Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Pim1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Pim1 a proto-oncogene serine/threonine kinase involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerced by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl- X(L)/BCL2L1. Phosphorylation of ASK1 an other proapoptotic protein, by PIM1, significantly decreases ASK1 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of p21Cip1, a regulator of cell cycle progression at G1, results in the relocation of p21Cip1 to the cytoplasm and enhanced p21Cip1 protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, p27Kip1, at both transcriptional and post- translational levels. Phosphorylation of p27Kip1,induces 14-3-3- proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. Isoform 2 is isolated as a monomer whereas isoform 1 complexes with other proteins. Binds to RP9. Isoform 1, but not isoform 2, binds BMX. Isoform 2 interacts with p27Kip1 and FOXO3. Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation. Interacts with HSP90, this interaction stabilizes PIM1 protein levels. Ubiquitinated form interacts with HSP70 and promotes its proteosomal degradation. Strongly induced in leukocytes by the JAK/STAT pathway in response to cytokines. Induced by different cellular stresses, heat shock and cytotoxic agents. Expressed primarily in cells of the hematopoietic and germline lineages. 2 isoforms of the human protein are produced by alternative initiation. Both isoforms are expressed in prostate cancer cell lines. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, CAMK; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; CAMK group; PIM family
Cellular Component: cytoplasm; plasma membrane; nucleus
Molecular Function: protein serine/threonine kinase activity; protein binding; manganese ion binding; transcription factor binding; ribosomal small subunit binding; ATP binding
Biological Process: cell proliferation; apoptosis; multicellular organismal development; negative regulation of transcription factor activity; protein amino acid autophosphorylation; cell cycle; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; protein amino acid phosphorylation; hyaluronan metabolic process; negative regulation of apoptosis
Reference #:  P11309 (UniProtKB)
Alt. Names/Synonyms: Oncogene PIM1; PIM; pim-1 kinase 44 kDa isoform; pim-1 oncogene; pim-1 oncogene (proviral integration site 1); PIM1; Proto-oncogene serine/threonine-protein kinase pim-1
Gene Symbols: PIM1
Molecular weight: 45,412 Da
Basal Isoelectric point: 6.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Pim1

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  KinBase  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 L34 QSRQRPQLSSDSPSA
0 2 R67 HSPRHSLRHSPGSGS
0 1 S69 PRHSLRHSPGSGSCG
0 1 P70 RHSLRHSPGSGSCGS
0 1 S95 LEVGMLLSkINsLAH
0 1 K96-ub EVGMLLSkINsLAHL
0 6 S99-p MLLSkINsLAHLRAA
0 1 T114-p PCNDLHAtKLAPGKE
0 1 S137-p QVGPLLGsGGFGSVY
0 1 K158-ub DNLPVAIkHVEKDRI
0 1 S189-p VLLKKVSsGFSGVIR
0 2 K260-ub GVLHRDIkDENILID
0 2 K274-ub DLNRGELkLIDFGSG
0 10 K285-ub FGSGALLkDTVYTDF
1 0 Y309 EWIRYHRYHGRSAAV
0 1 S352-p FFRQRVSsECQHLIR
  mouse

 
S32-p QPRQRPQsSSDSPSA
S61-p LSPGRRLsPssLRRR
S63-p PGRRLsPssLRRRCC
S64-p GRRLsPssLRRRCCS
S88-p LEVGMLLsKINsLAH
K89 EVGMLLsKINsLAHL
S92-p MLLsKINsLAHLRAR
T107 PCNDLHATKLAPGKE
S130 QVGPLLGSGGFGSVY
K151 DNLPVAIKHVEKDRI
S182 VLLKKVSSDFSGVIR
K253 GVLHRDIKDENILID
K267 DLSRGEIKLIDFGSG
K278 FGSGALLKDTVYTDF
Y302-p EWIRYHRyHGRSAAV
S345 FFRQTVSSECQHLIK
  rat

 
- gap
- gap
- gap
- gap
S4 ____MLLSKINSLAH
K5 ___MLLSKINSLAHL
S8 MLLSKINSLAHLRAA
N23 PCNDLHANKLAPGKE
S46 QVGPLLGSGGFGSVY
K67 DNLPVAIKHVEKDRI
S98 VLLKKVSSGFSGVIR
K169 GVLHRDIKDENILID
K183 DLNRGELKLIDFGSG
K194 FGSGALLKDTVYTDF
Y218 EWIRYHRYHGRSAAV
S261 YFRQRVSSECQHLIR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.