Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  La-related protein 6  

UniProtKB / Swiss-Prot ID :  LARP6_HUMAN

Gene Name (Synonyms) : 
LARP6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm. 

Protein Function :  Regulates the coordinated translation of type I collagen alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through high-affinity binding of a stem-loop structure in their 5' UTR. This regulation requires VIM and MYH10 filaments, and the helicase DHX9. 

Protein Sequence MAQSGGEARPGPKTAVQIRVAIQEAEDVDELEDEEEGAETRGAGDPARYLSPGWGSASEEEPSRGHSGTT...
Predicted Secondary Structure CCCCCCCCCCCCCCEEEEEEEECCHHHHHHHHHHCCCCHHCCCCCCHHHCCCCCCCHHHCCCCCCCCCCC...
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.---MAQSGG
---CCCCCC
16.55UniProtKB
Link-
56PhosphoserinePGWGSASEE
CCCCCHHHC
23.32HPRD
Link-
56PhosphoserinePGWGSASEE
CCCCCHHHC
23.32Phosphositeplus
Link-
56PhosphoserinePGWGSASEE
CCCCCHHHC
23.32SysPTM
Link-
56Phosphoserine.PGWGSASEE
CCCCCHHHC
23.32UniProtKB
Link-
58PhosphoserineWGSASEEEP
CCCHHHCCC
47.43HPRD
Link-
58PhosphoserineWGSASEEEP
CCCHHHCCC
47.43Phosphositeplus
Link-
58PhosphoserineWGSASEEEP
CCCHHHCCC
47.43SysPTM
Link-
58Phosphoserine.WGSASEEEP
CCCHHHCCC
47.43UniProtKB
Link-
409PhosphoserineNCSTSPEIF
CCCCCHHHH
12.30HPRD
Link-
409PhosphoserineNCSTSPEIF
CCCCCHHHH
12.30Phosphositeplus
Link-
447PhosphoserineTQEKSPGTS
CCCCCCCCC
28.01HPRD
Link-
447PhosphoserineTQEKSPGTS
CCCCCCCCC
28.01Phosphositeplus
Link-
447PhosphoserineTQEKSPGTS
CCCCCCCCC
28.01SysPTM
Link-
447Phosphoserine.TQEKSPGTS
CCCCCCCCC
28.01UniProtKB
Link-
451PhosphoserineSPGTSPLLS
CCCCCHHHH
21.33HPRD
Link-
451PhosphoserineSPGTSPLLS
CCCCCHHHH
21.33Phosphositeplus
Link-
451PhosphoserineSPGTSPLLS
CCCCCHHHH
21.33SysPTM
Link-
451Phosphoserine.SPGTSPLLS
CCCCCHHHH
21.33UniProtKB
Link-
455PhosphoserineSPLLSRKMQ
CHHHHHHHH
37.22Phosphositeplus
Link-
455PhosphoserineSPLLSRKMQ
CHHHHHHHH
37.22SysPTM
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
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-447 AND SER-451, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-58; SER-447 ANDSER-451, AND MASS SPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-447 AND SER-451, 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