Search Results

Overview

Uniprot IDQ03111
Protein NameProtein ENL
Gene NameMLLT1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
252 PPPKAAFKEPKMALK
342 STRGEKVKAESEPRE
469 KPPPPNSKVSGRRSP

Function

Chromatin reader 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 (PubMed:20159561, PubMed:20471948). Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated (PubMed:27105114). Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20) (PubMed:27105114). May play a role in leukemogenic gene transcription (PubMed:39794553)

Protein Sequence

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

Gene Ontology

Classification GO ID Description
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0008023 transcription elongation factor complex
Molecular Function GO:0003682 chromatin binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045893 positive regulation of DNA-templated transcription

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.