Pim1
entrez
18712
canonical
uniprot
P06803
canonical
ensembl
ENSMUSG00000024014
resolver
ensp
ENSMUSP00000024811
resolver
ensp
ENSMUSP00000156987
resolver
ensp
ENSMUSP00000157217
resolver
enst
ENSMUST00000234270
resolver
enst
ENSMUST00000234665
resolver
genesymbol
Pim1
resolver
genesymbol_syn
Pim-1
resolver
uniprot
A0A3Q4EGX3
resolver
uniprot
F6XDQ5
resolver
uniprot
Q8CFN8
resolver
uniprot_entry
A0A3Q4EGX3_MOUSE
resolver
uniprot_entry
PIM1_MOUSE
resolver
uniprot_sec
F6XDQ5
resolver
uniprot_sec
Q8CFN8
resolver
amino_acid_sequence
MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK
uniprot
proteins
disease_involvement
DISEASE: Note=Frequently activated by provirus insertion in murine leukemia virus-induced T-cell lymphomas.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed:15199164, PubMed:1825810). 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) (By similarity). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (PubMed:18438430). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (PubMed:18438430). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (PubMed:15280015). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (By similarity). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (By similarity). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (By similarity). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (By similarity). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (By similarity). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (By similarity). Also acts as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (PubMed:19687226). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex (PubMed:31548394). Acts as a negative regulator of innate immunity by mediating phosphorylation and inactivation of GBP1 in absence of infection: phosphorylation of GBP1 induces interaction with 14-3-3 protein sigma (SFN) and retention in the cytosol (By similarity). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (By similarity). Promotes brown adipocyte differentiation (PubMed:27923061). {ECO:0000250|UniProtKB:P11309, ECO:0000269|PubMed:15199164, ECO:0000269|PubMed:15280015, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:19687226, ECO:0000269|PubMed:27923061, ECO:0000269|PubMed:31548394}.
uniprot
proteins
mass_dalton
35451
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="K->M: Loss of autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:1825810
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P11309}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P11309}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
PIM subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10931201
uniprot
proteins
pubmed
15199164
uniprot
proteins
pubmed
15280015
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1825810
uniprot
proteins
pubmed
18438430
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19687226
uniprot
proteins
pubmed
27923061
uniprot
proteins
pubmed
3015420
uniprot
proteins
pubmed
31548394
uniprot
proteins
pubmed
7689870
uniprot
proteins
pubmed
8228813
uniprot
proteins
sequence_length
313
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1825810}. Nucleus {ECO:0000269|PubMed:1825810}. Cell membrane {ECO:0000269|PubMed:1825810}. Note=Mainly located in the cytoplasm.
uniprot
proteins