| UniProt ID | DPH1_HUMAN | |
|---|---|---|
| UniProt AC | Q9BZG8 | |
| Protein Name | 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305} | |
| Gene Name | DPH1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 443 | |
| Subcellular Localization | Nucleus . Cytoplasm . Punctate, primarily perinuclear localization. | |
| Protein Description | Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). When overexpressed, suppresses colony formation ability and growth rate of ovarian cancer cells. Acts also as a tumor suppressor in lung and breast cancers (By similarity). Plays a role in embryonic growth, organogenesis and postnatal survival (By similarity).. | |
| Protein Sequence | MRRQVMAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP | |
| 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 | VMAALVVSGAAEQGG HHHHHHHHCHHHHCC | 18.42 | 24043423 | |
| 43 (in isoform 1) | Ubiquitination | - | 72.71 | 21890473 | |
| 43 | Ubiquitination | QIPPEILKNPQLQAA CCCHHHHHCHHHHHH | 72.71 | 21906983 | |
| 56 | Phosphorylation | AAIRVLPSNYNFEIP HHHEECCCCCCCCCC | 48.03 | 18767875 | |
| 58 | Phosphorylation | IRVLPSNYNFEIPKT HEECCCCCCCCCCHH | 26.09 | 18767875 | |
| 64 | Ubiquitination | NYNFEIPKTIWRIQQ CCCCCCCHHHHHHHH | 59.30 | 21890473 | |
| 64 (in isoform 1) | Ubiquitination | - | 59.30 | 21890473 | |
| 69 | Ubiquitination | IPKTIWRIQQAQAKK CCHHHHHHHHHHHHH | 1.82 | 21963094 | |
| 75 | Ubiquitination | RIQQAQAKKVALQMP HHHHHHHHHHHHCCC | 35.38 | - | |
| 86 (in isoform 3) | Ubiquitination | - | 5.63 | 21890473 | |
| 86 | Ubiquitination | LQMPEGLLLFACTIV HCCCHHHHHHHHHHH | 5.63 | 22817900 | |
| 121 | Ubiquitination | ACCVDDFTARALGAD EEEECHHHHHHHCCC | 23.41 | 27667366 | |
| 121 (in isoform 3) | Ubiquitination | - | 23.41 | 21890473 | |
| 146 (in isoform 2) | Ubiquitination | - | 50.58 | 21890473 | |
| 148 (in isoform 3) | Ubiquitination | - | 3.75 | 21890473 | |
| 148 | Ubiquitination | MDTSAQDFRVLYVFV CCCCCCCEEEEEEEE | 3.75 | 21890473 | |
| 181 (in isoform 2) | Ubiquitination | - | 3.84 | 21890473 | |
| 198 | Ubiquitination | QAAAQELKAEYRVSV HHHHHHHHHHHCCCC | 38.12 | 21963094 | |
| 204 | Phosphorylation | LKAEYRVSVPQCKPL HHHHHCCCCCCCCCC | 21.05 | 23186163 | |
| 208 (in isoform 2) | Ubiquitination | - | 3.92 | 21890473 | |
| 209 | Ubiquitination | RVSVPQCKPLSPGEI CCCCCCCCCCCCCCC | 43.69 | 21963094 | |
| 212 | Phosphorylation | VPQCKPLSPGEILGC CCCCCCCCCCCCCCC | 39.11 | 27050516 | |
| 215 | Ubiquitination | CKPLSPGEILGCTSP CCCCCCCCCCCCCCC | 38.12 | 22817900 | |
| 220 | Phosphorylation | PGEILGCTSPRLSKE CCCCCCCCCCCCCCC | 39.71 | 25159151 | |
| 221 | Phosphorylation | GEILGCTSPRLSKEV CCCCCCCCCCCCCCE | 16.46 | 25159151 | |
| 226 (in isoform 1) | Ubiquitination | - | 71.07 | 21890473 | |
| 226 | Ubiquitination | CTSPRLSKEVEAVVY CCCCCCCCCEEEEEE | 71.07 | 22817900 | |
| 243 | Phosphorylation | DGRFHLESVMIANPN CCCEEEEEEEECCCC | 24.28 | - | |
| 250 | Ubiquitination | SVMIANPNVPAYRYD EEEECCCCCCCHHCC | 52.81 | 27667366 | |
| 256 | Phosphorylation | PNVPAYRYDPYSKVL CCCCCHHCCCHHHHH | 14.48 | - | |
| 261 | Ubiquitination | YRYDPYSKVLSREHY HHCCCHHHHHCHHHH | 41.15 | 21906983 | |
| 261 (in isoform 1) | Ubiquitination | - | 41.15 | 21890473 | |
| 274 | Ubiquitination | HYDHQRMQAARQEAI HHHHHHHHHHHHHHH | 33.78 | 21963094 | |
| 288 (in isoform 1) | Ubiquitination | - | 48.24 | 21890473 | |
| 288 | Ubiquitination | IATARSAKSWGLILG HHHHHHHHHHHHHHH | 48.24 | 21963094 | |
| 304 | Ubiquitination | LGRQGSPKILEHLES CCCCCCHHHHHHHHH | 62.71 | - | |
| 311 | Phosphorylation | KILEHLESRLRALGL HHHHHHHHHHHHHHH | 42.87 | - | |
| 382 | Ubiquitination | ISWQQPYPMDFYAGS CCCCCCCCCCEECCC | 23.66 | 21963094 | |
| 393 | Ubiquitination | YAGSSLGPWTVNHGQ ECCCCCCCCCCCCCC | 28.94 | 21963094 | |
| 414 | Ubiquitination | PGRPARGKVQEGSAR CCCCCCCCCCCCCCC | 34.88 | 21963094 | |
| 419 | Phosphorylation | RGKVQEGSARPPSAV CCCCCCCCCCCCCCE | 21.98 | 27251275 | |
| 424 | Phosphorylation | EGSARPPSAVACEDC CCCCCCCCCEEECCC | 37.75 | 25849741 | |
| 432 | Phosphorylation | AVACEDCSCRDEKVA CEEECCCCCCCCCCC | 25.22 | 23312004 |
| 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 DPH1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPH1_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 DPH1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RBM8A_HUMAN | RBM8A | physical | 11013075 | |
| UBC_HUMAN | UBC | physical | 18931663 | |
| TFCP2_HUMAN | TFCP2 | physical | 25416956 | |
| EF2_HUMAN | EEF2 | physical | 26344197 |
| 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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