Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Serine--tRNA ligase, cytoplasmic  

UniProtKB / Swiss-Prot ID :  SYSC_HUMAN

Gene Name (Synonyms) : 
SARS, SERS  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). 

Protein Sequence MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKK...
Predicted Secondary Structure CCCCHHHHHHCCCCCHHHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHC...
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
12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FRVDKGGDP
HHHCCCCCH
63.03Phosphositeplus
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQLVKADSE
HHHHHHHHH
55.88Phosphositeplus
Link
154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DVDNKVERI
CCCCEEEEE
40.80Phosphositeplus
Link
241PhosphoserineVAQLSQFDE
CCCCCCCCC
19.40HPRD
Link-
241PhosphoserineVAQLSQFDE
CCCCCCCCC
19.40PhosphoELM
Link-
241PhosphoserineVAQLSQFDE
CCCCCCCCC
19.40Phosphositeplus
Link-
241Phosphoserine.VAQLSQFDE
CCCCCCCCC
19.40UniProtKB
Link-
257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGSEKSDDN
CCCCCCCCC
61.96Phosphositeplus
Link-
266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SYDEKYLIA
CCCCCEEEC
42.32Phosphositeplus
Link
323N6-acetyllysineHQFEKIEQF
HHHEEEEEE
53.48HPRD
Link
323N6-acetyllysineHQFEKIEQF
HHHEEEEEE
53.48Phosphositeplus
Link
323N6-acetyllysine.HQFEKIEQF
HHHEEEEEE
53.48UniProtKB
Link
376Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AASKKLDLE
CCCCEEEEE
44.75Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SDHL_HUMANENSP00000234677STRING
SDHL_HUMANENSP00000234677STRING
SERB_HUMANENSP00000234677STRING
SERB_HUMANENSP00000234677STRING
SPYA_HUMANENSP00000234677STRING
SPYA_HUMANENSP00000234677STRING
GLYC_HUMANENSP00000234677STRING
GLYC_HUMANENSP00000234677STRING
GLYM_HUMANENSP00000234677STRING
GLYM_HUMANENSP00000234677STRING
CBS_HUMANENSP00000234677STRING
CBS_HUMANENSP00000234677STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00133L-Serine
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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-323, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures