HTATSF1
entrez
27336
canonical
uniprot
O43719
canonical
ensembl
ENSG00000102241
resolver
ensp
ENSP00000218364
resolver
ensp
ENSP00000442699
resolver
ensp
ENSP00000537055
resolver
ensp
ENSP00000537056
resolver
ensp
ENSP00000598676
resolver
enst
ENST00000218364
resolver
enst
ENST00000535601
resolver
enst
ENST00000866996
resolver
enst
ENST00000866997
resolver
enst
ENST00000928617
resolver
genesymbol
HTATSF1
resolver
hgnc
HGNC:5276
resolver
uniprot
D3DWG9
resolver
uniprot
Q59G06
resolver
uniprot
Q99730
resolver
uniprot_entry
HTSF1_HUMAN
resolver
uniprot_sec
D3DWG9
resolver
uniprot_sec
Q59G06
resolver
uniprot_sec
Q99730
resolver
amino_acid_sequence
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFRDPEEADYCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEANRGLRRSDSVSASERAGPSRARHFSEHPSTSKMNAQETATGMAFEEPIDEKKFEKTEDGGEFEEGASENNAKESSPEKEAEEGCPEKESEEGCPKRGFEGSCSQKESEEGNPVRGSEEDSPKKESKKKTLKNDCEENGLAKESEDDLNKESEEEVGPTKESEEDDSEKESDEDCSEKQSEDGSEREFEENGLEKDLDEEGSEKELHENVLDKELEENDSENSEFEDDGSEKVLDEEGSEREFDEDSDEKEEEEDTYEKVFDDESDEKEDEEYADEKGLEAADKKAEEGDADEKLFEESDDKEDEDADGKEVEDADEKLFEDDDSNEKLFDEEEDSSEKLFDDSDERGTLGGFGSVEEGPLSTGSSFILSSDDDDDDI
uniprot
proteins
function
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). {ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11780068, ECO:0000269|PubMed:30567737, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451, ECO:0000269|PubMed:9765201}.
uniprot
proteins
mass_dalton
85853
uniprot
proteins
mutagenesis
MUTAGEN 136; /note="Y->D: Loss of interaction with U snRNPs."; /evidence="ECO:0000269|PubMed:11780068"; MUTAGEN 155..156; /note="KF->AA: In 4A mutant; abolished binding to poly-ADP-ribosylated RPA1 and recruitment to DNA damage sites; when associated with 297-A-A-298."; /evidence="ECO:0000269|PubMed:35597237"; MUTAGEN 297..298; /note="KF->AA: In 4A mutant; abolished binding to poly-ADP-ribosylated RPA1 and recruitment to DNA damage sites; when associated with 155-A-A-156."; /evidence="ECO:0000269|PubMed:35597237"; MUTAGEN 748; /note="S->A: Impaired phosphorylation by CK2, leading to abolish interaction with TOPBP1."; /evidence="ECO:0000269|PubMed:35597237
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-748 by CK2 during S-phase in response to DNA damage promotes interaction with TOPBP1 and double-strand break (DSB) repair via homologous recombination. {ECO:0000269|PubMed:35597237}.
uniprot
proteins
protein_family
HTATSF1 family
uniprot
proteins
pubmed
10393184
uniprot
proteins
pubmed
10454543
uniprot
proteins
pubmed
10913173
uniprot
proteins
pubmed
11420046
uniprot
proteins
pubmed
11780068
uniprot
proteins
pubmed
15485897
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15905670
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30567737
uniprot
proteins
pubmed
32494006
uniprot
proteins
pubmed
34822310
uniprot
proteins
pubmed
35597237
uniprot
proteins
pubmed
36797247
uniprot
proteins
pubmed
8849451
uniprot
proteins
pubmed
9649438
uniprot
proteins
pubmed
9710584
uniprot
proteins
pubmed
9765201
uniprot
proteins
sequence_length
755
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:8849451}. Chromosome {ECO:0000269|PubMed:35597237}. Note=Recruited to DNA damage sites during S-phase following interaction with poly-ADP-ribosylated RPA1. {ECO:0000269|PubMed:35597237}.
uniprot
proteins