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Entry version 227 (05 Jun 2019)
Sequence version 4 (10 Oct 2018)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei67ATP1
Binding sitei121ATP; via carbonyl oxygen1
Binding sitei128ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei167Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi44 – 52ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P11309

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P11309

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-1 (EC:2.7.11.1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PIM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8986 PIM1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
164960 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P11309

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi68H → Y: Increased kinase activity. 1 Publication1
Mutagenesisi81P → S: Decreased kinase activity. 1 Publication1
Mutagenesisi82N → K: Decreased kinase activity. 1 Publication1
Mutagenesisi193L → F: Decreased kinase activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...
DisGeNETi
5292

Open Targets

More...
OpenTargetsi
ENSG00000137193

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33318

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2147

Drug and drug target database

More...
DrugBanki
DB03650 (3e)-3-[(4-Hydroxyphenyl)Imino]-1h-Indol-2(3h)-One
DB02656 2-(4-Morpholinyl)-8-Phenyl-4h-1-Benzopyran-4-One
DB07151 4-(4-hydroxy-3-methylphenyl)-6-phenylpyrimidin-2(5H)-one
DB00131 Adenosine monophosphate
DB04715 IMIDAZOPYRIDAZIN 1
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB04522 Phosphonoserine
DB04216 Quercetin
DB03777 Rbt205 Inhibitor
DB02010 Staurosporine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2158

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PIM1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
83305339

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000433491 – 313Serine/threonine-protein kinase pim-1Add BLAST313

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei8PhosphoserineCombined sources1 Publication1
Modified residuei23Phosphothreonine1 Publication1
Modified residuei98Phosphoserine1 Publication1
Modified residuei261Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P11309

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11309

MaxQB - The MaxQuant DataBase

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MaxQBi
P11309

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P11309

PeptideAtlas

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PeptideAtlasi
P11309

PRoteomics IDEntifications database

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PRIDEi
P11309

ProteomicsDB human proteome resource

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ProteomicsDBi
52741
52742 [P11309-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11309

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P11309

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000137193 Expressed in 216 organ(s), highest expression level in lower esophagus mucosa

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11309 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11309 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB017040
HPA003941

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Isoform 1 is isolated as a monomer whereas isoform 2 complexes with other proteins (By similarity). Binds to RP9 (By similarity). Isoform 2, but not isoform 1, binds BMX (PubMed:16186805). Isoform 1 interacts with CDKN1B and FOXO3 (PubMed:18593906). Interacts with BAD (By similarity). Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation (PubMed:12473674). Interacts with HSP90AA1, this interaction stabilizes PIM1 protein levels. Interacts (ubiquitinated form) with HSP70 and promotes its proteosomal degradation (PubMed:15798097). Interacts with CDKN1A (PubMed:12431783). Interacts with CDC25C (PubMed:16356754). Interacts (via N-terminal 96 residues) with CDC25A (By similarity). Interacts with MAP3K5 (PubMed:19749799). Interacts with MYC (By similarity). Interacts with CBX3 (PubMed:10664448).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111310, 60 interactors

Protein interaction database and analysis system

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IntActi
P11309, 22 interactors

Molecular INTeraction database

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MINTi
P11309

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000362608

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P11309

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00322

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P11309

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P11309

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 290Protein kinasePROSITE-ProRule annotationAdd BLAST253

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0583 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153394

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231357

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11309

KEGG Orthology (KO)

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KOi
K04702

Identification of Orthologs from Complete Genome Data

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OMAi
CQHLIKW

Database of Orthologous Groups

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OrthoDBi
930292at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P11309

