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P51149 (RAB7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-7a
Gene names
Name:RAB7A
Synonyms:RAB7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.11 Ref.23 Ref.26

Subunit structure

The GTP-bound form interacts with RAC1 By similarity. Interacts with NTRK1/TRKA 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. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.24 Ref.26

Subcellular location

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. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.23 Ref.26

Tissue specificity

Widely expressed; high expression found in skeletal muscle. Ref.27

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.27 Ref.28 Ref.29 Ref.30

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Sequence caution

The sequence BAA91390.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

The sequence BAF83410.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

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

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasmic vesicle
Endosome
Lysosome
Membrane
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 18272684. Source: GOC

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

bone resorption

Inferred from electronic annotation. Source: Ensembl

early endosome to late endosome transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

endocytosis

Traceable author statement PubMed 2115402. Source: ProtInc

endosome to lysosome transport

Inferred from mutant phenotype PubMed 18272684. Source: BHF-UCL

epidermal growth factor catabolic process

Inferred from mutant phenotype PubMed 18272684. Source: BHF-UCL

phagosome acidification

Inferred from mutant phenotype Ref.23. Source: UniProtKB

phagosome maturation

Traceable author statement Ref.18. Source: UniProtKB

phagosome-lysosome fusion

Inferred from mutant phenotype Ref.23. Source: UniProtKB

protein targeting to lysosome

Inferred from mutant phenotype PubMed 22115783. Source: BHF-UCL

protein transport

Traceable author statement Ref.18. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

alveolar lamellar body

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

late endosome

Inferred from direct assay Ref.11. Source: UniProtKB

lysosomal membrane

Traceable author statement. Source: Reactome

lysosome

Inferred from direct assay PubMed 15078902. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle

Inferred from direct assay Ref.23. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGDP binding

Inferred from direct assay PubMed 18272684. Source: BHF-UCL

GTP binding

Inferred from direct assay PubMed 18272684. Source: BHF-UCL

GTPase activity

Inferred from direct assay PubMed 18272684. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Ras-related protein Rab-7a
PRO_0000121121

Regions

Nucleotide binding15 – 228GTP
Nucleotide binding34 – 407GTP
Nucleotide binding63 – 675GTP
Nucleotide binding125 – 1284GTP
Nucleotide binding156 – 1572GTP
Motif37 – 459Effector region By similarity

Amino acid modifications

Modified residue721Phosphoserine Ref.17 Ref.20
Modified residue2071Cysteine methyl ester By similarity
Lipidation2051S-geranylgeranyl cysteine By similarity
Lipidation2071S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant321K → E.
Corresponds to variant rs11549759 [ dbSNP | Ensembl ].
VAR_037886
Natural variant1291L → 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. Ref.26 Ref.27 Ref.30
Corresponds to variant rs121909078 [ dbSNP | Ensembl ].
VAR_018722
Natural variant1571K → 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. Ref.29 Ref.30
Corresponds to variant rs121909081 [ dbSNP | Ensembl ].
VAR_037887
Natural variant1611N → 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. Ref.28 Ref.30
Corresponds to variant rs121909080 [ dbSNP | Ensembl ].
VAR_037888
Natural variant1621V → 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. Ref.26 Ref.27 Ref.30
Corresponds to variant rs121909079 [ dbSNP | Ensembl ].
VAR_018723

Experimental info

Mutagenesis81L → A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments. Ref.25
Mutagenesis101K → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. Ref.25
Mutagenesis221T → N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. Ref.10
Mutagenesis671Q → L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. Ref.10
Mutagenesis1801V → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. Ref.25
Mutagenesis1821L → 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. Ref.25
Mutagenesis1831Y → 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. Ref.25
Sequence conflict471T → I in AAD02565. Ref.3
Sequence conflict1081I → V in AAA86640. Ref.2
Sequence conflict1271I → V in AAA86640. Ref.2
Sequence conflict1801V → E in AAD02565. Ref.3

Secondary structure

............................. 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51149 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A2AF33B16A672971

FASTA20723,490
        10         20         30         40         50         60 
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ 

        70         80         90        100        110        120 
IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF 

       130        140        150        160        170        180 
VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV 

       190        200 
ELYNEFPEPI KLDKNDRAKA SAESCSC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy."
Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M., Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A., Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V.
Am. J. Hum. Genet. 72:722-727(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5268.
RefSeqNP_004628.4. NM_004637.5.
UniGeneHs.744853.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T91X-ray1.90A/B/C/D1-207[»]
1YHNX-ray3.00A1-207[»]
3LAWX-ray2.80A/B/C/D/E1-207[»]
ProteinModelPortalP51149.
SMRP51149. Positions 7-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113624. 36 interactions.
DIPDIP-39879N.
IntActP51149. 12 interactions.
MINTMINT-4999676.
STRING9606.ENSP00000265062.

PTM databases

PhosphoSiteP51149.

Polymorphism databases

DMDM1709999.

Proteomic databases

PaxDbP51149.
PeptideAtlasP51149.
PRIDEP51149.

Protocols and materials databases

DNASU7879.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265062; ENSP00000265062; ENSG00000075785.
GeneID7879.
KEGGhsa:7879.
UCSCuc003eks.1. human.

Organism-specific databases

CTD7879.
GeneCardsGC03P128444.
HGNCHGNC:9788. RAB7A.
HPACAB037131.
HPA006964.
MIM600882. phenotype.
602298. gene.
neXtProtNX_P51149.
Orphanet99936. Autosomal dominant Charcot-Marie-Tooth disease type 2B.
PharmGKBPA162400619.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidP51149.
KOK07897.
OMADYPDPIK.
PhylomeDBP51149.
TreeFamTF105605.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP51149.

Gene expression databases

ArrayExpressP51149.
BgeeP51149.
CleanExHS_RAB7A.
GenevestigatorP51149.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB7A. human.
EvolutionaryTraceP51149.
GeneWikiRAB7A.
GenomeRNAi7879.
NextBio30336.
PROP51149.
SOURCESearch...

Entry information

Entry nameRAB7A_HUMAN
AccessionPrimary (citable) accession number: P51149
Secondary accession number(s): A8K3V6, Q9NWJ0, Q9UPB0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM