Q12874 · SF3A3_HUMAN
- ProteinSplicing factor 3A subunit 3
- GeneSF3A3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids501 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310, PubMed:8022796).
The 17S U2 SnRNP complex 1 directly participates in early spliceosome assembly and 2 mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310).
Within the 17S U2 SnRNP complex, SF3A3 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230).
Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277).
The 17S U2 SnRNP complex 1 directly participates in early spliceosome assembly and 2 mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006, PubMed:34822310).
Within the 17S U2 SnRNP complex, SF3A3 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230).
Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277).
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 | catalytic step 2 spliceosome | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Cellular Component | U2 snRNP | |
Cellular Component | U2-type precatalytic spliceosome | |
Cellular Component | U2-type spliceosomal complex | |
Molecular Function | RNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA 3'-splice site recognition | |
Biological Process | mRNA processing | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | RNA splicing, via transesterification reactions | |
Biological Process | U2-type prespliceosome assembly |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSplicing factor 3A subunit 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ12874
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 174-180 | Loss of nuclear location. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 328 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000174318 | 1-501 | UniProt | Splicing factor 3A subunit 3 | |||
Sequence: METILEQQRRYHEEKERLMDVMAKEMLTKKSTLRDQINSDHRTRAMQDRYMEVSGNLRDLYDDKDGLRKEELNAISGPNEFAEFYNRLKQIKEFHRKHPNEICVPMSVEFEELLKARENPSEEAQNLVEFTDEEGYGRYLDLHDCYLKYINLKASEKLDYITYLSIFDQLFDIPKERKNAEYKRYLEMLLEYLQDYTDRVKPLQDQNELFGKIQAEFEKKWENGTFPGWPKETSSALTHAGAHLDLSAFSSWEELASLGLDRLKSALLALGLKCGGTLEERAQRLFSTKGKSLESLDTSLFAKNPKSKGTKRDTERNKDIAFLEAQIYEYVEILGEQRHLTHENVQRKQARTGEEREEEEEEQISESESEDEENEIIYNPKNLPLGWDGKPIPYWLYKLHGLNINYNCEICGNYTYRGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAVSLWAKLKLQKASERWQPDTEEEYEDSSGNVVNKKTYEDLKRQGLL | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 367 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 369 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 475 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:21349847, PubMed:32494006, PubMed:34822310, PubMed:36797247).
Part of the SF3A subcomplex of the 17S U2 SnRNP complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114, PubMed:11533230, PubMed:17098193, PubMed:21349847, PubMed:8022796).
SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 snRNP) (PubMed:10882114, PubMed:11533230).
Identified in the spliceosome 'E' complex, a precursor of the spliceosome 'A' complex (PubMed:10882114).
Identified in the spliceosome 'A' and 'B' complexes (PubMed:10882114, PubMed:29360106, PubMed:30315277, PubMed:8022796).
Identified in the spliceosome 'C' complex (PubMed:11991638).
Part of the SF3A subcomplex of the 17S U2 SnRNP complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114, PubMed:11533230, PubMed:17098193, PubMed:21349847, PubMed:8022796).
SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 snRNP) (PubMed:10882114, PubMed:11533230).
Identified in the spliceosome 'E' complex, a precursor of the spliceosome 'A' complex (PubMed:10882114).
Identified in the spliceosome 'A' and 'B' complexes (PubMed:10882114, PubMed:29360106, PubMed:30315277, PubMed:8022796).
Identified in the spliceosome 'C' complex (PubMed:11991638).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q12874 | ATXN1 P54253 | 6 | EBI-1051880, EBI-930964 | |
BINARY | Q12874 | HSPB1 P04792 | 2 | EBI-1051880, EBI-352682 | |
BINARY | Q12874 | HTT P42858 | 3 | EBI-1051880, EBI-466029 | |
BINARY | Q12874 | JPH3 Q8WXH2 | 3 | EBI-1051880, EBI-1055254 | |
XENO | Q12874 | ORF Q9Q2G4 | 3 | EBI-1051880, EBI-6248094 | |
BINARY | Q12874 | SF3A1 Q15459 | 10 | EBI-1051880, EBI-1054743 | |
BINARY | Q12874 | SF3A2 Q15428 | 2 | EBI-1051880, EBI-2462271 | |
BINARY | Q12874 | SF3B3 Q15393 | 3 | EBI-1051880, EBI-346977 | |
BINARY | Q12874 | TADA2A O75478 | 3 | EBI-1051880, EBI-742268 | |
BINARY | Q12874 | TRIM69 Q86WT6 | 3 | EBI-1051880, EBI-749955 | |
BINARY | Q12874 | ZNF212 Q9UDV6 | 4 | EBI-1051880, EBI-1640204 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 175-179 | Nuclear localization signal | ||||
Sequence: KERKN | ||||||
Region | 343-374 | Disordered | ||||
Sequence: ENVQRKQARTGEEREEEEEEQISESESEDEEN | ||||||
Compositional bias | 356-373 | Acidic residues | ||||
Sequence: REEEEEEQISESESEDEE | ||||||
Zinc finger | 406-437 | Matrin-type | ||||
Sequence: YNCEICGNYTYRGPKAFQRHFAEWRHAHGMRC |
Sequence similarities
Belongs to the SF3A3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length501
- Mass (Da)58,849
- Last updated1996-11-01 v1
- Checksum6E6F6EA17777E1E2
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 176 | in Ref. 2; CAA57388 | ||||
Sequence: E → G | ||||||
Compositional bias | 356-373 | Acidic residues | ||||
Sequence: REEEEEEQISESESEDEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U08815 EMBL· GenBank· DDBJ | AAA19625.1 EMBL· GenBank· DDBJ | mRNA | ||
X81789 EMBL· GenBank· DDBJ | CAA57388.1 EMBL· GenBank· DDBJ | mRNA | ||
AL603790 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07304.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX07305.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002395 EMBL· GenBank· DDBJ | AAH02395.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011523 EMBL· GenBank· DDBJ | AAH11523.1 EMBL· GenBank· DDBJ | mRNA |