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(Top) 1 Interactions 2 References 3 Further reading

RAB3A

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RAB3A

Identifiers

Aliases

RAB3A, member RAS oncogene family

External IDs

OMIM: 179490; MGI: 97843; HomoloGene: 20629; GeneCards: RAB3A; OMA:RAB3A - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.11	Start	18,196,784 bp^[1]
Band	19p13.11	End	18,204,042 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8 B3.3\|8 34.15 cM	Start	71,207,328 bp^[2]
Band	8 B3.3\|8 34.15 cM	End	71,211,323 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right frontal lobe

right hemisphere of cerebellum

Brodmann area 9

prefrontal cortex

nucleus accumbens

amygdala

putamen

hypothalamus

cingulate gyrus

spinal ganglia

Top expressed in

primary visual cortex

superior frontal gyrus

dentate gyrus of hippocampal formation granule cell

cerebellar cortex

central gray substance of midbrain

subiculum

dorsomedial hypothalamic nucleus

prefrontal cortex

habenula

primary motor cortex

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding ATPase binding GTP binding myosin V binding protein C-terminus binding protein binding ATPase activator activity GTP-dependent protein binding GTPase activity GDP-dissociation inhibitor binding
Cellular component	extracellular vesicle endosome clathrin-sculpted monoamine transport vesicle membrane membrane synaptic vesicle plasma membrane clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane clathrin-sculpted acetylcholine transport vesicle membrane axon terminal bouton acrosomal vesicle intracellular organelle clathrin-sculpted glutamate transport vesicle membrane cytosol secretory granule membrane anchored component of synaptic vesicle membrane vesicle protein-containing complex presynaptic active zone secretory granule perinuclear region of cytoplasm
Biological process	respiratory system process positive regulation of ATP-dependent activity axonogenesis lung development synaptic vesicle exocytosis regulation of short-term neuronal synaptic plasticity evoked neurotransmitter secretion mitochondrion organization response to electrical stimulus post-embryonic development constitutive secretory pathway maintenance of presynaptic active zone structure glutamate secretion regulation of exocytosis regulation of synaptic vesicle fusion to presynaptic active zone membrane neuromuscular synaptic transmission synaptic vesicle recycling sensory perception of touch protein transport positive regulation of exocytosis synaptic vesicle maturation neurotransmitter secretion positive regulation of regulated secretory pathway exocytosis neutrophil degranulation post-translational protein modification transport intracellular protein transport vesicle docking involved in exocytosis protein secretion Rab protein signal transduction protein localization to plasma membrane plasma membrane repair regulation of synaptic vesicle priming synaptic vesicle transport acrosomal vesicle exocytosis regulation of synaptic vesicle exocytosis calcium-ion regulated exocytosis synaptic vesicle clustering
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5864


19339

Ensembl


ENSG00000105649


ENSMUSG00000031840

UniProt


P20336


P63011

RefSeq (mRNA)


NM_002866


NM_001166399 NM_009001 NM_001328047 NM_001378892 NM_001378893

RefSeq (protein)


NP_002857 NP_002857.1


NP_001159871 NP_001314976 NP_033027 NP_001365821 NP_001365822

Location (UCSC)

Chr 19: 18.2 – 18.2 Mb

Chr 8: 71.21 – 71.21 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene.^[5]^[6]^[7] It is involved in calcium-triggered exocytosis in neurons.

Interactions[edit]

RAB3A has been shown to interact with:

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000105649 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031840 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ Rousseau-Merck MF, Zahraoui A, Bernheim A, Touchot N, Miglierina R, Tavitian A, Berger R (January 1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2". Genomics. 5 (4): 694–8. doi:10.1016/0888-7543(89)90110-9. PMID 2687157.

^ Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG (March 1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A". Mol Cell Biol. 15 (3): 1137–43. doi:10.1128/MCB.15.3.1137. PMC 230335. PMID 7532276.

^ "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".

^ ^a ^b Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.

^ Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/s0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654. S2CID 155875.

^ "Protein unc-13 homolog A". UniProt.

^ Ostermeier C, Brunger AT (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. S2CID 15162326.

^ Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.

^ Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (January 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.

^ Pereira-Leal JB, Strom M, Godfrey RF, Seabra MC (January 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. 301 (1): 92–7. doi:10.1016/s0006-291x(02)02963-7. PMID 12535645.

Further reading[edit]

Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE, Buss JE, Der CJ (1991). "Isoprenoid modification of rab proteins terminating in CC or CXC motifs". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6264–8. Bibcode:1991PNAS...88.6264K. doi:10.1073/pnas.88.14.6264. PMC 52063. PMID 1648736.

Zahraoui A, Touchot N, Chardin P, Tavitian A (1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". J. Biol. Chem. 264 (21): 12394–401. doi:10.1016/S0021-9258(18)63872-4. PMID 2501306.

Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA (1995). "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 11963–7. Bibcode:1994PNAS...9111963F. doi:10.1073/pnas.91.25.11963. PMC 45356. PMID 7991565.

McKiernan CJ, Brondyk WH, Macara IG (1993). "The Rab3A GTPase interacts with multiple factors through the same effector domain. Mutational analysis of cross-linking of Rab3A to a putative target protein". J. Biol. Chem. 268 (32): 24449–52. doi:10.1016/S0021-9258(20)80546-8. PMID 8226995.

Trask B, Fertitta A, Christensen M, Youngblom J, Bergmann A, Copeland A, de Jong P, Mohrenweiser H, Olsen A, Carrano A (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics. 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID 8432525.

Johannes L, Perez F, Laran-Chich MP, Henry JP, Darchen F (1996). "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II". Eur. J. Biochem. 239 (2): 362–8. doi:10.1111/j.1432-1033.1996.0362u.x. PMID 8706741.

Burton JL, Slepnev V, De Camilli PV (1997). "An evolutionarily conserved domain in a subfamily of Rabs is crucial for the interaction with the guanyl nucleotide exchange factor Mss4". J. Biol. Chem. 272 (6): 3663–8. doi:10.1074/jbc.272.6.3663. PMID 9013620.

Geppert M, Goda Y, Stevens CF, Südhof TC (1997). "The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion". Nature. 387 (6635): 810–4. doi:10.1038/42954. PMID 9194562. S2CID 4359038.

Martincic I, Peralta ME, Ngsee JK (1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". J. Biol. Chem. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.

Ostermeier C, Brunger AT (1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. S2CID 15162326.

Jung YJ, Lee TH, Lee JY, Kim JH, Park JB (1999). "Phosphatidic acid is important to the translocation of Rab3A from the cytosol to phospholipid membranes". NeuroReport. 10 (13): 2859–63. doi:10.1097/00001756-199909090-00029. PMID 10511453.

Sullivan M, Olsen AS, Houslay MD (2000). "Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND". Cell. Signal. 11 (10): 735–42. doi:10.1016/S0898-6568(99)00037-6. PMID 10574328.

Clabecq A, Henry JP, Darchen F (2000). "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP". J. Biol. Chem. 275 (41): 31786–91. doi:10.1074/jbc.M003705200. PMID 10859313.

Haynes LP, Evans GJ, Morgan A, Burgoyne RD (2001). "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells". J. Biol. Chem. 276 (13): 9726–32. doi:10.1074/jbc.M006959200. PMID 11134008.

Zhang Y, Luan Z, Liu A, Hu G (2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. PMID 11377421. S2CID 33119468.

Luo HR, Saiardi A, Nagata E, Ye K, Yu H, Jung TS, Luo X, Jain S, Sawa A, Snyder SH (2001). "GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase". Neuron. 31 (3): 439–51. doi:10.1016/S0896-6273(01)00384-1. PMID 11516400. S2CID 10990373.

Piiper A, Leser J, Lutz MP, Beil M, Zeuzem S (2001). "Subcellular distribution and function of Rab3A-D in pancreatic acinar AR42J cells". Biochem. Biophys. Res. Commun. 287 (3): 746–51. doi:10.1006/bbrc.2001.5651. PMID 11563859.

Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.

v t e PDB gallery
1zbd: STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A 3rab: GPPNHP-BOUND RAB3A AT 2.0 A RESOLUTION

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B
Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2
Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4
H+/K+ (3.6.3.10)	ATP4A
Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_olf G_αi GNAI1 GNAI2 GNAI3 Transducin GNAT1 GNAT2 Gustducin GNAT3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13
3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK
3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic
3.6.5.5-6: Polymerization motors	dynamin superfamily Dynamin Guanylate-binding protein Mitofusin-1 MX1 and MX2 OPA1 Tubulin

Membrane protein: vesicular transport proteins (TC 1F)

Synaptic vesicle

SNARE

Q-SNARE

Syntaxin
- STX1A
- STX1B
- STX2
- STX3
- STX4
- STX5
- STX6
- STX7
- STX8
- STX10
- STX11
- STX12
- STX16
- STX17
- STX18
- STX19

R-SNARE

Synaptotagmin

Other

Small GTPase: RAB3A

COPI

Coatomer
- COPA
- COPB1
- COPB2
- COPD/Archain
- COPE
- COPG
- COPG2
- COPZ1
- COPZ2

Small GTPase: ARF

COPII

Coatomer
- SEC23A/SEC24A
- SEC13/SEC31

Small GTPase: SAR1A

RME/Clathrin

Caveolae

Other/ungrouped

Vesicle formation

Adaptor protein complex 1:

Adaptor protein complex 2:

Adaptor protein complex 3:

Adaptor protein complex 4:

LMAN1

LYST

BLOC-1:

BLOC-2:

BLOC-3:

HPS1
HPS4

Coats:

Small GTPase

Dynamin
- DNM1
- DNM2
- DNM3

Other

Sorting nexins

SYNRG

Intracellular signaling peptides and proteins

MAP

see MAP kinase pathway

Calcium

G alpha subunitG_α
- GNAO1
- GNAI1
- GNAI2
- GNAI3
- GNAT1
- GNAT2
- GNAT3
- GNAZ
- GNAS
- GNAL
- GNAQ
- GNA11
- GNA12
- GNA13
- GNA14
- GNA15/GNA16

G beta-gamma complexG_β
- GNB1
- GNB2
- GNB3
- GNB4
- GNB5
G_γ
- GNGT1
- GNGT2
- GNG2
- GNG3
- GNG4
- GNG5
- GNG7
- GNG8
- GNG10
- GNG11
- GNG12
- GNG13
- BSCL2

Monomeric

Cyclin

Lipid

Other protein kinase

Serine/threonine:	Casein kinase 1 2 eIF-2 kinase EIF2AK3 Glycogen synthase kinase GSK1 GSK2 GSK-3 GSK3A GSK3B IκB kinase CHUK IKK2 IKBKG Interleukin-1 receptor associated kinase IRAK1 IRAK2 IRAK3 IRAK4 Lim kinase LIMK1 LIMK2 p21-activated kinases PAK1 PAK2 PAK3 PAK4 Rho-associated protein kinase ROCK1 ROCK2 Ribosomal s6 kinase RPS6KA1
Tyrosine:	ZAP70 Focal adhesion protein-tyrosine kinase PTK2 PTK2B BTK
Serine/threonine/tyrosine	Dual-specificity kinase DYRK1A DYRK1B DYRK2 DYRK3 DYRK4
Arginine	Arginine kinase McsB

Other protein phosphatase

Serine/threonine:

Protein phosphatase 2

Tyrosine:

both:

Dual-specificity phosphatase

Apoptosis

see apoptosis signaling pathway

GTP-binding protein regulators

see GTP-binding protein regulators

Other

This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=RAB3A&oldid=1191336031" Categories: ●Genes on human chromosome 19 ●Human chromosome 19 gene stubs Hidden categories: ●Articles with short description ●Short description matches Wikidata ●All stub articles ●This page was last edited on 22 December 2023, at 22:30 (UTC). ●Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization. ●Privacy policy ●About Wikipedia ●Disclaimers ●Contact Wikipedia ●Code of Conduct ●Developers ●Statistics ●Cookie statement ●Mobile view