| UniProt ID | MAP2_YEAST | |
|---|---|---|
| UniProt AC | P38174 | |
| Protein Name | Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175} | |
| Gene Name | MAP2 {ECO:0000255|HAMAP-Rule:MF_03175} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 421 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr.. | |
| Protein Sequence | MTDAEIENSPASDLKELNLENEGVEQQDQAKADESDPVESKKKKNKKKKKKKSNVKKIELLFPDGKYPEGAWMDYHQDFNLQRTTDEESRYLKRDLERAEHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAENLLAMEDPKSQGIGFPTGLSLNHCAAHFTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEINGETYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSKGDDY | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTDAEIENS ------CCHHHHCCC | 22369663 | ||
| 9 | Phosphorylation | TDAEIENSPASDLKE CHHHHCCCCHHHHHH | 22369663 | ||
| 12 | Phosphorylation | EIENSPASDLKELNL HHCCCCHHHHHHHCC | 22369663 | ||
| 35 | Phosphorylation | DQAKADESDPVESKK HHHHCCCCCHHHHHH | 22369663 | ||
| 40 | Phosphorylation | DESDPVESKKKKNKK CCCCHHHHHHHHCCC | 22890988 | ||
| 67 | Phosphorylation | LLFPDGKYPEGAWMD EECCCCCCCCCCCCC | 28889911 | ||
| 75 | Phosphorylation | PEGAWMDYHQDFNLQ CCCCCCCHHCCCCCC | 28889911 | ||
| 128 | Acetylation | DRIVPGMKLMDIADM HCCCCCCCHHHHHHH | 25381059 | ||
| 182 | Acetylation | FTPNAGDKTVLKYED CCCCCCCCEEEEEHH | 24489116 | ||
| 186 | Acetylation | AGDKTVLKYEDVMKV CCCCEEEEEHHEEEE | 24489116 | ||
| 295 | Phosphorylation | PIVKNGDTTKMEEGE EEEECCCCCCCCCCC | 27017623 | ||
| 329 | Phosphorylation | EVSHYARSAEDHQVM CEEEECCCCCCCCCC | 23749301 | ||
| 343 | Acetylation | MPTLDSAKNLLKTID CCCHHHHHHHHHHHH | 24489116 | ||
| 347 | Acetylation | DSAKNLLKTIDRNFG HHHHHHHHHHHHHCC | 22865919 | ||
| 370 | Acetylation | LDRLGQEKYLFALNN HHHHCCHHHHHHHHH | 24489116 |
| 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 MAP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAP2_YEAST !! | ||||||
* 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 MAP2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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