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Q03111 (ENL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ENL
Alternative name(s):
YEATS domain-containing protein 1
Gene names
Name:MLLT1
Synonyms:ENL, LTG19, YEATS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9 Ref.10

Subunit structure

Component of the super elongation complex (SEC), at least composed of AFF4, the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ALKBH4. Ref.9 Ref.10 Ref.12

Subcellular location

Nucleus.

Involvement in disease

A chromosomal aberration involving MLLT1 is associated with acute leukemias. Translocation t(11;19)(q23;p13.3) with KMT2A/MLL1. The result is a rogue activator protein.

Sequence similarities

Contains 1 YEATS domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Protein ENL
PRO_0000215938

Regions

Domain8 – 112105YEATS
Compositional bias272 – 2809Poly-Pro
Compositional bias319 – 3257Poly-Ser
Compositional bias374 – 38916Poly-Ser
Compositional bias457 – 4604Poly-Pro
Compositional bias463 – 4664Poly-Pro

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.13
Modified residue1551Phosphoserine Ref.6
Modified residue2921Phosphoserine Ref.5 Ref.8 Ref.11
Modified residue2961Phosphoserine Ref.5 Ref.11
Modified residue3591Phosphoserine Ref.11
Modified residue3611Phosphoserine Ref.11

Experimental info

Sequence conflict269 – 2702KG → NP in AAA58457. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03111 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: A8480BA0F8742173

FASTA55962,056
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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.
[10]"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.
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Human ALKBH4 interacts with proteins associated with transcription."
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALKBH4.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04285 mRNA. Translation: AAA58457.1.
D14539 mRNA. Translation: BAA03406.1.
PIRB44265.
RefSeqNP_005925.2. NM_005934.3.
UniGeneHs.10095.

3D structure databases

ProteinModelPortalQ03111.
SMRQ03111. Positions 29-136, 453-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110444. 28 interactions.
IntActQ03111. 12 interactions.
STRING9606.ENSP00000252674.

PTM databases

PhosphoSiteQ03111.

Polymorphism databases

DMDM116241350.

Proteomic databases

PaxDbQ03111.
PeptideAtlasQ03111.
PRIDEQ03111.

Protocols and materials databases

DNASU4298.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252674; ENSP00000252674; ENSG00000130382.
GeneID4298.
KEGGhsa:4298.
UCSCuc002mek.3. human.

Organism-specific databases

CTD4298.
GeneCardsGC19M006210.
HGNCHGNC:7134. MLLT1.
HPAHPA031166.
MIM159556. gene.
neXtProtNX_Q03111.
PharmGKBPA30848.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5033.
HOGENOMHOG000033834.
HOVERGENHBG004191.
InParanoidQ03111.
KOK15187.
OMASCSKPEK.
OrthoDBEOG71G9V5.
PhylomeDBQ03111.
TreeFamTF314586.

Gene expression databases

BgeeQ03111.
CleanExHS_MLLT1.
GenevestigatorQ03111.

Family and domain databases

InterProIPR005033. YEATS.
[Graphical view]
PANTHERPTHR23195. PTHR23195. 1 hit.
PfamPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEPS51037. YEATS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLLT1. human.
GeneWikiMLLT1.
GenomeRNAi4298.
NextBio16919.
PROQ03111.
SOURCESearch...

Entry information

Entry nameENL_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM