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Protein

Ras-related protein Rab-3A

Gene

RAB3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368GTPBy similarity
Nucleotide bindingi48 – 547GTPBy similarity
Nucleotide bindingi77 – 815GTPBy similarity
Nucleotide bindingi135 – 1384GTPBy similarity

GO - Molecular functioni

  1. ATPase activator activity Source: Ensembl
  2. GDP binding Source: GO_Central
  3. GTPase activity Source: UniProtKB
  4. GTP binding Source: UniProtKB-KW
  5. myosin V binding Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. constitutive secretory pathway Source: ParkinsonsUK-UCL
  3. glutamate secretion Source: Reactome
  4. intracellular protein transport Source: GO_Central
  5. lung development Source: Ensembl
  6. maintenance of presynaptic active zone structure Source: Ensembl
  7. metabolic process Source: GOC
  8. mitochondrion organization Source: Ensembl
  9. neuromuscular synaptic transmission Source: Ensembl
  10. neurotransmitter secretion Source: Reactome
  11. positive regulation of exocytosis Source: ParkinsonsUK-UCL
  12. positive regulation of regulated secretory pathway Source: UniProtKB
  13. post-embryonic development Source: Ensembl
  14. protein secretion Source: GO_Central
  15. Rab protein signal transduction Source: GO_Central
  16. regulation of short-term neuronal synaptic plasticity Source: ParkinsonsUK-UCL
  17. regulation of synaptic vesicle fusion to presynaptic membrane Source: ParkinsonsUK-UCL
  18. respiratory system process Source: Ensembl
  19. response to electrical stimulus Source: Ensembl
  20. sensory perception of touch Source: Ensembl
  21. synaptic transmission Source: Reactome
  22. synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  23. synaptic vesicle maturation Source: Ensembl
  24. synaptic vesicle recycling Source: ParkinsonsUK-UCL
  25. vesicle docking involved in exocytosis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_23947. GABA synthesis, release, reuptake and degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-3A
Gene namesi
Name:RAB3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9777. RAB3A.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. axon Source: ParkinsonsUK-UCL
  3. clathrin-sculpted acetylcholine transport vesicle membrane Source: Reactome
  4. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  5. clathrin-sculpted glutamate transport vesicle membrane Source: Reactome
  6. clathrin-sculpted monoamine transport vesicle membrane Source: Reactome
  7. cytosol Source: Ensembl
  8. endosome Source: GO_Central
  9. plasma membrane Source: Reactome
  10. protein complex Source: Ensembl
  11. secretory granule membrane Source: GO_Central
  12. synaptic vesicle Source: ParkinsonsUK-UCL
  13. terminal bouton Source: ParkinsonsUK-UCL
  14. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Ras-related protein Rab-3APRO_0000121076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi218 – 2181S-geranylgeranyl cysteine2 Publications
Modified residuei220 – 2201Cysteine methyl ester1 Publication
Lipidationi220 – 2201S-geranylgeranyl cysteine2 Publications

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP20336.
PaxDbiP20336.
PRIDEiP20336.

PTM databases

PhosphoSiteiP20336.

Expressioni

Tissue specificityi

Specifically expressed in brain.

Gene expression databases

BgeeiP20336.
CleanExiHS_RAB3A.
ExpressionAtlasiP20336. baseline and differential.
GenevestigatoriP20336.

Organism-specific databases

HPAiCAB009949.
HPA003160.

Interactioni

Subunit structurei

Heterodimer with RIMS2. Part of a ternary complex involving PCLO and EPAC2. Interacts with RPH3A and RPH3AL. Interacts with the exocyst complex through SEC15. Binds SYTL4 and RIMS1. Interacts with RAB3IP. Interacts with SGSM1 and SGSM3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi111802. 37 interactions.
IntActiP20336. 4 interactions.
MINTiMINT-3009239.
STRINGi9606.ENSP00000222256.

