Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ras-related protein Rab-7a  

UniProtKB / Swiss-Prot ID :  RAB7A_HUMAN

Gene Name (Synonyms) : 
RAB7A, RAB7  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Late endosome. Lysosome. Cytoplasmic vesicle, phagosome. Melanosome. Note=Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts (By similarity). Identified by mass spectrometry in melanosome  

Protein 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 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. 

Protein Sequence MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERF...
Predicted Secondary Structure CCCCCCCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCHHH...
Protein Variant
LocationDescription
32K -> E (in dbSNP:rs11549759). VAR_037886
129L -> F (in CMT2B; does not affectinteraction with NTRK1; results in higher
157K -> N (in CMT2B; does not affectinteraction with NTRK1; results in higher
161N -> T (in CMT2B; does not affectinteraction with NTRK1; results in higher
162V -> M (in CMT2B; does not affectinteraction with NTRK1; results in higher
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
17PhosphoserineILGDSGVGK
EEECCCCCH
33.31Phosphositeplus
Link
32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YVNKKFSNQ
HHCCCCCCC
49.15Phosphositeplus
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SNQYKATIG
CCCCCCCCC
29.32Phosphositeplus
Link
44noneTIGADFLTK
CCCEEEEEE
33.60HPRD
Link
72PhosphoserineERFQSLGVA
HHHHHHHHH
25.12HPRD
Link
72PhosphoserineERFQSLGVA
HHHHHHHHH
25.12PhosphoELM
Link
72PhosphoserineERFQSLGVA
HHHHHHHHH
25.12Phosphositeplus
Link
72PhosphoserineERFQSLGVA
HHHHHHHHH
25.12SysPTM
Link
72Phosphoserine.ERFQSLGVA
HHHHHHHHH
25.12UniProtKB
Link
101PhosphoserineKTLDSWRDE
HHHHHHHHH
27.42Phosphositeplus
Link
126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLGNKIDLE
EEEECCCCC
35.48Phosphositeplus
Link
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QVATKRAQA
CCCHHHHHH
35.68Phosphositeplus
Link
175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RNALKQETE
HHHHHCCCC
43.61Phosphositeplus
Link
183PhosphotyrosineEVELYNEFP
CCCCCCCCC
10.11HPRD
Link-
183PhosphotyrosineEVELYNEFP
CCCCCCCCC
10.11PhosphoELM
Link-
183PhosphotyrosineEVELYNEFP
CCCCCCCCC
10.11Phosphositeplus
Link-
183PhosphotyrosineEVELYNEFP
CCCCCCCCC
10.11SysPTM
Link-
183Phosphotyrosine.EVELYNEFP
CCCCCCCCC
10.11UniProtKB
Link-
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEPIKLDKN
CCCCCCCCC
62.44Phosphositeplus
Link-
205S-farnesyl cysteineSAESCSC
CCCCCCC
3.47HPRD
Link-
207S-farnesyl cysteineESCSC
CCCCC
8.30HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HGS_HUMANcolocalizationMINT-3369790MINT16962593
RAB4A_HUMANcolocalizationMINT-3369790MINT16962593
RAB14_HUMANcolocalizationMINT-3369790MINT16962593
RB11A_HUMANcolocalizationMINT-3369790MINT16962593
RAE1_HUMANin vitroHPRD:03805HPRD9563513
12576024
PGTB_HUMANin vitroHPRD:03805HPRD11591706
RAE1_HUMANENSP00000265062STRING
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Disease Reference
Kegg disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM disease
600882Charcot-Marie-Tooth disease 2B (CMT2B)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures