PIM2_MOUSE - dbPTM
PIM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIM2_MOUSE
UniProt AC Q62070
Protein Name Serine/threonine-protein kinase pim-2
Gene Name Pim2
Organism Mus musculus (Mouse).
Sequence Length 370
Subcellular Localization
Protein Description Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate..
Protein Sequence MARATNLNAAPSAGASGPPDSLPSTLAPPSPGSPAALPRASTPCGLSGFSGLNIRSTSSMLTKPLQGHPSPPVTPTQPPGGKDRAAFEAEYRLGPLLGKGGFGTVFAGHRVTDRRQVAIKVISRNRVLGWSTVSDSVTCPLEVALLWKVGEGNGHPGVIRLLDWFETPEGFMLVLERPMPAQDLFDYITEKGPLGESCSRSFFTQVVAAVQHCHARGVVHRDIKDENILIDLCRGSIKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGVLLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPCSRPSLEEILLDPWMQSPAEEKPINSSKGSPTPLPWSLLP
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
5 (in isoform 2)Phosphorylation-34.3827566939
8 (in isoform 2)Phosphorylation-35.8127566939
16 (in isoform 2)Phosphorylation-51.4127566939
33PhosphorylationLAPPSPGSPAALPRA
CCCCCCCCCCCCCCC
18.1025266776
41PhosphorylationPAALPRASTPCGLSG
CCCCCCCCCCCCCCC
33.8725266776
42PhosphorylationAALPRASTPCGLSGF
CCCCCCCCCCCCCCC
22.9327566939
47PhosphorylationASTPCGLSGFSGLNI
CCCCCCCCCCCCCCC
24.0725266776

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

Oops, there are no upstream regulatory protein records of PIM2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIM2_MOUSE !!

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 PIM2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOCS1_MOUSESocs1physical
11854514

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIM2_MOUSE

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Related Literatures of Post-Translational Modification

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