CPLM-001650

Genbank Nucleotide ID

Polypyrimidine tract-binding protein 3

Protein Synonyms/Alias

Regulator of differentiation 1; Rod1

Homo sapiens (Human)

Position	Peptide	Type	References
47	ANGNDSKKFKRDRPP	ubiquitination	[1]
65	SRVLHLRKIPCDVTE	ubiquitination	[1, 2]
92	VTNLLMLKGKSQAFL	ubiquitination	[3]
137	YSNHRELKTDNLPNQ	ubiquitination	[1, 2, 4, 5]
236	PVNAHYAKMALDGQN	ubiquitination	[4]
257	TLRIDFSKLTSLNVK	acetylation	[6]
257	TLRIDFSKLTSLNVK	ubiquitination	[3, 4]
264	KLTSLNVKYNNDKSR	acetylation	[6]
264	KLTSLNVKYNNDKSR	ubiquitination	[3]
389	YGDVHRVKIMFNKKE	ubiquitination	[1]
423	SGQRLYGKVLRATLS	acetylation	[6]
423	SGQRLYGKVLRATLS	ubiquitination	[1, 2, 3]
431	VLRATLSKHQAVQLP	ubiquitination	[1, 2, 3]
449	QEDQGLTKDFSNSPL	ubiquitination	[1, 2, 3, 4, 5, 7]
503	IEAGCSVKAFKFFQK	ubiquitination	[1, 2]
506	GCSVKAFKFFQKDRK	ubiquitination	[1, 2]
510	KAFKFFQKDRKMALI	acetylation	[6]
549	HLRVSFSKSTI****	acetylation	[6]
549	HLRVSFSKSTI****	ubiquitination	[4]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]

Functional Description

RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U).

DOMAIN 59 143 RRM 1.
DOMAIN 182 258 RRM 2.
DOMAIN 358 432 RRM 3.
DOMAIN 475 550 RRM 4.
MOD_RES 423 423 N6-acetyllysine.

Acetylation; Alternative splicing; Complete proteome; Differentiation; Erythrocyte maturation; mRNA processing; mRNA splicing; Reference proteome; Repeat; Repressor; RNA-binding.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IEA:InterPro.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; TAS:ProtInc.
GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
GO:0045595; P:regulation of cell differentiation; IEA:Compara.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.

IPR006536; HnRNP-L_PTB.
IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.