Q8IXI1 · MIRO2_HUMAN
- ProteinMitochondrial Rho GTPase 2
- GeneRHOT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids618 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (PubMed:22396657).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11-18 | GTP 1 (UniProtKB | ChEBI) | ||||
Sequence: GEAQVGKT | ||||||
Binding site | 57-61 | GTP 1 (UniProtKB | ChEBI) | ||||
Sequence: DYSEA | ||||||
Binding site | 118-121 | GTP 1 (UniProtKB | ChEBI) | ||||
Sequence: NKSD | ||||||
Binding site | 197 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 199 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 201 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 208 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 317 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 319 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 321 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 328 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 423-430 | GTP 2 (UniProtKB | ChEBI) | ||||
Sequence: GARGVGKS | ||||||
Binding site | 459-463 | GTP 2 (UniProtKB | ChEBI) | ||||
Sequence: QVNGQ | ||||||
Binding site | 524-527 | GTP 2 (UniProtKB | ChEBI) | ||||
Sequence: SKAD |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Molecular Function | calcium ion binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Biological Process | cellular homeostasis | |
Biological Process | mitochondrial outer membrane permeabilization | |
Biological Process | mitochondrion organization | |
Biological Process | mitochondrion transport along microtubule | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial Rho GTPase 2
- EC number
- Short namesMIRO-2; hMiro-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IXI1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-592 | Cytoplasmic | ||||
Sequence: MRRDVRILLLGEAQVGKTSLILSLVGEEFPEEVPPRAEEITIPADVTPEKVPTHIVDYSEAEQTDEELREEIHKANVVCVVYDVSEEATIEKIRTKWIPLVNGGTTQGPRVPIILVGNKSDLRSGSSMEAVLPIMSQFPEIETCVECSAKNLRNISELFYYAQKAVLHPTAPLYDPEAKQLRPACAQALTRIFRLSDQDLDQALSDEELNAFQKSCFGHPLAPQALEDVKTVVCRNVAGGVREDRLTLDGFLFLNTLFIQRGRHETTWTILRRFGYSDALELTADYLSPLIHVPPGCSTELNHLGYQFVQRVFEKHDQDRDGALSPVELQSLFSVFPAAPWGPELPRTVRTEAGRLPLHGYLCQWTLVTYLDVRSCLGHLGYLGYPTLCEQDQAHAITVTREKRLDQEKGQTQRSVLLCKVVGARGVGKSAFLQAFLGRGLGHQDTREQPPGYAIDTVQVNGQEKYLILCEVGTDGLLATSLDATCDVACLMFDGSDPKSFAHCASVYKHHYMDGQTPCLFVSSKADLPEGVAVSGPSPAEFCRKHRLPAPVPFSCAGPAEPSTTIFTQLATMAAFPHLVHAELHPSSFWLR | ||||||
Transmembrane | 593-615 | Helical; Anchor for type IV membrane protein | ||||
Sequence: GLLGVVGAAVAAVLSFSLYRVLV | ||||||
Topological domain | 616-618 | Mitochondrial intermembrane | ||||
Sequence: KSQ |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 13 | Causes constitutive activation inducing an aggregation of the mitochondrial network. | ||||
Sequence: A → V | ||||||
Mutagenesis | 18 | Induces an aggregation of the mitochondrial network. | ||||
Sequence: T → N | ||||||
Natural variant | VAR_026637 | 245 | in dbSNP:rs1139897 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026638 | 425 | in dbSNP:rs3177338 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 892 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 chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000239318 | 1-618 | UniProt | Mitochondrial Rho GTPase 2 | |||
Sequence: MRRDVRILLLGEAQVGKTSLILSLVGEEFPEEVPPRAEEITIPADVTPEKVPTHIVDYSEAEQTDEELREEIHKANVVCVVYDVSEEATIEKIRTKWIPLVNGGTTQGPRVPIILVGNKSDLRSGSSMEAVLPIMSQFPEIETCVECSAKNLRNISELFYYAQKAVLHPTAPLYDPEAKQLRPACAQALTRIFRLSDQDLDQALSDEELNAFQKSCFGHPLAPQALEDVKTVVCRNVAGGVREDRLTLDGFLFLNTLFIQRGRHETTWTILRRFGYSDALELTADYLSPLIHVPPGCSTELNHLGYQFVQRVFEKHDQDRDGALSPVELQSLFSVFPAAPWGPELPRTVRTEAGRLPLHGYLCQWTLVTYLDVRSCLGHLGYLGYPTLCEQDQAHAITVTREKRLDQEKGQTQRSVLLCKVVGARGVGKSAFLQAFLGRGLGHQDTREQPPGYAIDTVQVNGQEKYLILCEVGTDGLLATSLDATCDVACLMFDGSDPKSFAHCASVYKHHYMDGQTPCLFVSSKADLPEGVAVSGPSPAEFCRKHRLPAPVPFSCAGPAEPSTTIFTQLATMAAFPHLVHAELHPSSFWLRGLLGVVGAAVAAVLSFSLYRVLVKSQ | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 535 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with ARMCX3 (By similarity).
