Q3UHH1 · ZSWM8_MOUSE
- ProteinZinc finger SWIM domain-containing protein 8
- GeneZswim8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1832 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs) (PubMed:33184237).
The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation (By similarity).
Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target (By similarity).
May also acts as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation (By similarity).
The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation (By similarity).
Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target (By similarity).
May also acts as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation (By similarity).
Pathway
Protein modification; protein ubiquitination.
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 | Cul2-RING ubiquitin ligase complex | |
Cellular Component | Cul3-RING ubiquitin ligase complex | |
Cellular Component | cullin-RING ubiquitin ligase complex | |
Cellular Component | cytosol | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Molecular Function | zinc ion binding | |
Biological Process | positive regulation of miRNA catabolic process | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein ubiquitination |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger SWIM domain-containing protein 8
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3UHH1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000311803 | 1-1832 | Zinc finger SWIM domain-containing protein 8 | |||
Sequence: MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRTRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTDQCLTYEQITGWWYSVRTSASHSSASGHTGRSNGQSEVAAHACASMCDEMVTLWRLAVLDPALSPQRRRELCAQLRQWQLKVIENVKRGQHKKTLERLFPGFRPAVEACYFNWEEAYPLPGVTYSGTDRKLALCWARALPARPGASRSGGLEESRPRPLPTEPAVRPKEPGAKRKGLGEGISSQRGPRRLSAEGGDKALHKMGPSGGKAKVLGGTGSGGKSSAGSGSKRRLSSEDSSLEPDLAEMSLDDSSLALGAEASTFGGFPESPPPCPSSVGSRGPSTFLPEPPDTYEEDAGVYFSEGPEPPTASADHPGLLPGEVCTRDDLPSTDDSGSGLHKTKEAAPAVGEEDDDYQAYYLNAQDGAGGEEEKAEGGTGEEHDLFAGLKPLEQESRMEVLFACAEALHAHGYSNEASRLTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLTKAAFLLTVLSERPEHHSLAFRVGMFALELQRPPASTKALEVKLAYQESEVAALLKKIPRGPSEMSTIRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPVVSLTGSRPPSRNWTNEMPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQAKLKKILDKLLDRESQTHKPQTLSSFYSSSRPATANQRSPSKHGAPSAPGALQPLTSSSAGPAQPGNVAGAGPGPTEGFTEKNVPESSPHSPCEGLPPEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVDVGRCYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEETAGGSSTAREGATSCSGSGMRAAGEAGRGLPEGRGAPGTEPVTVAAAAVTAAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVPSSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVALSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLNPIHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEITTFSP | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 48 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 53 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 437 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 564 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1141 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1155 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1158 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1162 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1270 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1831 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 45-67 | Disordered | ||||
Sequence: RKQSAGPNSPTGGGGGGGSGGTR | ||||||
Zinc finger | 172-208 | SWIM-type | ||||
Sequence: YNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRI | ||||||
Region | 516-722 | Disordered | ||||
Sequence: PGASRSGGLEESRPRPLPTEPAVRPKEPGAKRKGLGEGISSQRGPRRLSAEGGDKALHKMGPSGGKAKVLGGTGSGGKSSAGSGSKRRLSSEDSSLEPDLAEMSLDDSSLALGAEASTFGGFPESPPPCPSSVGSRGPSTFLPEPPDTYEEDAGVYFSEGPEPPTASADHPGLLPGEVCTRDDLPSTDDSGSGLHKTKEAAPAVGEE | ||||||
Compositional bias | 697-720 | Basic and acidic residues | ||||
Sequence: DDLPSTDDSGSGLHKTKEAAPAVG | ||||||
Region | 800-821 | Disordered | ||||
Sequence: NPPDLKVEPPPAKGKKNKVSTS | ||||||
Region | 1018-1216 | Disordered | ||||
Sequence: SQTHKPQTLSSFYSSSRPATANQRSPSKHGAPSAPGALQPLTSSSAGPAQPGNVAGAGPGPTEGFTEKNVPESSPHSPCEGLPPEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVDV | ||||||
Compositional bias | 1020-1046 | Polar residues | ||||
Sequence: THKPQTLSSFYSSSRPATANQRSPSKH | ||||||
Compositional bias | 1146-1162 | Polar residues | ||||
Sequence: IDSSAPETTSDSSPTLS | ||||||
Compositional bias | 1176-1204 | Polar residues | ||||
Sequence: GRGQDSDSISSSSSDSLGSSSSSGSRRAS | ||||||
Region | 1435-1465 | Disordered | ||||
Sequence: STAREGATSCSGSGMRAAGEAGRGLPEGRGA |
Sequence similarities
Belongs to the ZSWIM8 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q3UHH1-1
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
- Length1,832
- Mass (Da)197,061
- Last updated2005-10-11 v1
- Checksum30BD7C1D3157F93B
Q3UHH1-2
- Name2
- Differences from canonical
- 669-702: Missing
Q3UHH1-3
- Name3
- Differences from canonical
- 806-812: Missing
Q3UHH1-4
- Name4
- Differences from canonical
- 1-895: Missing
- 1707-1734: VNYVHQFCVGAAKGVLSPFVLQEIVMET → NTSPPQDHCPPVSLPFLSQTSFLALTQS
- 1735-1832: Missing
Q3UHH1-5
- Name5
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A286YEE4 | A0A286YEE4_MOUSE | Zswim8 | 49 | ||
A0A286YCU1 | A0A286YCU1_MOUSE | Zswim8 | 360 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_029593 | 1-121 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029592 | 1-895 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029594 | 122-126 | in isoform 5 | |||
Sequence: LYSCL → MKRTF | ||||||
Sequence conflict | 599 | in Ref. 1; BAC26361 | ||||
Sequence: G → E | ||||||
Alternative sequence | VSP_029595 | 669-702 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 697-720 | Basic and acidic residues | ||||
Sequence: DDLPSTDDSGSGLHKTKEAAPAVG | ||||||
Alternative sequence | VSP_029596 | 770-771 | in isoform 5 | |||
Sequence: LF → RG | ||||||
Alternative sequence | VSP_029597 | 772-1832 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029598 | 806-812 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 1020-1046 | Polar residues | ||||
Sequence: THKPQTLSSFYSSSRPATANQRSPSKH | ||||||
Compositional bias | 1146-1162 | Polar residues | ||||
Sequence: IDSSAPETTSDSSPTLS | ||||||
Compositional bias | 1176-1204 | Polar residues | ||||
Sequence: GRGQDSDSISSSSSDSLGSSSSSGSRRAS | ||||||
Sequence conflict | 1317-1318 | in Ref. 3; BAC41457 | ||||
Sequence: QA → KS | ||||||
Sequence conflict | 1664 | in Ref. 2; AAH59058 | ||||
Sequence: R → L | ||||||
Alternative sequence | VSP_029599 | 1707-1734 | in isoform 4 | |||
Sequence: VNYVHQFCVGAAKGVLSPFVLQEIVMET → NTSPPQDHCPPVSLPFLSQTSFLALTQS | ||||||
Alternative sequence | VSP_029600 | 1735-1832 | in isoform 4 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK009454 EMBL· GenBank· DDBJ | BAB26298.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK029263 EMBL· GenBank· DDBJ | BAC26361.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147398 EMBL· GenBank· DDBJ | BAE27886.1 EMBL· GenBank· DDBJ | mRNA | ||
BC059058 EMBL· GenBank· DDBJ | AAH59058.1 EMBL· GenBank· DDBJ | mRNA | ||
BC085161 EMBL· GenBank· DDBJ | AAH85161.1 EMBL· GenBank· DDBJ | mRNA | ||
BC049362 EMBL· GenBank· DDBJ | AAH49362.1 EMBL· GenBank· DDBJ | mRNA | ||
BC151046 EMBL· GenBank· DDBJ | AAI51047.1 EMBL· GenBank· DDBJ | mRNA | ||
BC151056 EMBL· GenBank· DDBJ | AAI51057.1 EMBL· GenBank· DDBJ | mRNA | ||
BC151173 EMBL· GenBank· DDBJ | AAI51174.1 EMBL· GenBank· DDBJ | mRNA | ||
AB093273 EMBL· GenBank· DDBJ | BAC41457.3 EMBL· GenBank· DDBJ | mRNA |