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-1A  

UniProtKB / Swiss-Prot ID :  RAB1A_HUMAN

Gene Name (Synonyms) : 
RAB1A, RAB1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Golgi apparatus. Endoplasmic reticulum. 

Protein Function :  Probably required for transit of protein from the ER through Golgi compartment. Binds GTP and GDP and possesses intrinsic GTPase activity. 

Protein Sequence MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQ...
Predicted Secondary Structure CCCCCCCCCEEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEEEECCEEEEEEEEECCCC...
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-acetylserine---MSSMNP
---CCCCCC
37.99HPRD
Link-
2N-acetylserine.---MSSMNP
---CCCCCC
37.99UniProtKB
Link-
8PhosphotyrosineMNPEYDYLF
CCCCCCEEE
15.90Phosphositeplus
Link
10PhosphotyrosinePEYDYLFKL
CCCCEEEEE
17.09Phosphositeplus
Link
37PhosphothreonineDDTYTESYI
CCCCCCCCC
22.13HPRD
Link
40PhosphotyrosineYTESYISTI
CCCCCCCCC
7.83Phosphositeplus
Link
75PhosphothreonineERFRTITSS
HHHHHHHHH
26.37Phosphositeplus
Link-
79O-(2-cholinephosphoryl)serine; byLegionella AnkX.TITSSYYRG
HHHHHHHCC
19.96UniProtKB
Link
103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FNNVKQWLQ
HHHHHHHHH
37.57Phosphositeplus
Link
119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENVNKLLVG
CCCEEEEEE
38.63Phosphositeplus
Link
126S-nitrosocysteineVGNKCDLTT
EECCCCCCC
6.34dbSNO
Link
136PhosphotyrosineKVVDYTTAK
CCCCHHHHH
8.38Phosphositeplus
Link
181PhosphothreonineGPGATAGGA
CCCCCCCCC
31.58Phosphositeplus
Link-
187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGAEKSNVK
CCCCCCCCC
46.96Phosphositeplus
Link-
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSNVKIQST
CCCCCCCCC
39.00Phosphositeplus
Link-
194PhosphoserineVKIQSTPVK
CCCCCCCCC
37.85HPRD
Link-
204S-farnesyl cysteineSGGGCC
CCCCCC
2.55HPRD
Link-
204S-geranylgeranyl cysteine.SGGGCC
CCCCCC
2.55UniProtKB
Link-
205S-farnesyl cysteineGGGCC
CCCCC
7.65HPRD
Link
205S-geranylgeranyl cysteine.GGGCC
CCCCC
7.65UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SYT5_HUMANphysical interactionMINT-63964MINT16169070
ZN593_HUMANphysical interactionMINT-63965MINT16169070
CPNS1_HUMANphysical interactionMINT-63967MINT16169070
PSD7_HUMANphysical interactionMINT-63970MINT16169070
Q4VY09_HUMANphysical interactionMINT-2880667MINT16902405
Q4VY09_HUMANphysical interactionMINT-2883000MINT16902405
Q4VY09_HUMANphysical interactionMINT-2883227MINT16902405
Q4VY09_HUMANphysical interactionMINT-2981127MINT16902405
Q4VY09_HUMANphysical interactionMINT-2981160MINT16902405
Q4VY09_HUMANphysical interactionMINT-2981180MINT16902405
Q4VY09_HUMANdirect interactionMINT-2883082MINT16902405
Q59ED0_HUMANphysical interactionMINT-63971MINT16169070
RUSC2_HUMANphysical interactionMINT-61267MINT15796781
RIFK_HUMANphysical interactionMINT-63972MINT16169070
Q96IH1_HUMANphysical interactionMINT-63973MINT16169070
PRAF1_HUMANphysical interactionMINT-68421MINT16189514
CPNS1_HUMANphysical interactionEBI-735536
intact16169070
CREB1_HUMANphysical interactionEBI-735539
intact16169070
FSCN1_HUMANphysical interactionEBI-735542
intact16169070
ZEP1_HUMANphysical interactionEBI-735545
intact16169070
MOT3_HUMANphysical interactionEBI-735548
intact16169070
TBC17_HUMANphysical interactionEBI-735551
intact16169070
MARE3_HUMANphysical interactionEBI-737480
intact16169070
PSD7_HUMANphysical interactionEBI-737483
intact16169070
SYT5_HUMANphysical interactionEBI-737486
intact16169070
ZN593_HUMANphysical interactionEBI-737489
intact16169070
CDN1A_HUMANphysical interactionEBI-733058
intact16169070
RIFK_HUMANphysical interactionEBI-733061
intact16169070
ADCK1_HUMANphysical interactionEBI-735533
intact16169070
PRAF1_HUMANphysical interactionEBI-760264
intact16189514
RAE2_HUMANin vitroHPRD:01538HPRD9730828
8294464
SYT5_HUMANyeast 2-hybridHPRD:01538HPRD16169070
FSCN1_HUMANyeast 2-hybridHPRD:01538HPRD16169070
ADCK1_HUMANyeast 2-hybridHPRD:01538HPRD16169070
MOT3_HUMANyeast 2-hybridHPRD:01538HPRD16169070
TBC17_HUMANyeast 2-hybridHPRD:01538HPRD16169070
ZN593_HUMANyeast 2-hybridHPRD:01538HPRD16169070
MARE3_HUMANyeast 2-hybridHPRD:01538HPRD16169070
RIFK_HUMANyeast 2-hybridHPRD:01538HPRD16169070
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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
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: ISOPRENYLATION AT CYS-204 AND CYS-205, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures