCiuc007sxt.2. mouse.

Organism-specific databases

CTDi85403.
MGIiMGI:1921677. Eaf1.

Phylogenomic databases

eggNOGiKOG4795. Eukaryota.
ENOG4111KQJ. LUCA.
GeneTreeiENSGT00390000017724.
HOGENOMiHOG000070137.
HOVERGENiHBG054898.
InParanoidiQ9D4C5.
KOiK15186.
OMAiSHQQPYS.
OrthoDBiEOG7ZPNNJ.
PhylomeDBiQ9D4C5.
TreeFamiTF320864.

Miscellaneous databases

ChiTaRSiEaf1. mouse.
PROiQ9D4C5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D4C5.
CleanExiMM_EAF1.
GenevisibleiQ9D4C5. MM.

Family and domain databases

InterProiIPR027093. EAF_fam.
IPR019194. Tscrpt_elong_fac_Eaf_N.
[Graphical view]
PANTHERiPTHR15970. PTHR15970. 1 hit.
PfamiPF09816. EAF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: Brain cortex, Retina and Testis.
  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].
    Strain: C57BL/6J.
    Tissue: Embryonic brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiEAF1_MOUSE
AccessioniPrimary (citable) accession number: Q9D4C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 106 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

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.