Search Results

Overview

Uniprot IDO43719
Protein Name17S U2 SnRNP complex component HTATSF1
Gene NameHTATSF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 AEEPPQEKAPEPTDA
119 RKKGEKRKAESGWFH
221 EVAKFQLKGEYDASK
228 KGEYDASKKKKKCKD
239 KCKDYKKKLSMQQKQ
245 KKLSMQQKQLDWRPE
297 DLRVECSKFGQIRKL
303 SKFGQIRKLLLFDRH
410 SEHPSTSKMNAQETA
509 ESKKKTLKNDCEENG

Function

Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237)

Protein Sequence

10 MSGTNLDGND 20 EFDEQLRMQE 30 LYGDGKDGDT 40 QTDAGGEPDS 50 LGQQPTDTPY 60 EWDLDKKAWF 70 PKITEDFIAT 80 YQANYGFSND 90 GASSSTANVE 100 DVHARTAEEP 110 PQEKAPEPTD 120 ARKKGEKRKA 130 ESGWFHVEED 140 RNTNVYVSGL 150 PPDITVDEFI 160 QLMSKFGIIM 170 RDPQTEEFKV 180 KLYKDNQGNL 190 KGDGLCCYLK 200 RESVELALKL 210 LDEDEIRGYK 220 LHVEVAKFQL 230 KGEYDASKKK 240 KKCKDYKKKL 250 SMQQKQLDWR 260 PERRAGPSRM 270 RHERVVIIKN 280 MFHPMDFEDD 290 PLVLNEIRED 300 LRVECSKFGQ 310 IRKLLLFDRH 320 PDGVASVSFR 330 DPEEADYCIQ 340 TLDGRWFGGR 350 QITAQAWDGT 360 TDYQVEETSR 370 EREERLRGWE 380 AFLNAPEANR 390 GLRRSDSVSA 400 SERAGPSRAR 410 HFSEHPSTSK 420 MNAQETATGM 430 AFEEPIDEKK 440 FEKTEDGGEF 450 EEGASENNAK 460 ESSPEKEAEE 470 GCPEKESEEG 480 CPKRGFEGSC 490 SQKESEEGNP 500 VRGSEEDSPK 510 KESKKKTLKN 520 DCEENGLAKE 530 SEDDLNKESE 540 EEVGPTKESE 550 EDDSEKESDE 560 DCSEKQSEDG 570 SEREFEENGL 580 EKDLDEEGSE 590 KELHENVLDK 600 ELEENDSENS 610 EFEDDGSEKV 620 LDEEGSEREF 630 DEDSDEKEEE 640 EDTYEKVFDD 650 ESDEKEDEEY 660 ADEKGLEAAD 670 KKAEEGDADE 680 KLFEESDDKE 690 DEDADGKEVE 700 DADEKLFEDD 710 DSNEKLFDEE 720 EDSSEKLFDD 730 SDERGTLGGF 740 GSVEEGPLST 750 GSSFILSSDD DDDDI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Cellular Component GO:0005686 U2 snRNP
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0140463 chromatin-protein adaptor activity
Molecular Function GO:0160004 poly-ADP-D-ribose modification-dependent protein binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:1990166 protein localization to site of double-strand break
Biological Process GO:1903241 U2-type prespliceosome assembly

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] 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.

[6] 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.