Q03111 (ENL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein ENL

Alternative name(s):
YEATS domain-containing protein 1

Gene names

Name:	MLLT1
Synonyms:	ENL, LTG19, YEATS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9
Subunit structure	Component of the super elongation complex (SEC), at least composed of AFF4, the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Ref.8 Ref.9
Subcellular location	Nucleus.
Involvement in disease	A chromosomal aberration involving MLLT1 is associated with acute leukemias. Translocation t(11;19)(q23;p13.3) with MLL/HRX. The result is a rogue activator protein.
Sequence similarities	Contains 1 YEATS domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of protein kinase activity Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Traceable author statement Ref.3. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Traceable author statement PubMed 7991593. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AFF4	Q9UHB7	8	EBI-1384215,EBI-395282
DOT1L	Q8TEK3	4	EBI-1384215,EBI-2619253

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	Protein ENL		PRO_0000215938
Regions
	Domain	8 – 112	105	YEATS
	Compositional bias	272 – 280	9	Poly-Pro
	Compositional bias	319 – 325	7	Poly-Ser
	Compositional bias	374 – 389	16	Poly-Ser
	Compositional bias	457 – 460	4	Poly-Pro
	Compositional bias	463 – 466	4	Poly-Pro
Amino acid modifications
	Modified residue	155	1	Phosphoserine Ref.6
	Modified residue	292	1	Phosphoserine Ref.5 Ref.7 Ref.10
	Modified residue	296	1	Phosphoserine Ref.5 Ref.10
	Modified residue	359	1	Phosphoserine Ref.10
	Modified residue	361	1	Phosphoserine Ref.10
Experimental info
	Sequence conflict	269 – 270	2	KG → NP in AAA58457. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q03111 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: A8480BA0F8742173	FASTA	559	62,056
	10 20 30 40 50 60 MDNQCTVQVR LELGHRAQLR KKPTTEGFTH DWMVFVRGPE QCDIQHFVEK VVFWLHDSFP 70 80 90 100 110 120 KPRRVCKEPP YKVEESGYAG FIMPIEVHFK NKEEPRKVCF TYDLFLNLEG NPPVNHLRCE 130 140 150 160 170 180 KLTFNNPTTE FRYKLLRAGG VMVMPEGADT VSRPSPDYPM LPTIPLSAFS DPKKTKPSHG 190 200 210 220 230 240 SKDANKESSK TSKPHKVTKE HRERPRKDSE SKSSSKELER EQAKSSKDTS RKLGEGRLPK 250 260 270 280 290 300 EEKAPPPKAA FKEPKMALKE TKLESTSPKG GPPPPPPPPP RASSKRPATA DSPKPSAKKQ 310 320 330 340 350 360 KKSSSKGSRS APGTSPRTSS SSSFSDKKPA KDKSSTRGEK VKAESEPREA KKALEVEESN 370 380 390 400 410 420 SEDEASFKSE SAQSSPSNSS SSSDSSSDSD FEPSQNHSQG PLRSMVEDLQ SEESDEDDSS 430 440 450 460 470 480 SGEEAAGKTN PGRDSRLSFS DSESDNSADS SLPSREPPPP QKPPPPNSKV SGRRSPESCS 490 500 510 520 530 540 KPEKILKKGT YDKAYTDELV ELHRRLMALR ERNVLQQIVN LIEETGHFNV TNTTFDFDLF 550 SLDETTVRKL QSCLEAVAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias." Tkachuk D.C., Kohler S., Cleary M.L. Cell 71:691-700(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia." Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S., Kodera Y., Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R. Oncogene 8:2617-2625(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"ENL, the gene fused with HRX in t(11;19) leukemias, encodes a nuclear protein with transcriptional activation potential in lymphoid and myeloid cells." Rubnitz J.E., Morrissey J., Savage P.A., Cleary M.L. Blood 84:1747-1752(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[4]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[5]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-296, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, MASS SPECTROMETRY.
[8]	"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription." He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q. Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
[9]	"AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia." Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A. Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-296; SER-359 AND SER-361, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	L04285 mRNA. Translation: AAA58457.1. D14539 mRNA. Translation: BAA03406.1.
IPI	IPI00100630.
PIR	B44265.
RefSeq	NP_005925.2. NM_005934.3.
UniGene	Hs.10095.
3D structure databases
ProteinModelPortal	Q03111.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03111. 12 interactions.
STRING	9606.ENSP00000252674.
PTM databases
PhosphoSite	Q03111.
Polymorphism databases
DMDM	116241350.
Proteomic databases
PaxDb	Q03111.
PeptideAtlas	Q03111.
PRIDE	Q03111.
Protocols and materials databases
DNASU	4298.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252674; ENSP00000252674; ENSG00000130382.
GeneID	4298.
KEGG	hsa:4298.
UCSC	uc002mek.3. human.
Organism-specific databases
CTD	4298.
GeneCards	GC19M006210.
HGNC	HGNC:7134. MLLT1.
HPA	HPA031166.
MIM	159556. gene.
neXtProt	NX_Q03111.
PharmGKB	PA30848.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5033.
HOGENOM	HOG000033834.
HOVERGEN	HBG004191.
InParanoid	Q03111.
KO	K15187.
OMA	PEQCDIQ.
OrthoDB	EOG4CJVHC.
PhylomeDB	Q03111.
Gene expression databases
Bgee	Q03111.
CleanEx	HS_MLLT1.
Genevestigator	Q03111.
GermOnline	ENSG00000130382. Homo sapiens.
Family and domain databases
InterPro	IPR005033. YEATS. [Graphical view]
PANTHER	PTHR23195. PTHR23195. 1 hit.
Pfam	PF03366. YEATS. 1 hit. [Graphical view]
PROSITE	PS51037. YEATS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MLLT1. human.
GenomeRNAi	4298.
NextBio	16919.
SOURCE	Search...

Entry information

Entry name

ENL_HUMAN

Accession

Primary (citable) accession number: Q03111
Secondary accession number(s): Q14768

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 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.