| UniProt ID | DOHH_HUMAN | |
|---|---|---|
| UniProt AC | Q9BU89 | |
| Protein Name | Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000303|PubMed:16533814} | |
| Gene Name | DOHH {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000312|HGNC:HGNC:28662} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 302 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate produced by deoxyhypusine synthase/DHPS on a critical lysine of the eukaryotic translation initiation factor 5A/eIF-5A. This is the second step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. [PubMed: 16533814] | |
| Protein Sequence | MVTEQEVDAIGQTLVDPKQPLQARFRALFTLRGLGGPGAIAWISQAFDDDSALLKHELAYCLGQMQDARAIPMLVDVLQDTRQEPMVRHEAGEALGAIGDPEVLEILKQYSSDPVIEVAETCQLAVRRLEWLQQHGGEPAAGPYLSVDPAPPAEERDVGRLREALLDESRPLFERYRAMFALRNAGGEEAALALAEGLHCGSALFRHEVGYVLGQLQHEAAVPQLAAALARCTENPMVRHECAEALGAIARPACLAALQAHADDPERVVRESCEVALDMYEHETGRAFQYADGLEQLRGAPS | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MVTEQEVD -------CCCHHHHH | 8.31 | 22223895 | |
| 18 | Ubiquitination | GQTLVDPKQPLQARF HCCCCCCCCCHHHHH | 61.15 | 24816145 | |
| 30 | Phosphorylation | ARFRALFTLRGLGGP HHHHHHHHHCCCCCC | 19.18 | 24719451 | |
| 44 | Phosphorylation | PGAIAWISQAFDDDS CCHHHHHHHHCCCCH | 12.54 | - | |
| 81 | Phosphorylation | LVDVLQDTRQEPMVR HHHHHHHCCCCCCHH | 22.69 | 21406692 | |
| 144 | Phosphorylation | GEPAAGPYLSVDPAP CCCCCCCCCCCCCCC | 15.64 | 28796482 | |
| 200 | Glutathionylation | ALAEGLHCGSALFRH HHHHCCCCCHHHHHH | 5.76 | 22555962 | |
| 200 | S-nitrosylation | ALAEGLHCGSALFRH HHHHCCCCCHHHHHH | 5.76 | 24105792 | |
| 242 | S-nitrosylation | NPMVRHECAEALGAI CHHHHHHHHHHHHHH | 3.20 | 24105792 | |
| 254 | S-nitrosylation | GAIARPACLAALQAH HHHHHHHHHHHHHHC | 2.70 | 24105792 | |
| 272 | Phosphorylation | PERVVRESCEVALDM HHHHHHHHHHHHHHH | 12.66 | 28796482 | |
| 273 | Glutathionylation | ERVVRESCEVALDMY HHHHHHHHHHHHHHH | 4.12 | 22555962 | |
| 273 | S-nitrosylation | ERVVRESCEVALDMY HHHHHHHHHHHHHHH | 4.12 | 24105792 | |
| 280 | Phosphorylation | CEVALDMYEHETGRA HHHHHHHHHCCCCCC | 17.50 | 28796482 | |
| 284 | Phosphorylation | LDMYEHETGRAFQYA HHHHHCCCCCCHHHH | 33.60 | 28796482 | |
| 290 | Phosphorylation | ETGRAFQYADGLEQL CCCCCHHHHHHHHHH | 10.54 | 28796482 |
| 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 DOHH_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DOHH_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 DOHH_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| IDE_HUMAN | IDE | physical | 26186194 | |
| IF5A2_HUMAN | EIF5A2 | physical | 26186194 | |
| IF5A1_HUMAN | EIF5A | physical | 26186194 | |
| SK2L2_HUMAN | SKIV2L2 | physical | 26344197 | |
| IF5A2_HUMAN | EIF5A2 | physical | 28514442 | |
| IF5A1_HUMAN | EIF5A | physical | 28514442 | |
| IDE_HUMAN | IDE | 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. | ||||||
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