Search Results

Overview

Uniprot IDO60832
Protein NameH/ACA ribonucleoprotein complex subunit DKC1
Gene NameDKC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 AEVIILPKKHKKKKE
12 EVIILPKKHKKKKER
20 HKKKKERKSLPEEDV
394 SQKKLMIKQGLLDKH
43 FLIKPESKVAKLDTS
433 EVVAEVVKAPQVVAE
443 QVVAEAAKTAKRKRE
446 AEAAKTAKRKRESES
46 KPESKVAKLDTSQWP

Function

Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed:25219674, PubMed:32554502). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (PubMed:25219674). Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance (PubMed:19179534, PubMed:25219674). Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (PubMed:19179534)

Protein Sequence

10 MADAEVIILP 20 KKHKKKKERK 30 SLPEEDVAEI 40 QHAEEFLIKP 50 ESKVAKLDTS 60 QWPLLLKNFD 70 KLNVRTTHYT 80 PLACGSNPLK 90 REIGDYIRTG 100 FINLDKPSNP 110 SSHEVVAWIR 120 RILRVEKTGH 130 SGTLDPKVTG 140 CLIVCIERAT 150 RLVKSQQSAG 160 KEYVGIVRLH 170 NAIEGGTQLS 180 RALETLTGAL 190 FQRPPLIAAV 200 KRQLRVRTIY 210 ESKMIEYDPE 220 RRLGIFWVSC 230 EAGTYIRTLC 240 VHLGLLLGVG 250 GQMQELRRVR 260 SGVMSEKDHM 270 VTMHDVLDAQ 280 WLYDNHKDES 290 YLRRVVYPLE 300 KLLTSHKRLV 310 MKDSAVNAIC 320 YGAKIMLPGV 330 LRYEDGIEVN 340 QEIVVITTKG 350 EAICMAIALM 360 TTAVISTCDH 370 GIVAKIKRVI 380 MERDTYPRKW 390 GLGPKASQKK 400 LMIKQGLLDK 410 HGKPTDSTPA 420 TWKQEYVDYS 430 ESAKKEVVAE 440 VVKAPQVVAE 450 AAKTAKRKRE 460 SESESDETPP 470 AAPQLIKKEK 480 KKSKKDKKAK 490 AGLESGAEPG 500 DGDSDTTKKK 510 KKKKKAKEVE LVSE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072589 box H/ACA scaRNP complex
Cellular Component GO:0031429 box H/ACA snoRNP complex
Cellular Component GO:0090661 box H/ACA telomerase RNP complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005697 telomerase holoenzyme complex
Molecular Function GO:0034513 box H/ACA snoRNA binding
Molecular Function GO:0009982 pseudouridine synthase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003720 telomerase activity
Molecular Function GO:0070034 telomerase RNA binding
Biological Process GO:0000495 box H/ACA sno(s)RNA 3'-end processing
Biological Process GO:0000455 enzyme-directed rRNA pseudouridine synthesis
Biological Process GO:1990481 mRNA pseudouridine synthesis
Biological Process GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Biological Process GO:0032212 positive regulation of telomere maintenance via telomerase
Biological Process GO:1904867 protein localization to Cajal body
Biological Process GO:1904872 regulation of telomerase RNA localization to Cajal body
Biological Process GO:0006396 RNA processing
Biological Process GO:0006364 rRNA processing
Biological Process GO:0031118 rRNA pseudouridine synthesis
Biological Process GO:0090666 scaRNA localization to Cajal body
Biological Process GO:0031120 snRNA pseudouridine synthesis
Biological Process GO:0090669 telomerase RNA stabilization
Biological Process GO:0007004 telomere maintenance via telomerase

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] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] 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.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] 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.

[7] 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.