TreeFam database of animal gene trees

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TreeFami
TF320810

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF037993 STPK_Pim-1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
MLLSKINSLA HLRAAPCNDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG
60 70 80 90 100
SVYSGIRVSD NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF
110 120 130 140 150
SGVIRLLDWF ERPDSFVLIL ERPEPVQDLF DFITERGALQ EELARSFFWQ
160 170 180 190 200
VLEAVRHCHN CGVLHRDIKD ENILIDLNRG ELKLIDFGSG ALLKDTVYTD
210 220 230 240 250
FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI PFEHDEEIIR
260 270 280 290 300
GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA
310
EIHLHSLSPG PSK
Length:313
Mass (Da):35,686
Last modified:October 10, 2018 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i35BA76D3668E69A3
GO
Isoform 2 (identifier: P11309-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPHEPHEPLT...PCADILEVGM

Note: Initiates from CTG codon.2 Publications
Show »
Length:404
Mass (Da):45,412
Checksum:i18C421B7CFF87818
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti15 – 16AP → RA in AAA60089 (PubMed:3475233).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04100453Y → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041005124E → Q1 PublicationCorresponds to variant dbSNP:rs35760989Ensembl.1
Natural variantiVAR_041006135E → K1 PublicationCorresponds to variant dbSNP:rs200523275Ensembl.1
Natural variantiVAR_041007142E → D1 PublicationCorresponds to variant dbSNP:rs33989191Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0598291M → MPHEPHEPLTPPFSALPDPA GAPSRRQSRQRPQLSSDSPS AFRASRSHSRNATRSHSHSH SPRHSLRHSPGSGSCGSSSG HRPCADILEVGM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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 No translation available.
CH471081 Genomic DNA Translation: EAX03934.1
BC020224 mRNA Translation: AAH20224.1
AF386792 Genomic DNA Translation: AAK70871.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4830.1 [P11309-1]

Protein sequence database of the Protein Information Resource

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PIRi
JU0327 TVHUP1

NCBI Reference Sequences

More...
RefSeqi
NP_001230115.1, NM_001243186.1 [P11309-2]
NP_002639.1, NM_002648.3 [P11309-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000373509; ENSP00000362608; ENSG00000137193 [P11309-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5292

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5292

UCSC genome browser

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UCSCi
uc003onk.4 human [P11309-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
CH471081 Genomic DNA Translation: EAX03934.1
BC020224 mRNA Translation: AAH20224.1
AF386792 Genomic DNA Translation: AAK70871.1
CCDSiCCDS4830.1 [P11309-1]
PIRiJU0327 TVHUP1
RefSeqiNP_001230115.1, NM_001243186.1 [P11309-2]
NP_002639.1, NM_002648.3 [P11309-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XQZX-ray2.10A14-313[»]
1XR1X-ray2.10A14-313[»]
1XWSX-ray1.80A1-313[»]
1YHSX-ray2.15A33-305[»]
1YI3X-ray2.50A33-305[»]
1YI4X-ray2.40A33-305[»]
1YWVX-ray2.00A29-313[»]
1YXSX-ray2.20A29-313[»]
1YXTX-ray2.00A29-313[»]
1YXUX-ray2.24A/B/C/D29-313[»]
1YXVX-ray2.00A29-313[»]
1YXXX-ray2.00A29-313[»]
2BIKX-ray1.80B1-313[»]
2BILX-ray2.55B1-313[»]
2BZHX-ray1.90B1-313[»]
2BZIX-ray1.90B1-313[»]
2BZJX-ray2.05A1-313[»]
2BZKX-ray2.45B1-313[»]
2C3IX-ray1.90B1-313[»]
2J2IX-ray1.90B1-312[»]
2O3PX-ray2.24A29-313[»]
2O63X-ray2.00A29-313[»]
2O64X-ray2.44A29-313[»]
2O65X-ray2.85A29-313[»]
2OBJX-ray2.50A1-313[»]
2OI4X-ray2.20X1-313[»]
2XIXX-ray2.40A14-313[»]
2XIYX-ray2.20A14-313[»]
2XIZX-ray2.21A14-313[»]
2XJ0X-ray3.10A14-313[»]
2XJ1X-ray2.13A14-313[»]
2XJ2X-ray2.20A14-313[»]
3A99X-ray1.60A15-313[»]
3BGPX-ray2.80A1-313[»]
3BGQX-ray2.00A1-313[»]
3BGZX-ray2.40A1-313[»]
3BWFX-ray2.35A1-313[»]
3C4EX-ray1.98A/B/C/D33-305[»]
3CXWX-ray2.10A1-313[»]
3CY2X-ray2.01A1-313[»]
3CY3X-ray2.15A1-313[»]
3DCVX-ray2.70A2-313[»]
3F2AX-ray1.90A14-313[»]
3JPVX-ray2.35A1-312[»]
3JXWX-ray2.80A29-313[»]
3JY0X-ray2.40A29-313[»]
3JYAX-ray2.10A29-313[»]
3MA3X-ray2.30A2-312[»]
3QF9X-ray2.20A1-312[»]
3R00X-ray2.10A29-313[»]
3R01X-ray2.60A29-313[»]
3R02X-ray1.95A29-313[»]
3R04X-ray1.70A29-313[»]
3T9IX-ray2.60A2-313[»]
3UIXX-ray2.20A29-313[»]
3UMWX-ray2.08A29-313[»]
3UMXX-ray2.55A29-313[»]
3VBQX-ray1.85A29-313[»]
3VBTX-ray2.23A29-313[»]
3VBVX-ray2.08A29-313[»]
3VBWX-ray2.48A29-313[»]
3VBXX-ray2.03A29-313[»]
3VBYX-ray2.27A29-313[»]
3VC4X-ray2.23A29-313[»]
3WE8X-ray1.95A33-305[»]
4A7CX-ray2.30A30-313[»]
4ALUX-ray2.60A2-313[»]
4ALVX-ray2.59A2-313[»]
4ALWX-ray1.92A2-313[»]
4AS0X-ray2.30A33-305[»]
4BZNX-ray1.90A2-313[»]
4BZOX-ray2.10A2-313[»]
4DTKX-ray1.86A30-305[»]
4ENXX-ray2.80A29-313[»]
4ENYX-ray2.80A29-313[»]
4GW8X-ray2.00A1-312[»]
4I41X-ray2.70A29-305[»]
4IAAX-ray2.85A29-313[»]
4JX3X-ray2.50A1-313[»]
4JX7X-ray2.40A1-313[»]
4K0YX-ray1.95A33-306[»]
4K18X-ray2.05A32-308[»]
4K1BX-ray2.08A33-305[»]
4LL5X-ray2.00A29-313[»]
4LM5X-ray2.25A29-313[»]
4LMUX-ray2.38A29-313[»]
4MBIX-ray2.30A29-313[»]
4MBLX-ray2.60A29-313[»]
4MEDX-ray2.80A29-313[»]
4MTAX-ray2.20A28-313[»]
4N6YX-ray2.60A2-313[»]
4N6ZX-ray2.20A2-313[»]
4N70X-ray2.10A2-313[»]
4RBLX-ray2.55A29-313[»]
4RC2X-ray2.10A29-313[»]
4RC3X-ray2.34A29-313[»]
4RC4X-ray2.65A29-313[»]
4RPVX-ray3.05A1-313[»]
4TY1X-ray2.70A33-305[»]
4WRSX-ray2.20A33-305[»]
4WSYX-ray2.30A33-305[»]
4WT6X-ray2.30A33-305[»]
4XH6X-ray2.04A29-313[»]
4XHKX-ray1.90B1-313[»]
5C1QX-ray3.00B29-313[»]
5DGZX-ray2.50A29-313[»]
5DHJX-ray2.46A29-313[»]
5DIAX-ray1.96A29-313[»]
5DWRX-ray2.00A2-313[»]
5EOLX-ray2.20A33-305[»]
5IISX-ray2.10A32-308[»]
5IPJX-ray2.10A33-305[»]
5KCXX-ray2.20A29-313[»]
5KGDX-ray1.98A30-305[»]
5KGEX-ray2.23A30-305[»]
5KGGX-ray1.95A30-305[»]
5KGIX-ray2.13A30-305[»]
5KGKX-ray2.66A30-305[»]
5KZIX-ray2.10A33-305[»]
5MZLX-ray1.96A1-313[»]
5N4NX-ray2.09A1-313[»]
5N4OX-ray2.22A1-313[»]
5N4RX-ray2.13A1-313[»]
5N4UX-ray2.20A1-313[»]
5N4VX-ray1.85A1-313[»]
5N4XX-ray2.20A1-313[»]
5N4YX-ray2.56A1-313[»]
5N4ZX-ray2.26A1-313[»]
5N50X-ray1.92A1-313[»]
5N51X-ray2.12A1-313[»]
5N52X-ray2.25A1-313[»]
5N5LX-ray1.97A1-313[»]
5N5MX-ray2.21A1-313[»]
5NDTX-ray1.99A1-313[»]
5O11X-ray2.40A29-313[»]
5O12X-ray2.40A29-313[»]
5O13X-ray2.44A29-313[»]
5TELX-ray2.21A33-306[»]
5TEXX-ray2.15A33-306[»]
5TOEX-ray2.30A34-306[»]
5TURX-ray2.95A1-313[»]
5V80X-ray2.25A29-313[»]
5V82X-ray1.89A29-313[»]
5VUAX-ray2.20B29-313[»]
5VUBX-ray2.00B29-313[»]
5VUCX-ray2.00B29-313[»]
6AYDX-ray3.00A1-312[»]
6BSKX-ray2.57A30-305[»]
6MT0X-ray2.20A33-305[»]
6NO9X-ray1.71A33-305[»]
6QXKX-ray2.10B1-312[»]
DisProtiDP00322
SMRiP11309
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111310, 60 interactors
IntActiP11309, 22 interactors
MINTiP11309
STRINGi9606.ENSP00000362608

Chemistry databases

BindingDBiP11309
ChEMBLiCHEMBL2147
DrugBankiDB03650 (3e)-3-[(4-Hydroxyphenyl)Imino]-1h-Indol-2(3h)-One
DB02656 2-(4-Morpholinyl)-8-Phenyl-4h-1-Benzopyran-4-One
DB07151 4-(4-hydroxy-3-methylphenyl)-6-phenylpyrimidin-2(5H)-one
DB00131 Adenosine monophosphate
DB04715 IMIDAZOPYRIDAZIN 1
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester
DB04522 Phosphonoserine
DB04216 Quercetin
DB03777 Rbt205 Inhibitor
DB02010 Staurosporine
GuidetoPHARMACOLOGYi2158

PTM databases

iPTMnetiP11309
PhosphoSitePlusiP11309

Polymorphism and mutation databases

BioMutaiPIM1
DMDMi83305339

Proteomic databases

EPDiP11309
jPOSTiP11309
MaxQBiP11309
PaxDbiP11309
PeptideAtlasiP11309
PRIDEiP11309
ProteomicsDBi52741
52742 [P11309-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5292
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5292
DisGeNETi5292

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PIM1
HGNCiHGNC:8986 PIM1
HPAiCAB017040
HPA003941
MIMi164960 gene
neXtProtiNX_P11309
OpenTargetsiENSG00000137193
PharmGKBiPA33318

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000153394
HOGENOMiHOG000231357
InParanoidiP11309
KOiK04702
OMAiCQHLIKW
OrthoDBi930292at2759
PhylomeDBiP11309
TreeFamiTF320810

Enzyme and pathway databases

ReactomeiR-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SignaLinkiP11309
SIGNORiP11309

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PIM1 human
EvolutionaryTraceiP11309

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PIM1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5292

Protein Ontology

More...
PROi
PR:P11309

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000137193 Expressed in 216 organ(s), highest expression level in lower esophagus mucosa
ExpressionAtlasiP11309 baseline and differential
GenevisibleiP11309 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPIM1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11309
Secondary accession number(s): Q38RT9, Q5T7H7, Q96RG3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 10, 2018
Last modified: June 5, 2019
This is version 227 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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