Q9EQH2
PR
Gene name |
Erap1 (Appils, Arts1) |
Protein name |
Endoplasmic reticulum aminopeptidase 1 |
Names |
ARTS-1, Adipocyte-derived leucine aminopeptidase, A-LAP, Aminopeptidase PILS, Puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP, VEGF-induced aminopeptidase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:80898 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9EQH2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9EQH2-F1 | Predicted | AlphaFoldDB |
63 variants for Q9EQH2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389290852 | 14 | V>A | No | EVA | |
| rs251394381 | 23 | S>N | No | EVA | |
| rs8279826 | 25 | I>T | No | EVA | |
| rs8279827 | 28 | L>P | No | EVA | |
| rs261778197 | 35 | S>P | No | EVA | |
| rs3389267885 | 62 | T>I | No | EVA | |
| rs50979851 | 77 | R>Q | No | EVA | |
| rs236868652 | 83 | I>V | No | EVA | |
| rs3389221581 | 85 | H>L | No | EVA | |
| rs8279847 | 129 | L>F | No | EVA | |
| rs3389294475 | 142 | A>D | No | EVA | |
| rs3404466475 | 152 | Y>S | No | EVA | |
| rs3412056191 | 154 | S>N | No | EVA | |
| rs8279846 | 155 | T>P | No | EVA | |
| rs8279845 | 157 | R>G | No | EVA | |
| rs3389306076 | 222 | E>D | No | EVA | |
| rs3389291958 | 236 | V>G | No | EVA | |
| rs3389301116 | 286 | F>C | No | EVA | |
| rs3389290845 | 294 | K>Q | No | EVA | |
| rs248572274 | 303 | F>L | No | EVA | |
| rs46506458 | 339 | I>T | No | EVA | |
| rs1132077108 | 342 | H>Q | No | EVA | |
| rs1132669258 | 343 | E>D | No | EVA | |
| rs3404276295 | 355 | M>I | No | EVA | |
| rs3403654206 | 356 | E>A | No | EVA | |
| rs3411253494 | 356 | E>Q | No | EVA | |
| rs3404357759 | 359 | N>T | No | EVA | |
| rs3389267896 | 439 | D>E | No | EVA | |
| rs3389294431 | 443 | A>V | No | EVA | |
| rs3389309131 | 455 | Q>L | No | EVA | |
| rs3389267926 | 459 | Y>H | No | EVA | |
| rs3389277862 | 467 | L>Q | No | EVA | |
| rs3389286677 | 545 | F>L | No | EVA | |
| rs3389301122 | 580 | L>V | No | EVA | |
| rs47982101 | 591 | V>A | No | EVA | |
| rs3389252069 | 592 | G>E | No | EVA | |
| rs3389301072 | 596 | Y>* | No | EVA | |
| rs3389260815 | 606 | W>* | No | EVA | |
| rs3389306078 | 612 | L>H | No | EVA | |
| rs3389277806 | 620 | I>M | No | EVA | |
| rs46253102 | 655 | N>S | No | EVA | |
| rs3404449406 | 684 | V>L | No | EVA | |
| rs3403654290 | 685 | E>A | No | EVA | |
| rs3403591719 | 685 | E>Q | No | EVA | |
| rs3402942038 | 686 | T>P | No | EVA | |
| rs243409669 | 706 | T>I | No | EVA | |
| rs3389289127 | 713 | E>K | No | EVA | |
| rs3389294457 | 714 | R>K | No | EVA | |
| rs227221398 | 728 | N>S | No | EVA | |
| rs3404449361 | 769 | E>D* | No | EVA | |
| rs3404276365 | 770 | G>D | No | EVA | |
| rs3404528602 | 771 | W>* | No | EVA | |
| rs3404466464 | 772 | D>Y | No | EVA | |
| rs3403591693 | 775 | Y>* | No | EVA | |
| rs216766321 | 775 | Y>F | No | EVA | |
| rs3404415351 | 776 | S>R | No | EVA | |
| rs3404449455 | 778 | Y>S | No | EVA | |
| rs3404361608 | 780 | S>P | No | EVA | |
| rs3389301140 | 795 | C>S | No | EVA | |
| rs3389291916 | 815 | I>L | No | EVA | |
| rs3404415320 | 833 | V>L | No | EVA | |
| rs3389286699 | 888 | K>E | No | EVA | |
| rs3389294425 | 918 | I>L | No | EVA |
No associated diseases with Q9EQH2
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| 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. |
| integral component of membrane | The component of a 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. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
9 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. |
| endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
| interleukin-6 receptor binding | Binding to an interleukin-6 receptor. |
| metalloaminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue 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. |
| metalloexopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
| peptide binding | Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds. |
| tumor necrosis factor receptor binding | Binding to a tumor necrosis factor receptor. |
| zinc ion binding | Binding to a zinc ion (Zn). |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| adaptive immune response | An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). |
| antigen processing and presentation of endogenous peptide antigen via MHC class I | The process in which an antigen-presenting cell expresses a peptide antigen of endogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. |
