Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aminoacyl tRNA synthase complex-interacting multifunctional protein 1  

UniProtKB / Swiss-Prot ID :  AIMP1_HUMAN

Gene Name (Synonyms) : 
AIMP1, EMAP2, SCYE1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle, secretory vesicle (By similarity). Secreted (By similarity). Endoplasmic reticulum (By similarity). Golgi apparatus (By similarity). Note=Enriched in secretory vesicles of pancreatic alpha cells and secre 

Protein Function :  Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7. 

Protein Sequence MANNDAVLKRLEQKGAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIEELKQELIQAE...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
79P -> A (in dbSNP:rs1134648). VAR_025212
104T -> A (in dbSNP:rs2230254). VAR_029156
117T -> A (in dbSNP:rs2230255). VAR_050124
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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
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
33N6-acetyllysineVSLLKEKAI
63.56HPRD
Link-
33N6-acetyllysine.VSLLKEKAI
63.56UniProtKB
Link-
84PhosphothreonineFPSGTPLHA
27.32HPRD
Link-
99PhosphoserineNVIQSTAVT
13.75HPRD
Link-
107PhosphoserineTTVSSGTKE
46.26HPRD
Link-
109PhosphothreonineVSSGTKEQI
33.10HPRD
Link-
140PhosphoserineKKQQSIAGS
16.35Phosphositeplus
Link-
161S-nitrosocysteineLRIGCIITA
1.57dbSNO
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
OMIM disease
260600Leukodystrophy, hypomyelinating, 3 (HLD3)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-33, 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