CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002817
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 U2 small nuclear ribonucleoprotein A' 
Protein Synonyms/Alias
 U2 snRNP A' 
Gene Name
 SNRPA1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
138YRLYVIYKVPQVRVLubiquitination[1]
151VLDFQKVKLKERQEAubiquitination[1]
172KRGAQLAKDIARRSKacetylation[2]
179KDIARRSKTFNPGAGubiquitination[3, 4, 5, 6]
191GAGLPTDKKKGGPSPubiquitination[4]
192AGLPTDKKKGGPSPGubiquitination[4]
205PGDVEAIKNAIANASubiquitination[3, 4, 5, 6]
221LAEVERLKGLLQSGQubiquitination[1, 3, 4, 5, 6]
Reference
 [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] 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]
 [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] 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]
 [6] 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
Functional Description
 This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA. 
Sequence Annotation
 REPEAT 20 41 LRR 1.
 REPEAT 43 64 LRR 2.
 REPEAT 65 86 LRR 3.
 REPEAT 89 110 LRR 4.
 DOMAIN 123 161 LRRCT.
 MOD_RES 172 172 N6-acetyllysine.
 MOD_RES 178 178 Phosphoserine.
 MOD_RES 197 197 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Leucine-rich repeat; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 255 AA 
Protein Sequence
MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS DNEIRKLDGF 60
PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL VELGDLDPLA SLKSLTYLSI 120
LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV KLKERQEAEK MFKGKRGAQL AKDIARRSKT 180
FNPGAGLPTD KKKGGPSPGD VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD 240
DGEEEMEEDT VTNGS 255 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005686; C:U2 snRNP; TAS:ProtInc.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 
Interpro
 IPR001611; Leu-rich_rpt.
 IPR003603; U2A'_phosphoprotein32A_C. 
Pfam
  
SMART
 SM00446; LRRcap 
PROSITE
 PS51450; LRR 
PRINTS