CPLM-012041

Genbank Nucleotide ID

Serine/arginine-rich splicing factor 5

Protein Synonyms/Alias

Delayed-early protein HRS; Pre-mRNA-splicing factor SRP40; Splicing factor, arginine/serine-rich 5

Homo sapiens (Human)

Position	Peptide	Type	References
25	KDVERFFKGYGRIRD	ubiquitination	[1, 2, 3]
60	AVYELDGKELCSERV	ubiquitination	[4]
125	RVSWQDLKDFMRQAG	ubiquitination	[1, 2, 3, 5, 6, 7]
163	DLKNAIEKLSGKEIN	acetylation	[7]
163	DLKNAIEKLSGKEIN	ubiquitination	[7]
167	AIEKLSGKEINGRKI	acetylation	[7, 8, 9, 10]
167	AIEKLSGKEINGRKI	ubiquitination	[2]

[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] 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]
[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] 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]
[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] 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]
[7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[8] 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]
[9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.

DOMAIN 4 74 RRM 1.
DOMAIN 108 181 RRM 2.
MOD_RES 167 167 N6-acetyllysine.
MOD_RES 227 227 Phosphoserine.
MOD_RES 229 229 Phosphoserine.
MOD_RES 231 231 Phosphoserine (By similarity).
MOD_RES 233 233 Phosphoserine.
MOD_RES 248 248 Phosphoserine (By similarity).
MOD_RES 250 250 Phosphoserine.
MOD_RES 253 253 Phosphoserine.
MOD_RES 263 263 Phosphoserine (By similarity).
MOD_RES 265 265 Phosphoserine (By similarity).
MOD_RES 267 267 Phosphoserine (By similarity).
MOD_RES 270 270 Phosphoserine (By similarity).

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO:0006376; P:mRNA splice site selection; TAS:ProtInc.
GO:0051726; P:regulation of cell cycle; IEA:Compara.
GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.

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