Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20337

- RAB3B_HUMAN

UniProt

P20337 - RAB3B_HUMAN

Protein

Ras-related protein Rab-3B

Gene

RAB3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (31 Oct 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. GDP binding Source: UniProt
    2. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. antigen processing and presentation Source: UniProt
    2. peptidyl-cysteine methylation Source: Ensembl
    3. positive regulation of dopamine uptake involved in synaptic transmission Source: UniProt
    4. protein transport Source: UniProtKB-KW
    5. regulation of exocytosis Source: Ensembl
    6. regulation of vesicle size Source: UniProt
    7. small GTPase mediated signal transduction Source: InterPro

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9778. RAB3B.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProt
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. perinuclear region of cytoplasm Source: UniProt
    5. plasma membrane Source: UniProtKB-SubCell
    6. secretory granule Source: Ensembl
    7. synaptic vesicle Source: Ensembl
    8. vesicle Source: UniProt

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34133.

    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. 7 interactions.
    STRINGi9606.ENSP00000360718.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MASVTDGKTG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA    50
    FVSTVGIDFK VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL 100
    MYDITNEESF NAVQDWATQI KTYSWDNAQV ILVGNKCDME EERVVPTEKG 150
    QLLAEQLGFD FFEASAKENI SVRQAFERLV DAICDKMSDS LDTDPSMLGS 200
    SKNTRLSDTP PLLQQNCSC 219
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi38258903.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS560.1.
    PIRi D34323.
    RefSeqi NP_002858.2. NM_002867.3.
    UniGenei Hs.123072.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DZ8 X-ray 1.90 A 18-190 [» ]
    ProteinModelPortali P20337.
    SMRi P20337. Positions 18-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111803. 7 interactions.
    STRINGi 9606.ENSP00000360718.

    PTM databases

    PhosphoSitei P20337.

    Polymorphism databases

    DMDMi 38258903.

    Proteomic databases

    MaxQBi P20337.
    PaxDbi P20337.
    PeptideAtlasi P20337.
    PRIDEi P20337.

    Protocols and materials databases

    DNASUi 5865.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371655 ; ENSP00000360718 ; ENSG00000169213 .
    GeneIDi 5865.
    KEGGi hsa:5865.
    UCSCi uc001cth.3. human.

    Organism-specific databases

    CTDi 5865.
    GeneCardsi GC01M052373.
    HGNCi HGNC:9778. RAB3B.
    HPAi CAB023293.
    HPA003159.
    MIMi 179510. gene.
    neXtProti NX_P20337.
    PharmGKBi PA34133.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P20337.
    KOi K06108.
    OMAi WFDFFEA.
    OrthoDBi EOG7JQBPC.
    PhylomeDBi P20337.
    TreeFami TF313199.

    Miscellaneous databases

    EvolutionaryTracei P20337.
    GeneWikii RAB3B.
    GenomeRNAii 5865.
    NextBioi 22778.
    PROi P20337.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20337.
    CleanExi HS_RAB3B.
    Genevestigatori P20337.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 144 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