RBGPR_HUMAN
ID RBGPR_HUMAN Reviewed; 1393 AA.
AC Q9H2M9; A6H8V0; O75872; Q9HAB0; Q9UFJ7; Q9UQ15;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Rab3 GTPase-activating protein non-catalytic subunit;
DE AltName: Full=RGAP-iso;
DE AltName: Full=Rab3 GTPase-activating protein 150 kDa subunit;
DE AltName: Full=Rab3-GAP p150;
DE Short=Rab3-GAP150;
DE AltName: Full=Rab3-GAP regulatory subunit;
GN Name=RAB3GAP2; Synonyms=KIAA0839;
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9733780; DOI=10.1074/jbc.273.38.24781;
RA Nagano F., Sasaki T., Fukui K., Asakura T., Imazumi K., Takai Y.;
RT "Molecular cloning and characterization of the noncatalytic subunit of the
RT Rab3 subfamily-specific GTPase-activating protein.";
RL J. Biol. Chem. 273:24781-24785(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 930-1393.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-901, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND IDENTIFICATION BY
RP 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-450 AND SER-916, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP VARIANT MARTS1 CYS-1052.
RX PubMed=16532399; DOI=10.1086/502681;
RA Aligianis I.A., Morgan N.V., Mione M., Johnson C.A., Rosser E.,
RA Hennekam R.C.M., Adams G., Trembath R.C., Pilz D.T., Stoodley N.,
RA Moore A.T., Wilson S., Maher E.R.;
RT "Mutation in Rab3 GTPase-activating protein (RAB3GAP) noncatalytic subunit
RT in a kindred with Martsolf syndrome.";
RL Am. J. Hum. Genet. 78:702-707(2006).
RN [18]
RP VARIANT WARBM2 167-PHE--THR-169 DEL.
RX PubMed=20967465; DOI=10.1007/s00439-010-0896-2;
RA Borck G., Wunram H., Steiert A., Volk A.E., Korber F., Roters S.,
RA Herkenrath P., Wollnik B., Morris-Rosendahl D.J., Kubisch C.;
RT "A homozygous RAB3GAP2 mutation causes Warburg Micro syndrome.";
RL Hum. Genet. 129:45-50(2011).
RN [19]
RP VARIANT MARTS1 CYS-426.
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: Regulatory subunit of a GTPase activating protein that has
CC specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3
CC proteins are involved in regulated exocytosis of neurotransmitters and
CC hormones. Rab3 GTPase-activating complex specifically converts active
CC Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and
CC brain development. May participate in neurodevelopmental processes such
CC as proliferation, migration and differentiation before synapse
CC formation, and non-synaptic vesicular release of neurotransmitters.
CC {ECO:0000269|PubMed:9733780}.
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:Q5U1Z0,
CC ECO:0000269|PubMed:22337587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, it is enriched in the
CC synaptic soluble fraction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2M9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2M9-2; Sequence=VSP_013311, VSP_013312;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9733780}.
CC -!- DISEASE: Martsolf syndrome 1 (MARTS1) [MIM:212720]: An autosomal
CC recessive disease characterized by congenital cataracts, intellectual
CC disability, and hypogonadism. {ECO:0000269|PubMed:16532399,
CC ECO:0000269|PubMed:23420520}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Warburg micro syndrome 2 (WARBM2) [MIM:614225]: A rare
CC syndrome characterized by microcephaly, microphthalmia, microcornia,
CC congenital cataracts, optic atrophy, cortical dysplasia, in particular
CC corpus callosum hypoplasia, severe intellectual disability, spastic
CC diplegia, and hypogonadism. {ECO:0000269|PubMed:20967465}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the Rab3-GAP regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AF004828; AAC35881.1; -; mRNA.
DR EMBL; AF255648; AAG44636.1; -; mRNA.
DR EMBL; AB020646; BAA74862.2; -; mRNA.
DR EMBL; AK021928; BAB13939.1; -; mRNA.
DR EMBL; AK291234; BAF83923.1; -; mRNA.
DR EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93304.1; -; Genomic_DNA.
DR EMBL; BC146760; AAI46761.1; -; mRNA.
DR EMBL; AL117631; CAB56022.1; -; mRNA.
DR CCDS; CCDS31028.1; -. [Q9H2M9-1]
DR PIR; T17332; T17332.
