ID PIM1_HUMAN Reviewed; 313 AA. AC P11309; Q38RT9; Q5T7H7; Q96RG3; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2018, sequence version 4. DT 27-MAR-2024, entry version 255. DE RecName: Full=Serine/threonine-protein kinase pim-1; DE EC=2.7.11.1 {ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054, ECO:0000269|PubMed:15808862, ECO:0000269|PubMed:31548394}; GN Name=PIM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=2205533; DOI=10.1016/0378-1119(90)90195-w; RA Reeves R., Spies G.A., Kiefer M., Barr P.J., Power M.; RT "Primary structure of the putative human oncogene, pim-1."; RL Gene 90:303-307(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3475233; DOI=10.1016/0378-1119(87)90352-0; RA Zakut-Houri R., Hazum S., Givol D., Telerman A.; RT "The cDNA sequence and gene analysis of the human pim oncogene."; RL Gene 54:105-111(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3329709; RA Domen J., von Lindern M., Hermans A., Breuer M., Grosveld G., Berns A.; RT "Comparison of the human and mouse PIM-1 cDNAs: nucleotide sequence and RT immunological identification of the in vitro synthesized PIM-1 protein."; RL Oncogene Res. 1:103-112(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3429489; DOI=10.1002/jcb.240350204; RA Meeker T.C., Nagarajan L., Ar-Rushdi A., Croce C.M.; RT "Cloning and characterization of the human PIM-1 gene: a putative oncogene RT related to the protein kinases."; RL J. Cell. Biochem. 35:105-112(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE INITIATION, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH BMX. RX PubMed=16186805; DOI=10.1038/sj.onc.1209058; RA Xie Y., Xu K., Dai B., Guo Z., Jiang T., Chen H., Qiu Y.; RT "The 44 kDa Pim-1 kinase directly interacts with tyrosine kinase Etk/BMX RT and protects human prostate cancer cells from apoptosis induced by RT chemotherapeutic drugs."; RL Oncogene 25:70-78(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-202 (ISOFORM 1). RX PubMed=11460166; DOI=10.1038/35085588; RA Pasqualucci L., Neumeister P., Goossens T., Nanjangud G., Chaganti R.S.K., RA Kuppers R., Dalla-Favera R.; RT "Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell RT lymphomas."; RL Nature 412:341-346(2001). RN [10] RP CHARACTERIZATION. RX PubMed=2837645; DOI=10.1128/mcb.8.4.1498-1503.1988; RA Telerman A., Amson R., Zakut-Houri R., Givol D.; RT "Identification of the human pim-1 gene product as a 33-kilodalton RT cytoplasmic protein with tyrosine kinase activity."; RL Mol. Cell. Biol. 8:1498-1503(1988). RN [11] RP FUNCTION, AND ALTERNATIVE INITIATION. RX PubMed=1825810; DOI=10.1002/j.1460-2075.1991.tb07994.x; RA Saris C.J., Domen J., Berns A.; RT "The pim-1 oncogene encodes two related protein-serine/threonine kinases by RT alternative initiation at AUG and CUG."; RL EMBO J. 10:655-664(1991). RN [12] RP FUNCTION IN PHOSPHORYLATION OF CBX3. RX PubMed=10664448; DOI=10.1016/s0014-5793(00)01105-4; RA Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.; RT "Identification of heterochromatin protein 1 (HP1) as a phosphorylation RT target by Pim-1 kinase and the effect of phosphorylation on the RT transcriptional repression function of HP1."; RL FEBS Lett. 467:17-21(2000). RN [13] RP SUBCELLULAR LOCATION, AND FUNCTION IN PHOSPHORYLATION OF CDKN1A. RX PubMed=12431783; DOI=10.1016/s0167-4889(02)00347-6; RA Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J., Magnuson N.S.; RT "Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 RT kinase."; RL Biochim. Biophys. Acta 1593:45-55(2002). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=12680209; RA Ionov Y., Le X., Tunquist B.J., Sweetenham J., Sachs T., Ryder J., RA Johnson T., Lilly M.B., Kraft A.S.; RT "Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear RT localization is necessary for its biologic effects."; RL Anticancer Res. 23:167-178(2003). RN [15] RP PHOSPHORYLATION, AND UBIQUITINATION. RX PubMed=12473674; DOI=10.1074/jbc.m208246200; RA Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.; RT "Protein phosphatase 2A regulates the stability of Pim protein kinases."; RL J. Biol. Chem. 278:4800-4805(2003). RN [16] RP FUNCTION, AND INDUCTION. RX PubMed=15528381; DOI=10.4049/jimmunol.173.10.6409; RA Stout B.A., Bates M.E., Liu L.Y., Farrington N.N., Bertics P.J.; RT "IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 RT and STAT5 and promote Pim-1 and cyclin D3 protein expression in human RT eosinophils."; RL J. Immunol. 