Structurei

3D structure databases

ProteinModelPortaliP20336.
SMRiP20336. Positions 18-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 599Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP20336.
KOiK07882.
OMAiQLTEQPA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP20336.
TreeFamiTF313199.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA
60 70 80 90 100
FVSTVGIDFK VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL
110 120 130 140 150
MYDITNEESF NAVQDWSTQI KTYSWDNAQV LLVGNKCDME DERVVSSERG
160 170 180 190 200
RQLADHLGFE FFEASAKDNI NVKQTFERLV DVICEKMSES LDTADPAVTG
210 220
AKQGPQLSDQ QVPPHQDCAC
Length:220
Mass (Da):24,984
Last modified:January 31, 1991 - v1
Checksum:i08B59F8C9BD2EB40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701R → K in AAF67748 (PubMed:10574328).Curated
Sequence conflicti180 – 1801V → E in AAF67748 (PubMed:10574328).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28210 mRNA. Translation: AAA60242.1.
AF157809
, AF157806, AF157807, AF157808 Genomic DNA. Translation: AAD46811.1.
AF254795 mRNA. Translation: AAF67748.1.
AF498931 mRNA. Translation: AAM21079.1.
AK289559 mRNA. Translation: BAF82248.1.
AC068499 Genomic DNA. Translation: AAF67385.1.
CH471106 Genomic DNA. Translation: EAW84672.1.
BC011782 mRNA. Translation: AAH11782.1.
CCDSiCCDS12372.1.
PIRiC34323.
RefSeqiNP_002857.1. NM_002866.4.
UniGeneiHs.27744.

Genome annotation databases

EnsembliENST00000222256; ENSP00000222256; ENSG00000105649.
GeneIDi5864.
KEGGihsa:5864.
UCSCiuc002nie.2. human.

Polymorphism databases

DMDMi131801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28210 mRNA. Translation: AAA60242.1.
AF157809
, AF157806, AF157807, AF157808 Genomic DNA. Translation: AAD46811.1.
AF254795 mRNA. Translation: AAF67748.1.
AF498931 mRNA. Translation: AAM21079.1.
AK289559 mRNA. Translation: BAF82248.1.
AC068499 Genomic DNA. Translation: AAF67385.1.
CH471106 Genomic DNA. Translation: EAW84672.1.
BC011782 mRNA. Translation: AAH11782.1.
CCDSiCCDS12372.1.
PIRiC34323.
RefSeqiNP_002857.1. NM_002866.4.
UniGeneiHs.27744.

3D structure databases

ProteinModelPortaliP20336.
SMRiP20336. Positions 18-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111802. 37 interactions.
IntActiP20336. 4 interactions.
MINTiMINT-3009239.
STRINGi9606.ENSP00000222256.

PTM databases

PhosphoSiteiP20336.

Polymorphism databases

DMDMi131801.

Proteomic databases

MaxQBiP20336.
PaxDbiP20336.
PRIDEiP20336.

Protocols and materials databases

DNASUi5864.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222256; ENSP00000222256; ENSG00000105649.
GeneIDi5864.
KEGGihsa:5864.
UCSCiuc002nie.2. human.

Organism-specific databases

CTDi5864.
GeneCardsiGC19M018307.
HGNCiHGNC:9777. RAB3A.
HPAiCAB009949.
HPA003160.
MIMi179490. gene.
neXtProtiNX_P20336.
PharmGKBiPA34132.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP20336.
KOiK07882.
OMAiQLTEQPA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP20336.
TreeFamiTF313199.

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_23947. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

GeneWikiiRAB3A.
GenomeRNAii5864.
NextBioi22774.
PROiP20336.
SOURCEiSearch...

Gene expression databases

BgeeiP20336.
CleanExiHS_RAB3A.
ExpressionAtlasiP20336. baseline and differential.
GenevestigatoriP20336.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion."
    Zahraoui A., Touchot N., Chardin P., Tavitian A.
    J. Biol. Chem. 264:12394-12401(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND."
    Sullivan M., Olsen A.S., Houslay M.D.
    Cell. Signal. 11:735-742(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Functional cloning and characterization of human fetal brain cDNAs."
    Liu Y., Li J., He J.J.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  9. Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220, METHYLATION AT CYS-220.
  10. "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."
    Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.
    Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRAB3A_HUMAN
AccessioniPrimary (citable) accession number: P20336
Secondary accession number(s): A8K0J4, Q9NYE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1991
Last sequence update: January 31, 1991
Last modified: March 31, 2015
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.