DR RefSeq; NP_036546.2; NM_012414.3. [Q9H2M9-1]
DR AlphaFoldDB; Q9H2M9; -.
DR BioGRID; 117317; 89.
DR IntAct; Q9H2M9; 10.
DR MINT; Q9H2M9; -.
DR STRING; 9606.ENSP00000351832; -.
DR GlyGen; Q9H2M9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2M9; -.
DR PhosphoSitePlus; Q9H2M9; -.
DR SwissPalm; Q9H2M9; -.
DR BioMuta; RAB3GAP2; -.
DR DMDM; 62511132; -.
DR EPD; Q9H2M9; -.
DR jPOST; Q9H2M9; -.
DR MassIVE; Q9H2M9; -.
DR MaxQB; Q9H2M9; -.
DR PaxDb; Q9H2M9; -.
DR PeptideAtlas; Q9H2M9; -.
DR PRIDE; Q9H2M9; -.
DR ProteomicsDB; 80569; -. [Q9H2M9-1]
DR ProteomicsDB; 80570; -. [Q9H2M9-2]
DR Antibodypedia; 20736; 137 antibodies from 24 providers.
DR DNASU; 25782; -.
DR Ensembl; ENST00000358951.7; ENSP00000351832.2; ENSG00000118873.17. [Q9H2M9-1]
DR GeneID; 25782; -.
DR KEGG; hsa:25782; -.
DR MANE-Select; ENST00000358951.7; ENSP00000351832.2; NM_012414.4; NP_036546.2.
DR UCSC; uc057pnr.1; human. [Q9H2M9-1]
DR CTD; 25782; -.
DR DisGeNET; 25782; -.
DR GeneCards; RAB3GAP2; -.
DR GeneReviews; RAB3GAP2; -.
DR HGNC; HGNC:17168; RAB3GAP2.
DR HPA; ENSG00000118873; Low tissue specificity.
DR MalaCards; RAB3GAP2; -.
DR MIM; 212720; phenotype.
DR MIM; 609275; gene.
DR MIM; 614225; phenotype.
DR neXtProt; NX_Q9H2M9; -.
DR OpenTargets; ENSG00000118873; -.
DR Orphanet; 401830; Autosomal recessive spastic paraplegia type 69.
DR Orphanet; 1387; Cataract-intellectual disability-hypogonadism syndrome.
DR Orphanet; 2510; Micro syndrome.
DR PharmGKB; PA142671105; -.
DR VEuPathDB; HostDB:ENSG00000118873; -.
DR eggNOG; KOG2727; Eukaryota.
DR GeneTree; ENSGT00390000005794; -.
DR HOGENOM; CLU_006591_0_0_1; -.
DR InParanoid; Q9H2M9; -.
DR OMA; LGCLDIW; -.
DR OrthoDB; 790713at2759; -.
DR PhylomeDB; Q9H2M9; -.
DR TreeFam; TF314817; -.
DR PathwayCommons; Q9H2M9; -.
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 SignaLink; Q9H2M9; -.
DR BioGRID-ORCS; 25782; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; RAB3GAP2; human.
DR GeneWiki; RAB3GAP2; -.
DR GenomeRNAi; 25782; -.
DR Pharos; Q9H2M9; Tbio.
DR PRO; PR:Q9H2M9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H2M9; protein.
DR Bgee; ENSG00000118873; Expressed in choroid plexus epithelium and 210 other tissues.
DR ExpressionAtlas; Q9H2M9; baseline and differential.
DR Genevisible; Q9H2M9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0030234; F:enzyme regulator activity; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
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:1903061; P:positive regulation of protein lipidation; IMP:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR InterPro; IPR026059; Rab3GAP2.
DR InterPro; IPR029257; RAB3GAP2_C.
DR InterPro; IPR032839; RAB3GAP_N.
DR PANTHER; PTHR12472; PTHR12472; 1.
DR Pfam; PF14656; RAB3GAP2_C; 1.
DR Pfam; PF14655; RAB3GAP2_N; 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..1393
FT /note="Rab3 GTPase-activating protein non-catalytic
FT subunit"
FT /id="PRO_0000191662"
FT REGION 36..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMG7"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U1Z0"
FT VAR_SEQ 205..206
FT /note="NE -> VV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013311"
FT VAR_SEQ 207..1393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013312"
FT VARIANT 167..169
FT /note="Missing (in WARBM2)"
FT /evidence="ECO:0000269|PubMed:20967465"
FT /id="VAR_066675"
FT VARIANT 426
FT /note="R -> C (in MARTS1)"
FT /evidence="ECO:0000269|PubMed:23420520"
FT /id="VAR_086021"
FT VARIANT 863
FT /note="T -> A (in dbSNP:rs12045447)"
FT /id="VAR_021588"
FT VARIANT 1052
FT /note="G -> C (in MARTS1; may cause exon skipping;
FT dbSNP:rs121434310)"
FT /evidence="ECO:0000269|PubMed:16532399"
FT /id="VAR_029881"
FT VARIANT 1092
FT /note="S -> T (in dbSNP:rs2289189)"
FT /id="VAR_021589"
FT CONFLICT 289
FT /note="G -> R (in Ref. 1; AAC35881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1393 AA; 155985 MW; 4138F60B5199211E CRC64;
MACSIVQFCY FQDLQAARDF LFPHLREEIL SGALRRDPSK STDWEDDGWG AWEENEPQEP
EEEGNTCKTQ KTSWLQDCVL SLSPTNDLMV IAREQKAVFL VPKWKYSDKG KEEMQFAVGW
SGSLNVEEGE CVTSALCIPL ASQKRSSTGR PDWTCIVVGF TSGYVRFYTE NGVLLLAQLL
NEDPVLQLKC RTYEIPRHPG VTEQNEELSI LYPAAIVTID GFSLFQSLRA CRNQVAKAAA
SGNENIQPPP LAYKKWGLQD IDTIIDHASV GIMTLSPFDQ MKTASNIGGF NAAIKNSPPA
MSQYITVGSN PFTGFFYALE GSTQPLLSHV ALAVASKLTS ALFNAASGWL GWKSKHEEEA
VQKQKPKVEP ATPLAVRFGL PDSRRHGESI CLSPCNTLAA VTDDFGRVIL LDVARGIAIR
MWKGYRDAQI GWIQTVEDLH ERVPEKADFS PFGNSQGPSR VAQFLVIYAP RRGILEVWST
QQGPRVGAFN VGKHCRLLYP GYKIMGLNNV TSQSWQPQTY QICLVDPVSG SVKTVNVPFH
LALSDKKSER AKDMHLVKKL AALLKTKSPN LDLVETEIKE LILDIKYPAT KKQALESILA
SERLPFSCLR NITQTLMDTL KSQELESVDE GLLQFCANKL KLLQLYESVS QLNSLDFHLD
TPFSDNDLAL LLRLDEKELL KLQALLEKYK QENTRTNVRF SDDKDGVLPV KTFLEYLEYE
KDVLNIKKIS EEEYVALGSF FFWKCLHGES STEDMCHTLE SAGLSPQLLL SLLLSVWLSK
EKDILDKPQS ICCLHTMLSL LSKMKVAIDE TWDSQSVSPW WQQMRTACIQ SENNGAALLS
AHVGHSVAAQ ISNNMTEKKF SQTVLGADSE ALTDSWEALS LDTEYWKLLL KQLEDCLILQ
TLLHSKGNTQ TSKVSSLQAE PLPRLSVKKL LEGGKGGIAD SVAKWIFKQD FSPEVLKLAN
EERDAENPDE PKEGVNRSFL EVSEMEMDLG AIPDLLHLAY EQFPCSLELD VLHAHCCWEY
VVQWNKDPEE ARFFVRSIEH LKQIFNAHVQ NGIALMMWNT FLVKRFSAAT YLMDKVGKSP
KDRLCRRDVG MSDTAMTSFL GSCLDLLQIL MEADVSRDEI QVPVLDTEDA WLSVEGPISI
VELALEQKHI HYPLVEHHSI LCSILYAVMR FSLKTVKPLS LFDSKGKNAF FKDLTSIQLL
PSGEMDPNFI SVRQQFLLKV VSAAVQAQHS ATKVKDPTEE ATPTPFGKDQ DWPALAVDLA
HHLQVSEDVV RRHYVGELYN YGVDHLGEEA ILQVHDKEVL ASQLLVLTGQ RLAHALLHTQ
TKEGMELLAR LPPTLCTWLK AMDPQDLQNT EVPIATTAKL VNKVIELLPE KHGQYGLALH
LIEAVEAISL PSL