173:6409-6417(2004). RN [17] RP UBIQUITINATION, INTERACTION WITH HSP90AA1 AND HSP70, AND INDUCTION. RX PubMed=15798097; DOI=10.1158/1541-7786.mcr-04-0192; RA Shay K.P., Wang Z., Xing P.X., McKenzie I.F., Magnuson N.S.; RT "Pim-1 kinase stability is regulated by heat shock proteins and the RT ubiquitin-proteasome pathway."; RL Mol. Cancer Res. 3:170-181(2005). RN [18] RP FUNCTION IN PHOSPHORYLATION OF CDC25C, AND INTERACTION WITH CDC25C. RX PubMed=16356754; DOI=10.1016/j.biocel.2005.10.010; RA Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.; RT "The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and RT activates the G2/M specific phosphatase Cdc25C."; RL Int. J. Biochem. Cell Biol. 38:430-443(2006). RN [19] RP FUNCTION IN CELL CYCLE PROGRESSION, AND PHOSPHORYLATION OF CDKN1B AND RP FOXO3. RX PubMed=18593906; DOI=10.1158/0008-5472.can-08-0634; RA Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.; RT "Pim kinases promote cell cycle progression by phosphorylating and down- RT regulating p27Kip1 at the transcriptional and posttranscriptional levels."; RL Cancer Res. 68:5076-5085(2008). RN [20] RP FUNCTION. RX PubMed=18056989; DOI=10.1074/jbc.m707773200; RA Xie Y., Xu K., Linn D.E., Yang X., Guo Z., Shimelis H., Nakanishi T., RA Ross D.D., Chen H., Fazli L., Gleave M.E., Qiu Y.; RT "The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its RT multimerization and drug-resistant activity in human prostate cancer RT cells."; RL J. Biol. Chem. 283:3349-3356(2008). RN [21] RP FUNCTION IN PHOSPHORYLATION OF MAP3K5. RX PubMed=19749799; DOI=10.1038/onc.2009.276; RA Gu J.J., Wang Z., Reeves R., Magnuson N.S.; RT "PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis."; RL Oncogene 28:4261-4271(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP INTERACTION WITH EPSTEIN-BARR VIRUS EBNA6 (MICROBIAL INFECTION). RX PubMed=25121590; DOI=10.1371/journal.ppat.1004304; RA Banerjee S., Lu J., Cai Q., Sun Z., Jha H.C., Robertson E.S.; RT "EBNA3C augments Pim-1 mediated phosphorylation and degradation of p21 to RT promote B-cell proliferation."; RL PLoS Pathog. 10:E1004304-E1004304(2014). RN [24] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=31548394; DOI=10.1073/pnas.1904774116; RA Padi S.K.R., Singh N., Bearss J.J., Olive V., Song J.H., Cardo-Vila M., RA Kraft A.S., Okumura K.; RT "Phosphorylation of DEPDC5, a component of the GATOR1 complex, releases RT inhibition of mTORC1 and promotes tumor growth."; RL Proc. Natl. Acad. Sci. U.S.A. 116:20505-20510(2019). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND MUTAGENESIS OF PRO-81. RX PubMed=37797010; DOI=10.1126/science.adg2253; RA Fisch D., Pfleiderer M.M., Anastasakou E., Mackie G.M., Wendt F., Liu X., RA Clough B., Lara-Reyna S., Encheva V., Snijders A.P., Bando H., Yamamoto M., RA Beggs A.D., Mercer J., Shenoy A.R., Wollscheid B., Maslowski K.M., RA Galej W.P., Frickel E.M.; RT "PIM1 controls GBP1 activity to limit self-damage and to guard against RT pathogen infection."; RL Science 382:eadg2253-eadg2253(2023). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 33-305 IN COMPLEXES WITH RP ADENOSINE AND INHIBITORS STAUROSPORINE AND LY294002, CATALYTIC ACTIVITY, RP COFACTOR, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND RP PHOSPHORYLATION AT SER-8; THR-23; SER-98 AND SER-261. RX PubMed=15657054; DOI=10.1074/jbc.m413155200; RA Jacobs M.D., Black J., Futer O., Swenson L., Hare B., Fleming M., RA Saxena K.; RT "Pim-1 ligand-bound structures reveal the mechanism of serine/threonine RT kinase inhibition by LY294002."; RL J. Biol. Chem. 280:13728-13734(2005). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 14-313 OF APOPROTEIN AND IN RP COMPLEX WITH AMP-PNP, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY RP REGULATION. RX PubMed=15525646; DOI=10.1074/jbc.m409123200; RA Qian K.C., Wang L., Hickey E.R., Studts J., Barringer K., Peng C., RA Kronkaitis A., Li J., White A., Mische S., Farmer B.; RT "Structural basis of constitutive activity and a unique nucleotide binding RT mode of human Pim-1 kinase."; RL J. Biol. Chem. 280:6130-6137(2005). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-313 OF APOPROTEIN AND IN RP COMPLEXES WITH AMP-PNP AND INHIBITORS, PARTIAL PROTEIN SEQUENCE, CATALYTIC RP ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND MUTAGENESIS OF HIS-68; PRO-81; RP ASN-82 AND LEU-193. RX PubMed=15808862; DOI=10.1016/j.jmb.2005.02.039; RA Kumar A., Mandiyan V., Suzuki Y., Zhang C., Rice J., Tsai J., Artis D.R., RA Ibrahim P., Bremer R.; RT "Crystal structures of proto-oncogene kinase Pim1: a target of aberrant RT somatic hypermutations in diffuse large cell lymphoma."; RL J. Mol. Biol. 348:183-193(2005). RN [29] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-53; GLN-124; LYS-135 AND ASP-142. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity involved CC in cell survival and cell proliferation and thus providing a selective CC advantage in tumorigenesis (PubMed:15528381, PubMed:1825810, CC PubMed:31548394). Exerts its oncogenic activity through: the regulation CC of MYC transcriptional activity, the regulation of cell cycle CC progression and by phosphorylation and inhibition of proapoptotic CC proteins (BAD, MAP3K5, FOXO3) (PubMed:18593906). Phosphorylation of MYC CC leads to an increase of MYC protein stability and thereby an increase CC of transcriptional activity (By similarity). The stabilization of MYC CC exerted by PIM1 might explain partly the strong synergism between these CC two oncogenes in tumorigenesis (By similarity). Mediates survival CC signaling through phosphorylation of BAD, which induces release of the CC anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation CC of MAP3K5, another proapoptotic protein, by PIM1, significantly CC decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated CC phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 CC activation and cell apoptosis (PubMed:19749799). Stimulates cell cycle CC progression at the G1-S and G2-M transitions by phosphorylation of CC CDC25A and CDC25C (PubMed:16356754). Phosphorylation of CDKN1A, a CC regulator of cell cycle progression at G1, results in the relocation of CC CDKN1A to the cytoplasm and enhanced CDKN1A protein stability CC (PubMed:12431783). Promotes cell cycle progression and tumorigenesis by CC down-regulating expression of a regulator of cell cycle progression, CC CDKN1B, at both transcriptional and post-translational levels CC (PubMed:18593906). Phosphorylation of CDKN1B, induces 14-3-3 proteins CC binding, nuclear export and proteasome-dependent degradation CC (PubMed:18593906). May affect the structure or silencing of chromatin CC by phosphorylating HP1 gamma/CBX3 (PubMed:10664448). Acts also as a CC regulator of homing and migration of bone marrow cells involving CC functional interaction with the CXCL12-CXCR4 signaling axis (By CC similarity). Acts as a positive regulator of mTORC1 signaling by CC mediating phosphorylation and inhibition of DEPDC5 component of the CC GATOR1 complex (PubMed:31548394). Acts as a negative regulator of CC innate immunity by mediating phosphorylation and inactivation of GBP1 CC in absence of infection: phosphorylation of GBP1 induces interaction CC with 14-3-3 protein sigma (SFN) and retention in the cytosol CC (PubMed:37797010). Also phosphorylates and activates the ATP-binding CC cassette transporter ABCG2, allowing resistance to drugs through their CC excretion from cells (PubMed:18056989). Promotes brown adipocyte CC differentiation (By similarity). {ECO:0000250|UniProtKB:P06803, CC ECO:0000269|PubMed:10664448, ECO:0000269|PubMed:12431783, CC ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:16356754, CC ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:1825810, CC ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19749799, CC ECO:0000269|PubMed:31548394, ECO:0000269|PubMed:37797010}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054, CC ECO:0000269|PubMed:15808862, ECO:0000269|PubMed:31548394, CC ECO:0000269|PubMed:37797010}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15525646, CC ECO:0000269|PubMed:15657054, ECO:0000269|PubMed:15808862, CC ECO:0000269|PubMed:37797010}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054, CC ECO:0000269|PubMed:15808862}; CC -!- SUBUNIT: Interacts with RP9 (By similarity). Interacts with HSP90AA1, CC this interaction stabilizes PIM1 protein levels (PubMed:15798097). CC Interacts (ubiquitinated form) with HSP70 and promotes its proteasomal CC degradation (PubMed:15798097). {ECO:0000250|UniProtKB:P06803, CC ECO:0000269|PubMed:15798097}. CC -!- SUBUNIT: [Isoform 1]: Isoform 1 is isolated as a monomer whereas CC isoform 2 complexes with other proteins. CC {ECO:0000250|UniProtKB:P06803}. CC -!- SUBUNIT: [Isoform 2]: Isoform 2, but not isoform 1, binds BMX. CC {ECO:0000269|PubMed:16186805}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA6; CC this interaction upregulates and stabilizes PIM1 and induces cell CC proliferation by inhibiting the growth suppressive properties of p21. CC {ECO:0000269|PubMed:25121590}. CC -!- INTERACTION: CC P11309; Q8N9N5: BANP; NbExp=3; IntAct=EBI-696621, EBI-744695; CC P11309; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-696621, EBI-10181188; CC P11309; P51813: BMX; NbExp=2; IntAct=EBI-696621, EBI-696657; CC P11309; P07954: FH; NbExp=3; IntAct=EBI-696621, EBI-1050358; CC P11309; P51116: FXR2; NbExp=3; IntAct=EBI-696621, EBI-740459; CC P11309; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-696621, EBI-5460660; CC P11309; Q5T203: NHLH1; NbExp=3; IntAct=EBI-696621, EBI-10197511; CC P11309; P39019: RPS19; NbExp=7; IntAct=EBI-696621, EBI-354451; CC P11309; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-696621, EBI-10178002; CC P11309; Q9Y2K1: ZBTB1; NbExp=3; IntAct=EBI-696621, EBI-2682961; CC P11309-1; P46527: CDKN1B; NbExp=2; IntAct=EBI-1018629, EBI-519280; CC P11309-1; O43524: FOXO3; NbExp=2; IntAct=EBI-1018629, EBI-1644164; CC P11309-1; Q9BZS1-1: FOXP3; NbExp=3; IntAct=EBI-1018629, EBI-9695448; CC P11309-2; Q9UNQ0: ABCG2; NbExp=5; IntAct=EBI-1018633, EBI-1569435; CC P11309-2; P51813: BMX; NbExp=6; IntAct=EBI-1018633, EBI-696657; CC P11309-2; P17252: PRKCA; NbExp=2; IntAct=EBI-1018633, EBI-1383528; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; Synonyms=Pim-1 {ECO:0000303|PubMed:18056989}; CC IsoId=P11309-1; Sequence=Displayed; CC Name=2; Synonyms=Pim-1L {ECO:0000303|PubMed:18056989}; CC IsoId=P11309-2; Sequence=VSP_059829; CC -!- TISSUE SPECIFICITY: Expressed primarily in cells of the hematopoietic CC and germline lineages. Isoform 1 and isoform 2 are both expressed in CC prostate cancer cell lines. {ECO:0000269|PubMed:16186805}. CC -!- INDUCTION: By interferon-gamma (IFNG) (PubMed:37797010). Strongly CC induced in leukocytes by the JAK/STAT pathway in response to cytokines. CC Induced by different cellular stresses, heat shock and cytotoxic agents CC (PubMed:15528381, PubMed:15798097, PubMed:16186805). CC {ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:15798097, CC ECO:0000269|PubMed:16186805, ECO:0000269|PubMed:37797010}. CC -!- PTM: Autophosphorylated on both serine/threonine and tyrosine residues. CC Phosphorylated. Interaction with PPP2CA promotes dephosphorylation. CC {ECO:0000269|PubMed:12473674}. CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. CC {ECO:0000269|PubMed:12473674, ECO:0000269|PubMed:15798097}. CC -!- MISCELLANEOUS: [Isoform 2]: Initiates from CTG codon. CC {ECO:0000269|PubMed:16186805, ECO:0000269|PubMed:1825810}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. PIM subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/261/PIM1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27903; AAA60090.1; -; Genomic_DNA. DR EMBL; M16750; AAA60089.1; -; mRNA. DR EMBL; M54915; AAA36447.1; -; mRNA. DR EMBL; M24779; AAA81553.1; -; mRNA. DR EMBL; DQ022562; AAY87461.1; -; mRNA. DR EMBL; AL353579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03934.1; -; Genomic_DNA. DR EMBL; BC020224; AAH20224.1; -; mRNA. DR EMBL; AF386792; AAK70871.1; -; Genomic_DNA. DR CCDS; CCDS4830.1; -. [P11309-1] DR PIR; JU0327; TVHUP1. DR RefSeq; NP_001230115.1; NM_001243186.1. [P11309-2] DR RefSeq; NP_002639.1; NM_002648.3. [P11309-1] DR PDB; 1XQZ; X-ray; 2.10 A; A=14-313. DR PDB; 1XR1; X-ray; 2.10 A; A=14-313. DR PDB; 1XWS; X-ray; 1.80 A; A=1-313. DR PDB; 1YHS; X-ray; 2.15 A; A=33-305. DR PDB; 1YI3; X-ray; 2.50 A; A=33-305. DR PDB; 1YI4; X-ray; 2.40 A; A=33-305. DR PDB; 1YWV; X-ray; 2.00 A; A=29-313. DR PDB; 1YXS; X-ray; 2.20 A; A=29-313. DR PDB; 1YXT; X-ray; 2.00 A; A=29-313. DR PDB; 1YXU; X-ray; 2.24 A; A/B/C/D=29-313. DR PDB; 1YXV; X-ray; 2.00 A; A=29-313. DR PDB; 1YXX; X-ray; 2.00 A; A=29-313. DR PDB; 2BIK; X-ray; 1.80 A; B=1-313. DR PDB; 2BIL; X-ray; 2.55 A; B=1-313. DR PDB; 2BZH; X-ray; 1.90 A; B=1-313. DR PDB; 2BZI; X-ray; 1.90 A; B=1-313. DR PDB; 2BZJ; X-ray; 2.05 A; A=1-313. DR PDB; 2BZK; X-ray; 2.45 A; B=1-313. DR PDB; 2C3I; X-ray; 1.90 A; B=1-313. DR PDB; 2J2I; X-ray; 1.90 A; B=1-312. DR PDB; 2O3P; X-ray; 2.24 A; A=29-313. DR PDB; 2O63; X-ray; 2.00 A; A=29-313. DR PDB; 2O64; X-ray; 2.44 A; A=29-313. DR PDB; 2O65; X-ray; 2.85 A; A=29-313. DR PDB; 2OBJ; X-ray; 2.50 A; A=1-313. DR PDB; 2OI4; X-ray; 2.20 A; X=1-313. DR PDB; 2XIX; X-ray; 2.40 A; A=14-313. DR PDB; 2XIY; X-ray; 2.20 A; A=14-313. DR PDB; 2XIZ; X-ray; 2.21 A; A=14-313. DR PDB; 2XJ0; X-ray; 3.10 A; A=14-313. DR PDB; 2XJ1; X-ray; 2.13 A; A=14-313. DR PDB; 2XJ2; X-ray; 2.20 A; A=14-313. DR PDB; 3A99; X-ray; 1.60 A; A=15-313. DR PDB; 3BGP; X-ray; 2.80 A; A=1-313. DR PDB; 3BGQ; X-ray; 2.00 A; A=1-313. DR PDB; 3BGZ; X-ray; 2.40 A; A=1-313. DR PDB; 3BWF; X-ray; 2.35 A; A=1-313. DR PDB; 3C4E; X-ray; 1.98 A; A/B/C/D=33-305. DR PDB; 3CXW; X-ray; 2.10 A; A=1-313. DR PDB; 3CY2; X-ray; 2.01 A; A=1-313. DR PDB; 3CY3; X-ray; 2.15 A; A=1-313. DR PDB; 3DCV; X-ray; 2.70 A; A=2-313. DR PDB; 3F2A; X-ray; 1.90 A; A=14-313. DR PDB; 3JPV; X-ray; 2.35 A; A=1-312. DR PDB; 3JXW; X-ray; 2.80 A; A=29-313. DR PDB; 3JY0; X-ray; 2.40 A; A=29-313. DR PDB; 3JYA; X-ray; 2.10 A; A=29-313. DR PDB; 3MA3; X-ray; 2.30 A; A=2-312. DR PDB; 3QF9; X-ray; 2.20 A; A=1-312. DR PDB; 3R00; X-ray; 2.10 A; A=29-313. DR PDB; 3R01; X-ray; 2.60 A; A=29-313. DR PDB; 3R02; X-ray; 1.95 A; A=29-313. DR PDB; 3R04; X-ray; 1.70 A; A=29-313. DR PDB; 3T9I; X-ray; 2.60 A; A=2-313. DR PDB; 3UIX; X-ray; 2.20 A; A=29-313. DR PDB; 3UMW; X-ray; 2.08 A; A=29-313. DR PDB; 3UMX; X-ray; 2.55 A; A=29-313. DR PDB; 3VBQ; X-ray; 1.85 A; A=29-313. DR PDB; 3VBT; X-ray; 2.23 A; A=29-313. DR PDB; 3VBV; X-ray; 2.08 A; A=29-313. DR PDB; 3VBW; X-ray; 2.48 A; A=29-313. DR PDB; 3VBX; X-ray; 2.03 A; A=29-313. DR PDB; 3VBY; X-ray; 2.27 A; A=29-313. DR PDB; 3VC4; X-ray; 2.23 A; A=29-313. DR PDB; 3WE8; X-ray; 1.95 A; A=33-305. DR PDB; 4A7C; X-ray; 2.30 A; A=30-313. DR PDB; 4ALU; X-ray; 2.60 A; A=2-313. DR PDB; 4ALV; X-ray; 2.59 A; A=2-313. DR PDB; 4ALW; X-ray; 1.92 A; A=2-313. DR PDB; 4AS0; X-ray; 2.30 A; A=33-305. DR PDB; 4BZN; X-ray; 1.90 A; A=2-313. DR PDB; 4BZO; X-ray; 2.10 A; A=2-313. DR PDB; 4DTK; X-ray; 1.86 A; A=30-305. DR PDB; 4ENX; X-ray; 2.80 A; A=29-313. DR PDB; 4ENY; X-ray; 2.80 A; A=29-313. DR PDB; 4GW8; X-ray; 2.00 A; A=1-312. DR PDB; 4I41; X-ray; 2.70 A; A=29-305. DR PDB; 4IAA; X-ray; 2.85 A; A=29-313. DR PDB; 4JX3; X-ray; 2.50 A; A=1-313. DR PDB; 4JX7; X-ray; 2.40 A; A=1-313. DR PDB; 4K0Y; X-ray; 1.95 A; A=33-306. DR PDB; 4K18; X-ray; 2.05 A; A=32-308. DR PDB; 4K1B; X-ray; 2.08 A; A=33-305. DR PDB; 4LL5; X-ray; 2.00 A; A=29-313. DR PDB; 4LM5; X-ray; 2.25 A; A=29-313. DR PDB; 4LMU; X-ray; 2.38 A; A=29-313. DR PDB; 4MBI; X-ray; 2.30 A; A=29-313. DR PDB; 4MBL; X-ray; 2.60 A; A=29-313. DR PDB; 4MTA; X-ray; 2.20 A; A=28-313. DR PDB; 4N6Y; X-ray; 2.60 A; A=2-313. DR PDB; 4N6Z; X-ray; 2.20 A; A=2-313. DR PDB; 4N70; X-ray; 2.10 A; A=2-313. DR PDB; 4RBL; X-ray; 2.55 A; A=29-313. DR PDB; 4RC2; X-ray; 2.10 A; A=29-313. DR PDB; 4RC3; X-ray; 2.34 A; A=29-313. DR PDB; 4RC4; X-ray; 2.65 A; A=29-313. DR PDB; 4RPV; X-ray; 3.05 A; A=1-313. DR PDB; 4TY1; X-ray; 2.70 A; A=33-305. DR PDB; 4WRS; X-ray; 2.20 A; A=33-305. DR PDB; 4WSY; X-ray; 2.30 A; A=33-305. DR PDB; 4WT6; X-ray; 2.30 A; A=33-305. DR PDB; 4XH6; X-ray; 2.04 A; A=29-313. DR PDB; 4XHK; X-ray; 1.90 A; B=1-313. DR PDB; 5C1Q; X-ray; 3.00 A; B=29-313. DR PDB; 5DGZ; X-ray; 2.50 A; A=29-313. DR PDB; 5DHJ; X-ray; 2.46 A; A=29-313. DR PDB; 5DIA; X-ray; 1.96 A; A=29-313. DR PDB; 5DWR; X-ray; 2.00 A; A=2-313. DR PDB; 5EOL; X-ray; 2.20 A; A=33-305. DR PDB; 5IIS; X-ray; 2.10 A; A=32-308. DR PDB; 5IPJ; X-ray; 2.10 A; A=33-305. DR PDB; 5KCX; X-ray; 2.20 A; A=29-313. DR PDB; 5KGD; X-ray; 1.98 A; A=30-305. DR PDB; 5KGE; X-ray; 2.23 A; A=30-305. DR PDB; 5KGG; X-ray; 1.95 A; A=30-305. DR PDB; 5KGI; X-ray; 2.13 A; A=30-305. DR PDB; 5KGK; X-ray; 2.66 A; A=30-305. DR PDB; 5KZI; X-ray; 2.10 A; A=33-305. DR PDB; 5MZL; X-ray; 1.96 A; A=1-313. DR PDB; 5N4N; X-ray; 2.09 A; A=1-313. DR PDB; 5N4O; X-ray; 2.22 A; A=1-313. DR PDB; 5N4R; X-ray; 2.13 A; A=1-313. DR PDB; 5N4U; X-ray; 2.20 A; A=1-313. DR PDB; 5N4V; X-ray; 1.85 A; A=1-313. DR PDB; 5N4X; X-ray; 2.20 A; A=1-313. DR PDB; 5N4Y; X-ray; 2.56 A; A=1-313. DR PDB; 5N4Z; X-ray; 2.26 A; A=1-313. DR PDB; 5N50; X-ray; 1.92 A; A=1-313. DR PDB; 5N51; X-ray; 2.12 A; A=1-313. DR PDB; 5N52; X-ray; 2.25 A; A=1-313. DR PDB; 5N5L; X-ray; 1.97 A; A=1-313. DR PDB; 5N5M; X-ray; 2.21 A; A=1-313. DR PDB; 5NDT; X-ray; 1.99 A; A=1-313. DR PDB; 5O11; X-ray; 2.40 A; A=29-313. DR PDB; 5O12; X-ray; 2.40 A; A=29-313. DR PDB; 5O13; X-ray; 2.44 A; A=29-313. DR PDB; 5TEL; X-ray; 2.21 A; A=33-306. DR PDB; 5TEX; X-ray; 2.15 A; A=33-306. DR PDB; 5TOE; X-ray; 2.30 A; A=34-306. DR PDB; 5TUR; X-ray; 2.95 A; A=1-313. DR PDB; 5V80; X-ray; 2.25 A; A=29-313. DR PDB; 5V82; X-ray; 1.89 A; A=29-313. DR PDB; 5VUA; X-ray; 2.20 A; B=29-313. DR PDB; 5VUB; X-ray; 2.00 A; B=29-313. DR PDB; 5VUC; X-ray; 2.00 A; B=29-313. DR PDB; 6AYD; X-ray; 3.00 A; A=1-312. DR PDB; 6BSK; X-ray; 2.57 A; A=30-305. DR PDB; 6KZI; X-ray; 2.80 A; A=29-313. DR PDB; 6L11; X-ray; 2.05 A; A=29-313. DR PDB; 6L12; X-ray; 1.87 A; A=29-313. DR PDB; 6L13; X-ray; 2.24 A; A=29-313. DR PDB; 6L14; X-ray; 1.95 A; A=29-313. DR PDB; 6L15; X-ray; 2.60 A; A=29-313. DR PDB; 6L16; X-ray; 2.10 A; A=29-313. DR PDB; 6L17; X-ray; 1.75 A; A=29-313. DR PDB; 6MT0; X-ray; 2.20 A; A=33-305. DR PDB; 6NO8; X-ray; 2.38 A; A=33-305. DR PDB; 6NO9; X-ray; 1.71 A; A=33-305. DR PDB; 6PCW; X-ray; 2.20 A; A=1-312. DR PDB; 6PDI; X-ray; 1.85 A; A=1-312. DR PDB; 6PDN; X-ray; 2.40 A; A=1-312. DR PDB; 6PDO; X-ray; 2.40 A; A=1-312. DR PDB; 6PDP; X-ray; 2.50 A; A=1-312. DR PDB; 6QXK; X-ray; 2.10 A; B=1-312. DR PDB; 6VRU; X-ray; 2.07 A; A=33-306. DR PDB; 6VRV; X-ray; 1.74 A; A=33-306. DR PDB; 6YKD; X-ray; 1.86 A; A=1-313. DR PDB; 7OOV; X-ray; 1.96 A; A=1-312. DR PDB; 7OOW; X-ray; 1.95 A; A=1-312. DR PDB; 7OOX; X-ray; 1.97 A; A=1-312. DR PDB; 7QB2; X-ray; 2.53 A; A=1-312. DR PDB; 7QFM; X-ray; 1.95 A; A=1-312. DR PDB; 7XSV; X-ray; 2.66 A; A=29-313. DR PDB; 7Z6U; X-ray; 2.28 A; A=1-313. DR PDB; 7ZUN; X-ray; 2.50 A; A=2-313. DR PDB; 8AFR; X-ray; 2.15 A; A=1-312. DR PDBsum; 1XQZ; -. DR PDBsum; 1XR1; -. DR PDBsum; 1XWS; -. DR PDBsum; 1YHS; -. DR PDBsum; 1YI3; -. DR PDBsum; 1YI4; -. DR PDBsum; 1YWV; -. DR PDBsum; 1YXS; -. DR PDBsum; 1YXT; -. DR PDBsum; 1YXU; -. DR PDBsum; 1YXV; -. DR PDBsum; 1YXX; -. DR PDBsum; 2BIK; -. DR PDBsum; 2BIL; -. DR PDBsum; 2BZH; -. DR PDBsum; 2BZI; -. DR PDBsum; 2BZJ; -. DR PDBsum; 2BZK; -. DR PDBsum; 2C3I; -. DR PDBsum; 2J2I; -. DR PDBsum; 2O3P; -. DR PDBsum; 2O63; -. DR PDBsum; 2O64; -. DR PDBsum; 2O65; -. DR PDBsum; 2OBJ; -. DR PDBsum; 2OI4; -. DR PDBsum; 2XIX; -. DR PDBsum; 2XIY; -. DR PDBsum; 2XIZ; -. DR PDBsum; 2XJ0; -. DR PDBsum; 2XJ1; -. DR PDBsum; 2XJ2; -. DR PDBsum; 3A99; -. DR PDBsum; 3BGP; -. DR PDBsum; 3BGQ; -. DR PDBsum; 3BGZ; -. DR PDBsum; 3BWF; -. DR PDBsum; 3C4E; -. DR PDBsum; 3CXW; -. DR PDBsum; 3CY2; -. DR PDBsum; 3CY3; -. DR PDBsum; 3DCV; -. DR PDBsum; 3F2A; -. DR PDBsum; 3JPV; -. DR PDBsum; 3JXW; -. DR PDBsum; 3JY0; -. DR PDBsum; 3JYA; -. DR PDBsum; 3MA3; -. DR PDBsum; 3QF9; -. DR PDBsum; 3R00; -. DR PDBsum; 3R01; -. DR PDBsum; 3R02; -. DR PDBsum; 3R04; -. DR PDBsum; 3T9I; -. DR PDBsum; 3UIX; -. DR PDBsum; 3UMW; -. DR PDBsum; 3UMX; -. DR PDBsum; 3VBQ; -. DR PDBsum; 3VBT; -. DR PDBsum; 3VBV; -. DR PDBsum; 3VBW; -. DR PDBsum; 3VBX; -. DR PDBsum; 3VBY; -. DR PDBsum; 3VC4; -. DR PDBsum; 3WE8; -. DR PDBsum; 4A7C; -. DR PDBsum; 4ALU; -. DR PDBsum; 4ALV; -. DR PDBsum; 4ALW; -. DR PDBsum; 4AS0; -. DR PDBsum; 4BZN; -. DR PDBsum; 4BZO; -. DR PDBsum; 4DTK; -. DR PDBsum; 4ENX; -. DR PDBsum; 4ENY; -. DR PDBsum; 4GW8; -. DR PDBsum; 4I41; -. DR PDBsum; 4IAA; -. DR PDBsum; 4JX3; -. DR PDBsum; 4JX7; -. DR PDBsum; 4K0Y; -. DR PDBsum; 4K18; -. DR PDBsum; 4K1B; -. DR PDBsum; 4LL5; -. DR PDBsum; 4LM5; -. DR PDBsum; 4LMU; -. DR PDBsum; 4MBI; -. DR PDBsum; 4MBL; -. DR PDBsum; 4MTA; -. DR PDBsum; 4N6Y; -. DR PDBsum; 4N6Z; -. DR PDBsum; 4N70; -. DR PDBsum; 4RBL; -. DR PDBsum; 4RC2; -. DR PDBsum; 4RC3; -. DR PDBsum; 4RC4; -. DR PDBsum; 4RPV; -. DR PDBsum; 4TY1; -. DR PDBsum; 4WRS; -. DR PDBsum; 4WSY; -. DR PDBsum; 4WT6; -. DR PDBsum; 4XH6; -. DR PDBsum; 4XHK; -. DR PDBsum; 5C1Q; -. DR PDBsum; 5DGZ; -. DR PDBsum; 5DHJ; -. DR PDBsum; 5DIA; -. DR PDBsum; 5DWR; -. DR PDBsum; 5EOL; -. DR PDBsum; 5IIS; -. DR PDBsum; 5IPJ; -. DR PDBsum; 5KCX; -. DR PDBsum; 5KGD; -. DR PDBsum; 5KGE; -. DR PDBsum; 5KGG; -. DR PDBsum; 5KGI; -. DR PDBsum; 5KGK; -. DR PDBsum; 5KZI; -. DR PDBsum; 5MZL; -. DR PDBsum; 5N4N; -. DR PDBsum; 5N4O; -. DR PDBsum; 5N4R; -. DR PDBsum; 5N4U; -. DR PDBsum; 5N4V; -. DR PDBsum; 5N4X; -. DR PDBsum; 5N4Y; -. DR PDBsum; 5N4Z; -. DR PDBsum; 5N50; -. DR PDBsum; 5N51; -. DR PDBsum; 5N52; -. DR PDBsum; 5N5L; -. DR PDBsum; 5N5M; -. DR PDBsum; 5NDT; -. DR PDBsum; 5O11; -. DR PDBsum; 5O12; -. DR PDBsum; 5O13; -. DR PDBsum; 5TEL; -. DR PDBsum; 5TEX; -. DR PDBsum; 5TOE; -. DR PDBsum; 5TUR; -. DR PDBsum; 5V80; -. DR PDBsum; 5V82; -. DR PDBsum; 5VUA; -. DR PDBsum; 5VUB; -. DR PDBsum; 5VUC; -. DR PDBsum; 6AYD; -. DR PDBsum; 6BSK; -. DR PDBsum; 6KZI; -. DR PDBsum; 6L11; -. DR PDBsum; 6L12; -. DR PDBsum; 6L13; -. DR PDBsum; 6L14; -. DR PDBsum; 6L15; -. DR PDBsum; 6L16; -. DR PDBsum; 6L17; -. DR PDBsum; 6MT0; -. DR PDBsum; 6NO8; -. DR PDBsum; 6NO9; -. DR PDBsum; 6PCW; -. DR PDBsum; 6PDI; -. DR PDBsum; 6PDN; -. DR PDBsum; 6PDO; -. DR PDBsum; 6PDP; -. DR PDBsum; 6QXK; -. DR PDBsum; 6VRU; -. DR PDBsum; 6VRV; -. DR PDBsum; 6YKD; -. DR PDBsum; 7OOV; -. DR PDBsum; 7OOW; -. DR PDBsum; 7OOX; -. DR PDBsum; 7QB2; -. DR PDBsum; 7QFM; -. DR PDBsum; 7XSV; -. DR PDBsum; 7Z6U; -. DR PDBsum; 7ZUN; -. DR PDBsum; 8AFR; -. DR AlphaFoldDB; P11309; -. DR SMR; P11309; -. DR BioGRID; 111310; 77. DR IntAct; P11309; 38. DR MINT; P11309; -. DR STRING; 9606.ENSP00000362608; -. DR BindingDB; P11309; -. DR ChEMBL; CHEMBL2147; -. DR DrugBank; DB08022; (2S)-1,3-benzothiazol-2-yl{2-[(2-pyridin-3-ylethyl)amino]pyrimidin-4-yl}ethanenitrile. DR DrugBank; DB03650; (3e)-3-[(4-Hydroxyphenyl)Imino]-1h-Indol-2(3h)-One. DR DrugBank; DB07242; (4R)-7,8-dichloro-1',9-dimethyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4'-piperidine]-4-carbonitrile. DR DrugBank; DB08166; (4R)-7-chloro-9-methyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4'-piperidine]-4-carbonitrile. DR DrugBank; DB08709; 2,3-diphenyl-1H-indole-7-carboxylic acid. DR DrugBank; DB01754; 3,4-Dihydroxy-1-Methylquinolin-2(1h)-One. DR DrugBank; DB07151; 4-(4-hydroxy-3-methylphenyl)-6-phenylpyrimidin-2(5H)-one. DR DrugBank; DB08707; 4-[3-(4-chlorophenyl)-2,1-benzisoxazol-5-yl]pyrimidin-2-amine. DR DrugBank; DB08705; 6-(5-BROMO-2-HYDROXYPHENYL)-2-OXO-4-PHENYL-1,2-DIHYDROPYRIDINE-3-CARBONITRILE. DR DrugBank; DB03777; Bisindolylmaleimide I. DR DrugBank; DB04522; Dexfosfoserine. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB03366; Imidazole. DR DrugBank; DB04715; IMIDAZOPYRIDAZIN 1. DR DrugBank; DB02656; LY-294002. DR DrugBank; DB08708; N-cyclohexyl-3-[3-(trifluoromethyl)phenyl][1,2,4]triazolo[4,3-b]pyridazin-6-amine. DR DrugBank; DB07524; N-phenyl-1H-pyrrolo[2,3-b]pyridin-3-amine. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine. DR DrugBank; DB02010; Staurosporine. DR DrugBank; DB08230; Tricetin. DR DrugCentral; P11309; -. DR GuidetoPHARMACOLOGY; 2158; -. DR GlyGen; P11309; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P11309; -. DR PhosphoSitePlus; P11309; -. DR BioMuta; PIM1; -. DR DMDM; 83305339; -. DR EPD; P11309; -. DR jPOST; P11309; -. DR MassIVE; P11309; -. DR MaxQB; P11309; -. DR PaxDb; 9606-ENSP00000362608; -. DR PeptideAtlas; P11309; -. DR ProteomicsDB; 52741; -. [P11309-1] DR ProteomicsDB; 52742; -. [P11309-2] DR Pumba; P11309; -. DR Antibodypedia; 1207; 831 antibodies from 38 providers. DR DNASU; 5292; -. DR Ensembl; ENST00000373509.6; ENSP00000362608.5; ENSG00000137193.14. [P11309-1] DR GeneID; 5292; -. DR KEGG; hsa:5292; -. DR MANE-Select; ENST00000373509.6; ENSP00000362608.5; NM_002648.4; NP_002639.1. DR UCSC; uc003onk.4; human. [P11309-1] DR AGR; HGNC:8986; -. DR CTD; 5292; -. DR DisGeNET; 5292; -. DR GeneCards; PIM1; -. DR HGNC; HGNC:8986; PIM1. DR HPA; ENSG00000137193; Tissue enhanced (bone). DR MIM; 164960; gene. DR neXtProt; NX_P11309; -. DR OpenTargets; ENSG00000137193; -. DR PharmGKB; PA33318; -. DR VEuPathDB; HostDB:ENSG00000137193; -. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00940000153394; -. DR HOGENOM; CLU_000288_63_0_1; -. DR InParanoid; P11309; -. DR OMA; GHRPCAD; -. DR OrthoDB; 4292089at2759; -. DR PhylomeDB; P11309; -. DR TreeFam; TF320810; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; P11309; -. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-9702518; STAT5 activation downstream of FLT3 ITD mutants. DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins. DR SignaLink; P11309; -. DR SIGNOR; P11309; -. DR BioGRID-ORCS; 5292; 53 hits in 1206 CRISPR screens. DR ChiTaRS; PIM1; human. DR EvolutionaryTrace; P11309; -. DR GeneWiki; PIM1; -. DR GenomeRNAi; 5292; -. DR Pharos; P11309; Tchem. DR PRO; PR:P11309; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P11309; Protein. DR Bgee; ENSG00000137193; Expressed in lower esophagus mucosa and 178 other cell types or tissues. DR ExpressionAtlas; P11309; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:1990748; P:cellular detoxification; IMP:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB. DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:BHF-UCL. DR GO; GO:1905062; P:positive regulation of cardioblast proliferation; IDA:BHF-UCL. DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl. DR GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl. DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0070561; P:vitamin D receptor signaling pathway; IMP:CACAO. DR CDD; cd14100; STKc_PIM1; 1. DR DisProt; DP00322; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR017348; PIM1/2/3. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22984; SERINE/THREONINE-PROTEIN KINASE PIM; 1. DR PANTHER; PTHR22984:SF29; SERINE_THREONINE-PROTEIN KINASE PIM-1; 1. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF037993; STPK_Pim-1; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P11309; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Apoptosis; ATP-binding; Cell cycle; KW Cell membrane; Cytoplasm; Direct protein sequencing; KW Host-virus interaction; Kinase; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Ubl conjugation. FT CHAIN 1..313 FT /note="Serine/threonine-protein kinase pim-1" FT /id="PRO_0000043349" FT DOMAIN 38..290 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 44..52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:15525646, FT ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862" FT BINDING 121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:15525646, FT ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862" FT BINDING 128 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:15525646, FT ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15657054, FT ECO:0007744|PubMed:23186163" FT MOD_RES 23 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15657054" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15657054" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15657054" FT VAR_SEQ 1 FT /note="M -> MPHEPHEPLTPPFSALPDPAGAPSRRQSRQRPQLSSDSPSAFRASRS FT HSRNATRSHSHSHSPRHSLRHSPGSGSCGSSSGHRPCADILEVGM (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:16186805" FT /id="VSP_059829" FT VARIANT 53 FT /note="Y -> H (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041004" FT VARIANT 124 FT /note="E -> Q (in dbSNP:rs35760989)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041005" FT VARIANT 135 FT /note="E -> K (in dbSNP:rs200523275)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041006" FT VARIANT 142 FT /note="E -> D (in dbSNP:rs33989191)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041007" FT MUTAGEN 68 FT /note="H->Y: Increased kinase activity." FT /evidence="ECO:0000269|PubMed:15808862" FT MUTAGEN 81 FT /note="P->S: Abolished kinase activity." FT /evidence="ECO:0000269|PubMed:15808862, FT ECO:0000269|PubMed:37797010" FT MUTAGEN 82 FT /note="N->K: Decreased kinase activity." FT /evidence="ECO:0000269|PubMed:15808862" FT MUTAGEN 193 FT /note="L->F: Decreased kinase activity." FT /evidence="ECO:0000269|PubMed:15808862" FT CONFLICT 15..16 FT /note="AP -> RA (in Ref. 2; AAA60089)" FT /evidence="ECO:0000305" FT TURN 6..9 FT /evidence="ECO:0007829|PDB:7OOX" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:7OOX" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:3A99" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 63..70 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:3A99" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:3C4E" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 88..96 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:3VBQ" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 129..136 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 141..160 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:3A99" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:3A99" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:4ALW" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 210..215 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 220..237 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 245..250 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 261..270 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 281..285 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:3A99" FT HELIX 296..303 FT /evidence="ECO:0007829|PDB:3A99" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:3F2A" SQ SEQUENCE 313 AA; 35686 MW; 35BA76D3668E69A3 CRC64; MLLSKINSLA HLRAAPCNDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG SVYSGIRVSD NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF SGVIRLLDWF ERPDSFVLIL ERPEPVQDLF DFITERGALQ EELARSFFWQ VLEAVRHCHN CGVLHRDIKD ENILIDLNRG ELKLIDFGSG ALLKDTVYTD FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI PFEHDEEIIR GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA EIHLHSLSPG PSK //