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Protein

Ras-related protein Rab-3B

Gene

RAB3B

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

Functioni

Protein transport. Probably involved in vesicular traffic (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379GTP
Nucleotide bindingi48 – 547GTPBy similarity
Nucleotide bindingi77 – 815GTPBy similarity
Nucleotide bindingi135 – 1384GTP
Nucleotide bindingi165 – 1673GTP

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • myosin V binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-3B
Gene namesi
Name:RAB3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9778. RAB3B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • endosome Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: GO_Central
  • secretory granule membrane Source: GO_Central
  • synaptic vesicle Source: GO_Central
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34133.

Polymorphism and mutation databases

BioMutaiRAB3B.
DMDMi38258903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Ras-related protein Rab-3BPRO_0000121081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901Phosphoserine1 Publication
Lipidationi217 – 2171S-geranylgeranyl cysteineBy similarity
Modified residuei219 – 2191Cysteine methyl esterBy similarity
Lipidationi219 – 2191S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP20337.
PaxDbiP20337.
PeptideAtlasiP20337.
PRIDEiP20337.

PTM databases

PhosphoSiteiP20337.

Expressioni

Gene expression databases

BgeeiP20337.
CleanExiHS_RAB3B.
GenevestigatoriP20337.

Organism-specific databases

HPAiCAB023293.
HPA003159.

Interactioni

Subunit structurei

Interacts with RIMS1, RIMS2, RPH3A and RPH3AL.By similarity

Protein-protein interaction databases

BioGridi111803. 15 interactions.
STRINGi9606.ENSP00000360718.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 214Combined sources
Beta strandi23 – 308Combined sources
Helixi35 – 4511Combined sources
Beta strandi51 – 555Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 668Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 766Combined sources
Helixi78 – 836Combined sources
Helixi85 – 928Combined sources
Beta strandi97 – 1037Combined sources
Helixi107 – 1115Combined sources
Helixi113 – 12311Combined sources
Beta strandi129 – 1357Combined sources
Helixi140 – 1423Combined sources
Helixi147 – 15711Combined sources
Beta strandi160 – 1634Combined sources
Turni166 – 1694Combined sources
Helixi172 – 18615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DZ8X-ray1.90A18-190[»]
ProteinModelPortaliP20337.
SMRiP20337. Positions 18-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20337.

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.
InParanoidiP20337.
KOiK06108.
OMAiWFDFFEA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP20337.
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.

P20337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVTDGKTG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA
60 70 80 90 100
FVSTVGIDFK VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL
110 120 130 140 150
MYDITNEESF NAVQDWATQI KTYSWDNAQV ILVGNKCDME EERVVPTEKG
160 170 180 190 200
QLLAEQLGFD FFEASAKENI SVRQAFERLV DAICDKMSDS LDTDPSMLGS
210
SKNTRLSDTP PLLQQNCSC
Length:219
Mass (Da):24,758
Last modified:October 31, 2003 - v2
Checksum:iB73A014B4295A60D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91T → H in AAA60243 (PubMed:2501306).Curated
Sequence conflicti40 – 401F → L in AAA60243 (PubMed:2501306).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28214 mRNA. Translation: AAA60243.1.
AF498932 mRNA. Translation: AAM21080.1.
AL589663, AL445685 Genomic DNA. Translation: CAH74098.1.
AL445685, AL589663 Genomic DNA. Translation: CAI17027.1.
BC005035 mRNA. Translation: AAH05035.1.
CCDSiCCDS560.1.
PIRiD34323.
RefSeqiNP_002858.2. NM_002867.3.
UniGeneiHs.123072.

Genome annotation databases

EnsembliENST00000371655; ENSP00000360718; ENSG00000169213.
GeneIDi5865.
KEGGihsa:5865.
UCSCiuc001cth.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28214 mRNA. Translation: AAA60243.1.
AF498932 mRNA. Translation: AAM21080.1.
AL589663, AL445685 Genomic DNA. Translation: CAH74098.1.
AL445685, AL589663 Genomic DNA. Translation: CAI17027.1.
BC005035 mRNA. Translation: AAH05035.1.
CCDSiCCDS560.1.
PIRiD34323.
RefSeqiNP_002858.2. NM_002867.3.
UniGeneiHs.123072.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DZ8X-ray1.90A18-190[»]
ProteinModelPortaliP20337.
SMRiP20337. Positions 18-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111803. 15 interactions.
STRINGi9606.ENSP00000360718.

PTM databases

PhosphoSiteiP20337.

Polymorphism and mutation databases

BioMutaiRAB3B.
DMDMi38258903.

Proteomic databases

MaxQBiP20337.
PaxDbiP20337.
PeptideAtlasiP20337.
PRIDEiP20337.

Protocols and materials databases

DNASUi5865.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371655; ENSP00000360718; ENSG00000169213.
GeneIDi5865.
KEGGihsa:5865.
UCSCiuc001cth.3. human.

Organism-specific databases

CTDi5865.
GeneCardsiGC01M052373.
HGNCiHGNC:9778. RAB3B.
HPAiCAB023293.
HPA003159.
MIMi179510. gene.
neXtProtiNX_P20337.
PharmGKBiPA34133.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP20337.
KOiK06108.
OMAiWFDFFEA.
OrthoDBiEOG7JQBPC.
PhylomeDBiP20337.
TreeFamiTF313199.

Miscellaneous databases

EvolutionaryTraceiP20337.
GeneWikiiRAB3B.
GenomeRNAii5865.
NextBioi22778.
PROiP20337.
SOURCEiSearch...

Gene expression databases

BgeeiP20337.
CleanExiHS_RAB3B.
GenevestigatoriP20337.

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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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.
  5. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Crystal structure of human RAB3B GTPase bound with GDP."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-190 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiRAB3B_HUMAN
AccessioniPrimary (citable) accession number: P20337
Secondary accession number(s): Q5VUL2, Q9BSI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 31, 2003
Last modified: May 27, 2015
This is version 151 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.