Send feedback

DPP7

gene
On this page

Also known as DPPIIDPP2

Summary

DPP7 (dipeptidyl peptidase 7, HGNC:14892) is a protein-coding gene on chromosome 9q34.3, encoding Dipeptidyl peptidase 2 (Q9UHL4). Plays an important role in the degradation of some oligopeptides.

The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.

Source: NCBI Gene 29952 — RefSeq curated summary.

At a glance

  • GWAS associations: 1
  • Clinical variants (ClinVar): 176 total
  • GTEx eGene: eQTL in 45 tissues, sQTL in 50 (q < 0.05)
  • ChEMBL bioactivity: 3 clinical-phase molecules tested; no curated mechanism-of-action drug
  • Constraint (gnomAD): pLI 0.00 (LoF-tolerant), LOEUF 1.71 (unconstrained)
  • MANE Select transcript: NM_013379
  • Notable: 176 clinical variants but no curated precision-oncology (CIViC) evidence yet

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:14892
Approved symbolDPP7
Namedipeptidyl peptidase 7
Location9q34.3
Locus typegene with protein product
StatusApproved
AliasesDPPII, DPP2
Ensembl geneENSG00000176978
Ensembl biotypeprotein_coding
OMIM610537
Entrez29952

Gene structure

Transcript identifiers

Ensembl transcripts: 65 — 28 nonsense_mediated_decay, 19 protein_coding, 13 retained_intron, 5 protein_coding_CDS_not_defined

MANE Select: ENST00000371579

Transcript support level (Ensembl TSL; 1 = fully mRNA-supported): TSL 1: 1, TSL 2: 4, TSL 3: 4, TSL 5: 4

ENST00000371579, ENST00000460830, ENST00000463619, ENST00000470766, ENST00000472306, ENST00000473532, ENST00000473703, ENST00000478597, ENST00000482088, ENST00000483783, ENST00000485456, ENST00000491807, ENST00000497375, ENST00000706871, ENST00000706872, ENST00000706873, ENST00000706874, ENST00000706875, ENST00000706876, ENST00000706877, ENST00000706878, ENST00000706879, ENST00000706880, ENST00000706881, ENST00000706882, ENST00000718334, ENST00000718335, ENST00000894943, ENST00000894944, ENST00000894945, ENST00000894946, ENST00000894947, ENST00000894948, ENST00000894949, ENST00000894950, ENST00000960839, ENST00000960840, ENST00000960841, ENST00000974671, ENST00000974674, ENST00000974676, ENST00001043763, ENST00001043764, ENST00001043765, ENST00001043766, ENST00001043767, ENST00001043768, ENST00001043770, ENST00001043771, ENST00001043772, ENST00001043775, ENST00001043777, ENST00001043778, ENST00001043779, ENST00001043780, ENST00001043781, ENST00001043782, ENST00001043783, ENST00001043784, ENST00001043785, ENST00001043786, ENST00001074124, ENST00001119542, ENST00001128159, ENST00001133320

RefSeq mRNA: 4 — MANE Select: NM_013379 NM_001438108, NM_001438109, NM_001438110, NM_013379

CCDS: CCDS7030

Canonical transcript exons

ENST00000371579 — 13 exons

ExonStartEnd
ENSE00001455574137114647137114733
ENSE00001923377137114463137114576
ENSE00003495678137114243137114382
ENSE00003538243137113361137113496
ENSE00003567909137113206137113287
ENSE00003570670137112953137113119
ENSE00003576072137112112137112230
ENSE00003609068137113865137114028
ENSE00003670167137112745137112805
ENSE00004034807137111690137111754
ENSE00004034808137111873137112029
ENSE00004034809137110546137110783
ENSE00004034810137110880137110950

Expression profiles

Bgee: expression breadth ubiquitous, 243 present calls, max score 99.31.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 61.1705 / max 398.7661, expressed in 1755 samples.

Highest expression (Bgee): adenohypophysis, hemisphere of cerebellum, uterine tube, granulocyte, lobe of thyroid gland.

Genetic regulation across tissues (GTEx eQTL / sQTL)

DPP7 is an eGene in GTEx v10 — its expression is genetically regulated (eQTL) in 45 tissues and its splicing (sQTL) in 50 (q < 0.05). Strongest associations first; slope = normalized effect of the lead variant’s alternative allele.

showing 20 of 95 significant tissue × QTL associations:

TissueQTLq-valueSlopeLead variant
Thyroidsqtl2.0e-122-1.059:137111973:C:G
Adipose Subcutaneoussqtl4.4e-121-0.919:137111973:C:G
Skin Not Sun Exposed Suprapubicsqtl3.4e-112-1.009:137111973:C:G
Cells Cultured fibroblastssqtl2.1e-103-1.209:137111973:C:G
Skin Sun Exposed Lower legsqtl9.4e-79-0.929:137111973:C:G
Muscle Skeletalsqtl3.4e-77-0.739:137111973:C:G
Testissqtl9.8e-77-1.249:137111973:C:G
Artery Tibialsqtl2.3e-72-0.809:137111973:C:G
Heart Atrial Appendagesqtl1.3e-69-1.079:137111973:C:G
Nerve Tibialsqtl6.8e-67-0.769:137111973:C:G
Whole Bloodsqtl1.9e-66-0.839:137111973:C:G
Adipose Visceral Omentumsqtl2.0e-66-0.939:137111973:C:G
Esophagus Muscularissqtl1.5e-65-0.839:137111973:C:G
Cells EBV-transformed lymphocytessqtl2.7e-59-1.339:137111973:C:G
Artery Aortasqtl6.2e-59-0.929:137111973:C:G
Breast Mammary Tissuesqtl8.6e-53-0.959:137111973:C:G
Adrenal Glandsqtl1.0e-52-1.219:137111973:C:G
Colon Transversesqtl2.2e-47-0.859:137111973:C:G
Heart Left Ventriclesqtl9.6e-46-0.949:137111973:C:G
Cells Cultured fibroblastseqtl5.0e-44-0.409:137114298:G:C

FANTOM5 promoters

1 alternative TSS:

Promoter IDTPM avgSamples expressed
10330561.17051755

Top tissues by expression

showing 100 of 251 tissues by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
adenohypophysisUBERON:000219699.31gold quality
right hemisphere of cerebellumUBERON:001489099.14gold quality
right uterine tubeUBERON:000130299.07gold quality
granulocyteCL:000009499.00gold quality
right lobe of thyroid glandUBERON:000111998.95gold quality
cerebellar hemisphereUBERON:000224598.93gold quality
left testisUBERON:000453398.93gold quality
left lobe of thyroid glandUBERON:000112098.91gold quality
apex of heartUBERON:000209898.91gold quality
right testisUBERON:000453498.91gold quality
right frontal lobeUBERON:000281098.88gold quality
cerebellar cortexUBERON:000212998.84gold quality
left adrenal gland cortexUBERON:003582598.72gold quality
Brodmann (1909) area 9UBERON:001354098.69gold quality
right adrenal gland cortexUBERON:003582798.64gold quality
pituitary glandUBERON:000000798.62gold quality
left adrenal glandUBERON:000123498.61gold quality
right atrium auricular regionUBERON:000663198.59gold quality
lower esophagus mucosaUBERON:003583498.58gold quality
C1 segment of cervical spinal cordUBERON:000646998.54gold quality
right adrenal glandUBERON:000123398.50gold quality
minor salivary glandUBERON:000183098.49gold quality
anterior cingulate cortexUBERON:000983598.44gold quality
body of stomachUBERON:000116198.32gold quality
metanephros cortexUBERON:001053398.32gold quality
muscle layer of sigmoid colonUBERON:003580598.31gold quality
olfactory segment of nasal mucosaUBERON:000538698.23gold quality
esophagogastric junction muscularis propriaUBERON:003584198.20gold quality
right coronary arteryUBERON:000162598.19gold quality
lower esophagusUBERON:001347398.19gold quality
lower esophagus muscularis layerUBERON:003583398.19gold quality
skin of abdomenUBERON:000141698.17gold quality
spleenUBERON:000210698.15gold quality
mucosa of stomachUBERON:000119998.13gold quality
thyroid glandUBERON:000204698.13gold quality
body of pancreasUBERON:000115098.11gold quality
skin of legUBERON:000151198.09gold quality
cardiac atriumUBERON:000208198.02gold quality
adrenal cortexUBERON:000123598.00gold quality
small intestine Peyer’s patchUBERON:000345498.00gold quality
upper lobe of left lungUBERON:000895297.96gold quality
ascending aortaUBERON:000149697.94gold quality
left coronary arteryUBERON:000162697.92gold quality
thoracic aortaUBERON:000151597.89gold quality
tibial nerveUBERON:000132397.88gold quality
hypothalamusUBERON:000189897.83gold quality
right lungUBERON:000216797.83gold quality
nucleus accumbensUBERON:000188297.76gold quality
omental fat padUBERON:001041497.76gold quality
left uterine tubeUBERON:000130397.75gold quality
peritoneumUBERON:000235897.70gold quality
right ovaryUBERON:000211897.67gold quality
putamenUBERON:000187497.63gold quality
saliva-secreting glandUBERON:000104497.55gold quality
caudate nucleusUBERON:000187397.54gold quality
descending thoracic aortaUBERON:000234597.52gold quality
cerebellumUBERON:000203797.51gold quality
right lobe of liverUBERON:000111497.49gold quality
coronary arteryUBERON:000162197.46gold quality
endocervixUBERON:000045897.43gold quality
left ovaryUBERON:000211997.33gold quality
vermiform appendixUBERON:000115497.29gold quality
stromal cell of endometriumCL:000225597.25gold quality
adipose tissue of abdominal regionUBERON:000780897.16gold quality
amygdalaUBERON:000187697.13gold quality
prefrontal cortexUBERON:000045197.05gold quality
adrenal glandUBERON:000236997.05gold quality
heart left ventricleUBERON:000208497.03gold quality
spinal cordUBERON:000224097.00gold quality
esophagusUBERON:000104396.96gold quality
body of uterusUBERON:000985396.91gold quality
transverse colonUBERON:000115796.86gold quality
upper lobe of lungUBERON:000894896.84gold quality
testisUBERON:000047396.82gold quality
mouth mucosaUBERON:000372996.73gold quality
lymph nodeUBERON:000002996.70gold quality
cardiac ventricleUBERON:000208296.56gold quality
esophagus mucosaUBERON:000246996.31gold quality
ectocervixUBERON:001224996.28gold quality
leukocyteCL:000073896.10gold quality
monocyteCL:000057696.09gold quality
heartUBERON:000094896.06gold quality
aortaUBERON:000094795.99gold quality
small intestineUBERON:000210895.98gold quality
zone of skinUBERON:000001495.93gold quality
gall bladderUBERON:000211095.81gold quality
hindlimb stylopod muscleUBERON:000425295.79gold quality
stomachUBERON:000094595.76gold quality
mucosa of transverse colonUBERON:000499195.75gold quality
gastrocnemiusUBERON:000138895.71gold quality
cortex of kidneyUBERON:000122595.44gold quality
subcutaneous adipose tissueUBERON:000219095.34gold quality
dorsolateral prefrontal cortexUBERON:000983495.31gold quality
neocortexUBERON:000195095.22gold quality
muscle of legUBERON:000138395.14gold quality
bone marrow cellCL:000209295.09gold quality
tendon of biceps brachiiUBERON:000818895.04gold quality
fundus of stomachUBERON:000116094.87gold quality
frontal cortexUBERON:000187094.84gold quality
prostate glandUBERON:000236794.83gold quality

Single-cell (SCXA)

Detected in 4 experiment(s), a significant marker in 3.

ExperimentMarker?Max mean expression
E-HCAD-13yes11.77
E-GEOD-93593yes4.01
E-MTAB-9221no685.06
E-ANND-3no0.00

HPA expression

RNA tissue specificity: Low tissue specificity

showing 60 of 80 HPA tissues / cells by nTPM:

Tissue / cellAxisnTPMProtein (IHC)
Choroid plexustissue132.4
Pituitary glandtissue101.2
Salivary glandtissue73.1medium
Pancreastissue54.9medium
Locus coeruleustissue49.3
Parathyroid glandtissue46.9medium
Nucleus accumbenstissue44.7
Vaginatissue43.0low
Heart muscletissue39.8low
Hippocampustissue39.3low
Seminal vesicletissue38.4medium
Postcentral gyrustissue37.3
Adrenal glandtissue34.0high
Bone marrowtissue31.3high
Adipose tissuetissue30.0medium
Thyroid glandtissue27.4medium
Spinal cordtissue25.6
Spleentissue24.7medium
Fallopian tubetissue24.5medium
Prostatetissue24.4medium
Skeletal muscletissue24.2not detected
Superior colliculitissue24.1
Stomach 1tissue23.9medium
Medulla oblongatatissue23.0
Lungtissue22.9high
Thalamustissue22.7
Substantia nigratissue22.7
Ponstissue22.6
Midbraintissue22.2
Duodenumtissue22.2low
Livertissue21.6medium
Corpus callosumtissue21.2
Cervixtissue20.1not detected
Lymph nodetissue20.1medium
Ovarytissue20.1low
Gallbladdertissue19.5medium
Testistissue19.3high
Tonguetissue18.8
Hypothalamustissue18.7
Urinary bladdertissue18.5medium
Cerebral cortextissue18.1medium
Somatosensory cortextissue18.1
Hippocampal formationtissue18.0
Skin 1tissue17.7high
Motor cortextissue17.4
Putamentissue17.2
Periaqueductal graytissue16.8
Prefrontal cortextissue16.7
Ventral forebraintissue16.6
Breasttissue16.5high
Entorhinal cortextissue16.3
Septumtissue16.3
Retrosplenial and cingulate cortextissue16.1
Placentatissue16.0high
Retrosplenial cortextissue16.0
Basal gangliatissue15.9medium
Kidneytissue15.9high
Temporal cortextissue15.8
Occipital cortextissue15.8
Insular cortextissue15.2

Brain sub-regions (HPA Brain Atlas): detected in 191; highest nTPM — Blood vessel (71.1), Arcuate nucleus (65.6), Nucleus ambiguus (59.9), Habenula (58.8), Lateral funiculus (white matter) (58.2).

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): KLF2

Functional genomics

gnomAD constraint: pLI 5.69e-33, LOEUF 1.71, missense Z -2.25 — population loss-of-function intolerance (pLI ≥ 0.9 = LoF-intolerant; lower LOEUF = more constrained). gnomAD

Regional missense constraint (gnomAD)

ENST00000371579 splits into 3 regions with different missense tolerance; 0 are missense-constrained. Missense variants in a constrained region (low observed/expected) are more likely to be pathogenic. gnomAD

Region (GRCh38)Missense obs / expo/eConstrained
9:137,110,651–137,114,006624 / 531.21.17no
9:137,114,007–137,114,29615 / 37.00.41no
9:137,114,297–137,114,713168 / 124.11.35no

Literature-anchored findings (GeneRIF, showing 5)

  • catalytic properties and inhibition of this proline-specific enzyme (PMID:12529175)
  • DPP II plays a minor role in the progression of malignant melanocytic lesions (PMID:18823758)
  • DPP2 is essential for maintaining lymphocytes and fibroblasts in G(0), and its inhibition results in apoptosis mediated by induction of c-Myc and p53. (PMID:19556882)
  • The constitutive expression of dipeptidyl peptidase II mRNA in chronic lymphocytic leukemia was demonstrated. (PMID:20534982)
  • human DPP7 structures reveal the molecular basis of specific inhibition and the architectural diversity of proline-specific peptidases (PMID:22952628)

Cross-species orthologs

8 orthologs

OrganismSymbolGene ID
danio_reriodpp7ENSDARG00000027750
mus_musculusDpp7ENSMUSG00000026958
rattus_norvegicusDpp7ENSRNOG00000012640
drosophila_melanogasterCG3734FBGN0038700
drosophila_melanogasterCG18493FBGN0038701
drosophila_melanogasterCG3739FBGN0038702
drosophila_melanogasterCG11626FBGN0038705
caenorhabditis_elegansWBGENE00019682

Paralogs (2): PRSS16 (ENSG00000112812), PRCP (ENSG00000137509)

Mouse-model phenotypes

Observed phenotypes of the mouse ortholog (MGI:1933213) from MGI (Alliance of Genome Resources) — knockout/mutant phenotypes, ranked by annotation count. 11 distinct phenotype terms.

Mouse phenotype (MP)Records
abnormal eating behavior1
hyperglycemia1
increased circulating insulin level1
hepatic steatosis1
increased liver weight1
impaired glucose tolerance1
insulin resistance1
increased percent body fat/body weight1
increased circulating glucose level1
increased abdominal fat pad weight1
increased epididymal fat pad weight1

Additional cross-species homologs

Sequence homologs in species beyond Ensembl Compara’s model organisms, by Diamond local protein alignment (% sequence identity; best hit per species). Lower-identity rows are more distant homologs. The matched accessions’ gene symbols aren’t in biobtree yet, so each row shows the UniProt accession.

OrganismUniProtIdentityMethod
Pongo abeliiQ5RBU799.2%Diamond
Bos taurusQ2TA1478.3%Diamond

Genomic neighbors (locus context)

Genes flanking this one on the chromosome (NCBI/Entrez gene neighborhood). Positional context only — some neighbors share regulatory elements (bidirectional promoters, antisense/overlapping transcripts), but chromosomal adjacency is not itself a functional relationship (see Interactions for that).

SymbolTypeEntrez
MIR3621ncRNA100500811
TMEM210protein-coding100505993
GRIN1protein-coding2902
LRRC26protein-coding389816
MAN1B1-DTncRNA100289341
UAP1L1protein-coding91373
MAN1B1protein-coding11253

Protein

Protein identifiers

Dipeptidyl peptidase 2 — Q9UHL4 (reviewed: Q9UHL4)

Alternative names: Dipeptidyl aminopeptidase II, Dipeptidyl peptidase 7, Dipeptidyl peptidase II, Quiescent cell proline dipeptidase

All UniProt accessions (8): A0A9L9PXE7, A0A9L9PXM1, A0A9L9PY12, A0ABB0MVF0, A0ABB0MVF1, Q9UHL4, R4GMV4, R4GN05

UniProt curated annotations — full annotation on UniProt →

Function. Plays an important role in the degradation of some oligopeptides.

Subunit / interactions. Homodimer.

Subcellular location. Lysosome. Cytoplasmic vesicle. Secreted.

Tissue specificity. Detected in seminal plasma (at protein level).

Post-translational modifications. N-glycosylated.

Similarity. Belongs to the peptidase S28 family.

RefSeq proteins (4): NP_001425037, NP_001425038, NP_001425039, NP_037511* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR008758Peptidase_S28Family
IPR029058AB_hydrolase_foldHomologous_superfamily
IPR042269Ser_carbopepase_S28_SKSHomologous_superfamily

Pfam: PF05577

Enzyme classification (BRENDA)

  • EC 3.4.14.2 — dipeptidyl-peptidase II (BRENDA: 10 organisms, 103 substrates, 205 inhibitors, 54 Km, 32 kcat entries)

Substrate kinetics (BRENDA)

37 substrates with measured Km, best-characterized 15. Km ranges are aggregated across organisms/conditions.

SubstrateKm (mM)Measurements
GLY-PRO-4-NITROANILIDE0.018–0.595
LYS-ALA-2-NAPHTHYLAMIDE0.087–0.5554
ALA-PRO-P-NITROANILIDE0.009–0.0413
GLY-PRO-P-NITROANILIDE0.07–0.2273
ALA-ALA-4-NITROANILIDE0.487–1.222
ARG-PRO-4-NITROANILIDE0.068–0.0862
GLY-L-PRO-4-NITROANILIDE0.36–1.12
L-LYS-L-ALA-7-AMIDO-4-METHYLCOUMARIN0.36–0.932
LYS-ALA-P-NITROANILIDE0.04–0.572
LYS-PRO-P-NITROANILIDE0.0192
ALA-ALA-ALA1.671
ALA-PRO-4-NITROANILIDE0.04571
ALA-PRO-AMINO-4-TRIFLUOROMETHYLCOUMARIN0.0321
ARG-PRO-2-NAPHTHYLAMIDE0.00861
ARG-PRO-P-NITROANILIDE0.041

UniProt features (50 total): helix 19, strand 13, glycosylation site 6, turn 4, active site 3, signal peptide 1, propeptide 1, sequence variant 1, sequence conflict 1, chain 1

Structure

Experimental structures (PDB)

3 structures by resolution:

PDBTitleMethodResolution (Å)
4EBBStructure of DPP2X-RAY DIFFRACTION2
3JYHHuman dipeptidyl peptidase DPP7X-RAY DIFFRACTION2.19
3N0THuman dipeptidil peptidase DPP7 complexed with inhibitor GSK237826AX-RAY DIFFRACTION2.45

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9UHL4-F194.440.92

Human Protein Atlas

Protein class: Enzymes, ENZYME proteins, Hydrolases, Peptidases, Serine-type peptidases, Predicted secreted proteins, Plasma proteins

Protein evidence: Evidence at protein level

Subcellular location (HPA, imaging): vesicles; golgi apparatus

Antibody reliability (HPA): IH enhanced · IF supported

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (3)

PositionRole
162charge relay system
418charge relay system
443charge relay system

Glycosylation sites (6)

TypePositions
N-linked (glcnac…) asparagine363, 428, 50, 86, 315, 356

Function

Pathways and Gene Ontology

Reactome pathways

1 curated (TAS) of 3; 0 disease pathways. Curated-first; evidence = TAS (manually curated) vs IEA (electronic inference).

3 pathways:

IDPathwayEvidence
R-HSA-6798695Neutrophil degranulationcurated
R-HSA-168256Immune System—
R-HSA-168249Innate Immune System—

MSigDB gene sets: 145 (showing top): REACTOME_INNATE_IMMUNE_SYSTEM, GOCC_SECRETORY_GRANULE, MODULE_151, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_UP, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_UP, GOBP_MACROMOLECULE_CATABOLIC_PROCESS, SHETH_LIVER_CANCER_VS_TXNIP_LOSS_PAM1, GROSS_HYPOXIA_VIA_ELK3_UP, BYSTRYKH_HEMATOPOIESIS_STEM_CELL_AND_BRAIN_QTL_CIS, KINSEY_TARGETS_OF_EWSR1_FLII_FUSION_DN, GOBP_PROTEIN_CATABOLIC_PROCESS, BURTON_ADIPOGENESIS_9, MODULE_114, GOCC_SECRETORY_VESICLE, GOCC_VESICLE_LUMEN

GO Biological Process (2): proteolysis (GO:0006508), protein catabolic process (GO:0030163)

GO Molecular Function (6): aminopeptidase activity (GO:0004177), serine-type peptidase activity (GO:0008236), dipeptidyl-peptidase activity (GO:0008239), serine-type exopeptidase activity (GO:0070008), peptidase activity (GO:0008233), hydrolase activity (GO:0016787)

GO Cellular Component (6): extracellular region (GO:0005576), vesicle (GO:0031982), azurophil granule lumen (GO:0035578), extracellular exosome (GO:0070062), lysosome (GO:0005764), cytoplasmic vesicle (GO:0031410)

Reactome top-level categories

2 top-level categories:

CategoryPathways
Innate Immune System1
Immune System1

GO top-level categories

18 GO namespaces:

CategoryTerms
exopeptidase activity3
protein metabolic process2
macromolecule catabolic process1
peptidase activity1
serine hydrolase activity1
serine-type peptidase activity1
hydrolase activity1
catalytic activity, acting on a protein1
catalytic activity1
cellular anatomical structure1
membrane-bounded organelle1
vacuolar lumen1
secretory granule lumen1
azurophil granule1
extracellular vesicle1
lytic vacuole1
cytoplasm1
intracellular vesicle1

Experimentally-supported GO annotations

GO terms backed by direct experimental evidence (ECO experimental codes) — 2 of 14 annotations. The rest are phylogenetic / computational / electronic (IEA).

2 experimentally-supported GO terms:

GO termNSEvidence
extracellular exosomeCChigh-throughput assay
vesicleCCdirect assay

Protein interactions and networks

STRING

showing 15 of 900 interactions by confidence (×1000):

Protein AProtein BPartner UniProtScore
DPP7DPP4P27487866
DPP7TIMM8BQ9Y5J9843
DPP7DPP8Q6V1X1808
DPP7DPP9Q86TI2790
DPP7TIMM8AO60220755
DPP7DPP3Q9NY33677
DPP7SDHDO14521663
DPP7SDHCQ99643660
DPP7PREPP48147655
DPP7CTSCP53634624
DPP7FAPQ12884610
DPP7SDHBP21912609
DPP7PEPDP12955593
DPP7GOLGA3Q08378569
DPP7DPP10Q8N608554

IntAct

Human interaction partners of DPP7 in IntAct, one row per partner (best MIscore; records = supporting IntAct interaction records).

4 partners by confidence:

PartnerInteraction typeMIscoreRecords
CFTRphysical association0.3701
TFAP2Aphysical association0.3701
TFAP2Cphysical association0.3701
XRN1physical association0.0001

BioGRID (41 interactions; top human partners by supporting records): ABI1 (Affinity Capture-MS), AIMP1 (Co-fractionation), CEP78 (Affinity Capture-MS), CFTR (PCA), CSK (Affinity Capture-MS), CSTB (Co-fractionation), DOK2 (Affinity Capture-MS), FBXO6 (Affinity Capture-MS), HCK (Affinity Capture-MS), KIAA1429 (Affinity Capture-MS), MAP2K1 (Affinity Capture-MS), MYCBP (Co-fractionation), MYL12B (Affinity Capture-MS), NUDT21 (Affinity Capture-RNA), OBSL1 (Affinity Capture-MS)

Disease & clinical

Genetic variants

Variant evidence for DPP7: 176 ClinVar records (0 pathogenic / likely pathogenic); 1 GWAS association.

ClinVar

176 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance137
Likely benign8
Benign0

SpliceAI

Top 10 splice-impact sites by Δscore (adjacent positions with the same effect merged into one range; 22 predictions of 977):

Position(s)EffectΔscoreSites
9:137110870donor_gain1.0000
9:137110878–137110879donor_loss1.00004
9:137110959acceptor_gain1.0000
9:137111921donor_gain1.0000
9:137112951–137112952donor_loss1.00005
9:137113120–137113121acceptor_loss1.00003
9:137113124acceptor_gain1.0000
9:137113208donor_gain1.0000
9:137113498acceptor_loss1.00002
9:137113863–137113864donor_loss1.00003

AlphaMissense

1,208 missense substitutions predicted likely pathogenic (of 3,187 scored), across 293 residues. Top 20 hotspot residues, ranked by the number of likely-pathogenic substitutions (of those reachable by a single-nucleotide change), then by mean score:

ResidueLikely-pathogenic substitutionsMean am_pathogenicityMax am_pathogenicity
D41880.9900.993
D13780.9770.987
H44380.9760.996
D44680.9680.978
H10780.9660.989
D33480.9640.982
F36880.9630.997
D36680.9610.987
D45480.9610.983
S16280.9600.991
D34880.9530.987
H44480.9470.981
D4180.9410.969
S18680.9330.993
F10480.9240.987
F41280.9070.977
F4380.8910.974
F8480.8900.977
H4280.8740.956
F26680.8660.964

HPA cancer prognostics

RNA cancer specificity: Low cancer specificity

Human Protein Atlas survival analysis — favorable = higher expression predicts better survival.

4 prognostic cancer types:

CancerPrognosticp-value
Kidney Renal Clear Cell Carcinoma (TCGA)favorable0.000116
Colon Adenocarcinoma (TCGA)unfavorable0.000188
Colon Adenocarcinoma (validation)unfavorable0.000506
Pancreatic Adenocarcinoma (TCGA)favorable0.000778

Disease associations

OMIM: gene MIM:610537 | disease phenotypes:

GWAS associations

1 associations:

StudyTraitp-value
GCST005024_111Pursuit maintenance gain2e-6

EFO canonical traits (from GWAS)

1 canonical traits:

EFO IDTrait name
EFO:0008433pursuit maintenance gain measurement

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (2): CHEMBL2111469 (SELECTIVITY GROUP), CHEMBL3976 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

Phase ≥1, by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 38,302 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

3 molecules by phase:

MoleculeNamePhasePatents
CHEMBL515387GOSOGLIPTIN4823
CHEMBL1422SITAGLIPTIN426,952
CHEMBL67279TALABOSTAT310,527

