P10155 · RO60_HUMAN
- ProteinRNA-binding protein RO60
- GeneRO60
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids538 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (PubMed:18056422, PubMed:26382853).
Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:26382853).
Regulates the expression of Alu retroelements as well as inflammatory genes (PubMed:26382853).
May play roles in cilia formation and/or maintenance (By similarity).
Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:26382853).
Regulates the expression of Alu retroelements as well as inflammatory genes (PubMed:26382853).
May play roles in cilia formation and/or maintenance (By similarity).
Miscellaneous
Antibodies against normal cellular SSA2 protein are found in sera from patients with systemic lupus erythematosus (SLE).
Features
Showing features for binding site.
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 | cytosol | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Molecular Function | U2 snRNA binding | |
Biological Process | cellular response to interferon-alpha | |
Biological Process | cilium assembly | |
Biological Process | immune system development | |
Biological Process | regulation of gene expression | |
Biological Process | response to UV | |
Biological Process | smoothened signaling pathway | |
Biological Process | transcription by RNA polymerase III |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein RO60
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP10155
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 589 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000174169 | 1-538 | UniProt | RNA-binding protein RO60 | |||
Sequence: MEESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTLDMI | |||||||
Modified residue | 4 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 19 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 224 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 359 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-369 | TROVE | ||||
Sequence: IANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGK | ||||||
Region | 120-284 | RNA-binding | ||||
Sequence: RIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRN | ||||||
Region | 361-538 | VWFA-like domain | ||||
Sequence: FKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTLDMI |
Domain
The horseshoe-shaped TROVE domain is built with 7 helical HEAT-like repeats, and is closed by the VWFA-like domain giving rise to a ring-shaped monomer. Single-stranded RNA is bound in the positively charged central cavity (By similarity).
The MIDAS-like motif in the VWFA-like domain binds divalent metal cations.
Sequence similarities
Belongs to the Ro 60 kDa family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P10155-1
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.
- NameLong
- Length538
- Mass (Da)60,671
- Last updated2004-09-27 v2
- ChecksumCD735B1DF2B13098
P10155-2
- NameShort
- Synonyms60E2
P10155-3
- Name3
- Differences from canonical
- 515-538: GMLDMCGFDTGALDVIRNFTLDMI → DTVK
P10155-4
- Name4
- Differences from canonical
- 529-538: VIRNFTLDMI → PCKIPY
P10155-5
- Name5
- Differences from canonical
- 515-538: GMLDMCGFDTGALDVIRNFTLDMI → ALQNTLLNKSF
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 136 | in Ref. 4; AAO47001/AAO47002 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_005911 | 195-205 | in isoform Short | |||
Sequence: LAIVTKYITKG → KHKIFIGKKGG | ||||||
Alternative sequence | VSP_005912 | 206-538 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 239 | in Ref. 1; AAA35493 | ||||
Sequence: R → K | ||||||
Alternative sequence | VSP_045262 | 515-538 | in isoform 3 | |||
Sequence: GMLDMCGFDTGALDVIRNFTLDMI → DTVK | ||||||
Alternative sequence | VSP_054041 | 515-538 | in isoform 5 | |||
Sequence: GMLDMCGFDTGALDVIRNFTLDMI → ALQNTLLNKSF | ||||||
Alternative sequence | VSP_045797 | 529-538 | in isoform 4 | |||
Sequence: VIRNFTLDMI → PCKIPY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04137 EMBL· GenBank· DDBJ | AAA35493.1 EMBL· GenBank· DDBJ | mRNA | ||
M25077 EMBL· GenBank· DDBJ | AAA35532.1 EMBL· GenBank· DDBJ | mRNA | ||
U44388 EMBL· GenBank· DDBJ | AAB81552.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
U44388 EMBL· GenBank· DDBJ | AAB81553.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY205314 EMBL· GenBank· DDBJ | AAO47001.1 EMBL· GenBank· DDBJ | mRNA | ||
AY205315 EMBL· GenBank· DDBJ | AAO47002.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314594 EMBL· GenBank· DDBJ | BAG37166.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136370 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471067 EMBL· GenBank· DDBJ | EAW91240.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW91243.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW91245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471067 EMBL· GenBank· DDBJ | EAW91247.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC036658 EMBL· GenBank· DDBJ | AAH36658.1 EMBL· GenBank· DDBJ | mRNA |