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P11309

- PIM1_HUMAN

UniProt

P11309 - PIM1_HUMAN

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Protein

Serine/threonine-protein kinase pim-1

Gene

PIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Cofactori

Magnesium.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581ATP
Binding sitei212 – 2121ATP; via carbonyl oxygen
Binding sitei219 – 2191ATP
Active sitei258 – 2581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi135 – 1439ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. manganese ion binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. ribosomal small subunit binding Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. cell proliferation Source: UniProtKB
  4. hyaluronan metabolic process Source: Ensembl
  5. multicellular organismal development Source: ProtInc
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: UniProtKB
  9. protein autophosphorylation Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP11309.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-1 (EC:2.7.11.1)
Gene namesi
Name:PIM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:8986. PIM1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591H → Y: Increased kinase activity. 1 Publication
Mutagenesisi172 – 1721P → S: Decreased kinase activity. 1 Publication
Mutagenesisi173 – 1731N → K: Decreased kinase activity. 1 Publication
Mutagenesisi284 – 2841L → F: Decreased kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA33318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Serine/threonine-protein kinase pim-1PRO_0000043349Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei114 – 1141Phosphothreonine1 Publication
Modified residuei189 – 1891Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.3 Publications
Ubiquitinated, leading to proteasomal degradation.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11309.
PaxDbiP11309.
PRIDEiP11309.

PTM databases

PhosphoSiteiP11309.

Expressioni

Tissue specificityi

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

Inductioni

Strongly induced in leukocytes by the JAK/STAT pathway in response to cytokines. Induced by different cellular stresses, heat shock and cytotoxic agents.3 Publications

Gene expression databases

BgeeiP11309.
CleanExiHS_PIM1.
GenevestigatoriP11309.

Organism-specific databases

HPAiCAB017040.
HPA003941.

Interactioni

Subunit structurei

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCG2Q9UNQ09EBI-1018629,EBI-1569435
BMXP518134EBI-696621,EBI-696657
RPS19P390197EBI-696621,EBI-354451

Protein-protein interaction databases

BioGridi111310. 34 interactions.
IntActiP11309. 8 interactions.
MINTiMINT-1412755.
STRINGi9606.ENSP00000362608.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni126 – 1283
Beta strandi129 – 1346
Beta strandi136 – 1405
Beta strandi142 – 1487
Turni149 – 1513
Beta strandi154 – 1618
Helixi162 – 1643
Beta strandi168 – 1703
Turni172 – 1743
Beta strandi176 – 1783
Helixi179 – 1879
Beta strandi189 – 1913
Beta strandi192 – 1943
Beta strandi197 – 2026
Beta strandi204 – 2129
Beta strandi215 – 2195
Helixi220 – 2278
Helixi232 – 25120
Helixi261 – 2633
Beta strandi264 – 2674
Turni268 – 2714
Beta strandi272 – 2754
Helixi278 – 2803
Helixi296 – 2983
Helixi301 – 3066
Helixi311 – 32818
Helixi336 – 3416
Helixi352 – 36110
Helixi366 – 3683
Helixi372 – 3765
Helixi379 – 3813
Helixi387 – 3948
Turni395 – 3984

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray2.30A93-403[»]
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[»]
3WE8X-ray1.95A124-396[»]
4A7CX-ray2.30A121-404[»]
4ALUX-ray2.60A93-404[»]
4ALVX-ray2.59A93-404[»]
4ALWX-ray1.92A93-404[»]
4AS0X-ray2.30A124-396[»]
4BZNX-ray1.90A93-404[»]
4BZOX-ray2.10A93-404[»]
4DTKX-ray1.86A121-396[»]
4ENXX-ray2.80A120-404[»]
4ENYX-ray2.80A120-404[»]
4GW8X-ray2.00A92-403[»]
4I41X-ray2.70A120-396[»]
4IAAX-ray2.85A120-404[»]
4JX3X-ray2.50A92-404[»]
4JX7X-ray2.40A92-404[»]
4K0YX-ray1.95A124-397[»]
4K18X-ray2.05A123-399[»]
4K1BX-ray2.08A124-396[»]
4LL5X-ray2.00A120-404[»]
4LM5X-ray2.25A120-404[»]
4LMUX-ray2.38A120-404[»]
4MBIX-ray2.30A120-404[»]
4MBLX-ray2.60A120-404[»]
4MEDX-ray2.80A120-404[»]
4N6YX-ray2.60A93-404[»]
4N6ZX-ray2.20A93-404[»]
4N70X-ray2.10A93-404[»]
DisProtiDP00322.
ProteinModelPortaliP11309.
SMRiP11309. Positions 104-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11309.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 381253Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiP11309.
KOiK04702.
OMAiFIIVMER.
OrthoDBiEOG7NW6B0.
PhylomeDBiP11309.
TreeFamiTF320810.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR017348. Ser/Thr_kinase_Pim-1.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037993. STPK_Pim-1. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P11309-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPHEPHEPLT PPFSALPDPA GAPSRRQSRQ RPQLSSDSPS AFRASRSHSR
60 70 80 90 100
NATRSHSHSH SPRHSLRHSP GSGSCGSSSG HRPCADILEV GMLLSKINSL
110 120 130 140 150
AHLRAAPCND LHATKLAPGK EKEPLESQYQ VGPLLGSGGF GSVYSGIRVS
160 170 180 190 200
DNLPVAIKHV EKDRISDWGE LPNGTRVPME VVLLKKVSSG FSGVIRLLDW
210 220 230 240 250
FERPDSFVLI LERPEPVQDL FDFITERGAL QEELARSFFW QVLEAVRHCH
260 270 280 290 300
NCGVLHRDIK DENILIDLNR GELKLIDFGS GALLKDTVYT DFDGTRVYSP
310 320 330 340 350
PEWIRYHRYH GRSAAVWSLG ILLYDMVCGD IPFEHDEEII RGQVFFRQRV
360 370 380 390 400
SSECQHLIRW CLALRPSDRP TFEEIQNHPW MQDVLLPQET AEIHLHSLSP

GPSK

Note: Initiates from CTG codon.

Length:404
Mass (Da):45,412
Last modified:December 6, 2005 - v3
Checksum:i18C421B7CFF87818
GO
Isoform 2 (identifier: P11309-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:313
Mass (Da):35,686
Checksum:i35BA76D3668E69A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1072AP → RA in AAA60089. (PubMed:3475233)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441Y → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041004
Natural varianti215 – 2151E → Q.1 Publication
VAR_041005
Natural varianti226 – 2261E → K.1 Publication
VAR_041006
Natural varianti233 – 2331E → D.1 Publication
VAR_041007

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191Missing in isoform 2. 4 PublicationsVSP_016530Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4830.1. [P11309-2]
PIRiJU0327. TVHUP1.
RefSeqiNP_001230115.1. NM_001243186.1. [P11309-1]
NP_002639.1. NM_002648.3. [P11309-2]
UniGeneiHs.81170.

Genome annotation databases

EnsembliENST00000373509; ENSP00000362608; ENSG00000137193. [P11309-2]
GeneIDi5292.
KEGGihsa:5292.
UCSCiuc003onk.3. human. [P11309-1]

Polymorphism databases

DMDMi83305339.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4830.1. [P11309-2 ]
PIRi JU0327. TVHUP1.
RefSeqi NP_001230115.1. NM_001243186.1. [P11309-1 ]
NP_002639.1. NM_002648.3. [P11309-2 ]
UniGenei Hs.81170.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XQZ X-ray 2.10 A 105-404 [» ]
1XR1 X-ray 2.10 A 105-404 [» ]
1XWS X-ray 1.80 A 92-404 [» ]
1YHS X-ray 2.15 A 124-396 [» ]
1YI3 X-ray 2.50 A 124-396 [» ]
1YI4 X-ray 2.40 A 124-396 [» ]
1YWV X-ray 2.00 A 120-404 [» ]
1YXS X-ray 2.20 A 120-404 [» ]
1YXT X-ray 2.00 A 120-404 [» ]
1YXU X-ray 2.24 A/B/C/D 120-404 [» ]
1YXV X-ray 2.00 A 120-404 [» ]
1YXX X-ray 2.00 A 120-404 [» ]
2BIK X-ray 1.80 B 92-404 [» ]
2BIL X-ray 2.55 B 92-404 [» ]
2BZH X-ray 1.90 B 92-404 [» ]
2BZI X-ray 1.90 B 92-404 [» ]
2BZJ X-ray 2.05 A 92-404 [» ]
2BZK X-ray 2.45 B 92-404 [» ]
2C3I X-ray 1.90 B 92-404 [» ]
2J2I X-ray 1.90 B 92-403 [» ]
2O3P X-ray 2.24 A 120-404 [» ]
2O63 X-ray 2.00 A 120-404 [» ]
2O64 X-ray 2.44 A 120-404 [» ]
2O65 X-ray 2.85 A 120-404 [» ]
2OBJ X-ray 2.50 A 92-404 [» ]
2OI4 X-ray 2.20 X 92-404 [» ]
2XIX X-ray 2.40 A 105-404 [» ]
2XIY X-ray 2.20 A 105-404 [» ]
2XIZ X-ray 2.21 A 105-404 [» ]
2XJ0 X-ray 3.10 A 105-404 [» ]
2XJ1 X-ray 2.13 A 105-404 [» ]
2XJ2 X-ray 2.20 A 105-404 [» ]
3A99 X-ray 1.60 A 106-404 [» ]
3BGP X-ray 2.80 A 92-404 [» ]
3BGQ X-ray 2.00 A 92-404 [» ]
3BGZ X-ray 2.40 A 92-404 [» ]
3BWF X-ray 2.35 A 92-404 [» ]
3C4E X-ray 1.98 A/B/C/D 124-396 [» ]
3CXW X-ray 2.10 A 92-404 [» ]
3CY2 X-ray 2.01 A 92-404 [» ]
3CY3 X-ray 2.15 A 92-404 [» ]
3DCV X-ray 2.70 A 93-404 [» ]
3F2A X-ray 1.90 A 105-404 [» ]
3JPV X-ray 2.35 A 92-403 [» ]
3JXW X-ray 2.80 A 120-404 [» ]
3JY0 X-ray 2.40 A 120-404 [» ]
3JYA X-ray 2.10 A 120-404 [» ]
3MA3 X-ray 2.30 A 93-403 [» ]
3QF9 X-ray 2.20 A 92-403 [» ]
3R00 X-ray 2.10 A 120-404 [» ]
3R01 X-ray 2.60 A 120-404 [» ]
3R02 X-ray 1.95 A 120-404 [» ]
3R04 X-ray 1.70 A 120-404 [» ]
3T9I X-ray 2.60 A 93-404 [» ]
3UIX X-ray 2.20 A 120-404 [» ]
3UMW X-ray 2.08 A 120-404 [» ]
3UMX X-ray 2.55 A 120-404 [» ]
3VBQ X-ray 1.85 A 120-404 [» ]
3VBT X-ray 2.23 A 120-404 [» ]
3VBV X-ray 2.08 A 120-404 [» ]
3VBW X-ray 2.48 A 120-404 [» ]
3VBX X-ray 2.03 A 120-404 [» ]
3VBY X-ray 2.27 A 120-404 [» ]
3VC4 X-ray 2.23 A 120-404 [» ]
3WE8 X-ray 1.95 A 124-396 [» ]
4A7C X-ray 2.30 A 121-404 [» ]
4ALU X-ray 2.60 A 93-404 [» ]
4ALV X-ray 2.59 A 93-404 [» ]
4ALW X-ray 1.92 A 93-404 [» ]
4AS0 X-ray 2.30 A 124-396 [» ]
4BZN X-ray 1.90 A 93-404 [» ]
4BZO X-ray 2.10 A 93-404 [» ]
4DTK X-ray 1.86 A 121-396 [» ]
4ENX X-ray 2.80 A 120-404 [» ]
4ENY X-ray 2.80 A 120-404 [» ]
4GW8 X-ray 2.00 A 92-403 [» ]
4I41 X-ray 2.70 A 120-396 [» ]
4IAA X-ray 2.85 A 120-404 [» ]
4JX3 X-ray 2.50 A 92-404 [» ]
4JX7 X-ray 2.40 A 92-404 [» ]
4K0Y X-ray 1.95 A 124-397 [» ]
4K18 X-ray 2.05 A 123-399 [» ]
4K1B X-ray 2.08 A 124-396 [» ]
4LL5 X-ray 2.00 A 120-404 [» ]
4LM5 X-ray 2.25 A 120-404 [» ]
4LMU X-ray 2.38 A 120-404 [» ]
4MBI X-ray 2.30 A 120-404 [» ]
4MBL X-ray 2.60 A 120-404 [» ]
4MED X-ray 2.80 A 120-404 [» ]
4N6Y X-ray 2.60 A 93-404 [» ]
4N6Z X-ray 2.20 A 93-404 [» ]
4N70 X-ray 2.10 A 93-404 [» ]
DisProti DP00322.
ProteinModelPortali P11309.
SMRi P11309. Positions 104-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111310. 34 interactions.
IntActi P11309. 8 interactions.
MINTi MINT-1412755.
STRINGi 9606.ENSP00000362608.

Chemistry

BindingDBi P11309.
ChEMBLi CHEMBL2147.
DrugBanki DB00131. Adenosine monophosphate.
GuidetoPHARMACOLOGYi 2158.

PTM databases

PhosphoSitei P11309.

Polymorphism databases

DMDMi 83305339.

Proteomic databases

MaxQBi P11309.
PaxDbi P11309.
PRIDEi P11309.

Protocols and materials databases

DNASUi 5292.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373509 ; ENSP00000362608 ; ENSG00000137193 . [P11309-2 ]
GeneIDi 5292.
KEGGi hsa:5292.
UCSCi uc003onk.3. human. [P11309-1 ]

Organism-specific databases

CTDi 5292.
GeneCardsi GC06P037137.
HGNCi HGNC:8986. PIM1.
HPAi CAB017040.
HPA003941.
MIMi 164960. gene.
neXtProti NX_P11309.
PharmGKBi PA33318.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119045.
HOGENOMi HOG000231357.
HOVERGENi HBG106681.
InParanoidi P11309.
KOi K04702.
OMAi FIIVMER.
OrthoDBi EOG7NW6B0.
PhylomeDBi P11309.
TreeFami TF320810.

Enzyme and pathway databases

SignaLinki P11309.

Miscellaneous databases

ChiTaRSi PIM1. human.
EvolutionaryTracei P11309.
GeneWikii PIM1.
GenomeRNAii 5292.
NextBioi 20450.
PROi P11309.
SOURCEi Search...

Gene expression databases

Bgeei P11309.
CleanExi HS_PIM1.
Genevestigatori P11309.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR017348. Ser/Thr_kinase_Pim-1.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF037993. STPK_Pim-1. 1 hit.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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 OF 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, IDENTIFICATION BY 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.
    , 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.

Entry informationi

Entry nameiPIM1_HUMAN
AccessioniPrimary (citable) accession number: P11309
Secondary accession number(s): Q38RT9, Q5T7H7, Q96RG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3