PharmGKB: 1 entry (CPIC guideline: no)

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: enzyme — S28: Lysosomal Pro-Xaa carboxypeptidase

Most potent curated ligand interactions (1 total), top 1:

LigandActionAffinityParameter
UAMC00039Inhibition10.1pKi

Binding affinities (BindingDB)

1097 measured of 1692 human assays (1707 total across all organisms); most potent 50 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValuePatent
[(2R)-1-[(2S)-2-aminopropanethioyl]pyrrolidin-2-yl]boronic acidIC500.2 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
Boronic acid derivativeIC500.2 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
N4-(4-chlorobenzyl)-2,4-diaminobutanoylpiperidineIC500.22 nM
(S)-2-Amino-4-[(4-chloro-benzyl)-methyl-amino]-1-piperidin-1-yl-butan-1-oneIC500.22 nM
2-(S)-Amino-4-(2-chloro-benzylamino)-1-piperidin-1-yl-butan-1-oneIC500.23 nM
2-(S)-Amino-4-(2-benzyloxy-benzylamino)-1-piperidin-1-yl-butan-1-oneIC500.39 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(4-fluoro-piperidin-1-yl)-butan-1-oneIC500.39 nM
2-(S)-Amino-4-(4-benzyloxy-benzylamino)-1-piperidin-1-yl-butan-1-oneIC500.41 nM
(S)-2,4-Diamino-N-((R)-1-boron-dihydroxide-pentyl)-butyramideIC500.48 nM
(R)-1-((S)-2,4-diaminobutanamido)pentylboronic acidIC500.48 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(4-methyl-piperidin-1-yl)-butan-1-oneIC500.55 nM
(S)-2-Amino-4-dibenzylamino-1-piperidin-1-yl-butan-1-oneIC500.6 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(3-fluoro-piperidin-1-yl)-butan-1-oneIC500.62 nM
(2S,4S)-4-(4-chlorobenzylamino)-2-amino-1-(piperidin-1-yl)pentan-1-oneIC500.62 nM
2-(S)-Amino-4-(4-methoxy-benzylamino)-1-piperidin-1-yl-butan-1-oneIC500.66 nM
(S)-2,4-Diamino-1-(2-boron-dihydroxide-pyrrolidin-1-yl)-butan-1-oneIC500.72 nM
2-(S)-Amino-1-piperidin-1-yl-4-[(pyridin-4-ylmethyl)-amino]-butan-1-oneIC500.75 nM
Boronic acid derivativeIC500.8 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
2-(S)-Amino-1-piperidin-1-yl-4-[(thiophen-2-ylmethyl)-amino]-butan-1-oneIC500.8 nM
(S)-2,4-diamino-1-((3aR,6aR)-hexahydrocyclopenta[b]pyrrol-1(2H)-yl)butan-1-oneIC500.88 nM
2-(S)-Amino-4-phenethylamino-1-piperidin-1-yl-butan-1-oneIC500.9 nM
(R)-1-((S)-2-aminopropanoyl)pyrrolidin-2-ylboronic acidIC501 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
Boronic acid derivativeIC501 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
N-alkyl Gly-boro-Pro derivativeIC501 nM
2-(S)-Amino-4-(cyclohexylmethyl-amino)-1-piperidin-1-yl-butan-1-oneIC501.1 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(3,6-dihydro-2H-pyridin-1-yl)-butan-1-oneIC501.1 nM
2-(S)-Amino-4-[(naphthalen-2-ylmethyl)-amino]-1-piperidin-1-yl-butan-1-oneIC501.1 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(3-methyl-piperidin-1-yl)-butan-1-oneIC501.13 nM
2-(S)-Amino-4-[(naphthalen-1-ylmethyl)-amino]-1-piperidin-1-yl-butan-1-oneIC501.31 nM
2-(S)-Amino-4-(3-chloro-benzylamino)-1-piperidin-1-yl-butan-1-oneIC501.34 nM
(S)-2-Amino-4-phenylamino-1-piperidin-1-yl-butan-1-oneIC501.5 nM
N-((S)-3-Amino-4-oxo-4-piperidin-1-yl-butyl)-acetamideIC501.5 nM
2-(S)-Amino-4-(3-methoxy-benzylamino)-1-piperidin-1-yl-butan-1-oneIC501.77 nM
N-((S)-3-Amino-4-oxo-4-piperidin-1-yl-butyl)-guanidineIC501.8 nM
N-alkyl Gly-boro-Pro derivativeIC501.8 nM
2-(S)-Amino-4-(3-phenyl-propylamino)-1-piperidin-1-yl-butan-1-oneIC501.91 nM
(S)-2-(S)-Amino-1-(2-boron-dihydroxide-pyrrolidin-1-yl)-hexan-1-oneIC502 nM
2-(S)-Amino-4-benzylamino-1-piperidin-1-yl-butan-1-oneIC502.03 nM
[(2R)-1-[(2S)-2-amino-2-cyclohexylacetyl]pyrrolidin-2-yl]boronic acidIC502.1 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
2-Cyclodecylamino-1-pyrrolidin-1-yl–2-borandihydroxy-ethanoneIC502.2 nM
(S)-2-Amino-4-(4-chloro-benzylamino)-1-(2-methyl-piperidin-1-yl)-butan-1-oneIC502.3 nM
3-[((S)-3-Amino-4-oxo-4-piperidin-1-yl-butylamino)-methyl]-benzonitrileIC502.7 nM
2-(S)-Amino-4-(2,4-dimethoxy-benzylamino)-1-piperidin-1-yl-butan-1-oneIC502.7 nM
(2S,3S)-2-amino-3-(4’-fluorobiphenyl-4-yl)-1-((S)-3-fluoropyrrolidin-1-yl)butan-1-oneIC502.7 nM
Boronic acid derivativeIC502.9 nMUS-11559537: Combination therapies using caspase-1 dependent anticancer agents and PGE2 antagonists
(2S,4S)-4-(4-chlorobenzylamino)-2-amino-1-(piperidin-1-yl)hexan-1-oneIC503.4 nM
2,6-Diamino-hexanoic acid ((R)-1-boron-dihydroxide-pentyl)-amideIC503.7 nM
(2S,4S)-4-(4-chlorobenzylamino)-2-amino-5-phenyl-1-(piperidin-1-yl)pentan-1-oneIC503.8 nM
1-((S)-2-Amino-4-benzylamino-butyryl)-piperidine-2-carbonitrileIC504 nM
2-Cyclooctonylamino-1-pyrrolidin-1-yl–2-borandihydroxy-ethanoneIC504 nM

ChEMBL bioactivities

647 potent at pChembl≥5 of 1214 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
10.09Ki0.082nMCHEMBL98869
10.09Ki0.082nMCHEMBL5723377
9.85IC500.14nMCHEMBL5723377
9.68IC500.21nMCHEMBL5723377
9.66IC500.22nMCHEMBL98869
9.66IC500.22nMCHEMBL98801
9.64IC500.23nMCHEMBL98762
9.41IC500.39nMCHEMBL99506
9.41IC500.39nMCHEMBL418979
9.39IC500.41nMCHEMBL99247
9.32IC500.48nMCHEMBL194354
9.32IC500.48nMCHEMBL398076
9.32IC500.48nMCHEMBL5723377
9.32IC500.48nMCHEMBL98869
9.26IC500.55nMCHEMBL98148
9.22IC500.6nMCHEMBL97970
9.21IC500.62nMCHEMBL215299
9.21IC500.62nMCHEMBL98060
9.18IC500.66nMCHEMBL99047
9.14IC500.72nMCHEMBL194428
9.12IC500.75nMCHEMBL99111
9.10IC500.8nMCHEMBL98423
9.06IC500.88nMCHEMBL397057
9.05IC500.9nMCHEMBL317312
9.00IC501nMCHEMBL372180
8.96IC501.1nMCHEMBL98860
8.96IC501.1nMCHEMBL100370
8.96IC501.1nMCHEMBL97977
8.95IC501.13nMCHEMBL317950
8.88IC501.31nMCHEMBL97884
8.87IC501.34nMCHEMBL317949
8.82IC501.5nMCHEMBL98415
8.82IC501.5nMCHEMBL440325
8.75IC501.77nMCHEMBL327499
8.74IC501.8nMCHEMBL196933
8.74IC501.8nMCHEMBL101401
8.72IC501.91nMCHEMBL430661
8.70IC502nMCHEMBL194852
8.69IC502.03nMCHEMBL99263
8.66IC502.2nMCHEMBL196267
8.64IC502.3nMCHEMBL319520
8.57IC502.7nMCHEMBL237336
8.57IC502.7nMCHEMBL330600
8.57IC502.7nMCHEMBL99260
8.47IC503.4nMCHEMBL215244
8.43IC503.7nMCHEMBL194517
8.42IC503.8nMCHEMBL214630
8.40IC504nMCHEMBL382974
8.40IC504nMCHEMBL329314
8.39IC504.1nMCHEMBL371130

