SF3B1
entrez
23451
canonical
uniprot
O75533
canonical
ensembl
ENSG00000115524
resolver
ensp
ENSP00000335321
resolver
ensp
ENSP00000402997
resolver
ensp
ENSP00000419896
resolver
ensp
ENSP00000498652
resolver
ensp
ENSP00000745936
resolver
ensp
ENSP00000745940
resolver
enst
ENST00000487698
resolver
enst
ENST00000652026
resolver
genesymbol
SF3B1
resolver
genesymbol_syn
SAP155
resolver
hgnc
HGNC:10768
resolver
uniprot
A0A494C0N7
resolver
uniprot
B4DGZ4
resolver
uniprot
E9PCH3
resolver
uniprot_entry
A0A494C0N7_HUMAN
resolver
uniprot_entry
B4DGZ4_HUMAN
resolver
uniprot_entry
SF3B1_HUMAN
resolver
uniprot_sec
E9PCH3
resolver
amino_acid_sequence
MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL
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:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310, PubMed:36104565). 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:32494006, PubMed:34822310, PubMed:36104565). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:36104565). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). {ECO:0000250|UniProtKB:Q99NB9, ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:36104565}.
uniprot
proteins
mass_dalton
145830
uniprot
proteins
mutagenesis
MUTAGEN 200; /note="W->A: Abolishes interaction with RBM39; when associated with A-218; A-232; A-254; A-293; A-310 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 218; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-232; A-254; A-293; A-310 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 223; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 227; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 232; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-254; A-293; A-310 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 235; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 244; /note="T->A: Slight inhibition of interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 248; /note="T->A: Slight inhibition of interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 254; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-293; A-310 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 257; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 261; /note="T->A: Slight inhibition of interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 267; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 273; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 278; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 293; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-310 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 296; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 303; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 310; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-338."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 313; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:12105215"; MUTAGEN 338; /note="W->A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-310."; /evidence="ECO:0000269|PubMed:24795046"; MUTAGEN 700; /note="K->E: Does not affect the stability of the SF3B complex interaction with U2AF65. Does not decrease the affinity to RNA."; /evidence="ECO:0000269|PubMed:27720643
uniprot
proteins
post_translational_modification
PTM: Phosphorylation occurs concomitantly with the splicing catalytic steps (PubMed:12105215, PubMed:9585501). Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis (PubMed:12105215). Phosphorylation by CDK11 enables the association between SF3B1 and U5 and U6 snRNAs in the activated spliceosome, thereby promoting spliceosome assembly (PubMed:36104565, PubMed:38059508). {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:36104565, ECO:0000269|PubMed:38059508, ECO:0000269|PubMed:9585501}.; PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99NB9}.
uniprot
proteins
protein_family
SF3B1 family
uniprot
proteins
pubmed
10882114
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12105215
uniprot
proteins
pubmed
12234937
uniprot
proteins
pubmed
12738865
uniprot
proteins
pubmed
15146077
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16432215
uniprot
proteins
pubmed
16603771
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17589525
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21062891
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21700224
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23512658
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24795046
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
26575292
uniprot
proteins
pubmed
27720643
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28541300
uniprot
proteins
pubmed
30567737
uniprot
proteins
pubmed
32494006
uniprot
proteins
pubmed
33509932
uniprot
proteins
pubmed
34023904
uniprot
proteins
pubmed
34365507
uniprot
proteins
pubmed
34822310
uniprot
proteins
pubmed
36104565
uniprot
proteins
pubmed
36797247
uniprot
proteins
pubmed
37813856
uniprot
proteins
pubmed
38059508
uniprot
proteins
pubmed
9585501
uniprot
proteins
sequence_length
1304
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Nucleus speckle {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm. {ECO:0000269|PubMed:12105215}.
uniprot
proteins