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P10536 (RAB1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-1B
Gene names
Name:Rab1b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Ref.3

Subunit structure

Interacts with MICAL1, MICAL2 and MICAL3. Interacts with GDI1; the interaction requires the GDP-bound state. Interacts with CHM/REP1; the interaction requires the GDP-bound form and is necessary for prenylation by GGTase II By similarity.

Subcellular location

Membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note: Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm. Ref.3

Post-translational modification

Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1) By similarity.

Miscellaneous

Rab-1B binds GTP and GDP and possesses intrinsic GTPase activity.

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Ras-related protein Rab-1B
PRO_0000121063

Regions

Nucleotide binding15 – 228GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding121 – 1244GTP By similarity
Region64 – 8320Switch 2 region; required for interaction with REP1/CHM By similarity
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue761O-(2-cholinephosphoryl)serine By similarity
Modified residue2011Cysteine methyl ester Potential
Lipidation2001S-geranylgeranyl cysteine Ref.4
Lipidation2011S-geranylgeranyl cysteine Ref.4

Experimental info

Mutagenesis211K → M: Abolishes GTP-binding. Ref.2
Mutagenesis651A → T: Reduced GTPase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P10536 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8D3EEDC2AEF4A2FE

FASTA20122,163
        10         20         30         40         50         60 
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ 

        70         80         90        100        110        120 
IWDTAGQERF RTVTSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG 

       130        140        150        160        170        180 
NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG 

       190        200 
GERPNLKIDS TPVKSASGGC C 

« Hide

References

[1]"Nucleotide sequence of a rat cDNA: rab1B, encoding a rab1-YPT related protein."
Zahraoui A., Touchot N., Chardin P., Tavitian A.
Nucleic Acids Res. 17:1770-1770(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Biochemical properties of the YPT-related rab1B protein. Comparison with rab1A."
Touchot N., Zahraoui A., Vielh E., Tavitian A.
FEBS Lett. 256:79-84(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-21 AND ALA-65.
[3]"Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments."
Plutner H., Cox A.D., Pind S., Khosravi-Far R., Bourne J.R., Schwaninger R., Der C.J., Balch W.E.
J. Cell Biol. 115:31-43(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[4]"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-200 AND CYS-201.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13905 mRNA. Translation: CAA32105.1.
PIRS06147.
UniGeneRn.155100.

3D structure databases

ProteinModelPortalP10536.
SMRP10536. Positions 5-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP10536. 1 interaction.
MINTMINT-4577563.
STRING10116.ENSRNOP00000027486.

PTM databases

PhosphoSiteP10536.

Proteomic databases

PaxDbP10536.
PRIDEP10536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD1359415. MGC105830.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP10536.
PhylomeDBP10536.

Gene expression databases

GenevestigatorP10536.

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...

Entry information

Entry nameRAB1B_RAT
AccessionPrimary (citable) accession number: P10536
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families