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Protein

Ras-related protein Rab-1B

Gene

RAB1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

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)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 23GTPCombined sources3 Publications9
Nucleotide bindingi33 – 40GTPCombined sources2 Publications8
Nucleotide bindingi63 – 67GTPCombined sources1 Publication5
Nucleotide bindingi121 – 124GTPCombined sources2 Publications4
Nucleotide bindingi151 – 153GTPCombined sources2 Publications3

GO - Molecular functioni

  • GTP binding Source: UniProtKB

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • COPII vesicle coating Source: Reactome
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • positive regulation of glycoprotein metabolic process Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of autophagosome assembly Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  • small GTPase mediated signal transduction Source: InterPro
  • virion assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174903-MONOMER.
ReactomeiR-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-8876198. RAB GEFs exchange GTP for GDP on RABs.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-1B
Gene namesi
Name:RAB1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:18370. RAB1B.

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67Q → L: No effect on GDI1 binding. Reduces, in vitro, but not, in vivo prenylation. No effect on interaction with REP1/CHM; 100-fold refuction in intrinsic GTPase activity. 3 Publications1
Mutagenesisi73I → N: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio. 1 Publication1
Mutagenesisi76S → A: Abolishes phosphocholination by Legionella AnkX. 1 Publication1
Mutagenesisi77Y → F: Abolishes AMPylation by Legionella DrrA. 1 Publication1
Mutagenesisi78Y → D: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association. 2 Publications1
Mutagenesisi81A → D: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half. 1 Publication1
Mutagenesisi103L → R: No effect on prenylation. 1 Publication1
Mutagenesisi110A → D: No effect on prenylation. 1 Publication1
Mutagenesisi121N → I: Prevent formation of autophagosomes. 1 Publication1
Mutagenesisi137K → E: No effect on prenylation. 1 Publication1
Mutagenesisi144G → N: No effect on prenylation. 1 Publication1

Organism-specific databases

DisGeNETi81876.
OpenTargetsiENSG00000174903.
PharmGKBiPA34108.

Polymorphism and mutation databases

BioMutaiRAB1B.
DMDMi23396834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001210611 – 201Ras-related protein Rab-1BAdd BLAST201

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei76O-(2-cholinephosphoryl)serine; by Legionella AnkX3 Publications1
Modified residuei77O-AMP-tyrosine; by Legionella DrrA1 Publication1
Lipidationi200S-geranylgeranyl cysteine1 Publication1
Modified residuei201Cysteine methyl esterSequence analysis1
Lipidationi201S-geranylgeranyl cysteine1 Publication1

Post-translational modificationi

Prenylated; by GGTase II, only after interaction of the substrate with Rab escort protein 1 (REP1).2 Publications
AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB1B constitutively active. It is later de-AMPylated by L.pneumophila SidD, releasing RAB1B from bacterial phagosomes.1 Publication
Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB.

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ9H0U4.
MaxQBiQ9H0U4.
PaxDbiQ9H0U4.
PeptideAtlasiQ9H0U4.
PRIDEiQ9H0U4.
TopDownProteomicsiQ9H0U4.

PTM databases

iPTMnetiQ9H0U4.
PhosphoSitePlusiQ9H0U4.
SwissPalmiQ9H0U4.

Expressioni

Gene expression databases

BgeeiENSG00000174903.
CleanExiHS_RAB1B.
ExpressionAtlasiQ9H0U4. baseline and differential.
GenevisibleiQ9H0U4. HS.

Organism-specific databases

HPAiCAB010225.
HPA056141.

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.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-1045214,EBI-5323863
OCRLQ019682EBI-1045214,EBI-6148898
PITPNC1Q9UKF7-14EBI-1045214,EBI-11687286

Protein-protein interaction databases

BioGridi123619. 73 interactors.
DIPiDIP-42462N.
IntActiQ9H0U4. 12 interactors.
MINTiMINT-1343701.
STRINGi9606.ENSP00000310226.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 16Combined sources11
Beta strandi17 – 20Combined sources4
Helixi21 – 30Combined sources10
Helixi36 – 41Combined sources6
Beta strandi42 – 52Combined sources11
Beta strandi55 – 64Combined sources10
Helixi68 – 70Combined sources3
Helixi71 – 75Combined sources5
Turni76 – 80Combined sources5
Beta strandi82 – 89Combined sources8
Helixi93 – 97Combined sources5
Helixi99 – 109Combined sources11
Beta strandi115 – 121Combined sources7
Turni126 – 128Combined sources3
Helixi133 – 142Combined sources10
Beta strandi147 – 149Combined sources3
Turni152 – 154Combined sources3
Helixi158 – 171Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JZAX-ray1.80A3-174[»]
3NKVX-ray1.70A/B3-174[»]
4HLQX-ray3.30B/D/F/H/J3-174[»]
4I1OX-ray2.70A/C/E/G3-174[»]
5SZHX-ray2.30B1-201[»]
5SZKX-ray2.80B2-201[»]
ProteinModelPortaliQ9H0U4.
SMRiQ9H0U4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0U4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 83Switch 2 region; required for interaction with REP1/CHMAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi37 – 45Effector regionBy similarity9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
GeneTreeiENSGT00860000133677.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9H0U4.
KOiK07875.
OMAiDHDSFEN.
OrthoDBiEOG091G0LA6.
PhylomeDBiQ9H0U4.
TreeFamiTF300097.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H0U4-1 [UniParc]FASTAAdd to basket

