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Protein

Serine/threonine-protein kinase pim-1

Gene

PIM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei158ATP1
Binding sitei212ATP; via carbonyl oxygen1
Binding sitei219ATP1
Active sitei258Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi135 – 143ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • ribosomal small subunit binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • cell proliferation Source: UniProtKB
  • hyaluronan metabolic process Source: Ensembl
  • multicellular organism development Source: ProtInc
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • vitamin D receptor signaling pathway Source: CACAO
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

BioCyciZFISH:HS06287-MONOMER.
SignaLinkiP11309.
SIGNORiP11309.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8986. PIM1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159H → Y: Increased kinase activity. 1 Publication1
Mutagenesisi172P → S: Decreased kinase activity. 1 Publication1
Mutagenesisi173N → K: Decreased kinase activity. 1 Publication1
Mutagenesisi284L → F: Decreased kinase activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi5292.
OpenTargetsiENSG00000137193.
PharmGKBiPA33318.

Chemistry databases

ChEMBLiCHEMBL2147.
DrugBankiDB00131. Adenosine monophosphate.
GuidetoPHARMACOLOGYi2158.

Polymorphism and mutation databases

BioMutaiPIM1.
DMDMi83305339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000433491 – 404Serine/threonine-protein kinase pim-1Add BLAST404

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99PhosphoserineCombined sources1 Publication1
Modified residuei114Phosphothreonine1 Publication1
Modified residuei189Phosphoserine1 Publication1
Modified residuei352Phosphoserine1 Publication1

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.
PeptideAtlasiP11309.
PRIDEiP11309.

PTM databases

iPTMnetiP11309.
PhosphoSitePlusiP11309.

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

BgeeiENSG00000137193.
CleanExiHS_PIM1.
ExpressionAtlasiP11309. baseline and differential.
GenevisibleiP11309. HS.

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
BANPQ8N9N53EBI-696621,EBI-744695
BEND7Q8N7W2-23EBI-696621,EBI-10181188
BMXP518134EBI-696621,EBI-696657
CDKN1BP465272EBI-696621,EBI-519280
FHP079543EBI-696621,EBI-1050358
FOXO3O435242EBI-696621,EBI-1644164
FOXP3Q9BZS1-13EBI-1018633,EBI-9695448
FXR2P511163EBI-696621,EBI-740459
HEXIM2Q96MH23EBI-696621,EBI-5460660
NHLH1Q5T2033EBI-696621,EBI-10197511
RPS19P390197EBI-696621,EBI-354451
TFPTG5E9B53EBI-696621,EBI-10178002
ZBTB1Q9Y2K13EBI-696621,EBI-2682961

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111310. 41 interactors.
IntActiP11309. 19 interactors.
MINTiMINT-1412755.
STRINGi9606.ENSP00000362608.

Chemistry databases

BindingDBiP11309.

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni126 – 128Combined sources3
Beta strandi129 – 134Combined sources6
Beta strandi136 – 140Combined sources5
Beta strandi142 – 148Combined sources7
Turni149 – 151Combined sources3
Beta strandi154 – 161Combined sources8
Helixi162 – 164Combined sources3
Beta strandi168 – 170Combined sources3
Turni172 – 174Combined sources3
Beta strandi176 – 178Combined sources3
Helixi179 – 187Combined sources9
Beta strandi189 – 191Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi197 – 202Combined sources6
Beta strandi204 – 212Combined sources9
Beta strandi215 – 219Combined sources5
Helixi220 – 227Combined sources8
Helixi232 – 251Combined sources20
Helixi261 – 263Combined sources3
Beta strandi264 – 267Combined sources4
Turni268 – 271Combined sources4
Beta strandi272 – 275Combined sources4
Helixi278 – 280Combined sources3
Helixi296 – 298Combined sources3
Helixi301 – 306Combined sources6
Helixi311 – 328Combined sources18
Helixi336 – 341Combined sources6
Helixi352 – 361Combined sources10
Helixi366 – 368Combined sources3
Helixi372 – 376Combined sources5
Helixi379 – 381Combined sources3
Helixi387 – 394Combined sources8
Turni395 – 398Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MTAX-ray2.20A119-404[»]
4N6YX-ray2.60A93-404[»]
4N6ZX-ray2.20A93-404[»]
4N70X-ray2.10A93-404[»]
4RBLX-ray2.55A120-404[»]
4RC2X-ray2.10A120-404[»]
4RC3X-ray2.34A120-404[»]
4RC4X-ray2.65A120-404[»]
4RPVX-ray3.05A1-404[»]
4TY1X-ray2.70A124-396[»]
4WRSX-ray2.20A124-396[»]
4WSYX-ray2.30A124-396[»]
4WT6X-ray2.30A124-396[»]
4XH6X-ray2.04A120-404[»]
4XHKX-ray1.90B92-404[»]
5C1QX-ray3.00B120-404[»]
5DGZX-ray2.50A120-404[»]
5DHJX-ray2.46A120-404[»]
5DIAX-ray1.96A120-404[»]
5DWRX-ray2.00A93-404[»]
5EOLX-ray2.20A124-396[»]
5IISX-ray2.10A123-399[»]
5IPJX-ray2.10A124-396[»]
DisProtiDP00322.
ProteinModelPortaliP11309.
SMRiP11309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11309.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini129 – 381Protein kinasePROSITE-ProRule annotationAdd BLAST253

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiP11309.
KOiK04702.
OMAiKDTIYTD.
OrthoDBiEOG091G0IMW.
PhylomeDBiP11309.
TreeFamiTF320810.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017348. PIM1/2/3.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti106 – 107AP → RA in AAA60089 (PubMed:3475233).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041004144Y → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041005215E → Q.1 Publication1
Natural variantiVAR_041006226E → K.1 Publication1
Natural variantiVAR_041007233E → D.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0165301 – 91Missing in isoform 2. 4 PublicationsAdd BLAST91

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [P11309-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4MTAX-ray2.20A119-404[»]
4N6YX-ray2.60A93-404[»]
4N6ZX-ray2.20A93-404[»]
4N70X-ray2.10A93-404[»]
4RBLX-ray2.55A120-404[»]
4RC2X-ray2.10A120-404[»]
4RC3X-ray2.34A120-404[»]
4RC4X-ray2.65A120-404[»]
4RPVX-ray3.05A1-404[»]
4TY1X-ray2.70A124-396[»]
4WRSX-ray2.20A124-396[»]
4WSYX-ray2.30A124-396[»]
4WT6X-ray2.30A124-396[»]
4XH6X-ray2.04A120-404[»]
4XHKX-ray1.90B92-404[»]
5C1QX-ray3.00B120-404[»]
5DGZX-ray2.50A120-404[»]
5DHJX-ray2.46A120-404[»]
5DIAX-ray1.96A120-404[»]
5DWRX-ray2.00A93-404[»]
5EOLX-ray2.20A124-396[»]
5IISX-ray2.10A123-399[»]
5IPJX-ray2.10A124-396[»]
DisProtiDP00322.
ProteinModelPortaliP11309.
SMRiP11309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111310. 41 interactors.
IntActiP11309. 19 interactors.
MINTiMINT-1412755.
STRINGi9606.ENSP00000362608.

Chemistry databases

BindingDBiP11309.
ChEMBLiCHEMBL2147.
DrugBankiDB00131. Adenosine monophosphate.
GuidetoPHARMACOLOGYi2158.

PTM databases

iPTMnetiP11309.
PhosphoSitePlusiP11309.

Polymorphism and mutation databases

BioMutaiPIM1.
DMDMi83305339.

Proteomic databases

MaxQBiP11309.
PaxDbiP11309.
PeptideAtlasiP11309.
PRIDEiP11309.

Protocols and materials databases

DNASUi5292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373509; ENSP00000362608; ENSG00000137193. [P11309-2]
GeneIDi5292.
KEGGihsa:5292.
UCSCiuc003onk.4. human. [P11309-1]

Organism-specific databases

CTDi5292.
DisGeNETi5292.
GeneCardsiPIM1.
HGNCiHGNC:8986. PIM1.
HPAiCAB017040.
HPA003941.
MIMi164960. gene.
neXtProtiNX_P11309.
OpenTargetsiENSG00000137193.
PharmGKBiPA33318.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiP11309.
KOiK04702.
OMAiKDTIYTD.
OrthoDBiEOG091G0IMW.
PhylomeDBiP11309.
TreeFamiTF320810.

Enzyme and pathway databases

BioCyciZFISH:HS06287-MONOMER.
SignaLinkiP11309.
SIGNORiP11309.

Miscellaneous databases

ChiTaRSiPIM1. human.
EvolutionaryTraceiP11309.
GeneWikiiPIM1.
GenomeRNAii5292.
PROiP11309.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137193.
CleanExiHS_PIM1.
ExpressionAtlasiP11309. baseline and differential.
GenevisibleiP11309. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR017348. PIM1/2/3.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 200 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.