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Overview

Uniprot IDQ9UHI6
Protein NameProbable ATP-dependent RNA helicase DDX20
Gene NameDDX20
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
473 SVPNQPLKKQIQKIE
474 VPNQPLKKQIQKIER
487 ERTLQIQKAHGDHMA
507 SVSGLSVKSKNNTKQ
509 SGLSVKSKNNTKQKL
519 TKQKLPVKSHSECGI
529 SECGIIEKATSPKEL

Function

The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)

Protein Sequence

10 MAAAFEASGA 20 LAAVATAMPA 30 EHVAVQVPAP 40 EPTPGPVRIL 50 RTAQDLSSPR 60 TRTGDVLLAE 70 PADFESLLLS 80 RPVLEGLRAA 90 GFERPSPVQL 100 KAIPLGRCGL 110 DLIVQAKSGT 120 GKTCVFSTIA 130 LDSLVLENLS 140 TQILILAPTR 150 EIAVQIHSVI 160 TAIGIKMEGL 170 ECHVFIGGTP 180 LSQDKTRLKK 190 CHIAVGSPGR 200 IKQLIELDYL 210 NPGSIRLFIL 220 DEADKLLEEG 230 SFQEQINWIY 240 SSLPASKQML 250 AVSATYPEFL 260 ANALTKYMRD 270 PTFVRLNSSD 280 PSLIGLKQYY 290 KVVNSYPLAH 300 KVFEEKTQHL 310 QELFSRIPFN 320 QALVFSNLHS 330 RAQHLADILS 340 SKGFPAECIS 350 GNMNQNQRLD 360 AMAKLKHFHC 370 RVLISTDLTS 380 RGIDAEKVNL 390 VVNLDVPLDW 400 ETYMHRIGRA 410 GRFGTLGLTV 420 TYCCRGEEEN 430 MMMRIAQKCN 440 INLLPLPDPI 450 PSGLMEECVD 460 WDVEVKAAVH 470 TYGIASVPNQ 480 PLKKQIQKIE 490 RTLQIQKAHG 500 DHMASSRNNS 510 VSGLSVKSKN 520 NTKQKLPVKS 530 HSECGIIEKA 540 TSPKELGCDR 550 QSEEQMKNSV 560 QTPVENSTNS 570 QHQVKEALPV 580 SLPQIPCLSS 590 FKIHQPYTLT 600 FAELVEDYEH 610 YIKEGLEKPV 620 EIIRHYTGPG 630 DQTVNPQNGF 640 VRNKVIEQRV 650 PVLASSSQSG 660 DSESDSDSYS 670 SRTSSQSKGN 680 KSYLEGSSDN 690 QLKDSESTPV 700 DDRISLEQPP 710 NGSDTPNPEK 720 YQESPGIQMK 730 TRLKEGASQR 740 AKQSRRNLPR 750 RSSFRLQTEA 760 QEDDWYDCHR 770 EIRLSFSDTY 780 QDYEEYWRAY 790 YRAWQEYYAA 800 ASHSYYWNAQ 810 RHPSWMAAYH 820 MNTIYLQEMM HSNQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0097504 Gemini of Cajal bodies
Cellular Component GO:0016020 membrane
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0090571 RNA polymerase II transcription repressor complex
Cellular Component GO:0032797 SMN complex
Cellular Component GO:0034719 SMN-Sm protein complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0042826 histone deacetylase binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003724 RNA helicase activity
Biological Process GO:0008285 negative regulation of cell population proliferation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0006396 RNA processing
Biological Process GO:0000387 spliceosomal snRNP assembly
Biological Process GO:0000244 spliceosomal tri-snRNP complex assembly

Reference

[1] 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.

[2] 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.