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P20336 (RAB3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-3A
Gene names
Name:RAB3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Tissue specificity

Specifically expressed in brain.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processExocytosis
Protein transport
Transport
   Cellular componentCell membrane
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from mutant phenotype PubMed 10859313. Source: GOC

axonogenesis

Inferred from electronic annotation. Source: Ensembl

glutamate secretion

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

maintenance of presynaptic active zone structure

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from electronic annotation. Source: Ensembl

neurotransmitter secretion

Traceable author statement. Source: Reactome

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of synaptic vesicle fusion to presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

respiratory system process

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

sensory perception of touch

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

synaptic transmission

Traceable author statement. Source: Reactome

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle maturation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

clathrin-sculpted acetylcholine transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted glutamate transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted monoamine transport vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Traceable author statement PubMed 9194562. Source: ProtInc

   Molecular_functionATPase activator activity

Inferred from electronic annotation. Source: Ensembl

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from mutant phenotype PubMed 10859313. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Ras-related protein Rab-3A
PRO_0000121076

Regions

Nucleotide binding29 – 368GTP By similarity
Nucleotide binding48 – 547GTP By similarity
Nucleotide binding77 – 815GTP By similarity
Nucleotide binding135 – 1384GTP By similarity
Motif51 – 599Effector region By similarity

Amino acid modifications

Modified residue2201Cysteine methyl ester Ref.9
Lipidation2181S-geranylgeranyl cysteine Ref.9 Ref.10
Lipidation2201S-geranylgeranyl cysteine Ref.9 Ref.10

Experimental info

Sequence conflict701R → K in AAF67748. Ref.2
Sequence conflict1801V → E in AAF67748. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P20336 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 08B59F8C9BD2EB40

FASTA22024,984
        10         20         30         40         50         60 
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK 

        70         80         90        100        110        120 
VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI 

       130        140        150        160        170        180 
KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV 

       190        200        210        220 
DVICEKMSES LDTADPAVTG AKQGPQLSDQ QVPPHQDCAC 

« Hide

References

« Hide 'large scale' references
[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(1989) [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(1999) [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 (APR-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 (APR-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. expand/collapse author list , 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(2004) [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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[9]"Isoprenoid modification of rab proteins terminating in CC or CXC motifs."
Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., Balch W.E., Buss J.E., Der C.J.
Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991) [PubMed] [Europe PMC] [Abstract]
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(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-218 AND CYS-220, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28210 mRNA. Translation: AAA60242.1.
AF157809 expand/collapse EMBL AC list , 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.
PIRC34323.
RefSeqNP_002857.1. NM_002866.4.
UniGeneHs.27744.

3D structure databases

ProteinModelPortalP20336.
SMRP20336. Positions 18-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111802. 22 interactions.
IntActP20336. 4 interactions.
MINTMINT-3009239.
STRING9606.ENSP00000222256.

PTM databases

PhosphoSiteP20336.

Polymorphism databases

DMDM131801.

Proteomic databases

PaxDbP20336.
PRIDEP20336.

Protocols and materials databases

DNASU5864.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222256; ENSP00000222256; ENSG00000105649.
GeneID5864.
KEGGhsa:5864.
UCSCuc002nie.2. human.

Organism-specific databases

CTD5864.
GeneCardsGC19M018307.
HGNCHGNC:9777. RAB3A.
HPACAB009949.
HPA003160.
MIM179490. gene.
neXtProtNX_P20336.
PharmGKBPA34132.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP20336.
KOK07882.
OMAQLTEQPA.
OrthoDBEOG7JQBPC.
PhylomeDBP20336.
TreeFamTF313199.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP20336.
BgeeP20336.
CleanExHS_RAB3A.
GenevestigatorP20336.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB3A.
GenomeRNAi5864.
NextBio22774.
PROP20336.
SOURCESearch...

Entry information

Entry nameRAB3A_HUMAN
AccessionPrimary (citable) accession number: P20336
Secondary accession number(s): A8K0J4, Q9NYE1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM