UniProt Accession

 SRSF7_HUMAN; Q16629; B4DLU6; G5E9M3; Q564D3 

Genbank Protein ID

 L22253; L41887; AB445102; AY166860; BT006745; AY513287; AK297161; AC074366; CH471053; CH471053; BC000997; BC017369; BC017908; BC022328 

Genbank Nucleotide ID

 AAA35495.1; AAA88098.1; BAI99737.1; AAN87842.1; AAP35391.1; AAT08040.1; BAG59658.1; AAX93102.1; EAX00365.1; EAX00366.1; AAH00997.1; AAH17369.1; AAH17908.1; AAH22328.1 

Protein Name

 Serine/arginine-rich splicing factor 7 

Protein Synonyms/Alias

 Splicing factor 9G8; Splicing factor, arginine/serine-rich 7 

Gene Name

 SRSF7 

Gene Synonyms/Alias

 SFRS7 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
12	GRYGGETKVYVGNLG	ubiquitination	[1, 2, 3]
24	NLGTGAGKGELERAF	acetylation	[4]
24	NLGTGAGKGELERAF	ubiquitination	[1, 2, 3, 5, 6, 7, 8]
70	AVRGLDGKVICGSRV	ubiquitination	[2, 6, 8]
112	RCYECGEKGHYAYDC	ubiquitination	[2, 8]
185	RSRSGSIKGSRYFQS	acetylation	[4]

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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] 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]
 [8] 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] 

Functional Description

 Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. 

Sequence Annotation

 DOMAIN 11 84 RRM.
 REPEAT 153 160 1.
 REPEAT 161 168 2.
 REPEAT 169 176 3.
 REPEAT 177 184 4.
 REPEAT 211 218 5; approximate.
 REPEAT 219 226 6; approximate.
 ZN_FING 104 120 CCHC-type.
 REGION 153 226 6 X 8 AA repeats of R-R-S-R-S-X-S-X.
 MOD_RES 24 24 N6-acetyllysine.
 MOD_RES 163 163 Phosphoserine (By similarity).
 MOD_RES 165 165 Phosphoserine (By similarity).
 MOD_RES 167 167 Phosphoserine (By similarity).
 MOD_RES 179 179 Phosphoserine (By similarity).
 MOD_RES 181 181 Phosphoserine (By similarity).
 MOD_RES 183 183 Phosphoserine (By similarity).
 MOD_RES 187 187 Phosphoserine (By similarity).
 MOD_RES 192 192 Phosphoserine.
 MOD_RES 194 194 Phosphoserine.
 MOD_RES 196 196 Phosphoserine.
 MOD_RES 223 223 Phosphoserine (By similarity).
 MOD_RES 225 225 Phosphoserine (By similarity).
 MOD_RES 227 227 Phosphoserine (By similarity).
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 233 233 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 238 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR001878; Znf_CCHC. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM
 SM00343; ZnF_C2HC 

PROSITE

 PS50102; RRM
 PS50158; ZF_CCHC 

PRINTS