RB3GP_HUMAN
ID RB3GP_HUMAN Reviewed; 981 AA.
AC Q15042; A6H8Z3; C9J837; Q659F5; Q8TBB4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rab3 GTPase-activating protein catalytic subunit;
DE AltName: Full=RAB3 GTPase-activating protein 130 kDa subunit;
DE AltName: Full=Rab3-GAP p130;
DE Short=Rab3-GAP;
GN Name=RAB3GAP1; Synonyms=KIAA0066, RAB3GAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 439-981 (ISOFORM 1), AND VARIANT SER-598.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 764-981.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9030515; DOI=10.1074/jbc.272.8.4655;
RA Fukui K., Sasaki T., Imazumi K., Matsuura Y., Nakanishi H., Takai Y.;
RT "Isolation and characterization of a GTPase activating protein specific for
RT the Rab3 subfamily of small G proteins.";
RL J. Biol. Chem. 272:4655-4658(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9852129; DOI=10.1074/jbc.273.51.34580;
RA Oishi H., Sasaki T., Nagano F., Ikeda W., Ohya T., Wada M., Ide N.,
RA Nakanishi H., Takai Y.;
RT "Localization of the Rab3 small G protein regulators in nerve terminals and
RT their involvement in Ca2+-dependent exocytosis.";
RL J. Biol. Chem. 273:34580-34585(1998).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-619;
RP ARG-700; ARG-728 AND ARG-753.
RX PubMed=10859313; DOI=10.1074/jbc.m003705200;
RA Clabecq A., Henry J.-P., Darchen F.;
RT "Biochemical characterization of Rab3-GTPase-activating protein reveals a
RT mechanism similar to that of Ras-GAP.";
RL J. Biol. Chem. 275:31786-31791(2000).
RN [8]
RP INVOLVEMENT IN WARBM1.
RX PubMed=15696165; DOI=10.1038/ng1517;
RA Aligianis I.A., Johnson C.A., Gissen P., Chen D., Hampshire D.,
RA Hoffmann K., Maina E.N., Morgan N.V., Tee L., Morton J., Ainsworth J.R.,
RA Horn D., Rosser E., Cole T.R.P., Stolte-Dijkstra I., Fieggen K.,
RA Clayton-Smith J., Megarbane A., Shield J.P., Newbury-Ecob R., Dobyns W.B.,
RA Graham J.M., Kjaer K.W., Warburg M., Bond J., Trembath R.C., Harris L.W.,
RA Takai Y., Mundlos S., Tannahill D., Woods C.G., Maher E.R.;
RT "Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro
RT syndrome.";
RL Nat. Genet. 37:221-223(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP INTERACTION WITH LMAN1.
RX PubMed=22337587; DOI=10.1074/mcp.m111.016444;
RA Haines D.S., Lee J.E., Beauparlant S.L., Kyle D.B., den Besten W.,
RA Sweredoski M.J., Graham R.L., Hess S., Deshaies R.J.;
RT "Protein interaction profiling of the p97 adaptor UBXD1 points to a role
RT for the complex in modulating ERGIC-53 trafficking.";
RL Mol. Cell. Proteomics 11:M111.016444-M111.016444(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-537; SER-664 AND
RP THR-908, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INVOLVEMENT IN MARTS2 AND WARBM1.
RX PubMed=30730599; DOI=10.1002/ajmg.a.61065;
RA Koparir A., Karatas O.F., Yilmaz S.S., Suer I., Ozer B., Yuceturk B.,
RA Ozen M.;
RT "Revealing the functions of novel mutations in RAB3GAP1 in Martsolf and
RT Warburg micro syndromes.";
RL Am. J. Med. Genet. A 179:579-587(2019).
RN [18]
RP VARIANTS WARBM1 PRO-18 AND VAL-24.
RX PubMed=23420520; DOI=10.1002/humu.22296;
RA Handley M.T., Morris-Rosendahl D.J., Brown S., Macdonald F., Hardy C.,
RA Bem D., Carpanini S.M., Borck G., Martorell L., Izzi C., Faravelli F.,
RA Accorsi P., Pinelli L., Basel-Vanagaite L., Peretz G., Abdel-Salam G.M.,
RA Zaki M.S., Jansen A., Mowat D., Glass I., Stewart H., Mancini G.,
RA Lederer D., Roscioli T., Giuliano F., Plomp A.S., Rolfs A., Graham J.M.,
RA Seemanova E., Poo P., Garcia-Cazorla A., Edery P., Jackson I.J.,
RA Maher E.R., Aligianis I.A.;
RT "Mutation spectrum in RAB3GAP1, RAB3GAP2, and RAB18 and genotype-phenotype
RT correlations in Warburg micro syndrome and Martsolf syndrome.";
RL Hum. Mutat. 34:686-696(2013).
CC -!- FUNCTION: Probable catalytic subunit of a GTPase activating protein
CC that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and
CC RAB3D). Rab3 proteins are involved in regulated exocytosis of
CC neurotransmitters and hormones. Specifically converts active Rab3-GTP
CC to the inactive form Rab3-GDP. Required for normal eye and brain
CC development. May participate in neurodevelopmental processes such as
CC proliferation, migration and differentiation before synapse formation,
CC and non-synaptic vesicular release of neurotransmitters.
CC {ECO:0000269|PubMed:10859313, ECO:0000269|PubMed:9030515}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for GTP-loaded RAB3A {ECO:0000269|PubMed:10859313};
CC -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed
CC of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex
CC interacts with DMXL2 (By similarity). Interacts with LMAN1
CC (PubMed:22337587). {ECO:0000250|UniProtKB:P69735,
CC ECO:0000269|PubMed:22337587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9852129}. Note=In
CC neurons, it is enriched in the synaptic soluble fraction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15042-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15042-3; Sequence=VSP_054068;
CC Name=3;
CC IsoId=Q15042-4; Sequence=VSP_054475, VSP_054476;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9030515}.
CC -!- DISEASE: Warburg micro syndrome 1 (WARBM1) [MIM:600118]: A rare,
CC autosomal recessive syndrome characterized by microcephaly,
CC microphthalmia, microcornia, congenital cataracts, optic atrophy,
CC cortical dysplasia, in particular corpus callosum hypoplasia, severe
CC intellectual disability, spastic diplegia, and hypogonadism.
CC {ECO:0000269|PubMed:15696165, ECO:0000269|PubMed:23420520,
CC ECO:0000269|PubMed:30730599}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Martsolf syndrome 2 (MARTS2) [MIM:619420]: An autosomal
CC recessive disorder characterized by congenital cataracts, mildly to
CC severely impaired intellectual development, and facial dysmorphism.
CC Other features include brain malformations, microcephaly, and
CC hypogonadism-hypogenitalism. {ECO:0000269|PubMed:30730599}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC071602; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH56411.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; D31886; BAA06684.1; -; mRNA.
DR EMBL; AC017031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022977; AAH22977.1; -; mRNA.
DR EMBL; BC071602; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC146809; AAI46810.1; -; mRNA.
DR EMBL; AL096752; CAH56411.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33294.1; -. [Q15042-1]
DR CCDS; CCDS54402.1; -. [Q15042-3]
DR RefSeq; NP_001165906.1; NM_001172435.1. [Q15042-3]
DR RefSeq; NP_036365.1; NM_012233.2. [Q15042-1]
DR AlphaFoldDB; Q15042; -.
DR BioGRID; 116590; 121.
DR IntAct; Q15042; 21.
DR STRING; 9606.ENSP00000411418; -.
DR GlyGen; Q15042; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15042; -.
DR PhosphoSitePlus; Q15042; -.
DR SwissPalm; Q15042; -.
DR BioMuta; RAB3GAP1; -.
DR DMDM; 62511099; -.
DR EPD; Q15042; -.
DR jPOST; Q15042; -.
DR MassIVE; Q15042; -.
DR MaxQB; Q15042; -.
DR PaxDb; Q15042; -.
DR PeptideAtlas; Q15042; -.
DR PRIDE; Q15042; -.
DR ProteomicsDB; 60390; -. [Q15042-1]
DR ProteomicsDB; 789; -.
DR ProteomicsDB; 8989; -.
DR Antibodypedia; 33565; 183 antibodies from 29 providers.
DR DNASU; 22930; -.
DR Ensembl; ENST00000264158.13; ENSP00000264158.8; ENSG00000115839.19. [Q15042-1]
DR Ensembl; ENST00000442034.5; ENSP00000411418.1; ENSG00000115839.19. [Q15042-3]
DR GeneID; 22930; -.
DR KEGG; hsa:22930; -.
DR MANE-Select; ENST00000264158.13; ENSP00000264158.8; NM_012233.3; NP_036365.1.
DR UCSC; uc002tuj.4; human. [Q15042-1]
DR CTD; 22930; -.
DR DisGeNET; 22930; -.
DR GeneCards; RAB3GAP1; -.
DR GeneReviews; RAB3GAP1; -.
DR HGNC; HGNC:17063; RAB3GAP1.
DR HPA; ENSG00000115839; Low tissue specificity.
DR MalaCards; RAB3GAP1; -.
DR MIM; 600118; phenotype.
DR MIM; 602536; gene.
DR MIM; 619420; phenotype.
DR neXtProt; NX_Q15042; -.
DR OpenTargets; ENSG00000115839; -.
DR Orphanet; 1387; Cataract-intellectual disability-hypogonadism syndrome.
DR Orphanet; 2510; Micro syndrome.
DR PharmGKB; PA134969639; -.
DR VEuPathDB; HostDB:ENSG00000115839; -.
DR eggNOG; KOG2390; Eukaryota.
DR GeneTree; ENSGT00390000006705; -.
DR HOGENOM; CLU_012561_1_0_1; -.
