Q15020 · SART3_HUMAN
- ProteinSquamous cell carcinoma antigen recognized by T-cells 3
- GeneSART3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids963 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385).
May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234).
May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689).
May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity).
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 | ASAP complex | |
Cellular Component | Cajal body | |
Cellular Component | cytoplasm | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | histone binding | |
Molecular Function | RNA binding | |
Molecular Function | U4 snRNA binding | |
Molecular Function | U6 snRNA binding | |
Molecular Function | U6atac snRNA binding | |
Molecular Function | ubiquitin-specific protease binding | |
Biological Process | cell morphogenesis | |
Biological Process | hematopoietic stem cell proliferation | |
Biological Process | homeostasis of number of cells | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | nucleosome assembly | |
Biological Process | regulation of gene expression | |
Biological Process | spliceosomal snRNP assembly | |
Biological Process | spliceosomal tri-snRNP complex assembly | |
Biological Process | transcription elongation-coupled chromatin remodeling |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSquamous cell carcinoma antigen recognized by T-cells 3
- Short namesSART-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 accessionQ15020
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_038802 | 23 | in dbSNP:rs2072579 | |||
Sequence: D → E | ||||||
Natural variant | VAR_038683 | 591 | found in a patient with disseminated superficial actinic porokeratosis; uncertain significance; dbSNP:rs118203954 | |||
Sequence: V → M | ||||||
Natural variant | VAR_038684 | 621 | in dbSNP:rs2287546 | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 873 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
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_0000223313 | 2-963 | UniProt | Squamous cell carcinoma antigen recognized by T-cells 3 | |||
Sequence: ATAAETSASEPEAESKAGPKADGEEDEVKAARTRRKVLSRAVAAATYKTMGPAWDQQEEGVSESDGDEYAMASSAESSPGEYEWEYDEEEEKNQLEIERLEEQLSINVYDYNCHVDLIRLLRLEGELTKVRMARQKMSEIFPLTEELWLEWLHDEISMAQDGLDREHVYDLFEKAVKDYICPNIWLEYGQYSVGGIGQKGGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESAIVEAARLEKVHSLFRRQLAIPLYDMEATFAEYEEWSEDPIPESVIQNYNKALQQLEKYKPYEEALLQAEAPRLAEYQAYIDFEMKIGDPARIQLIFERALVENCLVPDLWIRYSQYLDRQLKVKDLVLSVHNRAIRNCPWTVALWSRYLLAMERHGVDHQVISVTFEKALNAGFIQATDYVEIWQAYLDYLRRRVDFKQDSSKELEELRAAFTRALEYLKQEVEERFNESGDPSCVIMQNWARIEARLCNNMQKARELWDSIMTRGNAKYANMWLEYYNLERAHGDTQHCRKALHRAVQCTSDYPEHVCEVLLTMERTEGSLEDWDIAVQKTETRLARVNEQRMKAAEKEAALVQQEEEKAEQRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLPQTYGARGKGRTQLSLLPRALQRPSAAAPQAENGPAAAPAVAAPAATEAPKMSNADFAKLFLRK | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 10 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 16 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 215 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 650 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 650 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 657 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 769 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 769 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 778 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 795 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 852 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 906 | UniProt | Omega-N-methylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with AGO1 and AGO2 (PubMed:17932509).
Interacts with PRPF3 and USP4; the interaction with PRPF3 is direct and recruits USP4 to its substrate PRPF3 (PubMed:15314151, PubMed:20595234).
Interacts with USP15; the interaction is direct (PubMed:24526689).
Interacts with HIV-1 Tat (PubMed:11959860).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q15020 | K4 F5HFL9 | 2 | EBI-308619, EBI-14032776 | |
BINARY | Q15020 | RNPS1 Q15287 | 5 | EBI-308619, EBI-395959 | |
BINARY | Q15020 | ZNF620 Q6ZNG0 | 3 | EBI-308619, EBI-4395669 | |
BINARY | Q15020 | ZNF71 Q9NQZ8 | 3 | EBI-308619, EBI-7138235 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, repeat, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MATAAETSASEPEAESKAGPKADGEEDEVKAARTRR | ||||||
Region | 2-351 | Mediates interaction with PRPF3 | ||||
Sequence: ATAAETSASEPEAESKAGPKADGEEDEVKAARTRRKVLSRAVAAATYKTMGPAWDQQEEGVSESDGDEYAMASSAESSPGEYEWEYDEEEEKNQLEIERLEEQLSINVYDYNCHVDLIRLLRLEGELTKVRMARQKMSEIFPLTEELWLEWLHDEISMAQDGLDREHVYDLFEKAVKDYICPNIWLEYGQYSVGGIGQKGGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESAIVEAARLEKVHSLFRRQLAIPLYDMEATFAEYEEWSEDPIPESVIQNYNKALQQLEKYKPYEEALLQAEAPRLAEYQAYIDFEMKIGDPARIQLIFERALVENCLVPDLWIRYS | ||||||
Compositional bias | 16-35 | Basic and acidic residues | ||||
Sequence: SKAGPKADGEEDEVKAARTR | ||||||
Coiled coil | 21-46 | |||||
Sequence: KADGEEDEVKAARTRRKVLSRAVAAA | ||||||
Region | 50-90 | Disordered | ||||
Sequence: TMGPAWDQQEEGVSESDGDEYAMASSAESSPGEYEWEYDEE | ||||||
Coiled coil | 82-110 | |||||
Sequence: EYEWEYDEEEEKNQLEIERLEEQLSINVY | ||||||
Repeat | 126-158 | HAT 1 | ||||
Sequence: GELTKVRMARQKMSEIFPLTEELWLEWLHDEIS | ||||||
Repeat | 164-195 | HAT 2 | ||||
Sequence: LDREHVYDLFEKAVKDYICPNIWLEYGQYSVG | ||||||
Repeat | 201-237 | HAT 3 | ||||
Sequence: GGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESA | ||||||
Repeat | 242-275 | HAT 4 | ||||
Sequence: ARLEKVHSLFRRQLAIPLYDMEATFAEYEEWSED | ||||||
Repeat | 324-356 | HAT 5 | ||||
Sequence: GDPARIQLIFERALVENCLVPDLWIRYSQYLDR | ||||||
Repeat | 359-391 | HAT 6 | ||||
Sequence: KVKDLVLSVHNRAIRNCPWTVALWSRYLLAMER | ||||||
Repeat | 394-430 | HAT 7 | ||||
Sequence: VDHQVISVTFEKALNAGFIQATDYVEIWQAYLDYLRR | ||||||
Repeat | 487-520 | HAT 8 | ||||
Sequence: NNMQKARELWDSIMTRGNAKYANMWLEYYNLERA | ||||||
Region | 487-520 | Required for interaction with USP4 | ||||
Sequence: NNMQKARELWDSIMTRGNAKYANMWLEYYNLERA | ||||||
Region | 537-953 | Necessary and sufficient for U6 snRNA binding | ||||
Sequence: CTSDYPEHVCEVLLTMERTEGSLEDWDIAVQKTETRLARVNEQRMKAAEKEAALVQQEEEKAEQRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLPQTYGARGKGRTQLSLLPRALQRPSAAAPQAENGPAAAPAVAAPAATEAPKMSN | ||||||
Coiled coil | 559-619 | |||||
Sequence: LEDWDIAVQKTETRLARVNEQRMKAAEKEAALVQQEEEKAEQRKRARAEKKALKKKKKIRG | ||||||
Compositional bias | 590-605 | Basic and acidic residues | ||||
Sequence: LVQQEEEKAEQRKRAR | ||||||
Region | 590-694 | Disordered | ||||
Sequence: LVQQEEEKAEQRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPK | ||||||
Region | 600-670 | Required for nuclear localization | ||||
Sequence: QRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKC | ||||||
Motif | 601-617 | Nuclear localization signal | ||||
Sequence: RKRARAEKKALKKKKKI | ||||||
Compositional bias | 676-694 | Basic and acidic residues | ||||
Sequence: EPPSKQKEKAASLKRDMPK | ||||||
Domain | 704-782 | RRM 1 | ||||
Sequence: ITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVD | ||||||
Domain | 801-878 | RRM 2 | ||||
Sequence: HKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNP | ||||||
Region | 878-898 | Disordered | ||||
Sequence: PPQRKVPEKPETRKAPGGPML | ||||||
Region | 920-948 | Disordered | ||||
Sequence: LQRPSAAAPQAENGPAAAPAVAAPAATEA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q15020-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length963
- Mass (Da)109,935
- Last updated1996-11-01 v1
- Checksum06B26CEB8B19102A
Q15020-2
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Inactive in U4/U6 snRNP recycling.
Q15020-3
- Name3
Q15020-4
- Name4
- Differences from canonical
- 401-436: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YHU8 | H0YHU8_HUMAN | SART3 | 144 | ||
F8VZM2 | F8VZM2_HUMAN | SART3 | 156 | ||
F8VVK9 | F8VVK9_HUMAN | SART3 | 111 | ||
F8W667 | F8W667_HUMAN | SART3 | 305 | ||
A0A499FI31 | A0A499FI31_HUMAN | SART3 | 981 | ||
A0A494C0L2 | A0A494C0L2_HUMAN | SART3 | 263 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-35 | Basic and acidic residues | ||||
Sequence: SKAGPKADGEEDEVKAARTR | ||||||
Alternative sequence | VSP_017248 | 105-129 | in isoform 3 | |||
Sequence: LSINVYDYNCHVDLIRLLRLEGELT → VGPGVGSGHLPVFQVLGSPCPGPPP | ||||||
Alternative sequence | VSP_017249 | 130-963 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017250 | 351-364 | in isoform 2 | |||
Sequence: SQYLDRQLKVKDLV → RSTTESKGFGFICT | ||||||
Alternative sequence | VSP_017251 | 365-963 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_057284 | 401-436 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 590-605 | Basic and acidic residues | ||||
Sequence: LVQQEEEKAEQRKRAR | ||||||
Compositional bias | 676-694 | Basic and acidic residues | ||||
Sequence: EPPSKQKEKAASLKRDMPK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020880 EMBL· GenBank· DDBJ | BAA78384.1 EMBL· GenBank· DDBJ | mRNA | ||
AF387506 EMBL· GenBank· DDBJ | AAK69347.1 EMBL· GenBank· DDBJ | mRNA | ||
D63879 EMBL· GenBank· DDBJ | BAA09929.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290209 EMBL· GenBank· DDBJ | BAF82898.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008119 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC010206 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF455716 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF511170 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC032601 EMBL· GenBank· DDBJ | AAH32601.1 EMBL· GenBank· DDBJ | mRNA | ||
BC041638 EMBL· GenBank· DDBJ | AAH41638.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093784 EMBL· GenBank· DDBJ | AAH93784.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103706 EMBL· GenBank· DDBJ | AAI03707.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111983 EMBL· GenBank· DDBJ | AAI11984.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143253 EMBL· GenBank· DDBJ | AAI43254.1 EMBL· GenBank· DDBJ | mRNA |