P09012 · SNRPA_HUMAN
- ProteinU1 small nuclear ribonucleoprotein A
- GeneSNRPA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids282 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Cellular Component | U1 snRNP | |
Cellular Component | U4/U6 x U5 tri-snRNP complex | |
Molecular Function | DNA binding | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Molecular Function | U1 snRNA binding | |
Molecular Function | U1 snRNP binding | |
Biological Process | mRNA splicing, via spliceosome |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameU1 small nuclear ribonucleoprotein A
- Short namesU1 snRNP A; U1-A; U1A
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP09012
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 11 | Abolishes RNA binding. | ||||
Sequence: T → V | ||||||
Mutagenesis | 13 | Substantially reduces RNA binding. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 15 | Abolishes RNA binding. | ||||
Sequence: N → V | ||||||
Mutagenesis | 16 | Substantially reduces RNA binding. | ||||
Sequence: N → V | ||||||
Mutagenesis | 52 | Abolishes RNA binding. | ||||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 257 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000081887 | 2-282 | UniProt | U1 small nuclear ribonucleoprotein A | |||
Sequence: AVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK | |||||||
Modified residue | 60 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 131 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 152 | UniProt | Omega-N-methylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
U1 snRNP is composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Interacts with SFPQ; component of a snRNP-free complex with SFPQ. Interacts with IVNS1ABP (via BACK domain); the interaction is indirect (PubMed:30538201).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-89 | RRM 1 | ||||
Sequence: HTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKT | ||||||
Compositional bias | 100-118 | Basic and acidic residues | ||||
Sequence: TFVERDRKREKRKPKSQET | ||||||
Region | 100-132 | Disordered | ||||
Sequence: TFVERDRKREKRKPKSQETPATKKAVQGGGATP | ||||||
Domain | 208-282 | RRM 2 | ||||
Sequence: HILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK |
Sequence similarities
Belongs to the RRM U1 A/B'' family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length282
- Mass (Da)31,280
- Last updated2007-01-23 v3
- Checksum9426E83EE5A22894
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 100-118 | Basic and acidic residues | ||||
Sequence: TFVERDRKREKRKPKSQET |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M60784 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60779 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60780 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60781 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60782 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M60783 EMBL· GenBank· DDBJ | AAA61245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X06347 EMBL· GenBank· DDBJ | CAA29653.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000405 EMBL· GenBank· DDBJ | AAH00405.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008290 EMBL· GenBank· DDBJ | AAH08290.1 EMBL· GenBank· DDBJ | mRNA |