Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ras GTPase-activating protein 2  

UniProtKB / Swiss-Prot ID :  RASA2_HUMAN

Gene Name (Synonyms) : 
RASA2, GAP1M, RASGAP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Cytoplasm, perinuclear region. 

Protein Function :  Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4). 

Protein Sequence MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQ...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEECCEEEEEEEECCCCCCCCCCCCCCCCEEEEEECC...
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.---MAAAAP
---CCCCCC
13.05UniProtKB
Link-
208N6-acetyllysineRNDQKKTKV
CCEEEEEEE
66.33HPRD
Link-
208N6-acetyllysineRNDQKKTKV
CCEEEEEEE
66.33Phosphositeplus
Link-
208N6-acetyllysine.RNDQKKTKV
CCEEEEEEE
66.33UniProtKB
Link-
209N6-acetyllysineNDQKKTKVK
CEEEEEEEE
48.20HPRD
Link-
209N6-acetyllysineNDQKKTKVK
CEEEEEEEE
48.20Phosphositeplus
Link-
209N6-acetyllysine.NDQKKTKVK
CEEEEEEEE
48.20UniProtKB
Link-
211N6-acetyllysineQKKTKVKKK
EEEEEEEEC
62.02HPRD
Link-
211N6-acetyllysineQKKTKVKKK
EEEEEEEEC
62.02Phosphositeplus
Link-
211N6-acetyllysine.QKKTKVKKK
EEEEEEEEC
62.02UniProtKB
Link-
213N6-acetyllysineKTKVKKKTS
EEEEEECCC
50.54HPRD
Link-
213N6-acetyllysineKTKVKKKTS
EEEEEECCC
50.54Phosphositeplus
Link-
213N6-acetyllysine.KTKVKKKTS
EEEEEECCC
50.54UniProtKB
Link-
781PhosphothreonineEACGTIAVY
HHCCCCCCC
12.97Phosphositeplus
Link-
785PhosphotyrosineTIAVYQGPQ
CCCCCCCCC
9.95Phosphositeplus
Link-
795PhosphotyrosineEPDDYSNFV
CHHHHHHCC
16.94Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GNA12_HUMANENSP00000286364STRING
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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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208; LYS-209; LYS-211 ANDLYS-213, 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