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P51149

- RAB7A_HUMAN

UniProt

P51149 - RAB7A_HUMAN

Protein

Ras-related protein Rab-7a

Gene

RAB7A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228GTP2 Publications
    Nucleotide bindingi34 – 407GTP2 Publications
    Nucleotide bindingi63 – 675GTP2 Publications
    Nucleotide bindingi125 – 1284GTP2 Publications
    Nucleotide bindingi156 – 1572GTP2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. bone resorption Source: Ensembl
    3. cell death Source: UniProtKB-KW
    4. early endosome to late endosome transport Source: UniProtKB
    5. endocytosis Source: ProtInc
    6. endosome to lysosome transport Source: BHF-UCL
    7. epidermal growth factor catabolic process Source: BHF-UCL
    8. GTP catabolic process Source: GOC
    9. phagosome acidification Source: UniProtKB
    10. phagosome-lysosome fusion Source: UniProtKB
    11. phagosome maturation Source: UniProtKB
    12. protein targeting to lysosome Source: BHF-UCL
    13. protein transport Source: UniProtKB
    14. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    SignaLinkiP51149.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-7a
    Gene namesi
    Name:RAB7A
    Synonyms:RAB7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9788. RAB7A.

    Subcellular locationi

    Late endosome. Lysosome By similarity. Cytoplasmic vesiclephagosome By similarity. Melanosome By similarity. Cytoplasmic vesiclephagosome membrane; Lipid-anchor; Cytoplasmic side
    Note: Colocalizes with OSBPL1A at the late endosome. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes containing S.aureus or Mycobacterium By similarity.By similarity

    GO - Cellular componenti

    1. alveolar lamellar body Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: Ensembl
    4. intracellular membrane-bounded organelle Source: HPA
    5. late endosome Source: UniProtKB
    6. lysosomal membrane Source: Reactome
    7. lysosome Source: MGI
    8. melanosome Source: UniProtKB-SubCell
    9. phagocytic vesicle Source: UniProtKB
    10. phagocytic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2B (CMT2B) [MIM:600882]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291L → F in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909078 [ dbSNP | Ensembl ].
    VAR_018722
    Natural varianti157 – 1571K → N in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909081 [ dbSNP | Ensembl ].
    VAR_037887
    Natural varianti161 – 1611N → T in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909080 [ dbSNP | Ensembl ].
    VAR_037888
    Natural varianti162 – 1621V → M in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909079 [ dbSNP | Ensembl ].
    VAR_018723

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81L → A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments. 1 Publication
    Mutagenesisi10 – 101K → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. 1 Publication
    Mutagenesisi22 – 221T → N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. 1 Publication
    Mutagenesisi67 – 671Q → L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. 1 Publication
    Mutagenesisi180 – 1801V → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. 1 Publication
    Mutagenesisi182 – 1821L → A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-183. 1 Publication
    Mutagenesisi183 – 1831Y → A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-182. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi600882. phenotype.
    Orphaneti99936. Autosomal dominant Charcot-Marie-Tooth disease type 2B.
    PharmGKBiPA162400619.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Ras-related protein Rab-7aPRO_0000121121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721Phosphoserine2 Publications
    Lipidationi205 – 2051S-geranylgeranyl cysteineBy similarity
    Modified residuei207 – 2071Cysteine methyl esterBy similarity
    Lipidationi207 – 2071S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP51149.
    PaxDbiP51149.
    PeptideAtlasiP51149.
    PRIDEiP51149.

    PTM databases

    PhosphoSiteiP51149.

    Expressioni

    Tissue specificityi

    Widely expressed; high expression found in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiP51149.
    BgeeiP51149.
    CleanExiHS_RAB7A.
    GenevestigatoriP51149.

    Organism-specific databases

    HPAiCAB037131.
    HPA006964.

    Interactioni

    Subunit structurei

    The GTP-bound form interacts with RAC1 By similarity. Interacts with NTRK1/TRKA By similarity. Interacts with C9orf72 By similarity. Interacts with CHM, the substrate-binding subunit of the Rab geranylgeranyltransferase complex. Interacts with RILP, PSMA7, RNF115 and FYCO1. Interacts with the PIK3C3/VPS34-PIK3R4 complex. The GTP-bound form interacts with OSBPL1A. Interacts with CLN3.By similarity10 Publications

    Protein-protein interaction databases

    BioGridi113624. 42 interactions.
    DIPiDIP-39879N.
    IntActiP51149. 12 interactions.
    MINTiMINT-4999676.
    STRINGi9606.ENSP00000265062.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 147
    Helixi21 – 3010
    Beta strandi42 – 5413
    Beta strandi56 – 649
    Helixi68 – 703
    Beta strandi82 – 898
    Helixi93 – 975
    Helixi99 – 11012
    Helixi115 – 1173
    Beta strandi120 – 1256
    Helixi136 – 14510
    Beta strandi151 – 1533
    Turni156 – 1594
    Helixi162 – 18120

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T91X-ray1.90A/B/C/D1-207[»]
    1YHNX-ray3.00A1-207[»]
    3LAWX-ray2.80A/B/C/D/E1-207[»]
    ProteinModelPortaliP51149.
    SMRiP51149. Positions 7-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51149.

