PIM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIM2_HUMAN
• UniProt AC: Q9P1W9
• Protein Name: Serine/threonine-protein kinase pim-2
• Gene Name: PIM2
• Organism: Homo sapiens (Human).
• Sequence Length: 311
• 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 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: MLTKPLQGPPAPPGTPTPPPGGKDREAFEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDSVTCPLEVALLWKVGAGGGHPGVIRLLDWFETQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSRGVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAWSLLP

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
3	Phosphorylation	-----MLTKPLQGPP -----CCCCCCCCCC	29.35	-
15	Phosphorylation	GPPAPPGTPTPPPGG CCCCCCCCCCCCCCC	29.75	25159151
32	Phosphorylation	REAFEAEYRLGPLLG HHHHHHHHCHHHCCC	20.41	-
40	Ubiquitination	RLGPLLGKGGFGTVF CHHHCCCCCCCCEEE	56.69	21906983
61	Ubiquitination	DRLQVAIKVIPRNRV CCEEEEEEEECCCCC	25.11	21906983
89	Ubiquitination	LEVALLWKVGAGGGH HHHHHHHCCCCCCCC	30.66	21906983
132	Ubiquitination	LFDYITEKGPLGEGP HHHHHHHCCCCCCCC	58.12	-
165	Ubiquitination	GVVHRDIKDENILID CCCCCCCCCCCEEEE	64.38	21906983
179	Ubiquitination	DLRRGCAKLIDFGSG ECCCCHHHEEECCCC	50.48	21906983
195	Phosphorylation	LLHDEPYTDFDGTRV CCCCCCCCCCCCCCC	40.69	22817900
204	Phosphorylation	FDGTRVYSPPEWISR CCCCCCCCCCHHHHH	30.99	17287340

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PIM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIM2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PIM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUTC_HUMAN	CUTC	physical	16189514
BAD_HUMAN	BAD	physical	12954615
ZN821_HUMAN	ZNF821	physical	25416956
NUP98_HUMAN	NUP98	physical	26496610
PRCC_HUMAN	PRCC	physical	26496610
PPIL2_HUMAN	PPIL2	physical	26496610
TIM13_HUMAN	TIMM13	physical	26496610
GPKOW_HUMAN	GPKOW	physical	26496610
CLK4_HUMAN	CLK4	physical	26496610
TOE1_HUMAN	TOE1	physical	26496610
CCD84_HUMAN	CCDC84	physical	26496610

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195 AND SER-204, ANDMASS SPECTROMETRY.
PubMed: 17287340