CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015493
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein lin-28 homolog B 
Protein Synonyms/Alias
 Lin-28B 
Gene Name
 LIN28B 
Gene Synonyms/Alias
 CSDD2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
240APEEQSKKGPSVQKRacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 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. 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. Mediates MYC-mediated let-7 repression. Isoform 1, when overexpressed, stimulates growth of the breast adenocarcinoma cell line MCF-7. Isoform 2 has no effect on cell growth. 
Sequence Annotation
 DOMAIN 29 102 CSD.
 ZN_FING 127 144 CCHC-type 1.
 ZN_FING 149 166 CCHC-type 2.
 METAL 129 129 Zinc 1 (By similarity).
 METAL 132 132 Zinc 1 (By similarity).
 METAL 137 137 Zinc 1 (By similarity).
 METAL 142 142 Zinc 1 (By similarity).
 METAL 151 151 Zinc 2 (By similarity).
 METAL 154 154 Zinc 2 (By similarity).
 METAL 159 159 Zinc 2 (By similarity).
 METAL 164 164 Zinc 2 (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 250 AA 
Protein Sequence
MAEGGASKGG GEEPGKLPEP AEEESQVLRG TGHCKWFNVR MGFGFISMIN REGSPLDIPV 60
DVFVHQSKLF MEGFRSLKEG EPVEFTFKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTLQ 120
KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKNVA QPPASSQGRQ 180
EAESQPCTST LPREVGGGHG CTSPPFPQEA RAEISERSGR SPQEASSTKS SIAPEEQSKK 240
GPSVQKRKKT 250 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
 GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
 GO:0031123; P:RNA 3'-end processing; IMP:UniProtKB. 
Interpro
 IPR011129; Cold_shock_prot.
 IPR002059; CSP_DNA-bd.
 IPR012340; NA-bd_OB-fold.
 IPR001878; Znf_CCHC. 
Pfam
 PF00313; CSD
 PF00098; zf-CCHC 
SMART
 SM00357; CSP
 SM00343; ZnF_C2HC 
PROSITE
 PS50158; ZF_CCHC 
PRINTS
 PR00050; COLDSHOCK.