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P51159

- RB27A_HUMAN

UniProt

P51159 - RB27A_HUMAN

Protein

Ras-related protein Rab-27A

Gene

RAB27A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 249GTPBy similarity
    Nucleotide bindingi74 – 785GTPBy similarity
    Nucleotide bindingi133 – 1364GTPBy similarity
    Nucleotide bindingi163 – 1653GTPBy similarity

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation Source: UniProt
    2. blood coagulation Source: Ensembl
    3. cellular protein metabolic process Source: Reactome
    4. cytotoxic T cell degranulation Source: Ensembl
    5. exocytosis Source: UniProtKB
    6. melanocyte differentiation Source: Ensembl
    7. melanosome transport Source: Ensembl
    8. multivesicular body sorting pathway Source: UniProtKB
    9. natural killer cell degranulation Source: Ensembl
    10. positive regulation of exocytosis Source: UniProtKB
    11. protein targeting Source: Ensembl
    12. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Exocytosis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15550. Insulin processing.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-27A
    Short name:
    Rab-27
    Alternative name(s):
    GTP-binding protein Ram
    Gene namesi
    Name:RAB27A
    Synonyms:RAB27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9766. RAB27A.

    Subcellular locationi

    Membrane; Lipid-anchor. Melanosome. Late endosome. Lysosome
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles.

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. dendrite Source: UniProtKB
    3. exocytic vesicle Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi apparatus Source: Ensembl
    6. late endosome Source: UniProtKB
    7. lysosome Source: UniProtKB
    8. melanosome Source: UniProtKB
    9. multivesicular body membrane Source: UniProtKB
    10. photoreceptor outer segment Source: Ensembl
    11. secretory granule membrane Source: Ensembl

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Griscelli syndrome 2 (GS2) [MIM:607624]: Rare autosomal recessive disorder that results in pigmentary dilution of the skin and hair, the presence of large clumps of pigment in hair shafts, and an accumulation of melanosomes in melanocytes. GS2 patients also develop an uncontrolled T-lymphocyte and macrophage activation syndrome, known as hemophagocytic syndrome, leading to death in the absence of bone marrow transplantation. Neurological impairment is present in some patients, likely as a result of hemophagocytic syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731W → G in GS2; does not affect GTP binding; cannot interact with MLPH; significant reduction in interaction with UNC13D; abolishes localization to lysosomes. 1 Publication
    Corresponds to variant rs28938176 [ dbSNP | Ensembl ].
    VAR_010654
    Natural varianti130 – 1301L → P in GS2; strongly affects GTP binding; cannot interact with MLPH. 1 Publication
    VAR_011334
    Natural varianti152 – 1521A → P in GS2; may affect GTP binding; interferes with melanosome transport. 1 Publication
    VAR_011335

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231T → N: Abolishes interaction with UNC13D and localization to lysosomes. 1 Publication
    Mutagenesisi70 – 701L → P: Abolishes interaction with SYTL2. 1 Publication
    Mutagenesisi76 – 761A → V: Abolishes interaction with SYTL2. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi607624. phenotype.
    Orphaneti79477. Griscelli disease type 2.
    PharmGKBiPA34117.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 221220Ras-related protein Rab-27APRO_0000121221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Disulfide bondi123 ↔ 188By similarity
    Lipidationi219 – 2191S-geranylgeranyl cysteineBy similarity
    Modified residuei221 – 2211Cysteine methyl esterBy similarity
    Lipidationi221 – 2211S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP51159.
    PaxDbiP51159.
    PeptideAtlasiP51159.
    PRIDEiP51159.

    PTM databases

    PhosphoSiteiP51159.

    Expressioni

    Tissue specificityi

    Found in all the examined tissues except in brain. Low expression was found in thymus, kidney, muscle and placenta. Detected in melanocytes, and in most tumor cell lines examined. Expressed in cytotoxic T-lymphocytes (CTL) and mast cells.1 Publication

    Gene expression databases

    ArrayExpressiP51159.
    BgeeiP51159.
    CleanExiHS_RAB27A.
    GenevestigatoriP51159.

    Organism-specific databases

    HPAiCAB034046.
    HPA001333.

    Interactioni

    Subunit structurei

    Binds SYTL1, SLAC2B, MYRIP, SYTL3, SYTL4 and SYTL5. Interacts with RPH3A and RPH3A By similarity. Binds MLPH and SYTL2. Interacts with UNC13D.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi111811. 24 interactions.
    IntActiP51159. 11 interactions.
    MINTiMINT-1377654.
    STRINGi9606.ENSP00000337761.

    Structurei

    3D structure databases

    ProteinModelPortaliP51159.
    SMRiP51159. Positions 4-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi38 – 469Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiP51159.
    KOiK07885.
    OMAiDQRAVKE.
    OrthoDBiEOG7FFMSC.
    PhylomeDBiP51159.
    TreeFamiTF312895.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P51159-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR    50
    VVYRASGPDG ATGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD 100
    LTNEQSFLNV RNWISQLQMH AYCENPDIVL CGNKSDLEDQ RVVKEEEAIA 150
    LAEKYGIPYF ETSAANGTNI SQAIEMLLDL IMKRMERCVD KSWIPEGVVR 200
    SNGHASTDQL SEEKEKGACG C 221
    Length:221
    Mass (Da):24,868
    Last modified:October 17, 2006 - v3
    Checksum:i4A6A0C8C5CC41A20
    GO
    Isoform Short (identifier: P51159-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-153: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:213
    Mass (Da):24,041
    Checksum:i9A2B95ECB4BC2BFE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481E → P in AAC51195. (PubMed:9066979)Curated
    Sequence conflicti48 – 481E → P in AAD43049. (PubMed:10931946)Curated
    Sequence conflicti61 – 622AT → PV in AAC51195. (PubMed:9066979)Curated
    Sequence conflicti61 – 622AT → PV in AAD43049. (PubMed:10931946)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621T → S.
    Corresponds to variant rs1050930 [ dbSNP | Ensembl ].
    VAR_028206
    Natural varianti73 – 731W → G in GS2; does not affect GTP binding; cannot interact with MLPH; significant reduction in interaction with UNC13D; abolishes localization to lysosomes. 1 Publication
    Corresponds to variant rs28938176 [ dbSNP | Ensembl ].
    VAR_010654
    Natural varianti84 – 841L → F.
    Corresponds to variant rs4340274 [ dbSNP | Ensembl ].
    VAR_028207
    Natural varianti85 – 851T → P.
    Corresponds to variant rs719705 [ dbSNP | Ensembl ].
    VAR_028208
    Natural varianti130 – 1301L → P in GS2; strongly affects GTP binding; cannot interact with MLPH. 1 Publication
    VAR_011334
    Natural varianti152 – 1521A → P in GS2; may affect GTP binding; interferes with melanosome transport. 1 Publication
    VAR_011335

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei146 – 1538Missing in isoform Short. 1 PublicationVSP_005529

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38654 mRNA. Translation: AAC50271.2.
    U57094 mRNA. Translation: AAC51195.1.
    AF154840
    , AF154836, AF154837, AF154838, AF154839 Genomic DNA. Translation: AAD47629.1.
    AF125393 mRNA. Translation: AAD43049.1.
    AF443871 Genomic DNA. Translation: AAL39097.1.
    AF498953 mRNA. Translation: AAM21101.1.
    CR536496 mRNA. Translation: CAG38735.1.
    CR541693 mRNA. Translation: CAG46494.1.
    BC107680 mRNA. Translation: AAI07681.1.
    CCDSiCCDS10153.1. [P51159-1]
    PIRiI39198.
    RefSeqiNP_004571.2. NM_004580.4. [P51159-1]
    NP_899057.1. NM_183234.2. [P51159-1]
    NP_899058.1. NM_183235.2. [P51159-1]
    NP_899059.1. NM_183236.2. [P51159-1]
    XP_005254633.1. XM_005254576.2. [P51159-1]
    UniGeneiHs.654978.
    Hs.735555.

    Genome annotation databases

    EnsembliENST00000336787; ENSP00000337761; ENSG00000069974. [P51159-1]
    ENST00000396307; ENSP00000379601; ENSG00000069974. [P51159-1]
    ENST00000564609; ENSP00000455012; ENSG00000069974. [P51159-1]
    ENST00000569493; ENSP00000456059; ENSG00000069974. [P51159-1]
    GeneIDi5873.
    KEGGihsa:5873.
    UCSCiuc002aco.3. human. [P51159-1]

    Polymorphism databases

    DMDMi116242744.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    RAB27Abase

    RAB27A mutation db

    Mutations of the RAB27A gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38654 mRNA. Translation: AAC50271.2 .
    U57094 mRNA. Translation: AAC51195.1 .
    AF154840
    , AF154836 , AF154837 , AF154838 , AF154839 Genomic DNA. Translation: AAD47629.1 .
    AF125393 mRNA. Translation: AAD43049.1 .
    AF443871 Genomic DNA. Translation: AAL39097.1 .
    AF498953 mRNA. Translation: AAM21101.1 .
    CR536496 mRNA. Translation: CAG38735.1 .
    CR541693 mRNA. Translation: CAG46494.1 .
    BC107680 mRNA. Translation: AAI07681.1 .
    CCDSi CCDS10153.1. [P51159-1 ]
    PIRi I39198.
    RefSeqi NP_004571.2. NM_004580.4. [P51159-1 ]
    NP_899057.1. NM_183234.2. [P51159-1 ]
    NP_899058.1. NM_183235.2. [P51159-1 ]
    NP_899059.1. NM_183236.2. [P51159-1 ]
    XP_005254633.1. XM_005254576.2. [P51159-1 ]
    UniGenei Hs.654978.
    Hs.735555.

    3D structure databases

    ProteinModelPortali P51159.
    SMRi P51159. Positions 4-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111811. 24 interactions.
    IntActi P51159. 11 interactions.
    MINTi MINT-1377654.
    STRINGi 9606.ENSP00000337761.

    PTM databases

    PhosphoSitei P51159.

    Polymorphism databases

    DMDMi 116242744.

