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Protein

Serine/threonine-protein kinase pim-2

Gene

PIM2

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. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei61ATPPROSITE-ProRule annotation1
Active sitei163Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 46ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • male meiosis Source: ProtInc
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein autophosphorylation Source: GO_Central
  • protein phosphorylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of mitotic cell cycle Source: GO_Central
  • response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02350-MONOMER.
SignaLinkiQ9P1W9.
SIGNORiQ9P1W9.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-2 (EC:2.7.11.1)
Alternative name(s):
Pim-2h
Gene namesi
Name:PIM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8987. PIM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi11040.
OpenTargetsiENSG00000102096.
PharmGKBiPA33319.

Chemistry databases

ChEMBLiCHEMBL4523.
GuidetoPHARMACOLOGYi2159.

Polymorphism and mutation databases

BioMutaiPIM2.
DMDMi20139243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865321 – 311Serine/threonine-protein kinase pim-2Add BLAST311

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P1W9.
MaxQBiQ9P1W9.
PaxDbiQ9P1W9.
PeptideAtlasiQ9P1W9.
PRIDEiQ9P1W9.

PTM databases

iPTMnetiQ9P1W9.
PhosphoSitePlusiQ9P1W9.

Expressioni

Tissue specificityi

Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells. Weakly expressed in normal liver, but highly expressed in hepatocellular carcinoma tissues.1 Publication

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

BgeeiENSG00000102096.
CleanExiHS_PIM2.
ExpressionAtlasiQ9P1W9. baseline and differential.
GenevisibleiQ9P1W9. HS.

Organism-specific databases

HPAiHPA000285.

Interactioni

Subunit structurei

Interacts with MYC.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ZNF821O755413EBI-720425,EBI-740865

Protein-protein interaction databases

BioGridi116228. 17 interactors.
IntActiQ9P1W9. 18 interactors.
MINTiMINT-1432143.
STRINGi9606.ENSP00000365692.

Chemistry databases

BindingDBiQ9P1W9.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 31Combined sources4
Beta strandi32 – 39Combined sources8
Beta strandi45 – 51Combined sources7
Turni52 – 54Combined sources3
Beta strandi57 – 62Combined sources6
Turni66 – 68Combined sources3
Helixi82 – 91Combined sources10
Beta strandi97 – 99Combined sources3
Beta strandi102 – 106Combined sources5
Beta strandi113 – 117Combined sources5
Beta strandi120 – 124Combined sources5
Helixi125 – 132Combined sources8
Helixi137 – 156Combined sources20
Helixi166 – 168Combined sources3
Beta strandi169 – 172Combined sources4
Turni173 – 176Combined sources4
Beta strandi177 – 180Combined sources4
Helixi183 – 185Combined sources3
Helixi201 – 203Combined sources3
Helixi206 – 211Combined sources6
Helixi216 – 233Combined sources18
Helixi241 – 246Combined sources6
Helixi257 – 266Combined sources10
Helixi271 – 273Combined sources3
Helixi277 – 281Combined sources5
Helixi284 – 286Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWIX-ray2.80A/B1-311[»]
4X7QX-ray2.33A/B1-311[»]
ProteinModelPortaliQ9P1W9.
SMRiQ9P1W9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P1W9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 286Protein kinasePROSITE-ProRule annotationAdd BLAST255

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ9P1W9.
KOiK08806.
OMAiSDSATCP.
OrthoDBiEOG091G0IMW.
PhylomeDBiQ9P1W9.
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.

Q9P1W9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTKPLQGPP APPGTPTPPP GGKDREAFEA EYRLGPLLGK GGFGTVFAGH
60 70 80 90 100
RLTDRLQVAI KVIPRNRVLG WSPLSDSVTC PLEVALLWKV GAGGGHPGVI
110 120 130 140 150
RLLDWFETQE GFMLVLERPL PAQDLFDYIT EKGPLGEGPS RCFFGQVVAA
160 170 180 190 200
IQHCHSRGVV HRDIKDENIL IDLRRGCAKL IDFGSGALLH DEPYTDFDGT
210 220 230 240 250
RVYSPPEWIS RHQYHALPAT VWSLGILLYD MVCGDIPFER DQEILEAELH
260 270 280 290 300
FPAHVSPDCC ALIRRCLAPK PSSRPSLEEI LLDPWMQTPA EDVPLNPSKG
310
GPAPLAWSLL P
Length:311
Mass (Da):34,190
Last modified:October 1, 2000 - v1
Checksum:i160E56C368C67A69
GO

Sequence cautioni

The sequence AAC78506 differs from that shown. Reason: Frameshift at position 293.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66N → Y in BAF83620 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041008138G → D.1 PublicationCorresponds to variant rs35044770dbSNPEnsembl.1
Natural variantiVAR_041009280I → V.1 PublicationCorresponds to variant rs35208542dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77735 mRNA. Translation: AAC78506.1. Frameshift.
AK290931 mRNA. Translation: BAF83620.1.
AB042425 Genomic DNA. Translation: BAA95613.1.
AF207550 Genomic DNA. No translation available.
BC018111 mRNA. Translation: AAH18111.1.
CCDSiCCDS14312.1.
RefSeqiNP_006866.2. NM_006875.3.
UniGeneiHs.727148.

Genome annotation databases

EnsembliENST00000376509; ENSP00000365692; ENSG00000102096.
GeneIDi11040.
KEGGihsa:11040.
UCSCiuc004dls.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77735 mRNA. Translation: AAC78506.1. Frameshift.
AK290931 mRNA. Translation: BAF83620.1.
AB042425 Genomic DNA. Translation: BAA95613.1.
AF207550 Genomic DNA. No translation available.
BC018111 mRNA. Translation: AAH18111.1.
CCDSiCCDS14312.1.
RefSeqiNP_006866.2. NM_006875.3.
UniGeneiHs.727148.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWIX-ray2.80A/B1-311[»]
4X7QX-ray2.33A/B1-311[»]
ProteinModelPortaliQ9P1W9.
SMRiQ9P1W9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116228. 17 interactors.
IntActiQ9P1W9. 18 interactors.
MINTiMINT-1432143.
STRINGi9606.ENSP00000365692.

Chemistry databases

BindingDBiQ9P1W9.
ChEMBLiCHEMBL4523.
GuidetoPHARMACOLOGYi2159.

PTM databases

iPTMnetiQ9P1W9.
PhosphoSitePlusiQ9P1W9.

Polymorphism and mutation databases

BioMutaiPIM2.
DMDMi20139243.

Proteomic databases

EPDiQ9P1W9.
MaxQBiQ9P1W9.
PaxDbiQ9P1W9.
PeptideAtlasiQ9P1W9.
PRIDEiQ9P1W9.

Protocols and materials databases

DNASUi11040.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376509; ENSP00000365692; ENSG00000102096.
GeneIDi11040.
KEGGihsa:11040.
UCSCiuc004dls.4. human.

Organism-specific databases

CTDi11040.
DisGeNETi11040.
GeneCardsiPIM2.
HGNCiHGNC:8987. PIM2.
HPAiHPA000285.
MIMi300295. gene.
neXtProtiNX_Q9P1W9.
OpenTargetsiENSG00000102096.
PharmGKBiPA33319.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ9P1W9.
KOiK08806.
OMAiSDSATCP.
OrthoDBiEOG091G0IMW.
PhylomeDBiQ9P1W9.
TreeFamiTF320810.

Enzyme and pathway databases

BioCyciZFISH:HS02350-MONOMER.
SignaLinkiQ9P1W9.
SIGNORiQ9P1W9.

Miscellaneous databases

ChiTaRSiPIM2. human.
EvolutionaryTraceiQ9P1W9.
GeneWikiiPIM2_(gene).
GenomeRNAii11040.
PROiQ9P1W9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102096.
CleanExiHS_PIM2.
ExpressionAtlasiQ9P1W9. baseline and differential.
GenevisibleiQ9P1W9. 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 nameiPIM2_HUMAN
AccessioniPrimary (citable) accession number: Q9P1W9
Secondary accession number(s): A8K4G6, Q99739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 145 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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.