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Q9H0U4

- RAB1B_HUMAN

UniProt

Q9H0U4 - RAB1B_HUMAN

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Protein

Ras-related protein Rab-1B

Gene

RAB1B

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTPBy similarity
Nucleotide bindingi63 – 675GTP
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB

GO - Biological processi

  1. ER to Golgi vesicle-mediated transport Source: UniProtKB
  2. positive regulation of glycoprotein metabolic process Source: UniProtKB
  3. protein transport Source: UniProtKB-KW
  4. small GTPase mediated signal transduction Source: InterPro
  5. virion assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-1B
Gene namesi
Name:RAB1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: 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

  1. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. Golgi apparatus Source: LIFEdb
  4. membrane Source: UniProtKB-KW
  5. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671Q → 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 Publications
Mutagenesisi73 – 731I → N: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio. 1 Publication
Mutagenesisi76 – 761S → A: Abolishes phosphocholination by Legionella AnkX. 1 Publication
Mutagenesisi77 – 771Y → F: Abolishes AMPylation by Legionella DrrA. 1 Publication
Mutagenesisi78 – 781Y → D: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association. 2 Publications
Mutagenesisi81 – 811A → D: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half. 1 Publication
Mutagenesisi103 – 1031L → R: No effect on prenylation. 1 Publication
Mutagenesisi110 – 1101A → D: No effect on prenylation. 1 Publication
Mutagenesisi121 – 1211N → I: Prevent formation of autophagosomes. 1 Publication
Mutagenesisi137 – 1371K → E: No effect on prenylation. 1 Publication
Mutagenesisi144 – 1441G → N: No effect on prenylation. 1 Publication

Organism-specific databases

PharmGKBiPA34108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ras-related protein Rab-1BPRO_0000121061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei76 – 761O-(2-cholinephosphoryl)serine; by Legionella AnkX3 Publications
Modified residuei77 – 771O-AMP-tyrosine; by Legionella DrrA1 Publication
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).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

MaxQBiQ9H0U4.
PaxDbiQ9H0U4.
PeptideAtlasiQ9H0U4.
PRIDEiQ9H0U4.

PTM databases

PhosphoSiteiQ9H0U4.

Expressioni

Gene expression databases

BgeeiQ9H0U4.
CleanExiHS_RAB1B.
ExpressionAtlasiQ9H0U4. baseline and differential.
GenevestigatoriQ9H0U4.

Organism-specific databases

HPAiCAB010225.

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
OCRLQ019682EBI-1045214,EBI-6148898

Protein-protein interaction databases

BioGridi123619. 29 interactions.
DIPiDIP-42462N.
IntActiQ9H0U4. 9 interactions.
MINTiMINT-1343701.
STRINGi9606.ENSP00000310226.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1611
Beta strandi17 – 204
Helixi21 – 3010
Helixi36 – 416
Beta strandi42 – 5211
Beta strandi55 – 6410
Helixi68 – 703
Helixi71 – 755
Turni76 – 805
Beta strandi82 – 898
Helixi93 – 975
Helixi99 – 10911
Beta strandi115 – 1217
Turni126 – 1283
Helixi133 – 14210
Beta strandi147 – 1493
Turni152 – 1543
Helixi158 – 17114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9H0U4.
SMRiQ9H0U4. Positions 4-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0U4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 8320Switch 2 region; required for interaction with REP1/CHMAdd
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.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9H0U4.
KOiK07875.
OMAiTMHASEY.
OrthoDBiEOG7VB2H4.
PhylomeDBiQ9H0U4.
TreeFamiTF300097.

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.

Q9H0U4 [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:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi23396834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS31613.1.
RefSeqi NP_112243.1. NM_030981.2.
UniGenei Hs.300816.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JZA X-ray 1.80 A 3-174 [» ]
3NKV X-ray 1.70 A/B 3-174 [» ]
4HLQ X-ray 3.30 B/D/F/H/J 3-174 [» ]
4I1O X-ray 2.70 A/C/E/G 3-174 [» ]
ProteinModelPortali Q9H0U4.
SMRi Q9H0U4. Positions 4-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123619. 29 interactions.
DIPi DIP-42462N.
IntActi Q9H0U4. 9 interactions.
MINTi MINT-1343701.
STRINGi 9606.ENSP00000310226.

PTM databases

PhosphoSitei Q9H0U4.

Polymorphism databases

DMDMi 23396834.

Proteomic databases

MaxQBi Q9H0U4.
PaxDbi Q9H0U4.
PeptideAtlasi Q9H0U4.
PRIDEi Q9H0U4.

Protocols and materials databases

DNASUi 81876.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311481 ; ENSP00000310226 ; ENSG00000174903 .
GeneIDi 81876.
KEGGi hsa:81876.
UCSCi uc001ohf.3. human.

Organism-specific databases

CTDi 81876.
GeneCardsi GC11P066036.
H-InvDB HIX0034908.
HIX0128663.
HGNCi HGNC:18370. RAB1B.
HPAi CAB010225.
MIMi 612565. gene.
neXtProti NX_Q9H0U4.
PharmGKBi PA34108.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118937.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi Q9H0U4.
KOi K07875.
OMAi TMHASEY.
OrthoDBi EOG7VB2H4.
PhylomeDBi Q9H0U4.
TreeFami TF300097.

Enzyme and pathway databases

Reactomei REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

ChiTaRSi RAB1B. human.
EvolutionaryTracei Q9H0U4.
GeneWikii RAB1B.
GenomeRNAii 81876.
NextBioi 72222.
PROi Q9H0U4.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0U4.
CleanExi HS_RAB1B.
ExpressionAtlasi Q9H0U4. baseline and differential.
Genevestigatori Q9H0U4.

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

« Hide 'large scale' publications
  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. 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.
    , 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. "Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites."
    Zoppino F.C., Militello R.D., Slavin I., Alvarez C., Colombo M.I.
    Traffic 11:1246-1261(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-121.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.

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: October 29, 2014
This is version 135 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

External Data

Dasty 3