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P11309 (PIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase pim-1
EC=2.7.11.1
Gene names
Name:PIM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proto-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. Ref.11 Ref.12 Ref.13 Ref.16 Ref.18 Ref.19 Ref.20

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.21 Ref.22 Ref.23

Cofactor

Magnesium. Ref.21 Ref.22 Ref.23

Subunit structure

Isoform 2 is isolated as a monomer whereas isoform 1 complexes with other proteins By similarity. Binds to RP9 By similarity. Isoform 1, but not isoform 2, binds BMX. Isoform 2 interacts with CDKN1B and FOXO3. Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation By similarity. Interacts with HSP90, this interaction stabilizes PIM1 protein levels. Interacts (ubiquitinated form) with HSP70 and promotes its proteosomal degradation. Interacts with CDKN1A. Interacts with CDC25C. Interacts (via N-terminal 96 residues) with CDC25A By similarity. Interacts with MAP3K5. Interacts with MYC By similarity. Ref.5 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Isoform 2: Cytoplasm. Nucleus Ref.5 Ref.13 Ref.14.

Isoform 1: Cell membrane Ref.5 Ref.13 Ref.14.

Tissue specificity

Expressed primarily in cells of the hematopoietic and germline lineages. Isoform 1 and isoform 2 are both expressed in prostate cancer cell lines. Ref.5

Induction

Strongly induced in leukocytes by the JAK/STAT pathway in response to cytokines. Induced by different cellular stresses, heat shock and cytotoxic agents. Ref.5 Ref.16 Ref.17 Ref.21 Ref.22 Ref.23

Post-translational modification

Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation. Ref.15 Ref.19 Ref.21

Ubiquitinated, leading to proteasomal degradation. Ref.15 Ref.17

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   DiseaseProto-oncogene
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from direct assay Ref.5. Source: UniProtKB

multicellular organismal development

Traceable author statement PubMed 2682662. Source: ProtInc

negative regulation of apoptotic process

Inferred from direct assay Ref.5. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S

Inferred from direct assay Ref.19. Source: UniProtKB

protein autophosphorylation

Inferred from mutant phenotype Ref.19. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.11. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.11Ref.19. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCG2Q9UNQ09EBI-1018629,EBI-1569435
BMXP518134EBI-696621,EBI-696657
RPS19P390197EBI-696621,EBI-354451

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P11309-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Initiates from CTG codon.
Isoform 2 (identifier: P11309-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Serine/threonine-protein kinase pim-1
PRO_0000043349

Regions

Domain129 – 381253Protein kinase
Nucleotide binding135 – 1439ATP By similarity

Sites

Active site2581Proton acceptor By similarity
Binding site1581ATP
Binding site2121ATP; via carbonyl oxygen
Binding site2191ATP

Amino acid modifications

Modified residue991Phosphoserine Ref.21
Modified residue1141Phosphothreonine Ref.21
Modified residue1891Phosphoserine Ref.21
Modified residue3521Phosphoserine Ref.21

Natural variations

Alternative sequence1 – 9191Missing in isoform 2.
VSP_016530
Natural variant1441Y → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.24
VAR_041004
Natural variant2151E → Q. Ref.24
VAR_041005
Natural variant2261E → K. Ref.24
VAR_041006
Natural variant2331E → D. Ref.24
VAR_041007

Experimental info

Mutagenesis1591H → Y: Increased kinase activity. Ref.23
Mutagenesis1721P → S: Decreased kinase activity. Ref.23
Mutagenesis1731N → K: Decreased kinase activity. Ref.23
Mutagenesis2841L → F: Decreased kinase activity. Ref.23
Sequence conflict106 – 1072AP → RA in AAA60089. Ref.2

Secondary structure

1 ......................................................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 18C421B7CFF87818

FASTA40445,412
        10         20         30         40         50         60 
MPHEPHEPLT PPFSALPDPA GAPSRRQSRQ RPQLSSDSPS AFRASRSHSR NATRSHSHSH 

        70         80         90        100        110        120 
SPRHSLRHSP GSGSCGSSSG HRPCADILEV GMLLSKINSL AHLRAAPCND LHATKLAPGK 

       130        140        150        160        170        180 
EKEPLESQYQ VGPLLGSGGF GSVYSGIRVS DNLPVAIKHV EKDRISDWGE LPNGTRVPME 

       190        200        210        220        230        240 
VVLLKKVSSG FSGVIRLLDW FERPDSFVLI LERPEPVQDL FDFITERGAL QEELARSFFW 

       250        260        270        280        290        300 
QVLEAVRHCH NCGVLHRDIK DENILIDLNR GELKLIDFGS GALLKDTVYT DFDGTRVYSP 

       310        320        330        340        350        360 
PEWIRYHRYH GRSAAVWSLG ILLYDMVCGD IPFEHDEEII RGQVFFRQRV SSECQHLIRW 

       370        380        390        400 
CLALRPSDRP TFEEIQNHPW MQDVLLPQET AEIHLHSLSP GPSK

« Hide

Isoform 2 [UniParc].

Checksum: 35BA76D3668E69A3
Show »

FASTA31335,686

References

« Hide 'large scale' references
[1]"Primary structure of the putative human oncogene, pim-1."
Reeves R., Spies G.A., Kiefer M., Barr P.J., Power M.
Gene 90:303-307(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[2]"The cDNA sequence and gene analysis of the human pim oncogene."
Zakut-Houri R., Hazum S., Givol D., Telerman A.
Gene 54:105-111(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Comparison of the human and mouse PIM-1 cDNAs: nucleotide sequence and immunological identification of the in vitro synthesized PIM-1 protein."
Domen J., von Lindern M., Hermans A., Breuer M., Grosveld G., Berns A.
Oncogene Res. 1:103-112(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Cloning and characterization of the human PIM-1 gene: a putative oncogene related to the protein kinases."
Meeker T.C., Nagarajan L., Ar-Rushdi A., Croce C.M.
J. Cell. Biochem. 35:105-112(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"The 44 kDa Pim-1 kinase directly interacts with tyrosine kinase Etk/BMX and protects human prostate cancer cells from apoptosis induced by chemotherapeutic drugs."
Xie Y., Xu K., Dai B., Guo Z., Jiang T., Chen H., Qiu Y.
Oncogene 25:70-78(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE INITIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH BMX.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Kidney.
[9]"Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas."
Pasqualucci L., Neumeister P., Goossens T., Nanjangud G., Chaganti R.S.K., Kuppers R., Dalla-Favera R.
Nature 412:341-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-293 (ISOFORM 2).
[10]"Identification of the human pim-1 gene product as a 33-kilodalton cytoplasmic protein with tyrosine kinase activity."
Telerman A., Amson R., Zakut-Houri R., Givol D.
Mol. Cell. Biol. 8:1498-1503(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG."
Saris C.J., Domen J., Berns A.
EMBO J. 10:655-664(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE INITIATION.
[12]"Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1."
Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.
FEBS Lett. 467:17-21(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX3, FUNCTION IN PHOSPHORYLATION CBX3.
[13]"Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 kinase."
Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J., Magnuson N.S.
Biochim. Biophys. Acta 1593:45-55(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION IN PHOSPHORYLATION OF CDKN1A, INTERACTION WITH CDKN1A.
[14]"Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear localization is necessary for its biologic effects."
Ionov Y., Le X., Tunquist B.J., Sweetenham J., Sachs T., Ryder J., Johnson T., Lilly M.B., Kraft A.S.
Anticancer Res. 23:167-178(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Protein phosphatase 2A regulates the stability of Pim protein kinases."
Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP2CA, PHOSPHORYLATION, UBIQUITINATION.
[16]"IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 and STAT5 and promote Pim-1 and cyclin D3 protein expression in human eosinophils."
Stout B.A., Bates M.E., Liu L.Y., Farrington N.N., Bertics P.J.
J. Immunol. 173:6409-6417(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[17]"Pim-1 kinase stability is regulated by heat shock proteins and the ubiquitin-proteasome pathway."
Shay K.P., Wang Z., Xing P.X., McKenzie I.F., Magnuson N.S.
Mol. Cancer Res. 3:170-181(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH HSPCA AND HSP70, INDUCTION.
[18]"The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C."
Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.
Int. J. Biochem. Cell Biol. 38:430-443(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25C, INTERACTION WITH CDC25C.
[19]"Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE PROGRESSION, INTERACTION WITH CDKN1B AND FOXO3, PHOSPHORYLATION OF CDKN1B AND FOXO3.
[20]"PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis."
Gu J.J., Wang Z., Reeves R., Magnuson N.S.
Oncogene 28:4261-4271(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAP3K5, INTERACTION WITH MAP3K5.
[21]"Pim-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002."
Jacobs M.D., Black J., Futer O., Swenson L., Hare B., Fleming M., Saxena K.
J. Biol. Chem. 280:13728-13734(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 124-396 IN COMPLEXES WITH ADENOSINE AND INHIBITORS STAUROSPORINE AND LY294002, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, MASS SPECTROMETRY, PHOSPHORYLATION AT SER-99; THR-114; SER-189 AND SER-352.
[22]"Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase."
Qian K.C., Wang L., Hickey E.R., Studts J., Barringer K., Peng C., Kronkaitis A., Li J., White A., Mische S., Farmer B.
J. Biol. Chem. 280:6130-6137(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 105-404 OF APOPROTEIN AND IN COMPLEX WITH AMP-PNP, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
[23]"Crystal structures of proto-oncogene kinase Pim1: a target of aberrant somatic hypermutations in diffuse large cell lymphoma."
Kumar A., Mandiyan V., Suzuki Y., Zhang C., Rice J., Tsai J., Artis D.R., Ibrahim P., Bremer R.
J. Mol. Biol. 348:183-193(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 120-404 OF APOPROTEIN AND IN COMPLEXES WITH AMP-PNP AND INHIBITORS, PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, MUTAGENESIS OF HIS-159; PRO-172; ASN-173 AND LEU-284.
[24]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-144; GLN-215; LYS-226 AND ASP-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M27903 Genomic DNA. Translation: AAA60090.1.
M16750 mRNA. Translation: AAA60089.1.
M54915 mRNA. Translation: AAA36447.1.
M24779 mRNA. Translation: AAA81553.1.
DQ022562 mRNA. Translation: AAY87461.1.
AL353579 Genomic DNA. Translation: CAI20316.1.
CH471081 Genomic DNA. Translation: EAX03934.1.
BC020224 mRNA. Translation: AAH20224.1.
AF386792 Genomic DNA. Translation: AAK70871.1.
IPIIPI00005014.
IPI00745060.
PIRTVHUP1. JU0327.
RefSeqNP_001230115.1. NM_001243186.1.
NP_002639.1. NM_002648.3.
UniGeneHs.81170.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XQZX-ray2.10A105-404[»]
1XR1X-ray2.10A105-404[»]
1XWSX-ray1.80A92-404[»]
1YHSX-ray2.15A124-396[»]
1YI3X-ray2.50A124-396[»]
1YI4X-ray2.40A124-396[»]
1YWVX-ray2.00A120-404[»]
1YXSX-ray2.20A120-404[»]
1YXTX-ray2.00A120-404[»]
1YXUX-ray2.24A/B/C/D120-404[»]
1YXVX-ray2.00A120-404[»]
1YXXX-ray2.00A120-404[»]
2BIKX-ray1.80B92-404[»]
2BILX-ray2.55B92-404[»]
2BZHX-ray1.90B92-404[»]
2BZIX-ray1.90B92-404[»]
2BZJX-ray2.05A92-404[»]
2BZKX-ray2.45B92-404[»]
2C3IX-ray1.90B92-404[»]
2J2IX-ray1.90B92-403[»]
2O3PX-ray2.24A120-404[»]
2O63X-ray2.00A120-404[»]
2O64X-ray2.44A120-404[»]
2O65X-ray2.85A120-404[»]
2OBJX-ray2.50A92-404[»]
2OI4X-ray2.20X92-404[»]
2XIXX-ray2.40A105-404[»]
2XIYX-ray2.20A105-404[»]
2XIZX-ray2.21A105-404[»]
2XJ0X-ray3.10A105-404[»]
2XJ1X-ray2.13A105-404[»]
2XJ2X-ray2.20A105-404[»]
3A99X-ray1.60A106-404[»]
3BGPX-ray2.80A92-404[»]
3BGQX-ray2.00A92-404[»]
3BGZX-ray2.40A92-404[»]
3BWFX-ray2.35A92-404[»]
3C4EX-ray1.98A/B/C/D124-396[»]
3CXWX-ray2.10A92-404[»]
3CY2X-ray2.01A92-404[»]
3CY3X-ray2.15A92-404[»]
3DCVX-ray2.70A93-404[»]
3F2AX-ray1.90A105-404[»]
3JPVX-ray2.35A92-403[»]
3JXWX-ray2.80A120-404[»]
3JY0X-ray2.40A120-404[»]
3JYAX-ray2.10A120-404[»]
3MA3X-ray2.30A92-403[»]
3QF9X-ray2.20A92-403[»]
3R00X-ray2.10A120-404[»]
3R01X-ray2.60A120-404[»]
3R02X-ray1.95A120-404[»]
3R04X-ray1.70A120-404[»]
3T9IX-ray2.60A93-404[»]
3UIXX-ray2.20A120-404[»]
3UMWX-ray2.08A120-404[»]
3UMXX-ray2.55A120-404[»]
3VBQX-ray1.85A120-404[»]
3VBTX-ray2.23A120-404[»]
3VBVX-ray2.08A120-404[»]
3VBWX-ray2.48A120-404[»]
3VBXX-ray2.03A120-404[»]
3VBYX-ray2.27A120-404[»]
3VC4X-ray2.23A120-404[»]
4A7CX-ray2.30A120-404[»]
4ALUX-ray2.60A93-404[»]
4ALVX-ray2.59A93-404[»]
4ALWX-ray1.92A93-404[»]
4AS0X-ray2.30A124-396[»]
4DTKX-ray1.86A121-396[»]
4ENXX-ray2.80A120-404[»]
4ENYX-ray2.80A120-404[»]
4GW8X-ray2.00A92-403[»]
DisProtDP00322.
ProteinModelPortalP11309.
ModBaseSearch...

Protein-protein interaction databases

IntActP11309. 6 interactions.
MINTMINT-1412755.
STRING9606.ENSP00000362608.

PTM databases

PhosphoSiteP11309.

Polymorphism databases

DMDM83305339.

Proteomic databases

PaxDbP11309.
PRIDEP11309.

Protocols and materials databases

DNASU5292.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373509; ENSP00000362608; ENSG00000137193.
GeneID5292.
KEGGhsa:5292.
UCSCuc003onk.3. human.

Organism-specific databases

CTD5292.
GeneCardsGC06P037137.
HGNCHGNC:8986. PIM1.
HPACAB017040.
HPA003941.
MIM164960. gene.
neXtProtNX_P11309.
PharmGKBPA33318.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231357.
HOVERGENHBG106681.
InParanoidP11309.
KOK04702.
OMAFIIVMER.

Enzyme and pathway databases

Pathway_Interaction_DBnfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Gene expression databases

BgeeP11309.
CleanExHS_PIM1.
GenevestigatorP11309.
GermOnlineENSG00000137193. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR017348. Ser/Thr_kinase_Pim-1.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037993. STPK_Pim-1. 1 hit.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP11309.
ChEMBLCHEMBL2147.
ChiTaRSPIM1. human.
DrugBankDB00131. Adenosine monophosphate.
EvolutionaryTraceP11309.
GenomeRNAi5292.
NextBio20450.
SOURCESearch...

Entry information

Entry namePIM1_HUMAN
AccessionPrimary (citable) accession number: P11309
Secondary accession number(s): Q38RT9, Q5T7H7, Q96RG3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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