PubChem BioAssay actives

728 with measured affinity, of 2395 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-piperidin-1-ylbutan-1-one343975: Inhibition of DPP2ki0.0001uM
(2S)-2-amino-4-[(4-chlorophenyl)methyl-methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0002uM
(2S)-2-amino-4-[(2-chlorophenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0002uM
(2S)-2-amino-4-[(4-phenylmethoxyphenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0004uM
(2S)-2-amino-4-[(2-phenylmethoxyphenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0004uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(4-fluoropiperidin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0004uM
[(1R)-1-[[(2S)-2,4-diaminobutanoyl]amino]pentyl]boronic acid305098: Inhibition of human DPP2ic500.0005uM
[(1S)-1-[[(2S)-2,4-diaminobutanoyl]amino]pentyl]boronic acid254911: Inhibitory concentration against human dipeptidylpeptidase 7ic500.0005uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(4-methylpiperidin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0006uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(3-fluoropiperidin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0006uM
(2S)-2-amino-4-(dibenzylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0006uM
(2S,4S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-piperidin-1-ylpentan-1-one270815: Inhibition of DPP2ic500.0006uM
(2S)-2-amino-4-[(4-methoxyphenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0007uM
[(2S)-1-[(2S)-2,4-diaminobutanoyl]pyrrolidin-2-yl]boronic acid254911: Inhibitory concentration against human dipeptidylpeptidase 7ic500.0007uM
(2S)-2-amino-1-piperidin-1-yl-4-(thiophen-2-ylmethylamino)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0008uM
(2S)-2-amino-1-piperidin-1-yl-4-(pyridin-4-ylmethylamino)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0008uM
(2S)-2-amino-4-(2-phenylethylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0009uM
(2S)-1-[(3aR,6aR)-3,3a,4,5,6,6a-hexahydro-2H-cyclopenta[b]pyrrol-1-yl]-2,4-diaminobutan-1-one305098: Inhibition of human DPP2ic500.0009uM
[(2R)-1-[2-[(4-pentyl-1-bicyclo[2.2.2]octanyl)amino]acetyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0010uM
(2S)-2-amino-4-(naphthalen-2-ylmethylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0011uM
(2S)-2-amino-4-(cyclohexylmethylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0011uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(3,6-dihydro-2H-pyridin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0011uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(3-methylpiperidin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0011uM
(2S)-2-amino-4-(naphthalen-1-ylmethylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0013uM
(2S)-2-amino-4-[(3-chlorophenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0013uM
N-[(3S)-3-amino-4-oxo-4-piperidin-1-ylbutyl]acetamide56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0015uM
(2S)-2-amino-4-anilino-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0015uM
2-[(3S)-3-amino-4-oxo-4-piperidin-1-ylbutyl]guanidine56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0018uM
(2S)-2-amino-4-[(3-methoxyphenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0018uM
[(2R)-1-[2-(cycloheptylamino)acetyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0018uM
(2S)-2-amino-4-(3-phenylpropylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0019uM
[(2S)-1-[(2S)-2-aminohexanoyl]pyrrolidin-2-yl]boronic acid254911: Inhibitory concentration against human dipeptidylpeptidase 7ic500.0020uM
(2S)-2-amino-4-(benzylamino)-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0020uM
[(2R)-1-[2-(cyclodecylamino)acetyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0022uM
(2S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-(2-methylpiperidin-1-yl)butan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0023uM
3-[[[(3S)-3-amino-4-oxo-4-piperidin-1-ylbutyl]amino]methyl]benzonitrile56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0027uM
(2S)-2-amino-4-[(2,4-dimethoxyphenyl)methylamino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0027uM
(2S,3S)-2-amino-3-[4-(4-fluorophenyl)phenyl]-1-[(3S)-3-fluoropyrrolidin-1-yl]butan-1-one393710: Inhibition of QPPic500.0027uM
(2S,4S)-2-amino-4-[(4-chlorophenyl)methylamino]-1-piperidin-1-ylhexan-1-one270815: Inhibition of DPP2ic500.0034uM
[(1S)-1-[[(2S)-2,6-diaminohexanoyl]amino]pentyl]boronic acid254911: Inhibitory concentration against human dipeptidylpeptidase 7ic500.0037uM
(2S,4S)-2-amino-4-[(4-chlorophenyl)methylamino]-5-phenyl-1-piperidin-1-ylpentan-1-one270815: Inhibition of DPP2ic500.0038uM
1-[(2S)-2-amino-4-(benzylamino)butanoyl]piperidine-2-carbonitrile56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0040uM
[(2R)-1-[2-(cyclooctylamino)acetyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0040uM
[(2R)-1-[2-(cyclohexylamino)acetyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0041uM
(2S)-2-amino-4-[bis[(4-chlorophenyl)methyl]amino]-1-piperidin-1-ylbutan-1-one56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0042uM
6-[[(3S)-3-amino-4-oxo-4-piperidin-1-ylbutyl]amino]pyridine-3-carbonitrile56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0046uM
[(1S)-1-[[(2S)-2,5-diaminopentanoyl]amino]pentyl]boronic acid254911: Inhibitory concentration against human dipeptidylpeptidase 7ic500.0047uM
4-methyl-3-[(1-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide2148261: Binding affinity to human DPP7 incubated for 45 mins by Kinobead based pull down assaykd0.0053uM
[(2R)-1-[(2R)-2-aminopropanoyl]pyrrolidin-2-yl]boronic acid255032: Inhibitory activity against human DPP7 using Ala-Pro-AMC in fluorometric assayic500.0063uM
1-[(2S)-2-amino-4-[(4-chlorophenyl)methylamino]butanoyl]piperidine-2-carbonitrile56221: Inhibition of human Dipeptidylpeptidase II (DPP II)ic500.0065uM

CTD chemical–gene interactions

40 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
sodium arsenitedecreases expression, increases expression2
UAMC00039decreases reaction, increases cleavage, increases abundance, decreases activity2
Valproic Aciddecreases expression, increases methylation2
bisphenol Fincreases expression1
methylmercuric chloridedecreases expression1
sodium arsenateincreases abundance, increases expression1
4-nitroanilineincreases abundance, increases cleavage, increases reaction, decreases reaction1
ferrous chloridedecreases expression1
nickel sulfatedecreases expression1
benzyloxycarbonylleucyl-leucyl-leucine aldehydeincreases abundance, increases cleavage, increases reaction1
alanylproline-4-nitroanilideincreases cleavage, decreases reaction1
ICG 001increases expression1
bisphenol Bincreases expression1
bisphenol Sincreases expression1
jinfukangaffects cotreatment, increases expression1
(+)-JQ1 compounddecreases expression1
bisphenol AFincreases expression1
Temozolomidedecreases expression1
Sunitinibincreases expression1
Air Pollutantsaffects expression, increases abundance1
Arbutindecreases expression1
Arsenicincreases abundance, increases expression1
Benzo(a)pyreneincreases expression1
Cisplatinaffects cotreatment, increases expression1
Diazinonincreases methylation1
Dipeptidesincreases abundance, increases cleavage, increases reaction, decreases reaction1
Estradiolincreases expression1
Ethyl Methanesulfonatedecreases expression1
Etoposideincreases abundance, increases cleavage, increases reaction1
Formaldehydedecreases expression1

ChEMBL screening assays

147 unique, capped per target: 142 binding, 4 functional, 1 admet

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL665781BindingSelectivity index of compound was determined for human Dipeptidylpeptidase IV to that of Dipeptidyl-peptidase IIDesign, synthesis, and SAR of potent and selective dipeptide-derived inhibitors for dipeptidyl peptidases. — *J Med Chem*
CHEMBL4617710ADMETInhibition of mammalian DPP7 (unknown origin) using H-Lys-Pro-AMC as substrate preincubated for 10 mins followed by substrate addition measured after 30 minsDiscovery of Cyclic Boronic Acid QPX7728, an Ultrabroad-Spectrum Inhibitor of Serine and Metallo-β-lactamases. — *J Med Chem*
CHEMBL5723296FunctionalAffinity Biochemical interaction: (enzymatic assay (fluorogenic substrate cleavage)) EUB0002750aCl DPP7Affinity Biochemical Literature for EUbOPEN Chemogenomic Library

Clinical trials (associated diseases)

Via MONDO — disease-level, not drug-specific.

Predicted chemistry — Sugi Predict

The predicted patent-compound landscape for DPP7 across ~30M SureChEMBL compounds — explore on Sugi Predict.