PIM1
Serine/threonine-protein kinase pim-1
Also known as: PIM, PIM1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P11309
- Gene
- PIM1
- Ensembl
- ENSG00000137193
- Chromosome
- 6
- Canonical length
- 313 aa
- Protein class
- Cancer-related genes, Enzymes, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nucleoli,Cytosol
OverviewNCBI Gene
The protein encoded by this gene belongs to the Ser/Thr protein kinase family, and PIM subfamily. This gene is expressed primarily in B-lymphoid and myeloid cell lines, and is overexpressed in hematopoietic malignancies and in prostate cancer. It plays a role in signal transduction in blood cells, contributing to both cell proliferation and survival, and thus provides a selective advantage in tumorigenesis. Both the human and orthologous mouse genes have been reported to encode two isoforms (with preferential cellular localization) resulting from the use of alternative in-frame translation initiation codons, the upstream non-AUG (CUG) and downstream AUG codons (PMIDs:16186805, 1825810).[provided by RefSeq, Aug 2011]
Canonical amino-acid sequenceUniProt
313 residues, UniProt reviewed canonical sequence.
>P11309|PIM1
1 MLLSKINSLA HLRAAPCNDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG SVYSGIRVSD
61 NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF SGVIRLLDWF ERPDSFVLIL
121 ERPEPVQDLF DFITERGALQ EELARSFFWQ VLEAVRHCHN CGVLHRDIKD ENILIDLNRG
181 ELKLIDFGSG ALLKDTVYTD FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI
241 PFEHDEEIIR GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA
301 EIHLHSLSPG PSKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PIM1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.28
- Highest tissue expression
- 207 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 207 nTPM
- esophagus: 191 nTPM
- adipose tissue: 142 nTPM
- vagina: 107 nTPM
- skin: 103 nTPM
- urinary bladder: 95 nTPM
Single-cell type
- esophageal apical cells: 1,769 nCPM
- urothelial cells: 385 nCPM
- decidual stromal cells: 302 nCPM
- esophageal suprabasal cells: 221 nCPM
- suprabasal keratinocytes: 205 nCPM
- erythrocytes: 205 nCPM
Immune cell
- basophil: 323 nTPM
- eosinophil: 114 nTPM
- MAIT T-cell: 78 nTPM
- neutrophil: 62 nTPM
- gdT-cell: 60 nTPM
- memory CD8 T-cell: 54 nTPM
Brain region
- medulla oblongata: 23 nTPM
- pons: 18 nTPM
- spinal cord: 18 nTPM
- midbrain: 17 nTPM
- white matter: 17 nTPM
- hypothalamus: 16 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.42
- gnomAD pLI
- 0.85
- gnomAD missense Z
- 1.96
- DepMap mean gene effect
- -0.21
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- apoptotic process
- cellular detoxification
- cellular response to type II interferon
- negative regulation of apoptotic process
- negative regulation of DNA-binding transcription factor activity
- negative regulation of innate immune response
- positive regulation of brown fat cell differentiation
- positive regulation of cardiac muscle cell proliferation
- positive regulation of cyclin-dependent protein serine/threonine kinase activity
- positive regulation of DNA-templated transcription
- positive regulation of protein serine/threonine kinase activity
- positive regulation of TORC1 signaling
- protein autophosphorylation
- protein phosphorylation
- protein stabilization
- regulation of hematopoietic stem cell proliferation
- regulation of mitotic cell cycle
- vitamin D receptor signaling pathway
- positive regulation of cardioblast proliferation
- regulation of transmembrane transporter activity
Molecular functions
- ATP binding
- manganese ion binding
- protein serine kinase activity
- protein serine/threonine kinase activator activity
- protein serine/threonine kinase activity
- ribosomal small subunit binding
- transcription factor binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PIM1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PIM1 as an antibody target. Whether an autoantibody or antibody against PIM1 could matter depends on whether native PIM1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PIM1 is annotated at the cell surface, where native PIM1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label PIM1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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