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P10536

- RAB1B_RAT

UniProt

P10536 - RAB1B_RAT

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Protein

Ras-related protein Rab-1B

Gene

Rab1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Rab1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity).By similarity1 Publication

Enzyme regulationi

Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP).Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-1B
Gene namesi
Name:Rab1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1359415. MGC105830.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Preautophagosomal structure membrane By similarity; Lipid-anchor Curated; Cytoplasmic side Curated
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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → M: Abolishes GTP-binding. 1 Publication
Mutagenesisi65 – 651A → T: Reduced GTPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ras-related protein Rab-1BPRO_0000121063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei76 – 761O-(2-cholinephosphoryl)serineBy similarity
Lipidationi200 – 2001S-geranylgeranyl cysteine1 Publication
Modified residuei201 – 2011Cysteine methyl esterSequence Analysis
Lipidationi201 – 2011S-geranylgeranyl cysteine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP10536.
PRIDEiP10536.

PTM databases

PhosphoSiteiP10536.

Expressioni

Gene expression databases

GenevestigatoriP10536.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP10536. 1 interaction.
MINTiMINT-4577563.
STRINGi10116.ENSRNOP00000027486.

Structurei

3D structure databases

ProteinModelPortaliP10536.
SMRiP10536. Positions 5-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 8320Switch 2 region; required for interaction with REP1/CHMBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiP10536.
PhylomeDBiP10536.

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.

P10536 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI
60 70 80 90 100
ELDGKTIKLQ IWDTAGQERF RTVTSSYYRG AHGIIVVYDV TDQESYANVK
110 120 130 140 150
QWLQEIDRYA SENVNKLLVG NKSDLTTKKV VDNTTAKEFA DSLGVPFLET
160 170 180 190 200
SAKNATNVEQ AFMTMAAEIK KRMGPGAASG GERPNLKIDS TPVKSASGGC

C
Length:201
Mass (Da):22,163
Last modified:July 1, 1989 - v1
Checksum:i8D3EEDC2AEF4A2FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13905 mRNA. Translation: CAA32105.1.
PIRiS06147.
UniGeneiRn.155100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13905 mRNA. Translation: CAA32105.1 .
PIRi S06147.
UniGenei Rn.155100.

3D structure databases

ProteinModelPortali P10536.
SMRi P10536. Positions 5-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P10536. 1 interaction.
MINTi MINT-4577563.
STRINGi 10116.ENSRNOP00000027486.

PTM databases

PhosphoSitei P10536.

Proteomic databases

PaxDbi P10536.
PRIDEi P10536.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 1359415. MGC105830.

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi P10536.
PhylomeDBi P10536.

Gene expression databases

Genevestigatori P10536.

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. "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. Cited for: ISOPRENYLATION AT CYS-200 AND CYS-201.

Entry informationi

Entry nameiRAB1B_RAT
AccessioniPrimary (citable) accession number: P10536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3