DR InParanoid; Q15042; -.
DR OMA; IMTEDMH; -.
DR OrthoDB; 536022at2759; -.
DR PhylomeDB; Q15042; -.
DR TreeFam; TF314500; -.
DR PathwayCommons; Q15042; -.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SABIO-RK; Q15042; -.
DR SignaLink; Q15042; -.
DR SIGNOR; Q15042; -.
DR BioGRID-ORCS; 22930; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; RAB3GAP1; human.
DR GeneWiki; RAB3GAP1; -.
DR GenomeRNAi; 22930; -.
DR Pharos; Q15042; Tbio.
DR PRO; PR:Q15042; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15042; protein.
DR Bgee; ENSG00000115839; Expressed in hair follicle and 214 other tissues.
DR ExpressionAtlas; Q15042; baseline and differential.
DR Genevisible; Q15042; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:BHF-UCL.
DR GO; GO:0043010; P:camera-type eye development; IMP:BHF-UCL.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060325; P:face morphogenesis; IMP:BHF-UCL.
DR GO; GO:0021854; P:hypothalamus development; IMP:BHF-UCL.
DR GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:GO_Central.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0061646; P:positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1903061; P:positive regulation of protein lipidation; IMP:GO_Central.
DR GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR InterPro; IPR045700; Rab3GAP1.
DR InterPro; IPR045698; Rab3GAP1_C.
DR InterPro; IPR026147; Rab3GAP1_conserved.
DR PANTHER; PTHR21422; PTHR21422; 1.
DR Pfam; PF19533; Rab3-GAP_cat_C; 1.
DR Pfam; PF13890; Rab3-GTPase_cat; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cataract; Cytoplasm; Disease variant;
KW GTPase activation; Intellectual disability; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..981
FT /note="Rab3 GTPase-activating protein catalytic subunit"
FT /id="PRO_0000191655"
FT REGION 592..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UJ7"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UJ7"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UJ7"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 908
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..50
FT /note="MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEK
FT -> MFSLIS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054475"
FT VAR_SEQ 903
FT /note="R -> RLTESSDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054068"
FT VAR_SEQ 972..981
FT /note="GAFSSDTSFF -> VKIIDGDV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054476"
FT VARIANT 18
FT /note="T -> P (in WARBM1)"
FT /evidence="ECO:0000269|PubMed:23420520"
FT /id="VAR_086019"
FT VARIANT 24
FT /note="E -> V (in WARBM1)"
FT /evidence="ECO:0000269|PubMed:23420520"
FT /id="VAR_086020"
FT VARIANT 598
FT /note="N -> S (in dbSNP:rs10445686)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051716"
FT MUTAGEN 619
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:10859313"
FT MUTAGEN 700
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:10859313"
FT MUTAGEN 728
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10859313"
FT MUTAGEN 753
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:10859313"
SQ SEQUENCE 981 AA; 110524 MW; 0673611C5C49641C CRC64;
MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GNSLGKPLEK GIFTSGTWEE
KSDEISFADF KFSVTHHYLV QESTDKEGKD ELLEDVVPQS MQDLLGMNND FPPRAHCLVR
WYGLREFVVI APAAHSDAVL SESKCNLLLS SVSIALGNTG CQVPLFVQIH HKWRRMYVGE
CQGPGVRTDF EMVHLRKVPN QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RFTYVLQDWQ
QYFWPQQPPD IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
DLDPIQAPHW SVRVRKAENP QCLLGDFVTE FFKICRRKES TDEILGRSAF EEEGKETADI
THALSKLTEP ASVPIHKLSV SNMVHTAKKK IRKHRGVEES PLNNDVLNTI LLFLFPDAVS
EKPLDGTTST DNNNPPSESE DYNLYNQFKS APSDSLTYKL ALCLCMINFY HGGLKGVAHL
WQEFVLEMRF RWENNFLIPG LASGPPDLRC CLLHQKLQML NCCIERKKAR DEGKKTSASD
VTNIYPGDAG KAGDQLVPDN LKETDKEKGE VGKSWDSWSD SEEEFFECLS DTEELKGNGQ
ESGKKGGPKE MANLRPEGRL YQHGKLTLLH NGEPLYIPVT QEPAPMTEDL LEEQSEVLAK
LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCSLEDFVR WYSPRDYIEE EVIDEKGNVV
LKGELSARMK IPSNMWVEAW ETAKPIPARR QRRLFDDTRE AEKVLHYLAI QKPADLARHL
LPCVIHAAVL KVKEEESLEN ISSVKKIIKQ IISHSSKVLH FPNPEDKKLE EIIHQITNVE
ALIARARSLK AKFGTEKCEQ EEEKEDLERF VSCLLEQPEV LVTGAGRGHA GRIIHKLFVN
AQRAAAMTPP EEELKRMGSP EERRQNSVSD FPPPAGREFI LRTTVPRPAP YSKALPQRMY
SVLTKEDFRL AGAFSSDTSF F
