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Q9H0U4 (RAB1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.7

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

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 By similarity. Ref.8

Post-translational modification

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

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.

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.

Miscellaneous

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

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OCRLQ019682EBI-1045214,EBI-6148898

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Ras-related protein Rab-1B
PRO_0000121061

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5
Modified residue761O-(2-cholinephosphoryl)serine; by Legionella AnkX
Modified residue771O-AMP-tyrosine; by Legionella DrrA
Modified residue2011Cysteine methyl ester Potential
Lipidation2001S-geranylgeranyl cysteine Ref.6 Ref.8
Lipidation2011S-geranylgeranyl cysteine Ref.6 Ref.8

Experimental info

Mutagenesis671Q → 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. Ref.6 Ref.7 Ref.17
Mutagenesis731I → N: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio. Ref.7
Mutagenesis761S → A: Abolishes phosphocholination by Legionella AnkX. Ref.11
Mutagenesis771Y → F: Abolishes AMPylation by Legionella DrrA. Ref.16
Mutagenesis781Y → D: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association. Ref.7 Ref.8
Mutagenesis811A → D: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half. Ref.7
Mutagenesis1031L → R: No effect on prenylation. Ref.7
Mutagenesis1101A → D: No effect on prenylation. Ref.7
Mutagenesis1371K → E: No effect on prenylation. Ref.7
Mutagenesis1441G → N: No effect on prenylation. Ref.7

Secondary structure

................................ 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H0U4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9812FF4DAC34B2BE

FASTA20122,171
        10         20         30         40         50         60 
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ 

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

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

       190        200 
GERPNLKIDS TPVKPAGGGC C 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a novel human cDNA homology to rat ras-related rab1B cDNA."
Zhao Y., Yu L., Xin Y.R., Zhang M., Chen S.Y., Zhao S.Y.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Synovium.
[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: Pancreas.
[5]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-21; 28-46; 59-69; 80-100 AND 138-170, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"Prenylation of a Rab1B mutant with altered GTPase activity is impaired in cell-free systems but not in intact mammalian cells."
Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A.
Biochem. J. 318:1007-1014(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-200 AND CYS-201, INTERACTION WITH GDI1, MUTAGENESIS OF GLN-67.
[7]"The putative 'switch 2' domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein."
Overmeyer J.H., Wilson A.L., Erdman R.A., Maltese W.A.
Mol. Biol. Cell 9:223-235(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHM, FUNCTION, MUTAGENESIS OF GLN-67; ILE-73; TYR-78; ALA-81; LEU-103; ALA-110; LYS-137 AND GLY-144.
[8]"Membrane targeting of a Rab GTPase that fails to associate with Rab escort protein (REP) or guanine nucleotide dissociation inhibitor (GDI)."
Overmeyer J.H., Wilson A.L., Maltese W.A.
J. Biol. Chem. 276:20379-20386(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION, INTERACTION WITH GDI1 AND CHM, MUTAGENESIS OF TYR-78.
[9]"The MICAL proteins and rab1: a possible link to the cytoskeleton?"
Fischer J., Weide T., Barnekow A.
Biochem. Biophys. Res. Commun. 328:415-423(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICAL1; MICAL2 AND MICAL3.
[10]"Legionella pneumophila SidD is a deAMPylase that modifies Rab1."
Tan Y., Luo Z.Q.
Nature 475:506-509(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA SIDD, DEAMPYLATION AT TYR-77.
[11]"Modulation of Rab GTPase function by a protein phosphocholine transferase."
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX, PHOSPHORYLATION AT SER-76, MUTAGENESIS OF SER-76.
[12]"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination."
Tan Y., Arnold R.J., Luo Z.Q.
Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA LEM3, PHOSPHORYLATION AT SER-76.
[13]"Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins."
Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.
EMBO J. 31:1774-1784(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX AND LEM3, PHOSPHORYLATION AT SER-76.
[14]"De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila."
Neunuebel M.R., Chen Y., Gaspar A.H., Backlund P.S. Jr., Yergey A., Machner M.P.
Science 333:453-456(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH L.PNEUMOPHILA SIDD, DEAMPYLATION AT TYR-77.
[15]"RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity."
Schoebel S., Oesterlin L.K., Blankenfeldt W., Goody R.S., Itzen A.
Mol. Cell 36:1060-1072(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-174 IN COMPLEX WITH L.PNEUMOPHILA DRRA GEF DOMAIN.
[16]"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b."
Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S., Itzen A.
Science 329:946-949(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-174 IN COMPLEX WITH L.PNEUMOPHILA DRRA, AMPYLATION AT TYR-77, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-77.
[17]"Catalytic mechanism of a mammalian Rab.RabGAP complex in atomic detail."
Gavriljuk K., Gazdag E.M., Itzen A., Kotting C., Goody R.S., Gerwert K.
Proc. Natl. Acad. Sci. U.S.A. 109:21348-21353(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 3-174 IN COMPLEX WITH TBC1D20, MISCELLANEOUS, MUTAGENESIS OF GLN-67.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_112243.1. NM_030981.2.
UniGeneHs.300816.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9H0U4.
SMRQ9H0U4. Positions 4-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123619. 17 interactions.
DIPDIP-42462N.
IntActQ9H0U4. 9 interactions.
MINTMINT-1343701.
STRING9606.ENSP00000310226.

PTM databases

PhosphoSiteQ9H0U4.

Polymorphism databases

DMDM23396834.

Proteomic databases

PaxDbQ9H0U4.
PeptideAtlasQ9H0U4.
PRIDEQ9H0U4.

Protocols and materials databases

DNASU81876.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311481; ENSP00000310226; ENSG00000174903.
GeneID81876.
KEGGhsa:81876.
UCSCuc001ohf.3. human.

Organism-specific databases

CTD81876.
GeneCardsGC11P066036.
H-InvDBHIX0034908.
HIX0128663.
HGNCHGNC:18370. RAB1B.
HPACAB010225.
MIM612565. gene.
neXtProtNX_Q9H0U4.
PharmGKBPA34108.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9H0U4.
KOK07875.
OMAVESYIST.
OrthoDBEOG7VB2H4.
PhylomeDBQ9H0U4.
TreeFamTF300097.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9H0U4.
BgeeQ9H0U4.
CleanExHS_RAB1B.
GenevestigatorQ9H0U4.

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...

Other

ChiTaRSRAB1B. human.
EvolutionaryTraceQ9H0U4.
GeneWikiRAB1B.
GenomeRNAi81876.
NextBio72222.
PROQ9H0U4.
SOURCESearch...

Entry information

Entry nameRAB1B_HUMAN
AccessionPrimary (citable) accession number: Q9H0U4
Secondary accession number(s): A8K7S1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM