| UniProt ID | MTL5_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y4I5 | |
| Protein Name | Tesmin {ECO:0000303|PubMed:10191092} | |
| Gene Name | TESMIN {ECO:0000312|HGNC:HGNC:7446} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 508 | |
| Subcellular Localization | Cytoplasm . Nucleus . Predominantly localized to the cytoplasm. Translocates from the cytoplasm to the nucleus in the G2/M transition upon treatment with cadmium, cobalt or zinc. | |
| Protein Description | May have a role in spermatogenesis.. | |
| Protein Sequence | MEEGPLPGGLPSPEDAMVTELLSPEGPFASENIGLKAPVKYEEDEFHVFKEAYLGPADPKEPVLHAFNPALGADCKGQVKAKLAGGDSDGGELLGEYPGIPELSALEDVALLQAPQPPACNVHFLSSLLPAHRSPAVLPLGAWVLEGASHPGVRMIPVEIKEAGGTTTSNNPEEATLQNLLAQESCCKFPSSQELEDASCCSLKKDSNPMVICQLKGGTQMLCIDNSRTRELKALHLVPQYQDQNNYLQSDVPKPMTALVGRFLPASTKLNLITQQLEGALPSVVNGSAFPSGSTLPGPPKITLAGYCDCFASGDFCNNCNCNNCCNNLHHDIERFKAIKACLGRNPEAFQPKIGKGQLGNVKPQHNKGCNCRRSGCLKNYCECYEAQIMCSSICKCIGCKNYEESPERKTLMSMPNYMQTGGLEGSHYLPPTKFSGLPRFSHDRRPSSCISWEVVEATCACLLAQGEEAEKEHCSKCLAEQMILEEFGRCLSQILHTEFKSKGLKME | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | PLPGGLPSPEDAMVT CCCCCCCCHHHHHHH | 46.06 | 28348404 | |
| 19 | Phosphorylation | SPEDAMVTELLSPEG CHHHHHHHHHCCCCC | 14.08 | 28348404 | |
| 23 | Phosphorylation | AMVTELLSPEGPFAS HHHHHHCCCCCCCCC | 33.26 | 28348404 | |
| 40 | Acetylation | IGLKAPVKYEEDEFH CCCCCCCCCCCCCEE | 45.98 | 19608861 | |
| 134 | Phosphorylation | SLLPAHRSPAVLPLG HCCCCCCCCCEEECC | 13.82 | 21712546 | |
| 166 | Phosphorylation | EIKEAGGTTTSNNPE EEEECCCCCCCCCHH | 26.44 | 19690332 | |
| 167 | Phosphorylation | IKEAGGTTTSNNPEE EEECCCCCCCCCHHH | 31.34 | 19690332 | |
| 185 | Phosphorylation | QNLLAQESCCKFPSS HHHHHHHHHCCCCCC | 16.85 | 22817900 | |
| 283 | Phosphorylation | QLEGALPSVVNGSAF HHHCCCCCCCCCCCC | 39.28 | 28387310 | |
| 292 | Phosphorylation | VNGSAFPSGSTLPGP CCCCCCCCCCCCCCC | 38.63 | 28387310 | |
| 340 | Ubiquitination | IERFKAIKACLGRNP HHHHHHHHHHHCCCH | 37.60 | 29967540 | |
| 381 | Phosphorylation | RSGCLKNYCECYEAQ CCCCHHHHHHHHHHH | 6.50 | 22210691 | |
| 385 | Phosphorylation | LKNYCECYEAQIMCS HHHHHHHHHHHHHHH | 7.63 | 22210691 | |
| 403 | Phosphorylation | KCIGCKNYEESPERK HHHCCCCCCCCCCHH | 13.43 | 22210691 | |
| 406 | Phosphorylation | GCKNYEESPERKTLM CCCCCCCCCCHHHHH | 21.81 | 22210691 | |
| 414 | Phosphorylation | PERKTLMSMPNYMQT CCHHHHHCCCCHHHC | 33.91 | 28985074 | |
| 418 | Phosphorylation | TLMSMPNYMQTGGLE HHHCCCCHHHCCCCC | 5.68 | - | |
| 433 | Phosphorylation | GSHYLPPTKFSGLPR CCCCCCCCCCCCCCC | 42.66 | 28985074 |
| 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 MTL5_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MTL5_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 MTL5_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MTL5_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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY. | |