Q9H2M9 · RBGPR_HUMAN

  • Protein
    Rab3 GTPase-activating protein non-catalytic subunit
  • Gene
    RAB3GAP2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum membrane
Cellular Componentplasma membrane
Cellular Componentprotein-containing complex
Molecular Functionenzyme activator activity
Molecular Functionenzyme regulator activity
Molecular FunctionGTPase activator activity
Molecular Functionsmall GTPase binding
Biological Processestablishment of protein localization to endoplasmic reticulum membrane
Biological Processintracellular protein transport
Biological Processpositive regulation of autophagosome assembly
Biological Processpositive regulation of endoplasmic reticulum tubular network organization
Biological Processpositive regulation of protein lipidation
Biological Processregulation of GTPase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rab3 GTPase-activating protein non-catalytic subunit
  • Alternative names
    • RGAP-iso
    • Rab3 GTPase-activating protein 150 kDa subunit
    • Rab3-GAP p150 (Rab3-GAP150)
    • Rab3-GAP regulatory subunit

Gene names

    • Name
      RAB3GAP2
    • Synonyms
      KIAA0839

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9H2M9
  • Secondary accessions
    • A6H8V0
    • O75872
    • Q9HAB0
    • Q9UFJ7
    • Q9UQ15

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Endoplasmic reticulum
Note: In neurons, it is enriched in the synaptic soluble fraction.

Keywords

Disease & Variants

Involvement in disease

Martsolf syndrome 1 (MARTS1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal recessive disease characterized by congenital cataracts, intellectual disability, and hypogonadism.
  • See also
    MIM:212720
Natural variants in MARTS1
Variant IDPosition(s)ChangeDescription
VAR_086021426R>Cin MARTS1; abolishes GEF activity towards RAB18; dbSNP:rs587777167
VAR_0298811052G>Cin MARTS1; may cause exon skipping; dbSNP:rs121434310

Warburg micro syndrome 2 (WARBM2)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A 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 also
    MIM:614225
Natural variants in WARBM2
Variant IDPosition(s)ChangeDescription
VAR_066675167-169missingin WARBM2

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_066675167-169in WARBM2
Natural variantVAR_086021426in MARTS1; abolishes GEF activity towards RAB18; dbSNP:rs587777167
Natural variantVAR_021588863in dbSNP:rs12045447
Natural variantVAR_0298811052in MARTS1; may cause exon skipping; dbSNP:rs121434310
Natural variantVAR_0215891092in dbSNP:rs2289189

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001916621-1393UniProtRab3 GTPase-activating protein non-catalytic subunit
Modified residue39UniProtPhosphoserine
Modified residue (large scale data)372PRIDEPhosphothreonine
Modified residue450UniProtPhosphoserine
Modified residue (large scale data)450PRIDEPhosphoserine
Modified residue (large scale data)544PRIDEPhosphoserine
Modified residue (large scale data)568PRIDEPhosphoserine
Modified residue (large scale data)875PRIDEPhosphoserine
Modified residue901UniProtPhosphothreonine
Modified residue (large scale data)915PRIDEPhosphoserine
Modified residue916UniProtPhosphoserine
Modified residue (large scale data)916PRIDEPhosphoserine
Modified residue978UniProtPhosphoserine
Modified residue (large scale data)1242PRIDEPhosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Organism-specific databases

Interaction

Subunit

The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP1 and RAB3GAP2 (By similarity).
The Rab3 GTPase-activating complex interacts with DMXL2 (By similarity).
Interacts with LMAN1 (PubMed:22337587).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region36-67Disordered

Sequence similarities

Belongs to the Rab3-GAP regulatory subunit family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    1,393
  • Mass (Da)
    155,985
  • Last updated
    2001-03-01 v1
  • Checksum
    4138F60B5199211E
MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVLSLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGFTSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAASGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALEGSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAAVTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWSTQQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKKSERAKDMHLVKKLAALLKTKSPNLDLVETEIKELILDIKYPATKKQALESILASERLPFSCLRNITQTLMDTLKSQELESVDEGLLQFCANKLKLLQLYESVSQLNSLDFHLDTPFSDNDLALLLRLDEKELLKLQALLEKYKQENTRTNVRFSDDKDGVLPVKTFLEYLEYEKDVLNIKKISEEEYVALGSFFFWKCLHGESSTEDMCHTLESAGLSPQLLLSLLLSVWLSKEKDILDKPQSICCLHTMLSLLSKMKVAIDETWDSQSVSPWWQQMRTACIQSENNGAALLSAHVGHSVAAQISNNMTEKKFSQTVLGADSEALTDSWEALSLDTEYWKLLLKQLEDCLILQTLLHSKGNTQTSKVSSLQAEPLPRLSVKKLLEGGKGGIADSVAKWIFKQDFSPEVLKLANEERDAENPDEPKEGVNRSFLEVSEMEMDLGAIPDLLHLAYEQFPCSLELDVLHAHCCWEYVVQWNKDPEEARFFVRSIEHLKQIFNAHVQNGIALMMWNTFLVKRFSAATYLMDKVGKSPKDRLCRRDVGMSDTAMTSFLGSCLDLLQILMEADVSRDEIQVPVLDTEDAWLSVEGPISIVELALEQKHIHYPLVEHHSILCSILYAVMRFSLKTVKPLSLFDSKGKNAFFKDLTSIQLLPSGEMDPNFISVRQQFLLKVVSAAVQAQHSATKVKDPTEEATPTPFGKDQDWPALAVDLAHHLQVSEDVVRRHYVGELYNYGVDHLGEEAILQVHDKEVLASQLLVLTGQRLAHALLHTQTKEGMELLARLPPTLCTWLKAMDPQDLQNTEVPIATTAKLVNKVIELLPEKHGQYGLALHLIEAVEAISLPSL

Q9H2M9-2

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5QJG4A0A8I5QJG4_HUMANRAB3GAP2885
A0A8I5QJC9A0A8I5QJC9_HUMANRAB3GAP21358
F8WDJ2F8WDJ2_HUMANRAB3GAP282
A0A8I5KRP1A0A8I5KRP1_HUMANRAB3GAP21368
A0A8I5KRK1A0A8I5KRK1_HUMANRAB3GAP21381
A0A8I5KSQ5A0A8I5KSQ5_HUMANRAB3GAP21360
A0A8I5KWJ9A0A8I5KWJ9_HUMANRAB3GAP21305
A0A8I5KUS2A0A8I5KUS2_HUMANRAB3GAP2328
A0A8I5KYQ0A0A8I5KYQ0_HUMANRAB3GAP21397
A0A8I5KY07A0A8I5KY07_HUMANRAB3GAP21359
A0A8I5KZB3A0A8I5KZB3_HUMANRAB3GAP21418

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_013311205-206in isoform 2
Alternative sequenceVSP_013312207-1393in isoform 2
Sequence conflict289in Ref. 1; AAC35881

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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