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-5A  

UniProtKB / Swiss-Prot ID :  RAB5A_HUMAN

Gene Name (Synonyms) : 
RAB5A, RAB5  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity). Early endosome membrane; Lipid-anchor (By similarity). Melanosome. Note=Enriched in stage I melanosomes. 

Protein Function :  Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. 

Protein Sequence MASRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEEE...
Protein Variant -
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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
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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
2N-acetylalanine.---MASRGA
---CCCCCC
14.13UniProtKB
Link-
51PhosphoserineEFQESTIGA
CCCCCCCCE
17.97HPRD
Link
116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KNWVKELQR
HHHHHHHHH
44.30Phosphositeplus
Link
123PhosphoserineQRQASPNIV
HHHCCCCCE
15.33Phosphositeplus
Link
202PhosphothreonineGVDLTEPTQ
EEECCCCCC
35.14HPRD
Link-
202PhosphothreonineGVDLTEPTQ
EEECCCCCC
35.14PhosphoELM
Link-
202PhosphothreonineGVDLTEPTQ
EEECCCCCC
35.14Phosphositeplus
Link-
202PhosphothreonineGVDLTEPTQ
EEECCCCCC
35.14SysPTM
Link-
202Phosphothreonine.GVDLTEPTQ
EEECCCCCC
35.14UniProtKB
Link-
205PhosphothreonineLTEPTQPTR
CCCCCCCCC
40.73HPRD
Link-
205PhosphothreonineLTEPTQPTR
CCCCCCCCC
40.73PhosphoELM
Link-
205PhosphothreonineLTEPTQPTR
CCCCCCCCC
40.73Phosphositeplus
Link-
205PhosphothreonineLTEPTQPTR
CCCCCCCCC
40.73SysPTM
Link-
205Phosphothreonine.LTEPTQPTR
CCCCCCCCC
40.73UniProtKB
Link-
208PhosphothreoninePTQPTRNQC
CCCCCCCCC
32.22HPRD
Link-
208PhosphothreoninePTQPTRNQC
CCCCCCCCC
32.22PhosphoELM
Link-
208PhosphothreoninePTQPTRNQC
CCCCCCCCC
32.22Phosphositeplus
Link-
208PhosphothreoninePTQPTRNQC
CCCCCCCCC
32.22SysPTM
Link-
208Phosphothreonine.PTQPTRNQC
CCCCCCCCC
32.22UniProtKB
Link-
212S-farnesyl cysteineTRNQCCSN
CCCCCCCC
2.91HPRD
Link-
212S-geranylgeranyl cysteine.TRNQCCSN
CCCCCCCC
2.91UniProtKB
Link-
213S-farnesyl cysteineRNQCCSN
CCCCCCC
2.92HPRD
Link-
213S-geranylgeranyl cysteine.RNQCCSN
CCCCCCC
2.92UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RASA1_HUMANphysical interactionMINT-18675MINT11536198
Q4VY09_HUMANphysical interactionMINT-2882874MINT16902405
Q4VY09_HUMANcolocalizationMINT-2883167MINT16902405
Q4VY09_HUMANphysical interactionMINT-2981030MINT16902405
Q4VY09_HUMANphysical interactionMINT-2981062MINT16902405
Q4VY09_HUMANdirect interactionMINT-2883115MINT16902405
DP13A_HUMANdirect interactionMINT-5207882MINT17581628
DP13A_HUMANdirect interactionMINT-5208011MINT17581628
DP13A_HUMANdirect interactionMINT-5208179MINT17581628
DP13A_HUMANdirect interactionMINT-5208195MINT17581628
RABE1_HUMANdirect interactionEBI-1040324
intact15378032
EEA1_HUMANphysical interaction
physical interaction
physical interaction
EBI-399450
EBI-399487
EBI-399
intact10491193
11870209
9697774
AGTR1_HUMANin vivo
yeast 2-hybrid
HPRD:01542HPRD11682489
RAE2_HUMANin vitroHPRD:01542HPRD9730828
8294464
RASA1_HUMANin vitroHPRD:01542HPRD11536198
DP13A_HUMANin vitro
in vivo
HPRD:01542HPRD15016378
DP13B_HUMANin vitroHPRD:01542HPRD15016378
RAB5A_HUMANin vivoHPRD:01542HPRD15782196
RIN3_HUMANENSP00000273047STRING
TSC2_HUMANENSP00000273047STRING
PRAF1_HUMANENSP00000273047STRING
ELAF_HUMANENSP00000273047STRING
RBNS5_HUMANENSP00000273047STRING
RIN2_HUMANENSP00000273047STRING
RABE1_HUMANENSP00000273047STRING
ALS2_HUMANENSP00000273047STRING
TRFE_HUMANENSP00000273047STRING
P85A_HUMANENSP00000273047STRING
RASA1_HUMANENSP00000273047STRING
EGFR_HUMANENSP00000273047STRING
US6NL_HUMANENSP00000273047STRING
EPS8_HUMANENSP00000273047STRING
DP13A_HUMANENSP00000273047STRING
TBC3A_HUMANENSP00000273047STRING
RIN1_HUMANENSP00000273047STRING
EEA1_HUMANENSP00000273047STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-202; THR-205 ANDTHR-208, AND MASS SPECTROMETRY.
Prenylation
ReferencePubMed
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation ofadjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-212 AND CYS-213, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures