UniProt Accession

 RU17_HUMAN; P08621; B3KUA3; P78493; P78494; Q15364; Q15686; Q15687; Q15689; Q99377; Q9UE45; Q9UE46; Q9UE47; Q9UE48; Q9UFQ6 

Genbank Protein ID

 X04654; X06814; X06815; X06817; X07402; X06816; X06812; X06811; X07401; X07403; M22636; M57939; M57929; M57930; M57932; M57934; M57937; M57939; M57929; M57930; M57932; M57934; M57937; M57935; M57929; M57930; M57932; M57934; AK096783; X84841; AL117507; CH471177; BC001315 

Genbank Nucleotide ID

 CAA28352.1; CAA29963.1; CAA29964.1; CAA29966.1; CAA30304.1; CAA29965.1; CAA29961.1; CAA29960.1; CAA30303.1; CAA30305.1; AAA03001.1; AAA36572.1; AAA36572.1; AAA36572.1; AAA36572.1; AAA36572.1; AAA36572.1; AAA36573.1; AAA36573.1; AAA36573.1; AAA36573.1; AAA36573.1; AAA36573.1; AAA36571.1; AAA36571.1; AAA36571.1; AAA36571.1; AAA36571.1; BAG53365.1; CAA59278.1; CAB55969.1; EAW52449.1; AAH01315.1 

Protein Name

 U1 small nuclear ribonucleoprotein 70 kDa 

Protein Synonyms/Alias

 U1 snRNP 70 kDa; U1-70K; snRNP70 

Gene Name

 SNRNP70 

Gene Synonyms/Alias

 RNPU1Z; RPU1; SNRP70; U1AP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	PYLPPLEKLPHEKHH	acetylation	[1]
27	PYLPPLEKLPHEKHH	ubiquitination	[2, 3, 4, 5]
32	LEKLPHEKHHNQPYC	acetylation	[6]
87	QEVETELKMWDPHND	ubiquitination	[3, 7]
103	NAQGDAFKTLFVARV	ubiquitination	[2, 3, 4, 8]
118	NYDTTESKLRREFEV	acetylation	[9]
118	NYDTTESKLRREFEV	ubiquitination	[3]
130	FEVYGPIKRIHMVYS	ubiquitination	[2, 3, 4]
162	RDMHSAYKHADGKKI	acetylation	[5, 9]
346	GPDGPEEKGRDRDRE	ubiquitination	[7, 10]

Reference

 [1] 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]
 [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] 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] 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]
 [5] 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]
 [6] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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

 Mediates the splicing of pre-mRNA by binding to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA. 

Sequence Annotation

 DOMAIN 103 181 RRM.
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 118 118 N6-acetyllysine.
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 268 268 Phosphoserine.
 MOD_RES 320 320 Phosphoserine.
 MOD_RES 410 410 Phosphoserine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 437 AA 

Protein Sequence

Gene Ontology

 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IMP:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR022023; U1snRNP70_N. 

Pfam

 PF00076; RRM_1
 PF12220; U1snRNP70_N 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS