Q96JC9 (EAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ELL-associated factor 1

Gene names

Name:

EAF1

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	268 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. Ref.1 Ref.4
Subunit structure	Interacts with ELL and ELL2. Ref.1
Subcellular location	Nucleus speckle. Nucleus › Cajal body. Note: Colocalizes with ELL to nuclear speckles. Also localized to Cajal (coiled) bodies. Ref.1 Ref.3
Tissue specificity	Strongly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, prostate, testis, small intestine and colon. Poorly expressed in thymus. Ref.1
Sequence similarities	Belongs to the EAF family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW 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
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MED26	O95402	5	EBI-769261,EBI-394392

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 268	268	ELL-associated factor 1		PRO_0000130334
Regions
	Region	182 – 262	81	Necessary for transactivation activity
	Compositional bias	127 – 168	42	Pro-rich
	Compositional bias	188 – 211	24	Ser-rich
Amino acid modifications
	Modified residue	150	1	N6-acetyllysine Ref.9
	Modified residue	157	1	Phosphothreonine Ref.8
	Modified residue	158	1	Phosphoserine Ref.7
	Modified residue	165	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
Experimental info
	Sequence conflict	97	1	Y → F in AAH41329. Ref.2
	Sequence conflict	252	1	T → A in AAH41329. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q96JC9 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0D78B586AABB0FA4	FASTA	268	29,042
	10 20 30 40 50 60 MNGTANPLLD REEHCLRLGE SFEKRPRASF HTIRYDFKPA SIDTSCEGEL QVGKGDEVTI 70 80 90 100 110 120 TLPHIPGSTP PMTVFKGNKR PYQKDCVLII NHDTGEYVLE KLSSSIQVKK TRAEGSSKIQ 130 140 150 160 170 180 ARMEQQPTRP PQTSQPPPPP PPMPFRAPTK PPVGPKTSPL KDNPSPEPQL DDIKRELRAE 190 200 210 220 230 240 VDIIEQMSSS SGSSSSDSES SSGSDDDSSS SGGEDNGPAS PPQPSHQQPY NSRPAVANGT 250 260 SRPQGSNQLM NTLRNDLQLS ESGSDSDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRANSCRIPTION ACTIVATION, INTERACTION WITH ELL AND ELL2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Bone marrow.
[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]	"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.
[4]	"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: ROLE IN ELL-TRANSCRIPTION ACTIVATION.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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-158 AND SER-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157 AND SER-165, MASS SPECTROMETRY.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF272973 mRNA. Translation: AAK58687.1. BC041329 mRNA. Translation: AAH41329.1.
IPI	IPI00878931.
RefSeq	NP_149074.3. NM_033083.6.
UniGene	Hs.716733.
3D structure databases
ProteinModelPortal	Q96JC9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96JC9. 16 interactions.
STRING	Q96JC9.
PTM databases
PhosphoSite	Q96JC9.
Polymorphism databases
DMDM	73919265.
Proteomic databases
PRIDE	Q96JC9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396842; ENSP00000380054; ENSG00000144597.
GeneID	85403.
KEGG	hsa:85403.
UCSC	uc003bzu.1. human.
Organism-specific databases
CTD	85403.
GeneCards	GC03P015468. GC03P015469.
H-InvDB	HIX0003102.
HGNC	HGNC:20907. EAF1.
MIM	608315. gene.
neXtProt	NX_Q96JC9.
PharmGKB	PA134897202.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06087.
GeneTree	ENSGT00390000017724.
HOGENOM	HBG715128.
HOVERGEN	HBG054898.
InParanoid	Q96JC9.
OMA	MPFRAPM.
OrthoDB	EOG4868DG.
PhylomeDB	Q96JC9.
Gene expression databases
ArrayExpress	Q96JC9.
Bgee	Q96JC9.
CleanEx	HS_EAF1.
Genevestigator	Q96JC9.
GermOnline	ENSG00000144597. Homo sapiens.
Family and domain databases
InterPro	IPR019194. Tscrpt_elong_fac_Eaf_N. [Graphical view]
KO	K15186.
Pfam	PF09816. EAF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	75962.
SOURCE	Search...

Entry information

Entry name

EAF1_HUMAN

Accession

Primary (citable) accession number: Q96JC9
Secondary accession number(s): Q8IW10

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.