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Protein

Protein ENL

Gene

MLLT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ENL
Alternative name(s):
YEATS domain-containing protein 1
Gene namesi
Name:MLLT1
Synonyms:ENL, LTG19, YEATS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:7134. MLLT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA30848.

Polymorphism and mutation databases

BioMutaiMLLT1.
DMDMi116241350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Protein ENLPRO_0000215938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei155 – 1551Phosphoserine1 Publication
Modified residuei292 – 2921Phosphoserine3 Publications
Modified residuei296 – 2961Phosphoserine2 Publications
Modified residuei359 – 3591Phosphoserine1 Publication
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei475 – 4751PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ03111.
PaxDbiQ03111.
PeptideAtlasiQ03111.
PRIDEiQ03111.

PTM databases

PhosphoSiteiQ03111.

Expressioni

Gene expression databases

BgeeiQ03111.
CleanExiHS_MLLT1.
GenevisibleiQ03111. HS.

Organism-specific databases

HPAiHPA031166.

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 ALKBH4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AFF4Q9UHB78EBI-1384215,EBI-395282
DOT1LQ8TEK36EBI-1384215,EBI-2619253

Protein-protein interaction databases

BioGridi110444. 35 interactions.
IntActiQ03111. 15 interactions.
STRINGi9606.ENSP00000252674.

Structurei

3D structure databases

ProteinModelPortaliQ03111.
SMRiQ03111. Positions 1-138, 453-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 112105YEATSPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi272 – 2809Poly-Pro
Compositional biasi319 – 3257Poly-Ser
Compositional biasi374 – 38916Poly-SerAdd
BLAST
Compositional biasi457 – 4604Poly-Pro
Compositional biasi463 – 4664Poly-Pro

Sequence similaritiesi

Contains 1 YEATS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5033.
GeneTreeiENSGT00440000039936.
HOGENOMiHOG000033834.
HOVERGENiHBG004191.
InParanoidiQ03111.
KOiK15187.
OMAiCFTYDLF.
OrthoDBiEOG71G9V5.
PhylomeDBiQ03111.
TreeFamiTF314586.

Family and domain databases

InterProiIPR005033. YEATS.
[Graphical view]
PANTHERiPTHR23195. PTHR23195. 1 hit.
PfamiPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEiPS51037. YEATS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03111-1 [UniParc]FASTAAdd to basket

« Hide

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

QSCLEAVAT
Length:559
Mass (Da):62,056
Last modified:October 17, 2006 - v2
Checksum:iA8480BA0F8742173
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2702KG → NP in AAA58457 (PubMed:1423624).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04285 mRNA. Translation: AAA58457.1.
D14539 mRNA. Translation: BAA03406.1.
CCDSiCCDS12160.1.
PIRiB44265.
RefSeqiNP_005925.2. NM_005934.3.
UniGeneiHs.10095.

Genome annotation databases

EnsembliENST00000252674; ENSP00000252674; ENSG00000130382.
GeneIDi4298.
KEGGihsa:4298.
UCSCiuc002mek.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04285 mRNA. Translation: AAA58457.1.
D14539 mRNA. Translation: BAA03406.1.
CCDSiCCDS12160.1.
PIRiB44265.
RefSeqiNP_005925.2. NM_005934.3.
UniGeneiHs.10095.

3D structure databases

ProteinModelPortaliQ03111.
SMRiQ03111. Positions 1-138, 453-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110444. 35 interactions.
IntActiQ03111. 15 interactions.
STRINGi9606.ENSP00000252674.

PTM databases

PhosphoSiteiQ03111.

Polymorphism and mutation databases

BioMutaiMLLT1.
DMDMi116241350.

Proteomic databases

MaxQBiQ03111.
PaxDbiQ03111.
PeptideAtlasiQ03111.
PRIDEiQ03111.

Protocols and materials databases

DNASUi4298.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252674; ENSP00000252674; ENSG00000130382.
GeneIDi4298.
KEGGihsa:4298.
UCSCiuc002mek.3. human.

Organism-specific databases

CTDi4298.
GeneCardsiGC19M006210.
HGNCiHGNC:7134. MLLT1.
HPAiHPA031166.
MIMi159556. gene.
neXtProtiNX_Q03111.
PharmGKBiPA30848.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5033.
GeneTreeiENSGT00440000039936.
HOGENOMiHOG000033834.
HOVERGENiHBG004191.
InParanoidiQ03111.
KOiK15187.
OMAiCFTYDLF.
OrthoDBiEOG71G9V5.
PhylomeDBiQ03111.
TreeFamiTF314586.

Miscellaneous databases

ChiTaRSiMLLT1. human.
GeneWikiiMLLT1.
GenomeRNAii4298.
NextBioi16919.
PROiQ03111.
SOURCEiSearch...

Gene expression databases

BgeeiQ03111.
CleanExiHS_MLLT1.
GenevisibleiQ03111. HS.

Family and domain databases

InterProiIPR005033. YEATS.
[Graphical view]
PANTHERiPTHR23195. PTHR23195. 1 hit.
PfamiPF03366. YEATS. 1 hit.
[Graphical view]
PROSITEiPS51037. YEATS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION IN THE SEC COMPLEX.
  13. "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.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENL_HUMAN
AccessioniPrimary (citable) accession number: Q03111
Secondary accession number(s): Q14768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.