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Details on Person UniProt:Q07955 SRSF1

Class:Id	ReferenceGeneProduct:72030
_chainChangeLog	initiator methionine:1 added on Fri February 6 2015;chain:2-248 added on Fri February 6 2015;initiator methionine:1 for 72030 removed on Fri Nov 03 2023;initiator methionine: for 72030 added on Fri Nov 03 2023;initiator methionine: for 72030 removed on Fri Aug 15 2025;initiator methionine:1 for 72030 added on Fri Aug 15 2025
_displayName	UniProt:Q07955 SRSF1
_timestamp	2025-08-15 21:41:42
chain	initiator methionine:1 chain:2-248
checksum	C28A0B2F112EA713
comment	FUNCTION Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. 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. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.SUBUNIT Consists of two polypeptides of p32 and p33. Identified in the spliceosome C complex (PubMed:11991638). Component of a ribonucleoprotein complex containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF (PubMed:24644279). In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1. Interacts with CCNL1, CCNL2 and CDK11B (PubMed:18216018). Interacts with RRP1B (PubMed:23604122). Interacts (when phosphorylated in its RS domain) with TNPO3; promoting nuclear import (PubMed:24449914). Interacts with ILDR1 (via C-terminus) and ILDR2 (By similarity).INTERACTION In nuclear speckles. Shuttles between the nucleus and the cytoplasm (PubMed:12215544, PubMed:20308322, PubMed:24449914, PubMed:9420331). Nuclear import is mediated via interaction with TNPO3 (PubMed:24449914).ALTERNATIVE PRODUCTS The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling.PTM Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed.PTM Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS May be due to intron retention.SIMILARITY Belongs to the splicing factor SR family.
description	recommendedName: fullName evidence="32"Serine/arginine-rich splicing factor 1 alternativeName: Alternative-splicing factor 1 shortName: ASF-1 alternativeName: Splicing factor, arginine/serine-rich 1 alternativeName: pre-mRNA-splicing factor SF2, P33 subunit
geneName	SRSF1 ASF SF2 SF2P33 SFRS1 OK/SW-cl.3
identifier	Q07955
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing Cytoplasm Direct protein sequencing Disease variant Intellectual disability Isopeptide bond Methylation mRNA processing mRNA splicing mRNA transport Nucleus Phosphoprotein Proteomics identification Reference proteome Repeat RNA-binding Spliceosome Transport Ubl conjugation
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15
name	SRSF1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8962352] ENSEMBL:ENSG00000136450 SRSF1 [Homo sapiens]
secondaryIdentifier	SRSF1_HUMAN B2R6Z7 D3DTZ3 Q13809
sequenceLength	248
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:153764] UniProt:Q07955-2 SRSF1 [Homo sapiens] [ReferenceIsoform:153765] UniProt:Q07955-3 SRSF1 [Homo sapiens] [ReferenceIsoform:405268] UniProt:Q07955-1 SRSF1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:72031] SRSF1 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:8980137] SRSF1 [cytosol] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q07955 SRSF1 (72030)