    Family & Domainsi

    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.
    InParanoidiP51149.
    KOiK07897.
    OMAiDYPDPIK.
    PhylomeDBiP51149.
    TreeFamiTF105605.

    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.

    P51149-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV    50
    MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD 100
    SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP 150
    YFETSAKEAI NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA 200
    SAESCSC 207
    Length:207
    Mass (Da):23,490
    Last modified:October 1, 1996 - v1
    Checksum:iA2AF33B16A672971
    GO

    Sequence cautioni

    The sequence EAW79303.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471T → I in AAD02565. 1 PublicationCurated
    Sequence conflicti108 – 1081I → V in AAA86640. (PubMed:9126495)Curated
    Sequence conflicti127 – 1271I → V in AAA86640. (PubMed:9126495)Curated
    Sequence conflicti180 – 1801V → E in AAD02565. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321K → E.
    Corresponds to variant rs11549759 [ dbSNP | Ensembl ].
    VAR_037886
    Natural varianti129 – 1291L → F in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909078 [ dbSNP | Ensembl ].
    VAR_018722
    Natural varianti157 – 1571K → N in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909081 [ dbSNP | Ensembl ].
    VAR_037887
    Natural varianti161 – 1611N → T in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909080 [ dbSNP | Ensembl ].
    VAR_037888
    Natural varianti162 – 1621V → M in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling. 1 Publication
    Corresponds to variant rs121909079 [ dbSNP | Ensembl ].
    VAR_018723

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93499 mRNA. Translation: CAA63763.1.
    U44104 mRNA. Translation: AAA86640.1.
    AF050175 Genomic DNA. Translation: AAD02565.1.
    AF498942 mRNA. Translation: AAM21090.1.
    AK000826 mRNA. Translation: BAA91390.1. Sequence problems.
    AK290721 mRNA. Translation: BAF83410.1. Sequence problems.
    BC008721 mRNA. Translation: AAH08721.2.
    CH471052 Genomic DNA. Translation: EAW79303.1. Sequence problems.
    CCDSiCCDS3052.1.
    PIRiJC5268.
    RefSeqiNP_004628.4. NM_004637.5.
    UniGeneiHs.744853.

    Genome annotation databases

    EnsembliENST00000265062; ENSP00000265062; ENSG00000075785.
    GeneIDi7879.
    KEGGihsa:7879.
    UCSCiuc003eks.1. human.

    Polymorphism databases

    DMDMi1709999.

    Cross-referencesi

    Web resourcesi

    Inherited peripheral neuropathies mutation db
    Leiden Muscular Dystrophy pages RAB7A, member RAS oncogene family (RAB7A)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93499 mRNA. Translation: CAA63763.1 .
    U44104 mRNA. Translation: AAA86640.1 .
    AF050175 Genomic DNA. Translation: AAD02565.1 .
    AF498942 mRNA. Translation: AAM21090.1 .
    AK000826 mRNA. Translation: BAA91390.1 . Sequence problems.
    AK290721 mRNA. Translation: BAF83410.1 . Sequence problems.
    BC008721 mRNA. Translation: AAH08721.2 .
    CH471052 Genomic DNA. Translation: EAW79303.1 . Sequence problems.
    CCDSi CCDS3052.1.
    PIRi JC5268.
    RefSeqi NP_004628.4. NM_004637.5.
    UniGenei Hs.744853.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T91 X-ray 1.90 A/B/C/D 1-207 [» ]
    1YHN X-ray 3.00 A 1-207 [» ]
    3LAW X-ray 2.80 A/B/C/D/E 1-207 [» ]
    ProteinModelPortali P51149.
    SMRi P51149. Positions 7-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113624. 42 interactions.
    DIPi DIP-39879N.
    IntActi P51149. 12 interactions.
    MINTi MINT-4999676.
    STRINGi 9606.ENSP00000265062.

    PTM databases

    PhosphoSitei P51149.

    Polymorphism databases

    DMDMi 1709999.

    Proteomic databases

    MaxQBi P51149.
    PaxDbi P51149.
    PeptideAtlasi P51149.
    PRIDEi P51149.

    Protocols and materials databases

    DNASUi 7879.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265062 ; ENSP00000265062 ; ENSG00000075785 .
    GeneIDi 7879.
    KEGGi hsa:7879.
    UCSCi uc003eks.1. human.

