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Protein

Ras-related protein Rab-1B

Gene

RAB1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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 sources4 Publications9
Nucleotide bindingi33 – 40GTPCombined sources3 Publications8
Nucleotide bindingi63 – 67GTPCombined sources2 Publications5
Nucleotide bindingi121 – 124GTPCombined sources3 Publications4
Nucleotide bindingi151 – 153GTPCombined sources3 Publications3

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • 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
  • post-translational protein modification Source: Reactome
  • protein transport Source: UniProtKB-KW
  • regulation of autophagosome assembly Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  • virion assembly Source: UniProtKB

Keywordsi

Biological processAutophagy, Protein transport, Transport
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-162658 Golgi Cisternae Pericentriolar Stack Reorganization
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-8873719 RAB geranylgeranylation
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

EuPathDBiHostDB:ENSG00000174903.14
HGNCiHGNC:18370 RAB1B
MIMi612565 gene
neXtProtiNX_Q9H0U4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67Q → L: No effect on GDI1 binding. Reduces prenylation in vitro, but not in vivo. No effect on interaction with REP1/CHM; 100-fold refunction 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)serine3 Publications1
Modified residuei77O-AMP-tyrosine1 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 and MICAL2. Interacts (GTP-bound form) with MICALCL, MICAL1 and MILCAL3. 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.13 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi123619, 86 interactors
DIPiDIP-42462N
IntActiQ9H0U4, 18 interactors
MINTiQ9H0U4
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[»]
5O74X-ray2.50B/D/F/H/J/L3-174[»]
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
GeneTreeiENSGT00900000140786
HOGENOMiHOG000233968
HOVERGENiHBG009351
InParanoidiQ9H0U4
KOiK07875
OMAiGQPIQQN
OrthoDBiEOG091G0LA6
PhylomeDBiQ9H0U4
TreeFamiTF300097

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51419 RAB, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiRAB1B_HUMAN
AccessioniPrimary (citable) accession number: Q9H0U4
Secondary accession number(s): A8K7S1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 173 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health