BTG2_HUMAN - dbPTM
BTG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTG2_HUMAN
UniProt AC P78543
Protein Name Protein BTG2
Gene Name BTG2
Organism Homo sapiens (Human).
Sequence Length 158
Subcellular Localization
Protein Description Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors (By similarity). Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth..
Protein Sequence MSHGKGTDMLPEIAAAVGFLSSLLRTRGCVSEQRLKVFSGALQEALTEHYKHHWFPEKPSKGSGYRCIRINHKMDPIISRVASQIGLSQPQLHQLLPSELTLWVDPYEVSYRIGEDGSICVLYEEAPLAASCGLLTCKNQVLLGRSSPSKNYVMAVSS
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
22PhosphorylationAAVGFLSSLLRTRGC
HHHHHHHHHHHHCCC
33.3024719451
58UbiquitinationKHHWFPEKPSKGSGY
HHHCCCCCCCCCCCC
55.6229967540
79O-linked_GlycosylationHKMDPIISRVASQIG
CCCCHHHHHHHHHHC
22.7929351928
83O-linked_GlycosylationPIISRVASQIGLSQP
HHHHHHHHHHCCCHH
21.3429351928
146PhosphorylationNQVLLGRSSPSKNYV
CCEEECCCCCCCCEE
44.8125849741
147PhosphorylationQVLLGRSSPSKNYVM
CEEECCCCCCCCEEE
31.6525849741
149PhosphorylationLLGRSSPSKNYVMAV
EECCCCCCCCEEEEE
35.1715788397

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
147SPhosphorylationKinaseMAPK1P28482
Uniprot
147SPhosphorylationKinaseMAPK3P27361
Uniprot
149SPhosphorylationKinaseMAPK14Q16539
Uniprot
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:19615363

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
147SPhosphorylation

15788397
149SPhosphorylation

15788397

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 BTG2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNOT1_HUMANCNOT1physical
17353931
CNO6L_HUMANCNOT6Lphysical
17353931
ANM1_HUMANPRMT1physical
8663146
ANM1_HUMANPRMT1physical
11856371
PICK1_RATPick1physical
11237868
CNOT8_HUMANCNOT8physical
11136725
HXC8_HUMANHOXC8physical
10617598
CNOT7_MOUSECnot7physical
9712883
SKP2_HUMANSKP2physical
19615363
CUL1_HUMANCUL1physical
22975506
SKP1_HUMANSKP1physical
22975506
SKP2_HUMANSKP2physical
22975506
SRA1_HUMANSRA1physical
20398657
CNOT8_HUMANCNOT8physical
25416956
CNOT7_HUMANCNOT7physical
25416956

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 BTG2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 inducesPin-1 binding in cytoplasm and cell death.";
Hong J.W., Ryu M.S., Lim I.K.;
J. Biol. Chem. 280:21256-21263(2005).
Cited for: PHOSPHORYLATION AT SER-147 AND SER-149, MUTAGENESIS OF SER-147;PRO-148 AND SER-149, INTERACTION WITH PIN1, AND FUNCTION.

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