| UniProt ID | ERMP1_HUMAN | |
|---|---|---|
| UniProt AC | Q7Z2K6 | |
| Protein Name | Endoplasmic reticulum metallopeptidase 1 {ECO:0000250|UniProtKB:Q6UPR8, ECO:0000312|HGNC:HGNC:23703} | |
| Gene Name | ERMP1 {ECO:0000312|HGNC:HGNC:23703} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 904 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures.. | |
| Protein Sequence | MEWGSESAAVRRHRVGVERREGAAAAPPPEREARAQEPLVDGCSGGGRTRKRSPGGSGGASRGAGTGLSEVRAALGLALYLIALRTLVQLSLQQLVLRGAAGHRGEFDALQARDYLEHITSIGPRTTGSPENEILTVHYLLEQIKLIEVQSNSLHKISVDVQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPRDGAQHAVLANCHFDSVANSPGASDDAVSCSVMLEVLRVLSTSSEALHHAVIFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILTDSIQRAGDNILAVLKHLATSDMLAAASKYRHGNMVFFDVLGLFVIAYPSRIGSIINYMVVMGVVLYLGKKFLQPKHKTGNYKKDFLCGLGITLISWFTSLVTVLIIAVFISLIGQSLSWYNHFYVSVCLYGTATVAKIILIHTLAKRFYYMNASAQYLGEVFFDISLFVHCCFLVTLTYQGLCSAFISAVWVAFPLLTKLCVHKDFKQHGAQGKFIAFYLLGMFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCAITFLLVCSGTFFPYSSNPANPKPKRVFLQHMTRTFHDLEGNAVKRDSGIWINGFDYTGISHITPHIPEINDSIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPPHFRLISKEQTPWDSIKLTFEATGPSHMSFYVRAHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVSEEHPEGMVTVAIAAHYLSGEDKRSPQLDALKEKFPDWTFPSAWVCTYDLFVF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEWGSESA -------CCCCCCHH | 9.85 | 22223895 | |
| 44 | Phosphorylation | EPLVDGCSGGGRTRK CCCCCCCCCCCCCCC | 46.10 | 25159151 | |
| 49 | Phosphorylation | GCSGGGRTRKRSPGG CCCCCCCCCCCCCCC | 43.76 | 24719451 | |
| 53 | Phosphorylation | GGRTRKRSPGGSGGA CCCCCCCCCCCCCCC | 30.82 | 30278072 | |
| 57 | Phosphorylation | RKRSPGGSGGASRGA CCCCCCCCCCCCCCC | 39.71 | 20068231 | |
| 61 | Phosphorylation | PGGSGGASRGAGTGL CCCCCCCCCCCCCCH | 34.22 | 27461979 | |
| 115 | Phosphorylation | DALQARDYLEHITSI CHHHHHHHHHHHHCC | 14.40 | - | |
| 126 | Phosphorylation | ITSIGPRTTGSPENE HHCCCCCCCCCCHHH | 38.35 | - | |
| 132 | Ubiquitination | RTTGSPENEILTVHY CCCCCCHHHHHHHHH | 45.02 | - | |
| 156 | Ubiquitination | VQSNSLHKISVDVQR ECCCCCEEEEEEEEC | 41.80 | - | |
| 169 | Ubiquitination | QRPTGSFSIDFLGGF ECCCCCEEEEECCCC | 23.97 | - | |
| 182 | N-linked_Glycosylation | GFTSYYDNITNVVVK CCCCCCCCCEEEEEE | 27.19 | UniProtKB CARBOHYD | |
| 326 | Phosphorylation | FQSGIIPSDTDFRIY HHCCCCCCCCCCEEE | 42.61 | - | |
| 356 | Ubiquitination | NGYIYHTKYDTADRI CCEEEEEECCHHHHH | 28.02 | 21906983 | |
| 362 | Methylation | TKYDTADRILTDSIQ EECCHHHHHHHHHHH | 24.29 | - | |
| 380 | Ubiquitination | DNILAVLKHLATSDM CCHHHHHHHHHHHHH | 29.94 | 21906983 | |
| 392 | Phosphorylation | SDMLAAASKYRHGNM HHHHHHHHHHHHCCE | 26.03 | - | |
| 393 | 2-Hydroxyisobutyrylation | DMLAAASKYRHGNMV HHHHHHHHHHHCCEE | 41.39 | - | |
| 393 | Ubiquitination | DMLAAASKYRHGNMV HHHHHHHHHHHCCEE | 41.39 | 21906983 | |
| 418 | Phosphorylation | AYPSRIGSIINYMVV HCHHHHHHHHHHHHH | 20.23 | 20068231 | |
| 422 | Phosphorylation | RIGSIINYMVVMGVV HHHHHHHHHHHHHHH | 4.85 | 20068231 | |
| 431 | Phosphorylation | VVMGVVLYLGKKFLQ HHHHHHHHHHHHHHC | 11.20 | 20068231 | |
| 704 | Ubiquitination | DLEGNAVKRDSGIWI HHCCCEEECCCCEEE | 48.34 | 21906983 | |
| 704 | 2-Hydroxyisobutyrylation | DLEGNAVKRDSGIWI HHCCCEEECCCCEEE | 48.34 | - | |
| 730 | N-linked_Glycosylation | TPHIPEINDSIRAHC CCCCCCCCHHHHHHH | 35.00 | 19159218 | |
| 758 | Acetylation | PVHFLIRKNWYLPAP EEEHHEECCCEECCC | 44.85 | 25825284 | |
| 758 | Ubiquitination | PVHFLIRKNWYLPAP EEEHHEECCCEECCC | 44.85 | 21906983 | |
| 768 | Phosphorylation | YLPAPEVSPRNPPHF EECCCCCCCCCCCCE | 19.24 | - | |
| 780 | Ubiquitination | PHFRLISKEQTPWDS CCEEEECCCCCCCCE | 47.01 | - | |
| 883 | Ubiquitination | SPQLDALKEKFPDWT CHHHHHHHHHCCCCC | 61.65 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ERMP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERMP1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ERMP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ERMP1_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730, AND MASSSPECTROMETRY. | |