    Organism-specific databases

    CTDi 7879.
    GeneCardsi GC03P128444.
    GeneReviewsi RAB7A.
    HGNCi HGNC:9788. RAB7A.
    HPAi CAB037131.
    HPA006964.
    MIMi 600882. phenotype.
    602298. gene.
    neXtProti NX_P51149.
    Orphaneti 99936. Autosomal dominant Charcot-Marie-Tooth disease type 2B.
    PharmGKBi PA162400619.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi P51149.
    KOi K07897.
    OMAi DYPDPIK.
    PhylomeDBi P51149.
    TreeFami TF105605.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    SignaLinki P51149.

    Miscellaneous databases

    ChiTaRSi RAB7A. human.
    EvolutionaryTracei P51149.
    GeneWikii RAB7A.
    GenomeRNAii 7879.
    NextBioi 30336.
    PROi P51149.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51149.
    Bgeei P51149.
    CleanExi HS_RAB7A.
    Genevestigatori P51149.

    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. "Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid."
      Vitelli R., Chiariello M., Lattero D., Bruni C.B., Bucci C.
      Biochem. Biophys. Res. Commun. 229:887-890(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene."
      Davies J.P., Cotter P.D., Ioannou Y.A.
      Genomics 41:131-134(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Kim J.Y., Park Y.B.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "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].
      Tissue: Brain.
    5. "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: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Lung.
    8. "Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes."
      Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C.
      EMBO J. 20:683-693(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LATE ENDOCYTOSIS, INTERACTION WITH RILP.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    10. "Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP."
      Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.
      Mol. Cell. Biol. 23:6494-6506(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHAGOSOMAL BIOGENESIS, MUTAGENESIS OF THR-22 AND GLN-67, SUBCELLULAR LOCATION.
    11. "Human VPS34 and p150 are Rab7 interacting partners."
      Stein M.P., Feng Y., Cooper K.L., Welford A.M., Wandinger-Ness A.
      Traffic 4:754-771(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PIK3C3/VPS34-PIK3R4 COMPLEX, SUBCELLULAR LOCATION.
    12. "The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes."
      Dong J., Chen W., Welford A., Wandinger-Ness A.
      J. Biol. Chem. 279:21334-21342(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMA7.
    13. "A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34."
      Wang T., Wong K.K., Hong W.
      Mol. Biol. Cell 15:815-826(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RILP.
    14. "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
      Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
      Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OSBPL1A.
    15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    16. "Novel RING E3 ubiquitin ligases in breast cancer."
      Burger A., Amemiya Y., Kitching R., Seth A.K.
      Neoplasia 8:689-695(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF115.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Rab7: roles in membrane trafficking and disease."
      Zhang M., Chen L., Wang S., Wang T.
      Biosci. Rep. 29:193-209(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    19. "FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport."
      Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A., Bjorkoy G., Johansen T.
      J. Cell Biol. 188:253-269(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYCO1.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Rab7: role of its protein interaction cascades in endo-lysosomal traffic."
      Wang T., Ming Z., Xiaochun W., Hong W.
      Cell. Signal. 23:516-521(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    23. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
      Seto S., Tsujimura K., Koide Y.
      Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    24. "Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
      Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
      Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLN3.
    25. "Structural basis for recruitment of RILP by small GTPase Rab7."
      Wu M., Wang T., Loh E., Hong W., Song H.
      EMBO J. 24:1491-1501(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GTP AND RILP, MUTAGENESIS OF LEU-8; LYS-10; VAL-180; LEU-182 AND TYR-183.
    26. "Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation."
      McCray B.A., Skordalakes E., Taylor J.P.
      Hum. Mol. Genet. 19:1033-1047(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF VARIANT CMT2B PHE-129 IN COMPLEX WITH GTP, CHARACTERIZATION OF VARIANTS CMT2B PHE-129 AND MET-162, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    27. Cited for: VARIANTS CMT2B PHE-129 AND MET-162, TISSUE SPECIFICITY.
    28. "A novel RAB7 mutation associated with ulcero-mutilating neuropathy."
      Houlden H., King R.H.M., Muddle J.R., Warner T.T., Reilly M.M., Orrell R.W., Ginsberg L.
      Ann. Neurol. 56:586-590(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2B THR-161.
    29. "Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene."
      Meggouh F., Bienfait H.M.E., Weterman M.A.J., de Visser M., Baas F.
      Neurology 67:1476-1478(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2B ASN-157.
    30. "Rab7 mutants associated with Charcot-Marie-Tooth disease exhibit enhanced NGF-stimulated signaling."
      Basuray S., Mukherjee S., Romero E., Wilson M.C., Wandinger-Ness A.
      PLoS ONE 5:E15351-E15351(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CMT2B PHE-129; ASN-157; THR-161 AND MET-162.

    Entry informationi

    Entry nameiRAB7A_HUMAN
    AccessioniPrimary (citable) accession number: P51149
    Secondary accession number(s): A8K3V6, Q9NWJ0, Q9UPB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 157 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3