| membrane protein ectodomain proteolysis | The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain). |
| 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. |
| positive regulation of angiogenesis | Any process that activates or increases angiogenesis. |
| 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. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| 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. |
| 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. |
22 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P40462 | TMA108 | Protein TMA108 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P32454 | APE2 | Aminopeptidase 2, mitochondrial | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P79171 | ANPEP | Aminopeptidase N | Felis catus (Cat) (Felis silvestris catus) | PR |
| Q9UIQ6 | LNPEP | Leucyl-cystinyl aminopeptidase | Homo sapiens (Human) | PR |
| Q9UKU6 | TRHDE | Thyrotropin-releasing hormone-degrading ectoenzyme | Homo sapiens (Human) | PR |
| P15144 | ANPEP | Aminopeptidase N | Homo sapiens (Human) | PR |
| P55786 | NPEPPS | Puromycin-sensitive aminopeptidase | Homo sapiens (Human) | PR |
| Q9NZ08 | ERAP1 | Endoplasmic reticulum aminopeptidase 1 | Homo sapiens (Human) | PR |
| P97449 | Anpep | Aminopeptidase N | Mus musculus (Mouse) | PR |
| Q11011 | Npepps | Puromycin-sensitive aminopeptidase | Mus musculus (Mouse) | PR |
| Q8C129 | Lnpep | Leucyl-cystinyl aminopeptidase | Mus musculus (Mouse) | PR |
| Q8K093 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | Mus musculus (Mouse) | PR |
| P15145 | ANPEP | Aminopeptidase N | Sus scrofa (Pig) | PR |
| Q10836 | Trhde | Thyrotropin-releasing hormone-degrading ectoenzyme | Rattus norvegicus (Rat) | PR |
| P97629 | Lnpep | Leucyl-cystinyl aminopeptidase | Rattus norvegicus (Rat) | PR |
| P15684 | Anpep | Aminopeptidase N | Rattus norvegicus (Rat) | PR |
| Q9JJ22 | Erap1 | Endoplasmic reticulum aminopeptidase 1 | Rattus norvegicus (Rat) | PR |
| Q0J5V5 | Os08g0398700 | Aminopeptidase M1-B | Oryza sativa subsp japonica (Rice) | PR |
| Q6Z6L4 | Os02g0218200 | Aminopeptidase M1-A | Oryza sativa subsp japonica (Rice) | PR |
| Q6K4E7 | Os09g0362800 | Aminopeptidase M1-D | Oryza sativa subsp japonica (Rice) | PR |
| Q17405 | AC3.5 | Aminopeptidase-like protein AC3.5 | Caenorhabditis elegans | PR |
| Q8VZH2 | APM1 | Aminopeptidase M1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPSLLPLVLT | FLSVSSPSWC | QNSDIESLKA | SNGDSFPWNN | MRLPEYMTPI | HYDLMIHANL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| STLTFWGKTE | VEIIASRPTS | TIIMHSHHLQ | ISKATLRRGA | GEMLSEEPLK | VLEYPAHEQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALLAAQPLLA | GSLYTVIIDY | AANLSESFHG | FYKSTYRTQE | GEMRILAATQ | FEPTAARMAF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PCFDEPALKA | SFSIKIKRDP | RHLAISNMPL | VKSVNVAEGL | IEDHFDITVK | MSTYLVAFII |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDFKSVSKMT | KSGVKVSVYA | VPDKINQADY | ALDAAVTLLE | FYEDYFNIPY | PLPKQDLAAI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PDFQSGAMEN | WGLTTYRESS | LLYDKEKSSA | SSKLGITMIV | SHELAHQWFG | NLVTMEWWND |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LWLNEGFAKF | MEFVSVTVTH | PELKVEDYFF | GKCFNAMEVD | ALNSSHPVST | PVENPAQIRE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MFDDVSYEKG | ACILNMLRDY | LSADTFKRGI | VQYLQKYSYK | NTKNEDLWNS | MMHICPTDGT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QTMDGFCSRS | QHSSSTSHWR | QEVVDVKTMM | NTWTLQKGFP | LITITVSGRN | VHMKQEHYMK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GSERFPETGY | LWHVPLTFIT | SKSDSVQRFL | LKTKTDVLIL | PEAVQWIKFN | VGMNGYYIVH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YADDGWASLS | GLLKEAHTTI | SSNDRASLIN | NAFQLVSIEK | LSIEKALDLT | LYLKNETEIM |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PIFQALNELI | PMYKLMEKRD | MIEVETQFKD | FLLKLLKDLI | DKQTWTDEGS | VSERMLRSQL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LLLACVRNYQ | PCVQRAERYF | REWKSSNGNM | SIPIDVTLAV | FAVGAQNTEG | WDFLYSKYQS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SLSSTEKSQI | EFSLCTSKDP | EKLQWLLDQS | FKGEIIKTQE | FPHILTLIGR | NPVGYPLAWK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FLRENWNKLV | QKFELGSSSI | AHMVMGTTDQ | FSTRARLEEV | KGFFSSLKEN | GSQLRCVQQT |
| 910 | 920 | ||||
| IETIEENIRW | MDKNFDKIRL | WLQKEKPELL |