Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
LIN28A (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
LIN28A Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let- 7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre- let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation. Monomer. During skeletal muscle differentiation, associated with translation initiation complexes in the polysomal compartment. Directly interacts with EIF3S2. Interaction with NCL is RNA-dependent. Interacts with ZCCHC11/TUT4. Can be negatively regulated by the interaction of microRNAs miR-125a and miR-125b with at least two miRNA responsive elements (miREs) in the 3'-UTR of this gene. These interactions may reduce both translation efficiency and mRNA abundance. Negatively regulated by retinoic acid. Expressed in embryonic stem cells (ES cells), placenta and testis. Belongs to the lin-28 family. Note: This description may include information from UniProtKB.
Protein type: Translation; RNA binding protein
Cellular Component: stress granule; cytoplasm; nucleolus; nucleus
Molecular Function: mRNA binding; protein binding; miRNA binding; DNA binding; zinc ion binding; RNA binding; translation initiation factor binding
Biological Process: regulation of transcription, DNA-dependent; positive regulation of translation; pre-microRNA processing; stem cell maintenance; positive regulation of neuron differentiation; RNA 3'-end processing; negative regulation of glial cell differentiation; germ cell development
Reference #:  Q9H9Z2 (UniProtKB)
Alt. Names/Synonyms: CSDD1; FLJ12457; LIN-28; lin-28 homolog A (C. elegans); Lin-28A; LIN28; LIN28A; LN28A; Protein lin-28 homolog A; RNA-binding protein LIN-28; ZCCHC1; Zinc finger CCHC domain-containing protein 1; zinc finger, CCHC domain containing 1
Gene Symbols: LIN28A
Molecular weight: 22,743 Da
Basal Isoelectric point: 8.35  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

LIN28A

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S3-p _____MGsVSNQQFA
0 1 S120-p GGVFCIGsERRPKGK
0 2 K187-u QGPSAQGkPTYFREE
0 3 S200-p EEEEEIHsPtLLPEA
0 1 T202-p EEEIHsPtLLPEAQN
  mouse

 
S3 _____MGSVSNQQFA
S120 GGVFCIGSERRPKGK
K187 QGPSSQGKPAYFREE
S200-p EEEEEIHsPALLPEA
A202 EEEIHsPALLPEAQN
  rat

 
S3 _____MGSVSNQQFA
S120 GGVFCIGSERRPKGK
K187 QGPSSQGKPVYFREE
S200 EEEEEIHSPTLLPEA
T202 EEEIHSPTLLPEAQN
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.