P51149 (RAB7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-7a

Gene names

Name:	RAB7A
Synonyms:	RAB7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Subunit structure	The GTP-bound form interacts with RAC1 By similarity. Interacts with NTRK1/TRKA By similarity. 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
Subcellular location	Late endosome. Lysosome By similarity. Cytoplasmic vesicle › phagosome By similarity. Melanosome By similarity. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side. Note: Co-localizes 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
Tissue specificity	Widely expressed; high expression found in skeletal muscle. Ref.26
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 regeneration 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
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 process	Protein transport Transport
Cellular component	Cytoplasmic vesicle Endosome Lysosome Membrane
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome bone resorption Inferred from electronic annotation. Source: Compara early endosome to late endosome transport Inferred from mutant phenotype Ref.11. Source: UniProtKB 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-lysosome fusion Inferred from mutant phenotype Ref.23. Source: UniProtKB protein targeting to lysosome Inferred from mutant phenotype PubMed 22115783. Source: BHF-UCL small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA alveolar lamellar body Inferred from electronic annotation. Source: Compara late endosome Inferred from direct assay Ref.11. Source: UniProtKB lysosomal membrane Traceable author statement. Source: Reactome 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_function	GDP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 207

207

Ras-related protein Rab-7a

PRO_0000121121

Regions

Nucleotide binding

15 – 22

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

125 – 128

4

GTP By similarity

Motif

37 – 45

9

Effector region By similarity

Amino acid modifications

Modified residue

72

1

Phosphoserine Ref.17 Ref.20

Modified residue

207

1

Cysteine methyl ester By similarity

Lipidation

205

1

S-geranylgeranyl cysteine By similarity

Lipidation

207

1

S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant

32

1

K → E.
Corresponds to variant rs11549759 [ dbSNP | Ensembl ].

VAR_037886

Natural variant

129

1

L → F 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.26 Ref.29
Corresponds to variant rs121909078 [ dbSNP | Ensembl ].

VAR_018722

Natural variant

157

1

K → 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.28 Ref.29
Corresponds to variant rs121909081 [ dbSNP | Ensembl ].

VAR_037887

Natural variant

161

1

N → 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.27 Ref.29
Corresponds to variant rs121909080 [ dbSNP | Ensembl ].

VAR_037888

Natural variant

162

1

V → M 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.26 Ref.29
Corresponds to variant rs121909079 [ dbSNP | Ensembl ].

VAR_018723

Experimental info

Mutagenesis

8

1

L → A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments. Ref.25

Mutagenesis

10

1

K → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. Ref.25

Mutagenesis

22

1

T → N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. Ref.10

Mutagenesis

67

1

Q → L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. Ref.10

Mutagenesis

180

1

V → A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments. Ref.25

Mutagenesis

182

1

L → 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

Mutagenesis

183

1

Y → 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 conflict

47

1

T → I in AAD02565. Ref.3

Sequence conflict

108

1

I → V in AAA86640. Ref.2

Sequence conflict

127

1

I → V in AAA86640. Ref.2

Sequence conflict

180

1

V → E in AAD02565. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

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.

.

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.

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.

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.

207

Helix Strand Turn

Details...

Beta strand

8 – 14

7

Helix

21 – 30

10

Beta strand

42 – 54

13

Beta strand

56 – 64

9

Helix

68 – 70

3

Beta strand

82 – 89

8

Helix

93 – 97

5

Helix

99 – 110

12

Helix

115 – 117

3

Beta strand

120 – 125

6

Helix

136 – 145

10

Beta strand

151 – 153

3

Turn

156 – 159

4

Helix

162 – 181

20

Sequences

	Sequence		Length	Mass (Da)
	P51149 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A2AF33B16A672971	FASTA	207	23,490
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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], MASS SPECTROMETRY. 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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 (3.0 ANGSTROMS) IN COMPLEX WITH RILP, MUTAGENESIS OF LEU-8; LYS-10; VAL-180; LEU-182 AND TYR-183.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

Leiden Muscular Dystrophy pages RAB7A, member RAS oncogene family (RAB7A)

Leiden Open Variation Database (LOVD)

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.

IPI

IPI00016342.

PIR

JC5268.

RefSeq

NP_004628.4. NM_004637.5.

UniGene

Hs.741172.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P51149.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39879N.

IntAct

P51149. 8 interactions.

MINT

MINT-4999676.

STRING

9606.ENSP00000265062.

PTM databases

PhosphoSite

P51149.

Polymorphism databases

DMDM

1709999.

Proteomic databases

PaxDb

P51149.

PeptideAtlas

P51149.

PRIDE

P51149.

Protocols and materials databases

DNASU

7879.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265062; ENSP00000265062; ENSG00000075785.

GeneID

7879.

KEGG

hsa:7879.

UCSC

uc003eks.1. human.

Organism-specific databases

CTD

7879.

GeneCards

GC03P128444.

HGNC

HGNC:9788. RAB7A.

HPA

HPA006964.

MIM

600882. phenotype.
602298. gene.

neXtProt

NX_P51149.

Orphanet

99936. Autosomal dominant Charcot-Marie-Tooth disease type 2B.

PharmGKB

PA162400619.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

P51149.

KO

K07897.

OMA

SPRDPEH.

OrthoDB

EOG4QFWF4.

PhylomeDB

P51149.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_2pathway. IL12-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P51149.

Bgee

P51149.

CleanEx

HS_RAB7A.

Genevestigator

P51149.

GermOnline

ENSG00000075785. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RAB7A. human.

EvolutionaryTrace

P51149.

GenomeRNAi

7879.

NextBio

30336.

SOURCE

Search...

Entry information

Entry name

RAB7A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.