UniProt ID | MFRN1_HUMAN | |
---|---|---|
UniProt AC | Q9NYZ2 | |
Protein Name | Mitoferrin-1 | |
Gene Name | SLC25A37 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 338 | |
Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein. |
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Protein Description | Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (By similarity).. | |
Protein Sequence | MELRSGSVGSQAVARRMDGDSRDGGGGKDATGSEDYENLPTSASVSTHMTAGAMAGILEHSVMYPVDSVKTRMQSLSPDPKAQYTSIYGALKKIMRTEGFWRPLRGVNVMIMGAGPAHAMYFACYENMKRTLNDVFHHQGNSHLANGIAGSMATLLHDAVMNPAEVVKQRLQMYNSQHRSAISCIRTVWRTEGLGAFYRSYTTQLTMNIPFQSIHFITYEFLQEQVNPHRTYNPQSHIISGGLAGALAAAATTPLDVCKTLLNTQENVALSLANISGRLSGMANAFRTVYQLNGLAGYFKGIQARVIYQMPSTAISWSVYEFFKYFLTKRQLENRAPY | |
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 |
---|---|---|---|---|---|
21 | Phosphorylation | ARRMDGDSRDGGGGK HHHCCCCCCCCCCCC | 37.49 | - | |
75 | Phosphorylation | SVKTRMQSLSPDPKA HHHHHHHHCCCCHHH | 22.82 | 26074081 | |
77 | Phosphorylation | KTRMQSLSPDPKAQY HHHHHHCCCCHHHHH | 32.29 | 26074081 | |
84 | Phosphorylation | SPDPKAQYTSIYGAL CCCHHHHHHHHHHHH | 13.81 | 26074081 | |
85 | Phosphorylation | PDPKAQYTSIYGALK CCHHHHHHHHHHHHH | 9.14 | 26074081 | |
86 | Phosphorylation | DPKAQYTSIYGALKK CHHHHHHHHHHHHHH | 14.63 | 26074081 | |
88 | Phosphorylation | KAQYTSIYGALKKIM HHHHHHHHHHHHHHH | 8.98 | 26074081 | |
97 | Phosphorylation | ALKKIMRTEGFWRPL HHHHHHHCCCCCCCC | 24.07 | 26074081 | |
121 | Phosphorylation | AGPAHAMYFACYENM CCHHHHHHHHHHHHH | 6.71 | 26552605 | |
125 | Phosphorylation | HAMYFACYENMKRTL HHHHHHHHHHHHHHH | 13.60 | 26552605 | |
151 | Phosphorylation | LANGIAGSMATLLHD HHHCHHHHHHHHHHH | 9.02 | - | |
198 | Phosphorylation | TEGLGAFYRSYTTQL CCCCCCHHHEEEEEE | 9.71 | - | |
325 | Phosphorylation | SVYEFFKYFLTKRQL HHHHHHHHHHHHHHH | 9.92 | - | |
328 | Phosphorylation | EFFKYFLTKRQLENR HHHHHHHHHHHHHHC | 17.81 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of MFRN1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MFRN1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MFRN1_HUMAN !! |
Kegg Disease | ||||||
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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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Phosphorylation | |
Reference | PubMed |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, AND MASSSPECTROMETRY. |