| UniProt ID | HEMH_YEAST | |
|---|---|---|
| UniProt AC | P16622 | |
| Protein Name | Ferrochelatase, mitochondrial | |
| Gene Name | HEM15 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 393 | |
| Subcellular Localization |
Mitochondrion inner membrane Peripheral membrane protein Matrix side. It is bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane. |
|
| Protein Description | Catalyzes the ferrous insertion into protoporphyrin IX.. | |
| Protein Sequence | MLSRTIRTQGSFLRRSQLTITRSFSVTFNMQNAQKRSPTGIVLMNMGGPSKVEETYDFLYQLFADNDLIPISAKYQKTIAKYIAKFRTPKIEKQYREIGGGSPIRKWSEYQATEVCKILDKTCPETAPHKPYVAFRYAKPLTAETYKQMLKDGVKKAVAFSQYPHFSYSTTGSSINELWRQIKALDSERSISWSVIDRWPTNEGLIKAFSENITKKLQEFPQPVRDKVVLLFSAHSLPMDVVNTGDAYPAEVAATVYNIMQKLKFKNPYRLVWQSQVGPKPWLGAQTAEIAEFLGPKVDGLMFIPIAFTSDHIETLHEIDLGVIGESEYKDKFKRCESLNGNQTFIEGMADLVKSHLQSNQLYSNQLPLDFALGKSNDPVKDLSLVFGNHEST | |
| 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 |
|---|---|---|---|---|---|
| 81 | Acetylation | KYQKTIAKYIAKFRT HHHHHHHHHHHHHCC | 33.08 | 22865919 | |
| 95 | Phosphorylation | TPKIEKQYREIGGGS CHHHHHHHHHHCCCC | 22.68 | 21440633 | |
| 102 | Phosphorylation | YREIGGGSPIRKWSE HHHHCCCCCCCCCCH | 22.04 | 22369663 | |
| 121 | Acetylation | EVCKILDKTCPETAP HHHHHHHCCCCCCCC | 48.89 | 24489116 | |
| 130 | Acetylation | CPETAPHKPYVAFRY CCCCCCCCCEEEEEC | 36.66 | 24489116 | |
| 147 | Acetylation | PLTAETYKQMLKDGV CCCHHHHHHHHHHHH | 36.33 | 24489116 | |
| 207 | Acetylation | PTNEGLIKAFSENIT CCCHHHHHHHHHHHH | 48.71 | 24489116 | |
| 354 | Ubiquitination | EGMADLVKSHLQSNQ HHHHHHHHHHHHHCC | 39.18 | 17644757 | |
| 375 | Ubiquitination | PLDFALGKSNDPVKD CCHHHCCCCCCCCCC | 47.11 | 17644757 | |
| 381 | Acetylation | GKSNDPVKDLSLVFG CCCCCCCCCHHHEEC | 59.34 | 24489116 | |
| 393 | Phosphorylation | VFGNHEST------- EECCCCCC------- | 39.38 | 21440633 |
| 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 HEMH_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HEMH_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 HEMH_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| HEMH_YEAST | HEM15 | physical | 11831847 | |
| NCE2_YEAST | NCE102 | genetic | 27317660 | |
| KCC2B_HUMAN | CAMK2B | physical | 27107014 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY. | |