| UniProt ID | SEMG1_HUMAN | |
|---|---|---|
| UniProt AC | P04279 | |
| Protein Name | Semenogelin-1 | |
| Gene Name | SEMG1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 462 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.; Alpha-inhibin-92 and alpha-inhibin-31, derived from the proteolytic degradation of semenogelin, inhibit the secretion of pituitary follicle-stimulating hormone.. | |
| Protein Sequence | MKPNIIFVLSLLLILEKQAAVMGQKGGSKGRLPSEFSQFPHGQKGQHYSGQKGKQQTESKGSFSIQYTYHVDANDHDQSRKSQQYDLNALHKTTKSQRHLGGSQQLLHNKQEGRDHDKSKGHFHRVVIHHKGGKAHRGTQNPSQDQGNSPSGKGISSQYSNTEERLWVHGLSKEQTSVSGAQKGRKQGGSQSSYVLQTEELVANKQQRETKNSHQNKGHYQNVVEVREEHSSKVQTSLCPAHQDKLQHGSKDIFSTQDELLVYNKNQHQTKNLNQDQQHGRKANKISYQSSSTEERRLHYGENGVQKDVSQSSIYSQTEEKAQGKSQKQITIPSQEQEHSQKANKISYQSSSTEERRLHYGENGVQKDVSQRSIYSQTEKLVAGKSQIQAPNPKQEPWHGENAKGESGQSTNREQDLLSHEQKGRHQHGSHGGLDIVIIEQEDDSDRHLAQHLNNDRNPLFT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 24 | Pyrrolidone_carboxylic_acid | KQAAVMGQKGGSKGR HHHHHHCCCCCCCCC | 24.11 | 2912989 | |
| 24 | Pyrrolidone_carboxylic_acid | KQAAVMGQKGGSKGR HHHHHHCCCCCCCCC | 24.11 | 2912989 | |
| 24 | Pyrrolidone_carboxylic_acid | KQAAVMGQKGGSKGR HHHHHHCCCCCCCCC | 24.11 | - | |
| 28 | Phosphorylation | VMGQKGGSKGRLPSE HHCCCCCCCCCCCCC | 40.37 | 22210691 | |
| 103 | Phosphorylation | SQRHLGGSQQLLHNK HHHHCCHHHHHHHCC | 16.98 | 30622161 | |
| 139 | Phosphorylation | GGKAHRGTQNPSQDQ CCCCCCCCCCCCCCC | 25.73 | 20187088 | |
| 143 | Phosphorylation | HRGTQNPSQDQGNSP CCCCCCCCCCCCCCC | 54.67 | 30622161 | |
| 156 | Phosphorylation | SPSGKGISSQYSNTE CCCCCCCCCCCCCCC | 21.76 | 25003641 | |
| 172 | Phosphorylation | RLWVHGLSKEQTSVS EEEEEECCHHHHCCC | 38.44 | 30622161 | |
| 173 | Acetylation | LWVHGLSKEQTSVSG EEEEECCHHHHCCCC | 59.91 | 25038526 | |
| 245 | Acetylation | LCPAHQDKLQHGSKD CCHHHHHHHHCCCCC | 43.40 | 25038526 | |
| 255 | Phosphorylation | HGSKDIFSTQDELLV CCCCCCCCCHHHEEE | 26.03 | 25693802 | |
| 256 | Phosphorylation | GSKDIFSTQDELLVY CCCCCCCCHHHEEEE | 29.32 | 25693802 | |
| 282 | Ubiquitination | QDQQHGRKANKISYQ HHHHHHHHHHCCCCC | 61.99 | 30230243 | |
| 287 | Phosphorylation | GRKANKISYQSSSTE HHHHHCCCCCCCCHH | 20.80 | 21406692 | |
| 288 | Phosphorylation | RKANKISYQSSSTEE HHHHCCCCCCCCHHH | 18.85 | 21406692 | |
| 290 | Phosphorylation | ANKISYQSSSTEERR HHCCCCCCCCHHHHH | 20.30 | 21406692 | |
| 291 | Phosphorylation | NKISYQSSSTEERRL HCCCCCCCCHHHHHH | 26.25 | 21406692 | |
| 292 | Phosphorylation | KISYQSSSTEERRLH CCCCCCCCHHHHHHH | 45.12 | 21406692 | |
| 293 | Phosphorylation | ISYQSSSTEERRLHY CCCCCCCHHHHHHHH | 43.76 | 21406692 | |
| 315 | Phosphorylation | DVSQSSIYSQTEEKA CCCHHHHCHHHHHHH | 9.18 | - | |
| 316 | Phosphorylation | VSQSSIYSQTEEKAQ CCHHHHCHHHHHHHC | 29.02 | - | |
| 318 | Phosphorylation | QSSIYSQTEEKAQGK HHHHCHHHHHHHCCC | 39.92 | - | |
| 334 | Phosphorylation | QKQITIPSQEQEHSQ CCCCCCCHHHHHHHH | 42.36 | 30622161 | |
| 347 | Phosphorylation | SQKANKISYQSSSTE HHHHHCCCCCCCCHH | 20.80 | 21406692 | |
| 348 | Phosphorylation | QKANKISYQSSSTEE HHHHCCCCCCCCHHH | 18.85 | 21406692 | |
| 350 | Phosphorylation | ANKISYQSSSTEERR HHCCCCCCCCHHHHH | 20.30 | 21406692 | |
| 351 | Phosphorylation | NKISYQSSSTEERRL HCCCCCCCCHHHHHH | 26.25 | 21406692 | |
| 352 | Phosphorylation | KISYQSSSTEERRLH CCCCCCCCHHHHHHH | 45.12 | 21406692 | |
| 353 | Phosphorylation | ISYQSSSTEERRLHY CCCCCCCHHHHHHHH | 43.76 | 21406692 | |
| 380 | Acetylation | SIYSQTEKLVAGKSQ HHHHHHHHHHCCCCC | 52.21 | 25038526 | |
| 407 | Phosphorylation | GENAKGESGQSTNRE CCCCCCCCCCCCCHH | 51.29 | 30622161 | |
| 410 | Phosphorylation | AKGESGQSTNREQDL CCCCCCCCCCHHHHH | 31.04 | 29888752 | |
| 411 | Phosphorylation | KGESGQSTNREQDLL CCCCCCCCCHHHHHH | 30.33 | 29888752 | |
| 419 | Phosphorylation | NREQDLLSHEQKGRH CHHHHHHHHHHCCCC | 32.07 | 30622161 |
| 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 SEMG1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEMG1_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 SEMG1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SEMG2_HUMAN | SEMG2 | physical | 9523691 | |
| GT252_HUMAN | COLGALT2 | physical | 26186194 | |
| CO4A2_HUMAN | COL4A2 | physical | 26186194 | |
| GT252_HUMAN | COLGALT2 | physical | 28514442 |
| 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. | ||||||
loading...