UniProt Accession

 SRSF1_HUMAN; Q07955; B2R6Z7; D3DTZ3; Q13809 

Genbank Protein ID

 M72709; M72709; M69040; AB062124; AK312781; CH471109; CH471109; BC010264; BC033785 

Genbank Nucleotide ID

 AAA35565.1; AAA35564.1; AAA03476.1; BAB93456.1; BAG35644.1; EAW94485.1; EAW94486.1; AAH10264.1; AAH33785.1 

Protein Name

 Serine/arginine-rich splicing factor 1 

Protein Synonyms/Alias

 Alternative-splicing factor 1; ASF-1; Splicing factor, arginine/serine-rich 1; pre-mRNA-splicing factor SF2, P33 subunit 

Gene Name

 SRSF1 

Gene Synonyms/Alias

 ASF; SF2; SF2P33; SFRS1; OK/SW-cl.3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
30	LPPDIRTKDIEDVFY	ubiquitination	[1, 2, 3, 4, 5]
38	DIEDVFYKYGAIRDI	acetylation	[6]
38	DIEDVFYKYGAIRDI	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9]
138	SGSWQDLKDHMREAG	ubiquitination	[1, 2, 3, 4, 5]
165	GVVEFVRKEDMTYAV	ubiquitination	[4]
174	DMTYAVRKLDNTKFR	ubiquitination	[1, 5]
179	VRKLDNTKFRSHEGE	acetylation	[6]
179	VRKLDNTKFRSHEGE	ubiquitination	[1, 4, 5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 16 91 RRM 1.
 DOMAIN 121 195 RRM 2.
 REGION 198 247 Interacts with SAFB1.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 38 38 N6-acetyllysine.
 MOD_RES 179 179 N6-acetyllysine.
 MOD_RES 199 199 Phosphoserine.
 MOD_RES 201 201 Phosphoserine (By similarity).
 MOD_RES 205 205 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 234 234 Phosphoserine.
 MOD_RES 238 238 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Spliceosome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 248 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016607; C:nuclear speck; IDA:MGI.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0060048; P:cardiac muscle contraction; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0000395; P:mRNA 5'-splice site recognition; IDA:UniProtKB.
 GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS