Q7KZF4 · SND1_HUMAN
- ProteinStaphylococcal nuclease domain-containing protein 1
- GeneSND1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids910 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:18453631, PubMed:28546213).
As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213).
Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934).
Plays a role in PIM1 regulation of MYB activity (PubMed:9809063).
Functions as a transcriptional coactivator for STAT5 (By similarity).
As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213).
Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934).
Plays a role in PIM1 regulation of MYB activity (PubMed:9809063).
Functions as a transcriptional coactivator for STAT5 (By similarity).
(Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).
(Microbial infection) Promotes SARS-CoV-2 RNA synthesis by binding to negative-sense RNA and the viral protein nsp9.
Catalytic activity
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | dense body | |
Cellular Component | extracellular exosome | |
Cellular Component | melanosome | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | RNAi effector complex | |
Molecular Function | cadherin binding | |
Molecular Function | endonuclease activity | |
Molecular Function | endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters | |
Molecular Function | nuclease activity | |
Molecular Function | RISC complex binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity | |
Molecular Function | transcription coregulator activity | |
Biological Process | miRNA catabolic process | |
Biological Process | mRNA catabolic process | |
Biological Process | osteoblast differentiation | |
Biological Process | regulation of cell cycle process | |
Biological Process | regulatory ncRNA-mediated gene silencing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStaphylococcal nuclease domain-containing protein 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7KZF4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 810 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), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000183180 | 2-910 | UniProt | Staphylococcal nuclease domain-containing protein 1 | |||
Sequence: ASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 103 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 193 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 240 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 421 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 426 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 426 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 431 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 513 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 641 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 645 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 779 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 781 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 781 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 785 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 908 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 909 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 909 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by PIM1 in vitro.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms a ternary complex with STAT6 and POLR2A (PubMed:12234934).
Associates with the RNA-induced silencing complex (RISC) (PubMed:14508492, PubMed:28546213).
Interacts with the RISC components AGO2, FMR1 and TNRC6A (PubMed:14508492, PubMed:28546213).
Interacts with GTF2E1 and GTF2E2 (PubMed:7651391).
Interacts with PIM1 (PubMed:9809063).
Interacts with STAT5 (By similarity).
Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By similarity).
Associates with the RNA-induced silencing complex (RISC) (PubMed:14508492, PubMed:28546213).
Interacts with the RISC components AGO2, FMR1 and TNRC6A (PubMed:14508492, PubMed:28546213).
Interacts with GTF2E1 and GTF2E2 (PubMed:7651391).
Interacts with PIM1 (PubMed:9809063).
Interacts with STAT5 (By similarity).
Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By similarity).
(Microbial infection) Interacts with EAV NSP1 (PubMed:12917451).
Binds to acidic transactivation domain of EBNA2 (PubMed:7651391).
Interacts with SARS-CoV-2 NSP9 (PubMed:37794589).
Binds to acidic transactivation domain of EBNA2 (PubMed:7651391).
Interacts with SARS-CoV-2 NSP9 (PubMed:37794589).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7KZF4 | G3BP1 Q13283 | 3 | EBI-1044112, EBI-1047359 | |
BINARY | Q7KZF4 | MTDH Q86UE4 | 9 | EBI-1044112, EBI-1046588 | |
BINARY | Q7KZF4 | PIWIL1 Q96J94 | 4 | EBI-1044112, EBI-527417 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-166 | TNase-like 1 | ||||
Sequence: TVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSE | ||||||
Domain | 193-328 | TNase-like 2 | ||||
Sequence: KPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRD | ||||||
Motif | 321-325 | Nuclear localization signal | ||||
Sequence: RRLRI | ||||||
Domain | 341-496 | TNase-like 3 | ||||
Sequence: KQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSK | ||||||
Motif | 388-392 | Nuclear localization signal | ||||
Sequence: KKLRP | ||||||
Domain | 525-660 | TNase-like 4 | ||||
Sequence: GRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAH | ||||||
Domain | 729-787 | Tudor | ||||
Sequence: APRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length910
- Mass (Da)101,997
- Last updated2004-07-05 v1
- ChecksumD58BF200F3F3D628
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7C597 | H7C597_HUMAN | SND1 | 231 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 274 | in Ref. 1; AAA80488 | ||||
Sequence: L → V | ||||||
Sequence conflict | 707-708 | in Ref. 1; AAA80488 | ||||
Sequence: LE → FQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22055 EMBL· GenBank· DDBJ | AAA80488.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BT009785 EMBL· GenBank· DDBJ | AAP88787.1 EMBL· GenBank· DDBJ | mRNA | ||
BC017180 EMBL· GenBank· DDBJ | AAH17180.3 EMBL· GenBank· DDBJ | mRNA |