« Hide

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

C
Length:201
Mass (Da):22,171
Last modified:March 1, 2001 - v1
Checksum:i9812FF4DAC34B2BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092437 mRNA. Translation: AAP97212.1.
AL136635 mRNA. Translation: CAB66570.1.
AK292086 mRNA. Translation: BAF84775.1.
AK315333 mRNA. Translation: BAG37733.1.
BC071169 mRNA. Translation: AAH71169.1.
CCDSiCCDS31613.1.
RefSeqiNP_112243.1. NM_030981.2.
UniGeneiHs.300816.

Genome annotation databases

EnsembliENST00000311481; ENSP00000310226; ENSG00000174903.
GeneIDi81876.
KEGGihsa:81876.
UCSCiuc001ohf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092437 mRNA. Translation: AAP97212.1.
AL136635 mRNA. Translation: CAB66570.1.
AK292086 mRNA. Translation: BAF84775.1.
AK315333 mRNA. Translation: BAG37733.1.
BC071169 mRNA. Translation: AAH71169.1.
CCDSiCCDS31613.1.
RefSeqiNP_112243.1. NM_030981.2.
UniGeneiHs.300816.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JZAX-ray1.80A3-174[»]
3NKVX-ray1.70A/B3-174[»]
4HLQX-ray3.30B/D/F/H/J3-174[»]
4I1OX-ray2.70A/C/E/G3-174[»]
5SZHX-ray2.30B1-201[»]
5SZKX-ray2.80B2-201[»]
ProteinModelPortaliQ9H0U4.
SMRiQ9H0U4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123619. 73 interactors.
DIPiDIP-42462N.
IntActiQ9H0U4. 12 interactors.
MINTiMINT-1343701.
STRINGi9606.ENSP00000310226.

PTM databases

iPTMnetiQ9H0U4.
PhosphoSitePlusiQ9H0U4.
SwissPalmiQ9H0U4.

Polymorphism and mutation databases

BioMutaiRAB1B.
DMDMi23396834.

Proteomic databases

EPDiQ9H0U4.
MaxQBiQ9H0U4.
PaxDbiQ9H0U4.
PeptideAtlasiQ9H0U4.
PRIDEiQ9H0U4.
TopDownProteomicsiQ9H0U4.

Protocols and materials databases

DNASUi81876.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311481; ENSP00000310226; ENSG00000174903.
GeneIDi81876.
KEGGihsa:81876.
UCSCiuc001ohf.4. human.

Organism-specific databases

CTDi81876.
DisGeNETi81876.
GeneCardsiRAB1B.
H-InvDBHIX0034908.
HIX0128663.
HGNCiHGNC:18370. RAB1B.
HPAiCAB010225.
HPA056141.
MIMi612565. gene.
neXtProtiNX_Q9H0U4.
OpenTargetsiENSG00000174903.
PharmGKBiPA34108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
GeneTreeiENSGT00860000133677.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9H0U4.
KOiK07875.
OMAiDHDSFEN.
OrthoDBiEOG091G0LA6.
PhylomeDBiQ9H0U4.
TreeFamiTF300097.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174903-MONOMER.
ReactomeiR-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-8876198. RAB GEFs exchange GTP for GDP on RABs.

Miscellaneous databases

ChiTaRSiRAB1B. human.
EvolutionaryTraceiQ9H0U4.
GeneWikiiRAB1B.
GenomeRNAii81876.
PROiQ9H0U4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174903.
CleanExiHS_RAB1B.
ExpressionAtlasiQ9H0U4. baseline and differential.
GenevisibleiQ9H0U4. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRAB1B_HUMAN
AccessioniPrimary (citable) accession number: Q9H0U4
Secondary accession number(s): A8K7S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 159 of the entry and version 1 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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 one 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.