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Q9H0U4

- RAB1B_HUMAN

UniProt

Q9H0U4 - RAB1B_HUMAN

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
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments.1 Publication

    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
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    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

    Membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Cytoplasm 1 Publication
    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. extracellular vesicular exosome Source: UniProt
    2. Golgi apparatus Source: LIFEdb
    3. membrane Source: UniProtKB-SubCell
    4. mitochondrion Source: Ensembl

    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
    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 cysteine2 Publications
    Modified residuei201 – 2011Cysteine methyl esterSequence Analysis
    Lipidationi201 – 2011S-geranylgeranyl cysteine2 Publications

    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

    ArrayExpressiQ9H0U4.
    BgeeiQ9H0U4.
    CleanExiHS_RAB1B.
    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. 18 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.
    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.

    Q9H0U4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI    50
    ELDGKTIKLQ IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK 100
    QWLQEIDRYA SENVNKLLVG NKSDLTTKKV VDNTTAKEFA DSLGIPFLET 150
    SAKNATNVEQ AFMTMAAEIK KRMGPGAASG GERPNLKIDS TPVKPAGGGC 200
    C 201
    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. 18 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.
    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

    ArrayExpressi Q9H0U4.
    Bgeei Q9H0U4.
    CleanExi HS_RAB1B.
    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

    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. "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.

    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 1, 2014
    This is version 134 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