Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002186
UniProt IDP11309
Primary gene name(s)PIM1
Synonym gene name(s)unknown
Protein nameSerine/threonine-protein kinase pim-1
Protein functionProto-oncogene with serine/threonine kinase activity 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 exerted 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 MAP3K5, an other 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. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. 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. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,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. {ECO:0000269|PubMed:10664448, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19749799}.
Subcellular locationIsoform 2: Cytoplasm. Nucleus.;
SUBCELLULAR LOCATION: Isoform 1: Cell membrane.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P11309
Gene Ontology
(Biological Process)
Complete annatation
apoptotic process [GO:0006915];
cell cycle [GO:0007049];
cell proliferation [GO:0008283];
hyaluronan metabolic process [GO:0030212];
multicellular organism development [GO:0007275];
negative regulation of apoptotic process [GO:0043066];
negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433];
positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659];
protein autophosphorylation [GO:0046777];
protein phosphorylation [GO:0006468];
vitamin D receptor signaling pathway [GO:0070561]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
manganese ion binding [GO:0030145];
protein serine/threonine kinase activity [GO:0004674];
ribosomal small subunit binding [GO:0043024];
transcription factor binding [GO:0008134]
Gene Ontology
(Cellular Component)
Complete annatation
cytoplasm [GO:0005737];
nucleus [GO:0005634];
plasma membrane [GO:0005886]
Protein-protein interaction111310
Phylogenetic treeP11309
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model

DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD3-2.747640226716433.77475828372553e-151.32927936570821e-13
AZA vs. DISU-0.3857203262149770.1279276914692850.693662597556833
AZA vs. IL70.7472651520693850.0001036990820665330.0156305626398885
AZA vs. SAHA-0.7302192107527510.004178657649224540.0547255303252916
DISU vs. CD32.349858062328946.33270214045467e-101.34071842788222e-08
DISU vs. IL71.123468139557781.06645650538306e-050.000923955851646532
DISU vs. SAHA-0.3414420068734740.2494385574212050.627401139043233
DMSO vs. AZA0.05377224255942570.7526524275108341
DMSO vs. CD32.793220266043533.33066907387547e-161.17234882238163e-14
DMSO vs. DISU0.4387974010110720.07274514745900350.5026452875778
DMSO vs. IL70.7002264262255819.92139987142648e-050.0118702462747424
DMSO vs. SAHA-0.7896943230354680.001684645262959860.0259339006721839
HIV vs. Mock in Activation0.4139868897955980.507629100005390.999983755607037
HIV vs. Mock in Latency-0.04942100247170670.9178752625051850.999834320637052
IL7 vs. CD33.5002687960683400
SAHA vs. CD31.995712977446636.67130104492486e-087.35453597271526e-07
SAHA vs. IL7-1.4788719888932.66008737259682e-092.78459423989753e-07
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) TRUE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.687883 0.000305467
