UniProt Accession

 RUXG_HUMAN; P62308; D6W5G6; Q15357; Q6IB86 

Genbank Protein ID

 X85373; CR456918; AC079338; CH471053; CH471053; BC000070; BC022432; BC066302; BC070166; BC071880; BC106055 

Genbank Nucleotide ID

 CAA59689.1; CAG33199.1; AAX81996.1; EAW99817.1; EAW99818.1; AAH00070.1; AAH22432.1; AAH66302.1; AAH70166.1; AAH71880.1; AAI06056.1 

Protein Name

 Small nuclear ribonucleoprotein G 

Protein Synonyms/Alias

 snRNP-G; Sm protein G; Sm-G; SmG 

Gene Name

 SNRPG 

Gene Synonyms/Alias

 PBSCG 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MSKAHPPELK	ubiquitination	[1]
10	KAHPPELKKFMDKKL	ubiquitination	[2]
11	AHPPELKKFMDKKLS	ubiquitination	[1, 2]
20	MDKKLSLKLNGGRHV	ubiquitination	[1, 2, 3, 4, 5]

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] 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]
 [3] 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]
 [4] 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]
 [5] 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

 Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. 

Sequence Annotation

  

Keyword

 3D-structure; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 76 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
 GO:0005683; C:U7 snRNP; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
 GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0034660; P:ncRNA metabolic process; TAS:Reactome.
 GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
 GO:0000387; P:spliceosomal snRNP assembly; TAS:Reactome.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 

Interpro

 IPR010920; LSM_dom.
 IPR001163; Ribonucl_LSM.
 IPR006649; Ribonucl_LSM_euk/arc. 

Pfam

 PF01423; LSM 

SMART

 SM00651; Sm 

PROSITE

  

PRINTS