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P51149

- RAB7A_HUMAN

UniProt

P51149 - RAB7A_HUMAN

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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

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

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
Complete GO annotation...

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: UniProtKB
  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. phagocytic vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiP51149.
CleanExiHS_RAB7A.
ExpressionAtlasiP51149. baseline and differential.
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 – 147Combined sources
Helixi21 – 3010Combined sources
Beta strandi42 – 5413Combined sources
Beta strandi56 – 649Combined sources
Helixi68 – 703Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 975Combined sources
Helixi99 – 11012Combined sources
Helixi115 – 1173Combined sources
Beta strandi120 – 1256Combined sources
Helixi136 – 14510Combined sources
Beta strandi151 – 1533Combined sources
Turni156 – 1594Combined sources
Helixi162 – 18120Combined sources

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.
GeneTreeiENSGT00760000119125.
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

        10         20         30         40         50
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV
60 70 80 90 100
MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD
110 120 130 140 150
SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP
160 170 180 190 200
YFETSAKEAI NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA

SAESCSC
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.
GeneTreei ENSGT00760000119125.
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

Bgeei P51149.
CleanExi HS_RAB7A.
ExpressionAtlasi P51149. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 158 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