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
unknown unknown unknown unknown unknown
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB01754 3,4-Dihydroxy-1-Methylquinolin-2(1h)-One experimental unknown unknown
DB00131 Adenosine monophosphate approved, nutraceutical unknown product of
DB02010 Staurosporine experimental unknown unknown
DB02656 2-(4-Morpholinyl)-8-Phenyl-4h-1-Benzopyran-4-One experimental unknown unknown
DB03650 (3e)-3-[(4-Hydroxyphenyl)Imino]-1h-Indol-2(3h)-One experimental unknown unknown
DB03777 Rbt205 Inhibitor experimental unknown unknown
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester experimental unknown unknown
DB04522 Phosphonoserine experimental unknown unknown
DB04530 S,S-(2-Hydroxyethyl)Thiocysteine experimental unknown unknown
DB04715 IMIDAZOPYRIDAZIN 1 experimental unknown unknown
DB07151 4-(4-hydroxy-3-methylphenyl)-6-phenylpyrimidin-2(5H)-one experimental unknown unknown
DB07524 N-phenyl-1H-pyrrolo[2,3-b]pyridin-3-amine experimental unknown unknown
DB08022 (2S)-1,3-benzothiazol-2-yl{2-[(2-pyridin-3-ylethyl)amino]pyrimidin-4-yl}ethanenitrile experimental unknown unknown
DB07242 (4R)-7,8-dichloro-1&,39;,9-dimethyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4&,39;-piperidine]-4-carbonitrile experimental unknown unknown
DB08166 (4R)-7-chloro-9-methyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4&,39;-piperidine]-4-carbonitrile experimental unknown unknown
DB08230 5,7-DIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE experimental unknown unknown
DB04216 Quercetin experimental unknown unknown
DB08705 6-(5-BROMO-2-HYDROXYPHENYL)-2-OXO-4-PHENYL-1,2-DIHYDROPYRIDINE-3-CARBONITRILE experimental unknown unknown
DB08707 4-[3-(4-chlorophenyl)-2,1-benzisoxazol-5-yl]pyrimidin-2-amine experimental unknown unknown
DB08708 N-cyclohexyl-3-[3-(trifluoromethyl)phenyl][1,2,4]triazolo[4,3-b]pyridazin-6-amine experimental unknown unknown
DB08709 2,3-diphenyl-1H-indole-7-carboxylic acid experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1XQZ X-ray 2.1Å A=105-404.
1XR1 X-ray 2.1Å A=105-404.
1XWS X-ray 1.8Å A=92-404.
1YHS X-ray 2.1Å A=124-396.
1YI3 X-ray 2.5Å A=124-396.
1YI4 X-ray 2.4Å A=124-396.
1YWV X-ray 2.0Å A=120-404.
1YXS X-ray 2.2Å A=120-404.
1YXT X-ray 2.0Å A=120-404.
1YXU X-ray 2.2Å A/B/C/D=120-404.
1YXV X-ray 2.0Å A=120-404.
1YXX X-ray 2.0Å A=120-404.
2BIK X-ray 1.8Å B=92-404.
2BIL X-ray 2.5Å B=92-404.
2BZH X-ray 1.9Å B=92-404.
2BZI X-ray 1.9Å B=92-404.
2BZJ X-ray 2.0Å A=92-404.
2BZK X-ray 2.4Å B=92-404.
2C3I X-ray 1.9Å B=92-404.
2J2I X-ray 1.9Å B=92-403.
2O3P X-ray 2.2Å A=120-404.
2O63 X-ray 2.0Å A=120-404.
2O64 X-ray 2.4Å A=120-404.
2O65 X-ray 2.8Å A=120-404.
2OBJ X-ray 2.5Å A=92-404.
2OI4 X-ray 2.2Å X=92-404.
2XIX X-ray 2.4Å A=105-404.
2XIY X-ray 2.2Å A=105-404.
2XIZ X-ray 2.2Å A=105-404.
2XJ0 X-ray 3.1Å A=105-404.
2XJ1 X-ray 2.1Å A=105-404.
2XJ2 X-ray 2.2Å A=105-404.
3A99 X-ray 1.6Å A=106-404.
3BGP X-ray 2.8Å A=92-404.
3BGQ X-ray 2.0Å A=92-404.
3BGZ X-ray 2.4Å A=92-404.
3BWF X-ray 2.3Å A=92-404.
3C4E X-ray 1.9Å A/B/C/D=124-396.
3CXW X-ray 2.1Å A=92-404.
3CY2 X-ray 2.0Å A=92-404.
3CY3 X-ray 2.1Å A=92-404.
3DCV X-ray 2.7Å A=93-404.
3F2A X-ray 1.9Å A=105-404.
3JPV X-ray 2.3Å A=92-403.
3JXW X-ray 2.8Å A=120-404.
3JY0 X-ray 2.4Å A=120-404.
3JYA X-ray 2.1Å A=120-404.
3MA3 X-ray 2.3Å A=93-403.
3QF9 X-ray 2.2Å A=92-403.
3R00 X-ray 2.1Å A=120-404.
3R01 X-ray 2.6Å A=120-404.
3R02 X-ray 1.9Å A=120-404.
3R04 X-ray 1.7Å A=120-404.
3T9I X-ray 2.6Å A=93-404.
3UIX X-ray 2.2Å A=120-404.
3UMW X-ray 2.0Å A=120-404.
3UMX X-ray 2.5Å A=120-404.
3VBQ X-ray 1.8Å A=120-404.
3VBT X-ray 2.2Å A=120-404.
3VBV X-ray 2.0Å A=120-404.
3VBW X-ray 2.4Å A=120-404.
3VBX X-ray 2.0Å A=120-404.
3VBY X-ray 2.2Å A=120-404.
3VC4 X-ray 2.2Å A=120-404.
3WE8 X-ray 1.9Å A=124-396.
4A7C X-ray 2.3Å A=121-404.
4ALU X-ray 2.6Å A=93-404.
4ALV X-ray 2.5Å A=93-404.
4ALW X-ray 1.9Å A=93-404.
4AS0 X-ray 2.3Å A=124-396.
4BZN X-ray 1.9Å A=93-404.
4BZO X-ray 2.1Å A=93-404.
4DTK X-ray 1.8Å A=121-396.
4ENX X-ray 2.8Å A=120-404.
4ENY X-ray 2.8Å A=120-404.
4GW8 X-ray 2.0Å A=92-403.
4I41 X-ray 2.7Å A=120-396.
4IAA X-ray 2.8Å A=120-404.
4JX3 X-ray 2.5Å A=92-404.
4JX7 X-ray 2.4Å A=92-404.
4K0Y X-ray 1.9Å A=124-397.
4K18 X-ray 2.0Å A=123-399.
4K1B X-ray 2.0Å A=124-396.
4LL5 X-ray 2.0Å A=120-404.
4LM5 X-ray 2.2Å A=120-404.
4LMU X-ray 2.3Å A=120-404.
4MBI X-ray 2.3Å A=120-404.
4MBL X-ray 2.6Å A=120-404.
4MED X-ray 2.8Å A=120-404.
4MTA X-ray 2.2Å A=119-404.
4N6Y X-ray 2.6Å A=93-404.
4N6Z X-ray 2.2Å A=93-404.
4N70 X-ray 2.1Å A=93-404.
4RBL X-ray 2.5Å A=120-404.
4RC2 X-ray 2.1Å A=120-404.
4RC3 X-ray 2.3Å A=120-404.
4RC4 X-ray 2.6Å A=120-404.
4RPV X-ray 3.0Å A=1-404.
4TY1 X-ray 2.7Å A=124-396.
4WRS X-ray 2.2Å A=124-396.
4WSY X-ray 2.3Å A=124-396.
4WT6 X-ray 2.3Å A=124-396.
4XH6 X-ray 2.0Å A=120-404.
4XHK X-ray 1.9Å B=92-404.
5C1Q X-ray 3.0Å B=120-404.
5DGZ X-ray 2.5Å A=120-404.
5DHJ X-ray 2.4Å A=120-404.
5DIA X-ray 1.9Å A=120-404.
5DWR X-ray 2.0Å A=93-404.
5EOL X-ray 2.2Å A=124-396.
5IIS X-ray 2.1Å A=123-399.
5IPJ X-ray 2.1Å A=124-396.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Tat upregulates 23898208

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04630 Jak-STAT signaling pathway - Homo sapiens (human)
hsa04933 AGE-RAGE signaling pathway in diabetic complications - Homo sapiens (human)
hsa05206 MicroRNAs in cancer - Homo sapiens (human)
hsa05221 Acute myeloid leukemia - Homo sapiens (human)