Search Results

Overview

Uniprot IDQ5BKZ1
Protein NameDBIRD complex subunit ZNF326
Gene NameZNF326
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
140 EAPYSRSKLRPGFME
264 KLAKPMEKISLSKSP
438 IKGKQAYKEQIKRES

Function

Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro

Protein Sequence

10 MDFEDDYTHS 20 ACRNTYQGFN 30 GMDRDYGPGS 40 YGGMDRDYGH 50 GSYGGQRSMD 60 SYLNQSYGMD 70 NHSGGGGGSR 80 FGPYESYDSR 90 SSLGGRDLYR 100 SGYGFNEPEQ 110 SRFGGSYGGR 120 FESSYRNSLD 130 SFGGRNQGGS 140 SWEAPYSRSK 150 LRPGFMEDRG 160 RENYSSYSSF 170 SSPHMKPAPV 180 GSRGRGTPAY 190 PESTFGSRNY 200 DAFGGPSTGR 210 GRGRGHMGDF 220 GSIHRPGIVV 230 DYQNKSTNVT 240 VAAARGIKRK 250 MMQPFNKPSG 260 TFIKKPKLAK 270 PMEKISLSKS 280 PTKTDPKNEE 290 EEKRRIEARR 300 EKQRRRREKN 310 SEKYGDGYRM 320 AFTCSFCKFR 330 TFEEKDIELH 340 LESSSHQETL 350 DHIQKQTKFD 360 KVVMEFLHEC 370 MVNKFKKTSI 380 RKQQTNNQTE 390 VVKIIEKDVM 400 EGVTVDDHMM 410 KVETVHCSAC 420 SVYIPALHSS 430 VQQHLKSPDH 440 IKGKQAYKEQ 450 IKRESVLTAT 460 SILNNPIVKA 470 RYERFVKGEN 480 PFEIQDHSQD 490 QQIEGDEEDE 500 EKIDEPIEEE 510 EDEDEEEEAE 520 EVGEVEEVEE 530 VEEVREGGIE 540 GEGNIQGVGE 550 GGEVGVVGEV 560 EGVGEVEEVE 570 ELEEETAKEE 580 PADFPVEQPE EN

Gene Ontology

Classification GO ID Description
Molecular Function GO:0000993 RNA polymerase II complex binding
Cellular Component GO:0044609 DBIRD complex
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006397 mRNA processing
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0032784 regulation of DNA-templated transcription elongation
Biological Process GO:0043484 regulation of RNA splicing
Biological Process GO:0008380 RNA splicing

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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.