SF3B2
entrez
10992
canonical
uniprot
Q13435
canonical
ensembl
ENSG00000087365
resolver
ensp
ENSP00000318861
resolver
ensp
ENSP00000563630
resolver
ensp
ENSP00000563633
resolver
enst
ENST00000322535
resolver
genesymbol
SF3B2
resolver
genesymbol_syn
SAP145
resolver
hgnc
HGNC:10769
resolver
uniprot
A8K485
resolver
uniprot
B4DT19
resolver
uniprot
Q7L4T5
resolver
uniprot
Q7Z627
resolver
uniprot
Q969K1
resolver
uniprot
Q96CM6
resolver
uniprot
Q9BWD2
resolver
uniprot_entry
SF3B2_HUMAN
resolver
uniprot_sec
A8K485
resolver
uniprot_sec
B4DT19
resolver
uniprot_sec
Q7L4T5
resolver
uniprot_sec
Q7Z627
resolver
uniprot_sec
Q969K1
resolver
uniprot_sec
Q96CM6
resolver
uniprot_sec
Q9BWD2
resolver
amino_acid_sequence
MATEHPEPPKAELQLPPPPPPGHYGAWAAQELQAKLAEIGAPIQGNREELVERLQSYTRQTGIVLNRPVLRGEDGDKAAPPPMSAQLPGIPMPPPPLGLPPLQPPPPPPPPPPGLGLGFPMAHPPNLGPPPPLRVGEPVALSEEERLKLAQQQAALLMQQEERAKQQGDHSLKEHELLEQQKRAAVLLEQERQQEIAKMGTPVPRPPQDMGQIGVRTPLGPRVAAPVGPVGPTPTVLPMGAPVPRPRGPPPPPGDENREMDDPSVGPKIPQALEKILQLKESRQEEMNSQQEEEEMETDARSSLGQSASETEEDTVSVSKKEKNRKRRNRKKKKKPQRVRGVSSESSGDREKDSTRSRGSDSPAADVEIEYVTEEPEIYEPNFIFFKRIFEAFKLTDDVKKEKEKEPEKLDKLENSAAPKKKGFEEEHKDSDDDSSDDEQEKKPEAPKLSKKKLRRMNRFTVAELKQLVARPDVVEMHDVTAQDPKLLVHLKATRNSVPVPRHWCFKRKYLQGKRGIEKPPFELPDFIKRTGIQEMREALQEKEEQKTMKSKMREKVRPKMGKIDIDYQKLHDAFFKWQTKPKLTIHGDLYYEGKEFETRLKEKKPGDLSDELRISLGMPVGPNAHKVPPPWLIAMQRYGPPPSYPNLKIPGLNSPIPESCSFGYHAGGWGKPPVDETGKPLYGDVFGTNAAEFQTKTEEEEIDRTPWGELEPSDEESSEEEEEEESDEDKPDETGFITPADSGLITPGGFSSVPAGMETPELIELRKKKIEEAMDGSETPQLFTVLPEKRTATVGGAMMGSTHIYDMSTVMSRKGPAPELQGVEVALAPEELELDPMAMTQKYEEHVREQQAQVEKEDFSDMVAEHAAKQKQKKRKAQPQDSRGGSKKYKEFKF
uniprot
proteins
disease_involvement
DISEASE: Craniofacial microsomia 1 (CFM1) [MIM:164210]: A form of craniofacial microsomia, a disorder characterized by a spectrum of craniofacial malformations ranging from isolated microtia with or without aural atresia to underdevelopment of the mandible, maxilla, orbit, facial soft tissue, and/or facial nerve. CFM1 is an autosomal dominant form characterized by mandibular hypoplasia, microtia, facial and preauricular skin tags, epibulbar dermoids, and lateral oral clefts. Affected individuals also present skeletal and cardiac abnormalities. {ECO:0000269|PubMed:34344887}. Note=The disease is caused by variants affecting the gene represented in this entry.
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: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:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B2 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:27720643). 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). {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}.
uniprot
proteins
mass_dalton
100228
uniprot
proteins
mutagenesis
MUTAGEN 471; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 495; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 502; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 506; /note="F->A: Does not affect methylation by PRMT9; when associated with A-510."; /evidence="ECO:0000269|PubMed:25979344"; MUTAGEN 507; /note="K->A: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-509."; /evidence="ECO:0000269|PubMed:25979344"; MUTAGEN 507; /note="K->R: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-509. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-508. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-509."; /evidence="ECO:0000269|PubMed:25979344"; MUTAGEN 508; /note="R->K: Abolishes interaction with SMN1; Abolishes methylation by PRMT9. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507 and R-509."; /evidence="ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:25979344"; MUTAGEN 509; /note="K->A: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-507."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 509; /note="K->R: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-507."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 510; /note="Y->A: Does not affect methylation by PRMT9; when associated with A-506."; /evidence="ECO:0000269|PubMed:25979344"; MUTAGEN 515; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 530; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013"; MUTAGEN 537; /note="R->K: Does not affect methylation by PRMT9."; /evidence="ECO:0000269|PubMed:25737013
uniprot
proteins
post_translational_modification
PTM: Methylation at Arg-508 by PRMT9 is required for the interaction with SMN1. {ECO:0000269|PubMed:25737013}.
uniprot
proteins
pubmed
10882114
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
12234937
uniprot
proteins
pubmed
12738865
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15146077
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16923959
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18318008
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
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25737013
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25979344
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
27720643
uniprot
proteins
pubmed
27905398
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28541300
uniprot
proteins
pubmed
32494006
uniprot
proteins
pubmed
33509932
uniprot
proteins
pubmed
34344887
uniprot
proteins
pubmed
34822310
uniprot
proteins
pubmed
36797247
uniprot
proteins
pubmed
8566756
uniprot
proteins
sequence_length
895
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300}. Nucleus speckle {ECO:0000269|PubMed:16923959}.
uniprot
proteins