U1 small nuclear ribonucleoprotein 70 kDa

Function

Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA.

Classification

Family (Pfam)

PF00076 RRM_1, PF12220 U1snRNP70_N

InterPro

Nucleotide-bd_a/b_plait_sf, RBD_domain_sf, RRM_dom, snRNP70_RRM, U1_U11-U12_snRNP_70-35kDa, U1snRNP70_N

Functional cluster

RRM RNA-Binding & Protein Kinases

Experimental structures · PDB · 11

• 2L5I NMR
• 2L5J NMR
• 3CW1 X-ray 5.49A
• 3PGW X-ray 4.40A
• 4PJO X-ray 3.30A
• 4PKD X-ray 2.50A
• 6QX9 EM 3.28A
• 7B0Y EM 3.60A
• 7VPX EM 3.00A
• 8R08 EM 6.10A
• 9QEQ EM 3.50A

A predicted model is available from AlphaFold.

Gene Ontology · 19

• GO:0043202 lysosomal lumen
• GO:0016607 nuclear speck
• GO:0005654 nucleoplasm
• GO:0005634 nucleus
• GO:0005681 spliceosomal complex
• GO:0005685 U1 snRNP
• GO:0071004 U2-type prespliceosome
• GO:0003729 mRNA binding
• GO:0003723 RNA binding
• GO:0030619 U1 snRNA binding
• GO:1990446 U1 snRNP binding
• GO:0071300 cellular response to retinoic acid
• GO:0071560 cellular response to transforming growth factor beta stimulus
• GO:0071356 cellular response to tumor necrosis factor
• GO:0000398 mRNA splicing, via spliceosome
• GO:1904715 negative regulation of chaperone-mediated autophagy
• GO:0061084 negative regulation of protein refolding
• GO:0043484 regulation of RNA splicing
• GO:0000387 spliceosomal snRNP assembly

Neighborhood · nearest proteins

Related proteins · sequence + function similarity

• U1 small nuclear ribonucleoprotein 70 kDa 1.00
• U1 small nuclear ribonucleoprotein 70 kDa 0.99
• U1 small nuclear ribonucleoprotein 70 kDa 0.94
• U1 small nuclear ribonucleoprotein 70 kDa 0.93
• U1 small nuclear ribonucleoprotein 70 kDa 0.83
• U1 small nuclear ribonucleoprotein 70 kDa 0.77
• U1 small nuclear ribonucleoprotein 70 kDa 0.70
• Luc7-like protein 3 0.69
• Luc7-like protein 3 0.69
• Luc7-like protein 3 0.69
• Luc7-like protein 3 0.69
• CLK4-associating serine/arginine rich protein 0.69

Co-cited proteins · studied together in the literature

• Gem-associated protein 5 1 shared papers
• Protein SCAF11 1 shared papers
• Zinc finger Ran-binding domain-containing protein 2 1 shared papers
• Small nuclear ribonucleoprotein Sm D1 3 shared papers
• Transformer-2 protein homolog beta 2 shared papers
• Putative RNA-binding protein Luc7-like 2 1 shared papers
• U1 small nuclear ribonucleoprotein 70 kDa 1 shared papers
• Sodium channel modifier 1 1 shared papers
• Splicing factor U2AF 35 kDa subunit 1 shared papers
• Serine/arginine-rich splicing factor 10 1 shared papers
• Splicing factor, proline- and glutamine-rich 1 shared papers
• U2 small nuclear ribonucleoprotein A' 2 shared papers

Literature · 39 cited papers

• Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat. Struct. Mol. Biol. · 2017
• FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP. Proc. Natl. Acad. Sci. U.S.A. · 2015
• Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression. J. Biol. Chem. · 2015
• Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein particle, reveals the mechanism of 5' splice site recognition. Elife · 2015
• An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
• Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
• Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. Mol. Cell. Proteomics · 2012
• System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. · 2011
• Initial characterization of the human central proteome. BMC Syst. Biol. · 2011
• Functional organization of the Sm core in the crystal structure of human U1 snRNP. EMBO J. · 2010
• Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
• Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. · 2009
• … and 27 more in the literature graph