Gene Symbol | LNPEP |
Entrez ID | 4012 |
Uniprot ID | Q9UIQ6 |
Description | leucyl/cystinyl aminopeptidase |
Chromosomal Location | chr5: 96,935,394-97,037,515 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0000209 |
protein polyubiquitination |
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
TAS |
BP |
GO:0002480 |
antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent |
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex following intracellular transport via a pathway not requiring TAP (transporter associated with antigen processing). The peptide is typically a fragment of a larger exogenous protein which has been degraded within the cell. Class I here refers to classical class I molecules. |
TAS |
BP |
GO:0006508 |
proteolysis |
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
IEA |
BP |
GO:0007165 |
signal transduction |
The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
IBA |
BP |
GO:0007267 |
cell-cell signaling |
Any process that mediates the transfer of information from one cell to another. This process includes signal transduction in the receiving cell and, where applicable, release of a ligand and any processes that actively facilitate its transport and presentation to the receiving cell. Examples include signaling via soluble ligands, via cell adhesion molecules and via gap junctions. |
TAS |
BP |
GO:0007565 |
female pregnancy |
The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth. |
TAS |
BP |
GO:0008217 |
regulation of blood pressure |
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure. |
IBA |
BP |
GO:0030163 |
protein catabolic process |
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
IEA |
BP |
GO:0043171 |
peptide catabolic process |
The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
IBA |
BP |
GO:0060395 |
SMAD protein signal transduction |
The cascade of processes by which a signal interacts with a receptor, causing a change in the activity of a SMAD protein, and ultimately effecting a change in the functioning of the cell. |
IEA |
BP |
GO:0061024 |
membrane organization |
A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. |
TAS |
CC |
GO:0005576 |
extracellular region |
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
IEA |
CC |
GO:0005622 |
intracellular |
The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. |
IDA |
CC |
GO:0005765 |
lysosomal membrane |
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. |
IDA |
CC |
GO:0005829 |
cytosol |
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
TAS |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
TAS |
CC |
GO:0005887 |
integral component of plasma membrane |
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
TAS |
CC |
GO:0016020 |
membrane |
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
IDA |
CC |
GO:0030659 |
cytoplasmic vesicle membrane |
The lipid bilayer surrounding a cytoplasmic vesicle. |
TAS |
CC |
GO:0031905 |
early endosome lumen |
The volume enclosed by the membrane of an early endosome. |
TAS |
CC |
GO:0048471 |
perinuclear region of cytoplasm |
Cytoplasm situated near, or occurring around, the nucleus. |
IEA |
MF |
GO:0004177 |
aminopeptidase activity |
Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain. |
EXP|TAS |
MF |
GO:0008237 |
metallopeptidase activity |
Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
TAS |
MF |
GO:0008270 |
zinc ion binding |
Interacting selectively and non-covalently with zinc (Zn) ions. |
IEA |
MF |
GO:0042277 |
peptide binding |
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds. |
IBA |
MF |
GO:0070006 |
metalloaminopeptidase activity |
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
IBA |
Domain ID | Description |
---|---|
IPR001930 |
Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase |
IPR014782 |
Peptidase M1, membrane alanine aminopeptidase, N-terminal |
IPR024571 |
ERAP1-like C-terminal domain |
IPR034016 |
Aminopeptidase N-type |
IPR034017 |
Cystinyl aminopeptidase |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa04614 |
Renin-angiotensin system |
KEGG |
UMLS CUI | UMLS Term |
---|---|
C0024668 |
Mammary Neoplasms, Experimental |
C0025261 |
Memory Disorders |
Tissue | Cell Type |
---|---|
appendix |
glandular cells |
appendix |
lymphoid tissue |
caudate |
neuronal cells |
cerebellum |
cells in granular layer |
cerebral cortex |
neuronal cells |
duodenum |
glandular cells |
endometrium |
glandular cells |
epididymis |
glandular cells |
fallopian tube |
glandular cells |
hippocampus |
neuronal cells |
kidney |
cells in tubules |
lung |
macrophages |
lymph node |
germinal center cells |
lymph node |
non-germinal center cells |
placenta |
trophoblastic cells |
prostate |
glandular cells |
rectum |
glandular cells |
skin |
epidermal cells |
spleen |
cells in red pulp |
spleen |
cells in white pulp |
testis |
Leydig cells |
tonsil |
germinal center cells |
tonsil |
non-germinal center cells |
urinary bladder |
urothelial cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
22789864 |
Yan et al. |
2012 |
Expression of apoptosis-related genes in the endometrium of polycystic ovary syndrome patients during the window of implantation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
TRIP10 |
9322 |
Q15642 |
0.00 |
SLC2A4 |
6517 |
P14672 |
0.59 |
REL |
5966 |
Q04864 |
0.63 |
TCF4 |
6925 |
P15884 |
0.63 |
PRDX3 |
10935 |
P30048 |
0.63 |
PRKD2 |
25865 |
Q9BZL6 |
0.63 |
FATE1 |
89885 |
Q969F0 |
0.63 |
CANX |
821 |
P27824 |
0.72 |
DROSHA |
29102 |
Q9NRR4 |
0.72 |
NDUFA13 |
51079 |
Q9P0J0 |
0.72 |
HEATR3 |
55027 |
Q7Z4Q2 |
0.72 |
GCC1 |
79571 |
Q96CN9 |
0.72 |
TMEM263 |
90488 |
Q8WUH6 |
0.72 |
TNKS2 |
80351 |
Q9H2K2 |
0.90 |
EWSR1 |
2130 |
Q01844 |
0.49 |
TMEM216 |
51259 |
Q9P0N5 |
0.49 |
TMEM17 |
200728 |
Q86X19 |
0.49 |
AP2B1 |
163 |
P63010 |
0.63 |
CD3E |
916 |
P07766 |
0.63 |
HLA-DPA1 |
3113 |
P20036 |
0.63 |
HLA-DRA |
3122 |
P01903 |
0.63 |
LGALS3 |
3958 |
P17931 |
0.63 |
LGALS8 |
3964 |
O00214 |
0.63 |
LGALS9 |
3965 |
O00182 |
0.63 |
SMAD9 |
4093 |
O15198 |
0.63 |
TNF |
7124 |
P01375 |
0.63 |
FBXO6 |
26270 |
Q9NRD1 |
0.63 |
SIAE |
54414 |
Q9HAT2 |
0.63 |
BTNL8 |
79908 |
Q6UX41 |
0.63 |
GPHA2 |
170589 |
Q96T91 |
0.63 |
FHOD1 |
29109 |
Q9Y613 |
0.65 |
TNKS |
8658 |
O95271 |
0.86 |