Found in a complex with KIF5B, OGT, RHOT1 and TRAK1 (PubMed:24995978).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IXI1 | SAR1A Q9NR31 | 3 | EBI-1396563, EBI-3920694 | |
BINARY | Q8IXI1 | TMEM14B Q9NUH8 | 3 | EBI-1396563, EBI-8638294 | |
BINARY | Q8IXI1 | TMEM86B Q8N661 | 3 | EBI-1396563, EBI-2548832 | |
BINARY | Q8IXI1 | TRAK1 Q9UPV9 | 4 | EBI-1396563, EBI-1105048 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-168 | Miro 1 | ||||
Sequence: RRDVRILLLGEAQVGKTSLILSLVGEEFPEEVPPRAEEITIPADVTPEKVPTHIVDYSEAEQTDEELREEIHKANVVCVVYDVSEEATIEKIRTKWIPLVNGGTTQGPRVPIILVGNKSDLRSGSSMEAVLPIMSQFPEIETCVECSAKNLRNISELFYYAQKAVLH | ||||||
Domain | 184-219 | EF-hand 1 | ||||
Sequence: ACAQALTRIFRLSDQDLDQALSDEELNAFQKSCFGH | ||||||
Domain | 304-339 | EF-hand 2 | ||||
Sequence: LGYQFVQRVFEKHDQDRDGALSPVELQSLFSVFPAA | ||||||
Domain | 414-576 | Miro 2 | ||||
Sequence: RSVLLCKVVGARGVGKSAFLQAFLGRGLGHQDTREQPPGYAIDTVQVNGQEKYLILCEVGTDGLLATSLDATCDVACLMFDGSDPKSFAHCASVYKHHYMDGQTPCLFVSSKADLPEGVAVSGPSPAEFCRKHRLPAPVPFSCAGPAEPSTTIFTQLATMAAF |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8IXI1-1
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
- Length618
- Mass (Da)68,118
- Last updated2006-06-13 v2
- ChecksumC72ECBCA33D04B6B
Q8IXI1-2
- Name2
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_019162 | 1-127 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 139 | in Ref. 1; CAD56957 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_019163 | 251-340 | in isoform 2 | |||
Sequence: FLFLNTLFIQRGRHETTWTILRRFGYSDALELTADYLSPLIHVPPGCSTELNHLGYQFVQRVFEKHDQDRDGALSPVELQSLFSVFPAAP → EAGCPPVPGECGEGAVPGAPPALSRCRFPLPEHALHPARPARDHLDHPAALRLQRCPGADCGLSLPSDPRAPRLQHGAQPPWLPVCAESV | ||||||
Alternative sequence | VSP_019164 | 341-618 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ517413 EMBL· GenBank· DDBJ | CAD56957.1 EMBL· GenBank· DDBJ | mRNA | ||
AY207375 EMBL· GenBank· DDBJ | AAP46090.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024450 EMBL· GenBank· DDBJ | BAB15740.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK090426 EMBL· GenBank· DDBJ | BAC03407.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AE006464 EMBL· GenBank· DDBJ | AAK61240.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Z92544 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471112 EMBL· GenBank· DDBJ | EAW85763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004327 EMBL· GenBank· DDBJ | AAH04327.1 EMBL· GenBank· DDBJ | mRNA | ||
BC014942 EMBL· GenBank· DDBJ | AAH14942.1 EMBL· GenBank· DDBJ | mRNA |