Q9H2M9 · RBGPR_HUMAN
- ProteinRab3 GTPase-activating protein non-catalytic subunit
- GeneRAB3GAP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1393 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulatory subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18 (PubMed:24891604, PubMed:9733780).
As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (By similarity).
Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (By similarity).
The Rab3GAP complex, acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604).
Required for recruiting and activating RAB18 at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604).
Required for normal eye and brain development (By similarity).
May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity).
As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (By similarity).
Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (By similarity).
The Rab3GAP complex, acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (PubMed:24891604).
Required for recruiting and activating RAB18 at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (PubMed:24891604).
Required for normal eye and brain development (By similarity).
May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (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 | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | enzyme activator activity | |
Molecular Function | enzyme regulator activity | |
Molecular Function | GTPase activator activity | |
Molecular Function | small GTPase binding | |
Biological Process | establishment of protein localization to endoplasmic reticulum membrane | |
Biological Process | intracellular protein transport | |
Biological Process | positive regulation of autophagosome assembly | |
Biological Process | positive regulation of endoplasmic reticulum tubular network organization | |
Biological Process | positive regulation of protein lipidation | |
Biological Process | regulation of GTPase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRab3 GTPase-activating protein non-catalytic subunit
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H2M9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In neurons, it is enriched in the synaptic soluble fraction.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Martsolf syndrome 1 (MARTS1)
- Note
- DescriptionAn autosomal recessive disease characterized by congenital cataracts, intellectual disability, and hypogonadism.
- See alsoMIM:212720
Natural variants in MARTS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086021 | 426 | R>C | in MARTS1; abolishes GEF activity towards RAB18; dbSNP:rs587777167 | |
VAR_029881 | 1052 | G>C | in MARTS1; may cause exon skipping; dbSNP:rs121434310 |
Warburg micro syndrome 2 (WARBM2)
- Note
- DescriptionA rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe intellectual disability, spastic diplegia, and hypogonadism.
- See alsoMIM:614225
Natural variants in WARBM2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_066675 | 167-169 | missing | in WARBM2 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_066675 | 167-169 | in WARBM2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_086021 | 426 | in MARTS1; abolishes GEF activity towards RAB18; dbSNP:rs587777167 | |||
Sequence: R → C | ||||||
Natural variant | VAR_021588 | 863 | in dbSNP:rs12045447 | |||
Sequence: T → A | ||||||
Natural variant | VAR_029881 | 1052 | in MARTS1; may cause exon skipping; dbSNP:rs121434310 | |||
Sequence: G → C | ||||||
Natural variant | VAR_021589 | 1092 | in dbSNP:rs2289189 | |||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,470 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000191662 | 1-1393 | UniProt | Rab3 GTPase-activating protein non-catalytic subunit | |||
Sequence: MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVLSLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGFTSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAASGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALEGSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAAVTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWSTQQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKKSERAKDMHLVKKLAALLKTKSPNLDLVETEIKELILDIKYPATKKQALESILASERLPFSCLRNITQTLMDTLKSQELESVDEGLLQFCANKLKLLQLYESVSQLNSLDFHLDTPFSDNDLALLLRLDEKELLKLQALLEKYKQENTRTNVRFSDDKDGVLPVKTFLEYLEYEKDVLNIKKISEEEYVALGSFFFWKCLHGESSTEDMCHTLESAGLSPQLLLSLLLSVWLSKEKDILDKPQSICCLHTMLSLLSKMKVAIDETWDSQSVSPWWQQMRTACIQSENNGAALLSAHVGHSVAAQISNNMTEKKFSQTVLGADSEALTDSWEALSLDTEYWKLLLKQLEDCLILQTLLHSKGNTQTSKVSSLQAEPLPRLSVKKLLEGGKGGIADSVAKWIFKQDFSPEVLKLANEERDAENPDEPKEGVNRSFLEVSEMEMDLGAIPDLLHLAYEQFPCSLELDVLHAHCCWEYVVQWNKDPEEARFFVRSIEHLKQIFNAHVQNGIALMMWNTFLVKRFSAATYLMDKVGKSPKDRLCRRDVGMSDTAMTSFLGSCLDLLQILMEADVSRDEIQVPVLDTEDAWLSVEGPISIVELALEQKHIHYPLVEHHSILCSILYAVMRFSLKTVKPLSLFDSKGKNAFFKDLTSIQLLPSGEMDPNFISVRQQFLLKVVSAAVQAQHSATKVKDPTEEATPTPFGKDQDWPALAVDLAHHLQVSEDVVRRHYVGELYNYGVDHLGEEAILQVHDKEVLASQLLVLTGQRLAHALLHTQTKEGMELLARLPPTLCTWLKAMDPQDLQNTEVPIATTAKLVNKVIELLPEKHGQYGLALHLIEAVEAISLPSL | |||||||
Modified residue | 39 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 450 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 875 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 901 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 915 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 916 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 916 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 978 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1242 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 36-67 | Disordered | ||||
Sequence: RDPSKSTDWEDDGWGAWEENEPQEPEEEGNTC |
Sequence similarities
Belongs to the Rab3-GAP regulatory subunit family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H2M9-1
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
- Length1,393
- Mass (Da)155,985
- Last updated2001-03-01 v1
- Checksum4138F60B5199211E
Q9H2M9-2
- Name2
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QJG4 | A0A8I5QJG4_HUMAN | RAB3GAP2 | 885 | ||
A0A8I5QJC9 | A0A8I5QJC9_HUMAN | RAB3GAP2 | 1358 | ||
F8WDJ2 | F8WDJ2_HUMAN | RAB3GAP2 | 82 | ||
A0A8I5KRP1 | A0A8I5KRP1_HUMAN | RAB3GAP2 | 1368 | ||
A0A8I5KRK1 | A0A8I5KRK1_HUMAN | RAB3GAP2 | 1381 | ||
A0A8I5KSQ5 | A0A8I5KSQ5_HUMAN | RAB3GAP2 | 1360 | ||
A0A8I5KWJ9 | A0A8I5KWJ9_HUMAN | RAB3GAP2 | 1305 | ||
A0A8I5KUS2 | A0A8I5KUS2_HUMAN | RAB3GAP2 | 328 | ||
A0A8I5KYQ0 | A0A8I5KYQ0_HUMAN | RAB3GAP2 | 1397 | ||
A0A8I5KY07 | A0A8I5KY07_HUMAN | RAB3GAP2 | 1359 | ||
A0A8I5KZB3 | A0A8I5KZB3_HUMAN | RAB3GAP2 | 1418 |
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF004828 EMBL· GenBank· DDBJ | AAC35881.1 EMBL· GenBank· DDBJ | mRNA | ||
AF255648 EMBL· GenBank· DDBJ | AAG44636.1 EMBL· GenBank· DDBJ | mRNA | ||
AB020646 EMBL· GenBank· DDBJ | BAA74862.2 EMBL· GenBank· DDBJ | mRNA | ||
AK021928 EMBL· GenBank· DDBJ | BAB13939.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291234 EMBL· GenBank· DDBJ | BAF83923.1 EMBL· GenBank· DDBJ | mRNA | ||
AC103590 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL445435 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471100 EMBL· GenBank· DDBJ | EAW93304.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC146760 EMBL· GenBank· DDBJ | AAI46761.1 EMBL· GenBank· DDBJ | mRNA | ||
AL117631 EMBL· GenBank· DDBJ | CAB56022.1 EMBL· GenBank· DDBJ | mRNA |