LN28B_HUMAN - dbPTM
LN28B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LN28B_HUMAN
UniProt AC Q6ZN17
Protein Name Protein lin-28 homolog B
Gene Name LIN28B
Organism Homo sapiens (Human).
Sequence Length 250
Subcellular Localization Nucleus. Nucleus, nucleolus . Cytoplasm . Predominantly nucleolar (PubMed:22118463). In Huh7 cells, predominantly cytoplasmic, with only a subset of cells exhibiting strong nuclear staining
however, the specificity of the polyclonal antibody used in
Protein Description Suppressor of microRNA (miRNA) biogenesis, including that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7 transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and sequester them in the nucleolus, away from the microprocessor complex, hence preventing their processing into mature miRNA. [PubMed: 22118463 Does not act on pri-miR21]
Protein Sequence MAEGGASKGGGEEPGKLPEPAEEESQVLRGTGHCKWFNVRMGFGFISMINREGSPLDIPVDVFVHQSKLFMEGFRSLKEGEPVEFTFKKSSKGLESIRVTGPGGSPCLGSERRPKGKTLQKRKPKGDRCYNCGGLDHHAKECSLPPQPKKCHYCQSIMHMVANCPHKNVAQPPASSQGRQEAESQPCTSTLPREVGGGHGCTSPPFPQEARAEISERSGRSPQEASSTKSSIAPEEQSKKGPSVQKRKKT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
25PhosphorylationPEPAEEESQVLRGTG
CCCHHHHHHHHHHCC		28.9525850435
54PhosphorylationSMINREGSPLDIPVD
EEECCCCCCCCCCCE		19.9629116813
90PhosphorylationVEFTFKKSSKGLESI
EEEEEEECCCCCCEE		37.5626074081
91PhosphorylationEFTFKKSSKGLESIR
EEEEEECCCCCCEEE		39.3526074081
96PhosphorylationKSSKGLESIRVTGPG
ECCCCCCEEEEECCC		22.2726074081
100PhosphorylationGLESIRVTGPGGSPC
CCCEEEEECCCCCCC		28.0126074081
105PhosphorylationRVTGPGGSPCLGSER
EEECCCCCCCCCCCC		20.5319664994
110PhosphorylationGGSPCLGSERRPKGK
CCCCCCCCCCCCCCC		18.2526074081
130PhosphorylationKPKGDRCYNCGGLDH
CCCCCCCCCCCCCCC		17.8722468782
184PhosphorylationQGRQEAESQPCTSTL
HCHHHHHHCCCCCCC		46.6126714015
202PhosphorylationVGGGHGCTSPPFPQE
CCCCCCCCCCCCCHH		49.1930266825
203PhosphorylationGGGHGCTSPPFPQEA
CCCCCCCCCCCCHHH		34.3530266825
215PhosphorylationQEARAEISERSGRSP
HHHHHHHHHHHCCCH		20.6121406692
218PhosphorylationRAEISERSGRSPQEA
HHHHHHHHCCCHHHH		34.2130242111
221PhosphorylationISERSGRSPQEASST
HHHHHCCCHHHHHHC		34.1730242111
226PhosphorylationGRSPQEASSTKSSIA
CCCHHHHHHCCCCCC		37.4821406692
227PhosphorylationRSPQEASSTKSSIAP
CCHHHHHHCCCCCCH		47.0721406692
228PhosphorylationSPQEASSTKSSIAPE
CHHHHHHCCCCCCHH		32.2421406692
240AcetylationAPEEQSKKGPSVQKR
CHHHHHHCCCCHHHC		79.7720167786
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseTRIM71Q2Q1W2
PMID:24602972
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LN28B_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LN28B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
24602972
LIN41_HUMANTRIM71physical
24602972
ELAV2_HUMANELAVL2physical
24778252
FBRL_HUMANFBLphysical
24778252
KRR1_HUMANKRR1physical
24778252
LARP4_HUMANLARP4physical
24778252
MK67I_HUMANNIFKphysical
24778252
NCBP1_HUMANNCBP1physical
24778252
NHP2_HUMANNHP2physical
24778252
NOP10_HUMANNOP10physical
24778252
PHAX_HUMANPHAXphysical
24778252
PURB_HUMANPURBphysical
24778252
PURA_HUMANPURAphysical
24778252
ZCHC3_HUMANZCCHC3physical
24778252
PTCD1_HUMANPTCD1physical
24778252
RUXG_HUMANSNRPGphysical
24778252
RALY_HUMANRALYphysical
24778252
NCBP2_HUMANNCBP2physical
24778252
RU2B_HUMANSNRPB2physical
24778252
LARP7_HUMANLARP7physical
24778252
RBM34_HUMANRBM34physical
24778252
RUXF_HUMANSNRPFphysical
24778252
SNRPA_HUMANSNRPAphysical
24778252
TRUB2_HUMANTRUB2physical
24778252
IF4A3_HUMANEIF4A3physical
24778252
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LN28B_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory