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Protein

Serine/threonine-protein kinase pim-1

Gene

PIM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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). 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 protein 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 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei67ATPPROSITE-ProRule annotation1
Binding sitei121ATP; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei128ATPPROSITE-ProRule annotation1
Active sitei167Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 52ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle
LigandATP-binding, Magnesium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-1 (EC:2.7.11.1)
Gene namesi
Name:PIM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 23

Organism-specific databases

VGNCiVGNC:32899 PIM1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865281 – 313Serine/threonine-protein kinase pim-1Add BLAST313

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphoserineBy similarity1
Modified residuei23PhosphothreonineBy similarity1
Modified residuei98PhosphoserineBy similarity1
Modified residuei261PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylated (By similarity). Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity).By similarity
Ubiquitinated, leading to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9N0P9
PRIDEiQ9N0P9

Expressioni

Gene expression databases

BgeeiENSBTAG00000000396

Interactioni

Subunit structurei

Binds to RP9. Interacts with CDKN1B and FOXO3. Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation. 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. Interacts with MAP3K5. Interacts with MYC.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000511

Structurei

3D structure databases

ProteinModelPortaliQ9N0P9
SMRiQ9N0P9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 290Protein kinasePROSITE-ProRule annotationAdd BLAST253

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000119045
HOGENOMiHOG000231357
HOVERGENiHBG106681
InParanoidiQ9N0P9
KOiK04702
OMAiCQHLIKW
OrthoDBiEOG091G0IMW
TreeFamiTF320810

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR017348 PIM1/2/3
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PIRSFiPIRSF037993 STPK_Pim-1, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

Q9N0P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSKINSLA HLRAAPCSDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG
60 70 80 90 100
SVYSGIRVAD NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF
110 120 130 140 150
SGVIRLLDWF ERPDSFVLIL ERPEPVQDLF DFITERGALQ EELARSFFWQ
160 170 180 190 200
VLEAVRHCHD CGVLHRDIKD ENILIDLNRG ELKLIDFGSG ALLKDTVYTD
210 220 230 240 250
FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI PFEHDEEIVR
260 270 280 290 300
GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA
310
EIHLHSLSPG PSK
Length:313
Mass (Da):35,630
Last modified:October 1, 2000 - v1
Checksum:i9EF40229A847AD47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF259078 mRNA Translation: AAF67200.1
RefSeqiNP_776569.1, NM_174144.2
UniGeneiBt.272

Genome annotation databases

EnsembliENSBTAT00000000511; ENSBTAP00000000511; ENSBTAG00000000396
GeneIDi281402
KEGGibta:281402

Similar proteinsi

Entry informationi

Entry nameiPIM1_BOVIN
AccessioniPrimary (citable) accession number: Q9N0P9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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