    Proteomic databases

    MaxQBi P51159.
    PaxDbi P51159.
    PeptideAtlasi P51159.
    PRIDEi P51159.

    Protocols and materials databases

    DNASUi 5873.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336787 ; ENSP00000337761 ; ENSG00000069974 . [P51159-1 ]
    ENST00000396307 ; ENSP00000379601 ; ENSG00000069974 . [P51159-1 ]
    ENST00000564609 ; ENSP00000455012 ; ENSG00000069974 . [P51159-1 ]
    ENST00000569493 ; ENSP00000456059 ; ENSG00000069974 . [P51159-1 ]
    GeneIDi 5873.
    KEGGi hsa:5873.
    UCSCi uc002aco.3. human. [P51159-1 ]

    Organism-specific databases

    CTDi 5873.
    GeneCardsi GC15M055495.
    HGNCi HGNC:9766. RAB27A.
    HPAi CAB034046.
    HPA001333.
    MIMi 603868. gene.
    607624. phenotype.
    neXtProti NX_P51159.
    Orphaneti 79477. Griscelli disease type 2.
    PharmGKBi PA34117.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P51159.
    KOi K07885.
    OMAi DQRAVKE.
    OrthoDBi EOG7FFMSC.
    PhylomeDBi P51159.
    TreeFami TF312895.

    Enzyme and pathway databases

    Reactomei REACT_15550. Insulin processing.

    Miscellaneous databases

    ChiTaRSi RAB27A. human.
    GeneWikii RAB27A.
    GenomeRNAii 5873.
    NextBioi 22812.
    PROi P51159.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51159.
    Bgeei P51159.
    CleanExi HS_RAB27A.
    Genevestigatori P51159.

    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. "Deficient geranylgeranylation of Ram/Rab27 in choroideremia."
      Seabra M.C., Ho Y.K., Anant J.S.
      J. Biol. Chem. 270:24420-24427(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PARTIAL PROTEIN SEQUENCE.
      Tissue: Retina.
    2. Seabra M.C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 99.
    3. "Molecular cloning and characterization of rab27a and rab27b, novel human rab proteins shared by melanocytes and platelets."
      Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.
      Biochem. Mol. Med. 60:27-37(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Melanocyte.
    4. "Cloning, mapping and characterization of the human RAB27A gene."
      Tolmachova T., Ramalho J.S., Anant J.S., Schultz R.A., Huxley C.M., Seabra M.C.
      Gene 239:109-116(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
      Tissue: Pituitary.
    6. "Genomic organization of the human RAB27A gene."
      Anderson P.D., Huizing M., Anikster Y., Gahl W.A.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM LONG).
    7. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Brain.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "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: Mammary gland.
    10. "Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions."
      Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T., Izumi T.
      FEBS Lett. 517:233-238(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLPH.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    12. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UNC13D, TISSUE SPECIFICITY, MUTAGENESIS OF THR-23, CHARACTERIZATION OF VARIANT GS2 GLY-73.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    14. "Secretory cytotoxic granule maturation and exocytosis require the effector protein hMunc13-4."
      Menager M.M., Menasche G., Romao M., Knapnougel P., Ho C.-H., Garfa M., Raposo G., Feldmann J., Fischer A., de Saint Basile G.
      Nat. Immunol. 8:257-267(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC13D, SUBCELLULAR LOCATION.
    15. "A newly identified isoform of Slp2a associates with Rab27a in cytotoxic T cells and participates in cytotoxic granule secretion."
      Menasche G., Menager M.M., Lefebvre J.M., Deutsch E., Athman R., Lambert N., Mahlaoui N., Court M., Garin J., Fischer A., de Saint Basile G.
      Blood 112:5052-5062(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SYTL2, MUTAGENESIS OF LEU-70 AND ALA-76.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome."
      Menasche G., Pastural E., Feldmann J., Certain S., Ersoy F., Dupuis S., Wulffraat N., Bianchi D., Fischer A., Le Deist F., de Saint Basile G.
      Nat. Genet. 25:173-176(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.
    19. "Evidence that Griscelli syndrome with neurological involvement is caused by mutations in RAB27A, not MYO5A."
      Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A., Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.
      Am. J. Hum. Genet. 71:407-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN GRISCELLI SYNDROME.
    20. "Biochemical and functional characterization of Rab27a mutations occurring in Griscelli syndrome patients."
      Menasche G., Feldmann J., Houdusse A., Desaymard C., Fischer A., Goud B., de Saint Basile G.
      Blood 101:2736-2742(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.
    21. "Characterization of the molecular defects in Rab27a, caused by RAB27A missense mutations found in patients with Griscelli syndrome."
      Bahadoran P., Busca R., Chiaverini C., Westbroek W., Lambert J., Bille K., Valony G., Fukuda M., Naeyaert J.-M., Ortonne J.-P., Ballotti R.
      J. Biol. Chem. 278:11386-11392(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS GS2 GLY-73; PRO-130 AND PRO-152.

    Entry informationi

    Entry nameiRB27A_HUMAN
    AccessioniPrimary (citable) accession number: P51159
    Secondary accession number(s): O00195
    , Q6FI40, Q9UIR9, Q9Y5U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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