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Protein

Serine/threonine-protein kinase pim-1

Gene

PIM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671ATPPROSITE-ProRule annotation
Binding sitei121 – 1211ATP; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei128 – 1281ATPPROSITE-ProRule annotation
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 529ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Serine/threonine-protein kinase pim-1PRO_0000086528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei23 – 231PhosphothreonineBy similarity
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity

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.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000511.

Structurei

3D structure databases

ProteinModelPortaliQ9N0P9.
SMRiQ9N0P9. Positions 32-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 290253Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ9N0P9.
KOiK04702.
OMAiKDTIYTD.
OrthoDBiEOG7NW6B0.
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]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ9N0P9.
SMRiQ9N0P9. Positions 32-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000511.

Proteomic databases

PaxDbiQ9N0P9.
PRIDEiQ9N0P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000511; ENSBTAP00000000511; ENSBTAG00000000396.
GeneIDi281402.
KEGGibta:281402.

Organism-specific databases

CTDi5292.

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ9N0P9.
KOiK04702.
OMAiKDTIYTD.
OrthoDBiEOG7NW6B0.
TreeFamiTF320810.

Miscellaneous databases

NextBioi20805393.

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...

Publicationsi

  1. "cDNA cloning, sequencing and characterization of bovine pim-1."
    Wang Z., Petersen K., Weaver M.S., Magnuson N.S.
    Vet. Immunol. Immunopathol. 78:177-195(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPIM1_BOVIN
AccessioniPrimary (citable) accession number: Q9N0P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.