SRSF2
entrez
6427
canonical
uniprot
Q01130
canonical
ensembl
ENSG00000161547
resolver
ensp
ENSP00000353089
resolver
ensp
ENSP00000376276
resolver
genesymbol
SRSF2
resolver
genesymbol_syn
SFRS2
resolver
hgnc
HGNC:10783
resolver
uniprot
B3KWD5
resolver
uniprot
B4DN89
resolver
uniprot
H0YG49
resolver
uniprot
Q53FN0
resolver
uniprot_entry
Q53FN0_HUMAN
resolver
uniprot_entry
SRSF2_HUMAN
resolver
uniprot_sec
B3KWD5
resolver
uniprot_sec
B4DN89
resolver
uniprot_sec
H0YG49
resolver
amino_acid_sequence
MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS
uniprot
proteins
function
FUNCTION: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment. {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21157427}.
uniprot
proteins
mass_dalton
25476
uniprot
proteins
post_translational_modification
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by SRPK2 and this causes its redistribution from the nuclear speckle to nucleoplasm and controls cell fate decision in response to cisplatin treatment. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2 nuclear translocation. {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21157427}.; PTM: Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal degradation. This effect is counterbalanced by HDAC6, which positively controls SRSF2 protein level by deacetylating it and preventing its proteasomal degradation. {ECO:0000269|PubMed:21157427, ECO:0000269|Ref.10}.
uniprot
proteins
protein_family
Splicing factor SR family
uniprot
proteins
pubmed
10757789
uniprot
proteins
pubmed
11980906
uniprot
proteins
pubmed
1373910
uniprot
proteins
pubmed
1465383
uniprot
proteins
pubmed
14684736
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1557353
uniprot
proteins
pubmed
1577277
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19592491
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21157427
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21296756
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
34237909
uniprot
proteins
pubmed
7543047
uniprot
proteins
pubmed
8139654
uniprot
proteins
pubmed
8261509
uniprot
proteins
pubmed
8302870
uniprot
proteins
pubmed
8361546
uniprot
proteins
pubmed
9237760
uniprot
proteins
pubmed
9447963
uniprot
proteins
sequence_length
221
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21157427}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21157427}. Nucleus speckle {ECO:0000269|PubMed:21157427}. Note=Phosphorylation by SRPK2 provokes its redistribution from the nuclear speckle to nucleoplasm.
uniprot
proteins