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PIM1 (pim-1 oncogene)

Written2000-08Jean-Loup Huret
Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France
Updated2013-04Sai-Ching Jim Yeung
The University of Texas M. D. Anderson Cancer Center, Department of General Internal Medicine, Ambulatory Treatment, Emergency Care, Department of Endocrine Neoplasia, Hormonal Disorders, 1515 Holcombe Boulevard, Unit 437, Houston, Texas 77030, USA

(Note : for Links provided by Atlas : click)

Identity

Other namesPIM
HGNC (Hugo) PIM1
LocusID (NCBI) 5292
Atlas_Id 261
Location 6p21.2
Location_base_pair Starts at 37137922 and ends at 37143204 bp from pter ( according to hg19-Feb_2009)  [Mapping PIM1.png]
Fusion genes
(updated 2016)
BCL6 (3q27.3) / PIM1 (6p21.2)PIM1 (6p21.2) / BCL6 (3q27.3)PIM1 (6p21.2) / DGCR2 (22q11.21)
PIM1 (6p21.2) / GBF1 (10q24.32)

DNA/RNA

Description PIM1 is a single gene with 5 introns and 6 exons that span 5 kb of DNA in the human genome (Meeker et al., 1987). The gene starts at 37137922 and ends at 37143204 base pairs from pter. It is highly conserved evolutionarily across species.
Transcription The mRNA sequence is 2,6 kb in length with a 941 bp coding region.

Protein

Description Size: 313 amino acids; molecular weight: 36 kDa.
The PIM1 gene has six exons, but there are two isoforms of PIM1 protein, 34 kDa and 44 kDa, due to protein synthesis using alternative sites of translation initiation (Saris et al., 1991). Both proteins show comparable kinase activities in vitro, but the 44 kDa isoform contains an N-terminal proline-rich motif that binds the ETK SH3 domain, and is recruited to the plasma membrane (Xie et al., 2006).
Expression The kinase activity of all the PIM proteins is constitutively active, and there are no regulatory domains in the amino acid sequences of the PIM proteins. Thus, unlike other kinases that are regulated by phosphorylation or binding to the plasma membrane, the activity of PIM1 is regulated primarily by transcription, translation and proteosomal degradation (Amaravadi and Thompson, 2005). The gene expression of PIM1 is increased by various cytokines, mitogens and hormones such as G-CSF, GM-CSF, erythropoietin, interleukins, Con A, PMA, interferons, and prolactin (Wang et al., 2001; Hogan et al., 2008; White, 2003). These factors act through the JAK/STAT pathway. The upregulation of PIM1 gene expression results from the binding site of STAT3 or STAT5 to the PIM1 gene promoter, and the ISFR/GAS-sequence (IFN-γ activation sequence) is an important binding site (Block et al., 2012; Matikainen et al., 1999; Yip-Schneider et al., 1995). PIM1 phosphorylates and stabilizes SOCS proteins (suppressor of cytokine signaling) to provide negative feedback regulation of the JAK/STAT pathway (Peltola et al., 2004).
NF-κB, as a downstream transcription factors, could also activate PIM1. In solid tumors, hypoxia would induce the PIM1 expression, independently of HIF1α and by Krueppel-like factor 5 (KLF5) upon DNA damage (Chen et al., 2009a). ERG, as a transcription factors, also plays a role in PIM1 expression in the initial stages of prostate carcinogenesis (Magistroni et al., 2011).
Because of multiple copies of AUUU(A) motifs in the 3'UTR and GC-rich regions in the 5'UTR, mRNA of PIM genes are short lived (Wang et al., 2005). Translation of PIM1 seems to be cap-dependent, and overexpression of elF4E would increase PIM1 protein level (Hoover et al., 1997). PIM RNA transcripts are regulatory targets of different miRNAs such as microRNAs miR1, miR-210, miR-33a, and miR328, implicating another layer of PIM expression regulation (Eiring et al., 2010; Huang et al., 2009; Nasser et al., 2008; Thomas et al., 2012).
At the post-translational level, the short half-life of PIM1 is primarily regulated by proteasomal degradation. PIM1 protein can be stabilized by the binding to HSP90 (Mizuno et al., 2001). On the other hand, binding to HSP70 would induce the ubiquitylation of PIM1 and proteasomal degradation (Shay et al., 2005). Also, in hypoxia, ubiquitin-mediated proteasomal degradation of PIM is prevented by HSP90 (Mizuno et al., 2001). PIM1 protein stability is further regulated by its phosphorylation status. PIM1 is able to autophosphorylate (Bullock et al., 2005). Phosphorylation by itself and/or other unknown kinases is important for PIM1 protein stability and function because PP2A phosphatase negatively regulates PIM1 stability (Losman et al., 2003).
Localisation PIM1 is highly expressed in lymphoid and hematopoietic tissues (bone marrow, thymus, spleen, and fetal liver) (Eichmann et al., 2000) as well as in some non-hematopoietic tissues (e.g., hippocampus, oral epithelium, and the prostate gland). In some myeloid and lymphoid leukemia cell lines, prostate cancer cell lines, and also HeLa cells, PIM have also been detected. The PIM1 protein can be detected subcellularly in the cytoplasm and the nucleus.
Function PIM1 phosphorylates a large subset of cellular substrates and thus regulates many different cellular processes such as cell cycle progression, cellular division, differentiation and apoptosis.
One of the cell-cycle-related targets of PIM1 is p21waf1 (Wang et al., 2002; Zhang et al., 2007). By phosphorylating the CDK inhibitor p21waf1 on T145, PIM1 lead to the nuclear export and inactivation of p21waf1. Phosphorylation of another CDK inhibitor p27Kip1 at Thr157 and Thr198 would induce its proteasomal degradation and cell cycle progression. Moreover, PIM1 seems to phosphorylate and inactivate the transcription factors of p27Kip1, FoxO1a and FoxO3a (Morishita et al., 2008). Another mechanism of p27Kip1 regulation is the phosphorylation of SKP2 at Thr417, which control its stability and ability to degrade p27 (Cen et al., 2010). Additionally, the phosphorylation of Cdc25A and Cdc25C would induce G1/S and G2/M transition, respectively (Bachmann et al., 2004). PIM1 also implicate in mitosis promotion by interacts with dynein/dynactin and HP1β (Magnuson et al., 2010).
Moreover, PIM1 is involved in genomic instability. By interaction with NuMA (nuclear mitotic apparatus protein), overexpression of PIM1 causes the loss of checkpoint control (Bhattacharya et al., 2002). Consequently, cells with abnormal mitotic spindles are not arrested in mitosis, producing polyploid and multinucleated daughter cells.
PIM1 can also act as an oncogenic survival factor because of its function in blocking apoptotic cell death. It is consensus that phosphorylation of BAD at S112 would induce its proteasomal degradation and thus shifts the apoptosis threshold (Peltola et al., 2004). The proapoptotic activity of ASK1 and PRAS40 would also be impaired by PIM1 phosphorylation (Gu et al., 2009; Zhang et al., 2009). Through inactivation of ASK1 and subsequently less phosphorylation of the stress kinases JNK and p38, caspase-3 activation would be less and thus reduce cell death. Moreover, the block of MDM2 and p53 degradation by PIM1 may induce senescence in embryonic fibroblasts and cancer cells (Hogan et al., 2008).
When bound to MYC at the E-box, PIM1 would participate in the complex's phosphorylation of histone H3 at S10 and thus participate in the stimulation of transcription of a specific subset of MYC-dependent genes (Zippo et al., 2007).
Additionally, PIM1 influences the activity of a number of transcriptional regulators, such as HP-1, PAP-1, TFAF2/SNX6, NFATc1, p100, RUNX, SOCS1, RelA/p65 and c-Myb (Bhattacharya et al., 2002; Evans and Fox, 2007; Ishibashi et al., 2001; Kim et al., 2010; Rainio et al., 2002; Winn et al., 2003).
PIM kinases also phosphorylate 4E-BP1, inhibiting its binding to elF-4E. Since elF-4E is a rate-limiting factor in protein synthesis, PIM kinases may also regulate 5' cap-dependent translation (Beharry et al., 2011).

Implicated in

Note
Entity t(3;6)(q27;p21.2) in diffuse large B-cell lymphoma (DLCL); chimeric BCL6 / PIM1
Note Only 1 case to date.
Hybrid/Mutated Gene 5' PIM1 fused to 3' BCL6; the substitution of the promoter of BCL6 causes deregulation of BCL6.
  
Entity Myeloid and lymphoid leukemias and other lymphomas
Oncogenesis PIM1 induces anti-apoptotic oncogenes such as BCR/ABL, FLT2, CBL or JAK2 (Adam et al., 2006; Mizuki et al., 2003; Naramura et al., 2011; Nieborowska-Skorska et al., 2002; Wernig et al., 2008). PIM1 mRNA is upregulated in acute myeloid leukemia (AML) along with MLL gene rearrangements, e.g., MLL/AF9 or MLL/ENL (Chen et al., 2008). The reason for PIM1 levels increase seems to be the constitutive activation of FLT3 or Hoxa9 (Hu et al., 2007). Additionally, PIM1 also involve in the several B-cell developmental disorders that are related to Kaposi sarcoma associated herpesvirus (KSHV) or the Epstein-Barr virus (EBV) (Bajaj et al., 2006; Cheng et al., 2009).
  
Entity Prostate cancer
Prognosis In more half of the prostate cancer samples, PIM1 is showed a relatively overexpression compared to benign lesions and the expression elevation correlated with a poor therapeutic outcome (Dhanasekaran et al., 2001).
Oncogenesis In mouse model, the synergistic effects of PIM1 and MYC showed obvious co-regulation in prostate cancer. The molecular mechanism for the oncogenic activity might because PIM1 phosphorylation of c-MYC would increase its half-life and also because PIM1 enhancement of transcriptional activity of c-MYC (Chen et al., 2009b; Mumenthaler et al., 2009). Moreover, PIM1 kinase is related to chemoresistance in prostate cancer cells, which is related to relatively aggressive or hormone-refractory prostate cancers. The high level of expression of PIM1 in high grade prostate intraepithelial neoplasia may indicate a role of PIM1 in the early prostate carcinogenesis. PIM1 is also found to be upregulated in patients undergoing androgen ablation therapy (van der Poel et al., 2010).
  
Entity Pancreatic cancer
Note Hypoxia-promoted genetic instability
Oncogenesis PIM1 increases in hypoxic condition, independently of HIF-1α (Reiser-Erkan et al., 2008). It is now proposed as a prognostic marker. Increase in PIM1 expression may partly account for resistance to chemotherapy.
  
Entity Sporadic malignant tumors
Oncogenesis Overexpression of PIM1 is founded in gastric carcinoma, squamous cell carcinoma, colorectal carcinoma, liver carcinoma (Shah et al., 2008), liposarcoma (Nga et al., 2010), and bladder cancer (Guo et al., 2010).
  

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KSHV reactivation from latency requires Pim-1 and Pim-3 kinases to inactivate the latency-associated nuclear antigen LANA.
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PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis.
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Hypoxia-inducible mir-210 regulates normoxic gene expression involved in tumor initiation.
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PMID 19782034
 
Pharmacologic inhibition of Pim kinases alters prostate cancer cell growth and resensitizes chemoresistant cells to taxanes.
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PMID 19825806
 
PIM1 protein kinase regulates PRAS40 phosphorylation and mTOR activity in FDCP1 cells.
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PMID 19276681
 
Regulation of Skp2 levels by the Pim-1 protein kinase.
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PMID 20663873
 
miR-328 functions as an RNA decoy to modulate hnRNP E2 regulation of mRNA translation in leukemic blasts.
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PMID 20211135
 
Overexpression of Pim-1 in bladder cancer.
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PMID 21143989
 
Pim-1 regulates RANKL-induced osteoclastogenesis via NF-?B activation and NFATc1 induction.
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PMID 21068407
 
Why target PIM1 for cancer diagnosis and treatment?
Magnuson NS, Wang Z, Ding G, Reeves R.
Future Oncol. 2010 Sep;6(9):1461-78. doi: 10.2217/fon.10.106. (REVIEW)
PMID 20919829
 
PIM-1 kinase expression in adipocytic neoplasms: diagnostic and biological implications.
Nga ME, Swe NN, Chen KT, Shen L, Lilly MB, Chan SP, Salto-Tellez M, Das K.
Int J Exp Pathol. 2010 Feb;91(1):34-43. doi: 10.1111/j.1365-2613.2009.00673.x. Epub 2009 Oct 28.
PMID 19878356
 
Pim1 regulates androgen-dependent survival signaling in prostate cancer cells.
van der Poel HG, Zevenhoven J, Bergman AM.
Urol Int. 2010;84(2):212-20. doi: 10.1159/000277601. Epub 2010 Mar 4.
PMID 20215828
 
The Pim protein kinases regulate energy metabolism and cell growth.
Beharry Z, Mahajan S, Zemskova M, Lin YW, Tholanikunnel BG, Xia Z, Smith CD, Kraft AS.
Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):528-33. doi: 10.1073/pnas.1013214108. Epub 2010 Dec 27.
PMID 21187426
 
ERG deregulation induces PIM1 over-expression and aneuploidy in prostate epithelial cells.
Magistroni V, Mologni L, Sanselicio S, Reid JF, Redaelli S, Piazza R, Viltadi M, Bovo G, Strada G, Grasso M, Gariboldi M, Gambacorti-Passerini C.
PLoS One. 2011;6(11):e28162. doi: 10.1371/journal.pone.0028162. Epub 2011 Nov 30.
PMID 22140532
 
Mutant Cbl proteins as oncogenic drivers in myeloproliferative disorders.
Naramura M, Nadeau S, Mohapatra B, Ahmad G, Mukhopadhyay C, Sattler M, Raja SM, Natarajan A, Band V, Band H.
Oncotarget. 2011 Mar;2(3):245-50.
PMID 21422499
 
IL-6 stimulates STAT3 and Pim-1 kinase in pancreatic cancer cell lines.
Block KM, Hanke NT, Maine EA, Baker AF.
Pancreas. 2012 Jul;41(5):773-81. doi: 10.1097/MPA.0b013e31823cdd10.
PMID 22273698
 
The proto-oncogene Pim-1 is a target of miR-33a.
Thomas M, Lange-Grunweller K, Weirauch U, Gutsch D, Aigner A, Grunweller A, Hartmann RK.
Oncogene. 2012 Feb 16;31(7):918-28. doi: 10.1038/onc.2011.278. Epub 2011 Jul 11.
PMID 21743487
 

Citation

This paper should be referenced as such :
Yeung, SCJ
PIM1 (pim-1 oncogene)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(10):704-708.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/PIM1ID261.html
History of this paper:
Huret, JL. PIM1 (pim-1 oncogene). Atlas Genet Cytogenet Oncol Haematol. 2000;4(4):183-184.
http://documents.irevues.inist.fr/bitstream/handle/2042/37662/08-2000-PIM1ID261.pdf


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 3 ]
  3q27 rearrangements (BCL6) in non Hodgkin lymphoma;t(3;Var)(q27;Var) in non Hodgkin lymphoma
Hodgkin lymphoma
t(3;6)(q27;p21) PIM1/BCL6

External links

Nomenclature
HGNC (Hugo)PIM1   8986
Cards
AtlasPIM1ID261
Entrez_Gene (NCBI)PIM1  5292  Pim-1 proto-oncogene, serine/threonine kinase
AliasesPIM
GeneCards (Weizmann)PIM1
Ensembl hg19 (Hinxton)ENSG00000137193 [Gene_View]  chr6:37137922-37143204 [Contig_View]  PIM1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000137193 [Gene_View]  chr6:37137922-37143204 [Contig_View]  PIM1 [Vega]
ICGC DataPortalENSG00000137193
TCGA cBioPortalPIM1
AceView (NCBI)PIM1
Genatlas (Paris)PIM1
WikiGenes5292
SOURCE (Princeton)PIM1
Genomic and cartography
GoldenPath hg19 (UCSC)PIM1  -     chr6:37137922-37143204 +  6p21   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)PIM1  -     6p21   [Description]    (hg38-Dec_2013)
EnsemblPIM1 - 6p21 [CytoView hg19]  PIM1 - 6p21 [CytoView hg38]
Mapping of homologs : NCBIPIM1 [Mapview hg19]  PIM1 [Mapview hg38]
OMIM164960   
Gene and transcription
Genbank (Entrez)AK301158 AK301314 AK309347 BC020224 DA434260
RefSeq transcript (Entrez)NM_001243186 NM_002648
RefSeq genomic (Entrez)NC_000006 NC_018917 NG_029601 NT_007592 NW_004929326
Consensus coding sequences : CCDS (NCBI)PIM1
Cluster EST : UnigeneHs.81170 [ NCBI ]
CGAP (NCI)Hs.81170
Alternative Splicing GalleryENSG00000137193
Gene ExpressionPIM1 [ NCBI-GEO ]   PIM1 [ EBI - ARRAY_EXPRESS ]   PIM1 [ SEEK ]   PIM1 [ MEM ]
Gene Expression Viewer (FireBrowse)PIM1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5292
GTEX Portal (Tissue expression)PIM1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP11309 (Uniprot)
NextProtP11309  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP11309
Splice isoforms : SwissVarP11309 (Swissvar)
PhosPhoSitePlusP11309
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)Kinase-like_dom    PIM1/2/3    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_dual-sp_kinase    Ser/Thr_kinase_AS   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Domain families : Smart (EMBL)S_TKc (SM00220)  
DMDM Disease mutations5292
Blocks (Seattle)PIM1
PDB (SRS)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
PDB (PDBSum)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
PDB (IMB)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
PDB (RSDB)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
Structural Biology KnowledgeBase1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
SCOP (Structural Classification of Proteins)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
CATH (Classification of proteins structures)1XQZ    1XR1    1XWS    1YHS    1YI3    1YI4    1YWV    1YXS    1YXT    1YXU    1YXV    1YXX    2BIK    2BIL    2BZH    2BZI    2BZJ    2BZK    2C3I    2J2I    2O3P    2O63    2O64    2O65    2OBJ    2OI4    2XIX    2XIY    2XIZ    2XJ0    2XJ1    2XJ2    3A99    3BGP    3BGQ    3BGZ    3BWF    3C4E    3CXW    3CY2    3CY3    3DCV    3F2A    3JPV    3JXW    3JY0    3JYA    3MA3    3QF9    3R00    3R01    3R02    3R04    3T9I    3UIX    3UMW    3UMX    3VBQ    3VBT    3VBV    3VBW    3VBX    3VBY    3VC4    3WE8    4A7C    4ALU    4ALV    4ALW    4AS0    4BZN    4BZO    4DTK    4ENX    4ENY    4GW8    4I41    4IAA    4JX3    4JX7    4K0Y    4K18    4K1B    4LL5    4LM5    4LMU    4MBI    4MBL    4MED    4MTA    4N6Y    4N6Z    4N70    4RBL    4RC2    4RC3    4RC4    4RPV    4TY1    4WRS    4WSY    4WT6    4XH6    4XHK    5C1Q    5DGZ    5DHJ    5DIA    5DWR   
SuperfamilyP11309
Human Protein AtlasENSG00000137193
Peptide AtlasP11309
HPRD01292
IPIIPI00005014   IPI00745060   
Protein Interaction databases
DIP (DOE-UCLA)P11309
IntAct (EBI)P11309
FunCoupENSG00000137193
BioGRIDPIM1
STRING (EMBL)PIM1
ZODIACPIM1
Ontologies - Pathways
QuickGOP11309
Ontology : AmiGOprotein serine/threonine kinase activity  protein binding  ATP binding  nucleus  cytoplasm  plasma membrane  protein phosphorylation  apoptotic process  cell cycle  multicellular organism development  transcription factor binding  cell proliferation  manganese ion binding  hyaluronan metabolic process  positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle  ribosomal small subunit binding  negative regulation of apoptotic process  negative regulation of sequence-specific DNA binding transcription factor activity  protein autophosphorylation  protein autophosphorylation  vitamin D receptor signaling pathway  
Ontology : EGO-EBIprotein serine/threonine kinase activity  protein binding  ATP binding  nucleus  cytoplasm  plasma membrane  protein phosphorylation  apoptotic process  cell cycle  multicellular organism development  transcription factor binding  cell proliferation  manganese ion binding  hyaluronan metabolic process  positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle  ribosomal small subunit binding  negative regulation of apoptotic process  negative regulation of sequence-specific DNA binding transcription factor activity  protein autophosphorylation  protein autophosphorylation  vitamin D receptor signaling pathway  
Pathways : KEGGJak-STAT signaling pathway    MicroRNAs in cancer    Acute myeloid leukemia   
NDEx Network
Atlas of Cancer Signalling NetworkPIM1
Wikipedia pathwaysPIM1
Orthology - Evolution
OrthoDB5292
GeneTree (enSembl)ENSG00000137193
Phylogenetic Trees/Animal Genes : TreeFamPIM1
Homologs : HomoloGenePIM1
Homology/Alignments : Family Browser (UCSC)PIM1
Gene fusions - Rearrangements
Fusion : MitelmanBCL6/PIM1 [3q27.3/6p21.2]  [t(3;6)(q27;p21)]  
Fusion : MitelmanPIM1/BCL6 [6p21.2/3q27.3]  [t(3;6)(q27;p21)]  
Fusion : TICdbPIM1 [6p21.2]  -  BCL6 [3q27.3]
Polymorphisms : SNP, variants
NCBI Variation ViewerPIM1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PIM1
dbVarPIM1
ClinVarPIM1
1000_GenomesPIM1 
Exome Variant ServerPIM1
ExAC (Exome Aggregation Consortium)PIM1 (select the gene name)
Genetic variants : HAPMAP5292
Genomic Variants (DGV)PIM1 [DGVbeta]
Mutations
ICGC Data PortalPIM1 
TCGA Data PortalPIM1 
Broad Tumor PortalPIM1
OASIS PortalPIM1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPIM1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch PIM1
DgiDB (Drug Gene Interaction Database)PIM1
DoCM (Curated mutations)PIM1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PIM1 (select a term)
intoGenPIM1
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)6:37137922-37143204  ENSG00000137193
CONAN: Copy Number AnalysisPIM1 
Mutations and Diseases : HGMDPIM1
OMIM164960   
MedgenPIM1
Genetic Testing Registry PIM1
NextProtP11309 [Medical]
TSGene5292
GENETestsPIM1
Huge Navigator PIM1 [HugePedia]
snp3D : Map Gene to Disease5292
BioCentury BCIQPIM1
ClinGenPIM1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5292
Chemical/Pharm GKB GenePA33318
Clinical trialPIM1
Miscellaneous
canSAR (ICR)PIM1 (select the gene name)
Probes
Litterature
PubMed178 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePIM1
EVEXPIM1
GoPubMedPIM1
iHOPPIM1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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