CPLM-023104

Genbank Nucleotide ID

RNA-binding protein Raly

Protein Synonyms/Alias

Autoantigen p542; Heterogeneous nuclear ribonucleoprotein C-like 2; hnRNP core protein C-like 2; hnRNP associated with lethal yellow protein homolog

Homo sapiens (Human)

Position	Peptide	Type	References
4	****MSLKLQASNVT	ubiquitination	[1, 2, 3]
13	QASNVTNKNDPKSIN	ubiquitination	[3, 4]
17	VTNKNDPKSINSRVF	ubiquitination	[3]
34	NLNTALVKKSDVETI	ubiquitination	[1, 2, 3]
44	DVETIFSKYGRVAGC	ubiquitination	[1, 3, 4]
55	VAGCSVHKGYAFVQY	ubiquitination	[2, 3, 4]
146	VPRAVPVKRPRVTVP	ubiquitination	[3]
159	VPLVRRVKTNVPVKL	ubiquitination	[3]
165	VKTNVPVKLFARSTA	acetylation	[5]
165	VKTNVPVKLFARSTA	ubiquitination	[1, 3]
179	AVTTSSAKIKLKSSE	ubiquitination	[3]
181	TTSSAKIKLKSSELQ	acetylation	[6]
181	TTSSAKIKLKSSELQ	ubiquitination	[3]
183	SSAKIKLKSSELQAI	acetylation	[6]
191	SSELQAIKTELTQIK	ubiquitination	[1]
216	EQIAAEQKANPDGKK	ubiquitination	[2, 3, 4]

[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] 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]
[3] 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]
[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] 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]
[6] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]

Functional Description

Probable-RNA binding protein. Could be a heterogeneous nuclear ribonucleoprotein (hnRNP). May be involved in pre-mRNA splicing (By similarity).

DOMAIN 21 92 RRM.
REGION 227 253 Epitope (recognized by BKRF1 antibodies).
MOD_RES 106 106 Phosphoserine.
MOD_RES 135 135 Phosphoserine.
MOD_RES 165 165 N6-acetyllysine.
MOD_RES 262 262 Phosphothreonine (By similarity).
MOD_RES 264 264 Phosphoserine (By similarity).
MOD_RES 286 286 Phosphothreonine.
MOD_RES 288 288 Phosphoserine.
MOD_RES 295 295 Phosphoserine.
MOD_RES 298 298 Phosphothreonine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; TAS:ProtInc.
GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.

IPR017347; hnRNP_C_Raly.
IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.