CPLM-017599

Genbank Nucleotide ID

Plasminogen activator inhibitor 1 RNA-binding protein

Protein Synonyms/Alias

PAI1 RNA-binding protein 1; PAI-RBP1; SERPINE1 mRNA-binding protein 1

Homo sapiens (Human)

Position	Peptide	Type	References
32	SDPFEVLKAAENKKK	ubiquitination	[1, 2, 3, 4]
37	VLKAAENKKKEAGGG	ubiquitination	[1, 3]
39	KAAENKKKEAGGGGV	ubiquitination	[2]
52	GVGGPGAKSAAQAAA	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
68	TNSNAAGKQLRKESQ	acetylation	[7, 8, 9]
68	TNSNAAGKQLRKESQ	ubiquitination	[1, 2, 3, 4, 6, 7, 10, 11]
72	AAGKQLRKESQKDRK	ubiquitination	[6]
92	SVGVVDKKEETQPPV	acetylation	[9]
122	QQLQGEGKIIDRRPE	acetylation	[7, 8, 9, 12]
122	QQLQGEGKIIDRRPE	ubiquitination	[1, 2, 7, 10, 11]
140	PRERRFEKPLEEKGE	acetylation	[7, 8, 12]
211	FSHYSGLKHEDKRGG	acetylation	[8, 9]
211	FSHYSGLKHEDKRGG	ubiquitination	[2, 7]
236	DELTESPKYIQKQIS	acetylation	[9]
236	DELTESPKYIQKQIS	ubiquitination	[10, 11]
240	ESPKYIQKQISYNYS	ubiquitination	[4]
294	EMTLDEWKAIQNKDR	ubiquitination	[10, 11]
303	IQNKDRAKVEFNIRK	ubiquitination	[6]
310	KVEFNIRKPNEGADG	ubiquitination	[6, 7]
320	EGADGQWKKGFVLHK	ubiquitination	[1, 4, 5, 6, 7]
321	GADGQWKKGFVLHKS	ubiquitination	[6]
329	GFVLHKSKSEEAHAE	ubiquitination	[6]
390	NRGSRTDKSSASAPD	ubiquitination	[1]

[1] 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]
[2] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[3] 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]
[4] 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]
[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] 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]
[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 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]
[10] 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]
[11] 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]
[12] 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]

Functional Description

May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay.

MOD_RES 25 25 Phosphoserine.
MOD_RES 68 68 N6-acetyllysine.
MOD_RES 122 122 N6-acetyllysine.
MOD_RES 140 140 N6-acetyllysine.
MOD_RES 211 211 N6-acetyllysine.
MOD_RES 234 234 Phosphoserine.
MOD_RES 244 244 Phosphotyrosine (By similarity).
MOD_RES 252 252 Phosphoserine (By similarity).
MOD_RES 330 330 Phosphoserine.
MOD_RES 391 391 Phosphoserine (By similarity).
MOD_RES 392 392 Phosphoserine.
MOD_RES 394 394 Phosphoserine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO:0005886; C:plasma membrane; IEA:Compara.
GO:0003730; F:mRNA 3'-UTR binding; IDA:HGNC.
GO:0043488; P:regulation of mRNA stability; NAS:HGNC.

IPR006861; HABP4_PAIRBP1-bd.
IPR027205; SERBP1.

PF04774; HABP4_PAI-RBP1