| UniProt ID | SMAD9_HUMAN | |
|---|---|---|
| UniProt AC | O15198 | |
| Protein Name | Mothers against decapentaplegic homolog 9 | |
| Gene Name | SMAD9 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 467 | |
| Subcellular Localization | Cytoplasm. Nucleus. In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity).. | |
| Protein Description | Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD).. | |
| Protein Sequence | MHSTTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQPPCSALPPSPSHAFSQSPCTASYPHSPGSPSEPESPYQHSVDTPPLPYHATEASETQSGQPVDATADRHVVLSIPNGDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MHSTTPISSL -----CCCCCCHHHH | 32.45 | 23401153 | |
| 8 | Phosphorylation | MHSTTPISSLFSFTS CCCCCCHHHHHHCCC | 23.38 | 23401153 | |
| 9 | Phosphorylation | HSTTPISSLFSFTSP CCCCCHHHHHHCCCH | 33.87 | 23401153 | |
| 12 | Phosphorylation | TPISSLFSFTSPAVK CCHHHHHHCCCHHHH | 32.67 | 23401153 | |
| 15 | Phosphorylation | SSLFSFTSPAVKRLL HHHHHCCCHHHHHHH | 14.62 | 20068231 | |
| 25 | Ubiquitination | VKRLLGWKQGDEEEK HHHHHCCCCCCHHHH | 42.47 | - | |
| 40 | Phosphorylation | WAEKAVDSLVKKLKK HHHHHHHHHHHHHHH | 28.59 | - | |
| 60 | Phosphorylation | DELERALSCPGQPSK HHHHHHHCCCCCCCC | 19.79 | 27499020 | |
| 82 | Phosphorylation | LDGRLQVSHRKGLPH CCCCEEEECCCCCCE | 12.47 | 26670566 | |
| 85 | Malonylation | RLQVSHRKGLPHVIY CEEEECCCCCCEEEE | 60.42 | 26320211 | |
| 85 | Ubiquitination | RLQVSHRKGLPHVIY CEEEECCCCCCEEEE | 60.42 | - | |
| 92 | Phosphorylation | KGLPHVIYCRVWRWP CCCCEEEEEEEEECC | 3.52 | - | |
| 136 | Phosphorylation | YHYRRVETPVLPPVL CCCCCCCCCCCCCEE | 18.81 | 30266825 | |
| 150 | Phosphorylation | LVPRHSEYNPQLSLL ECCCCCCCCHHHHHH | 34.85 | 27642862 | |
| 159 | Ubiquitination | PQLSLLAKFRSASLH HHHHHHHHHHHCCCC | 41.08 | 21890473 | |
| 159 (in isoform 2) | Ubiquitination | - | 41.08 | 21890473 | |
| 159 (in isoform 1) | Ubiquitination | - | 41.08 | 21890473 | |
| 159 | Ubiquitination | PQLSLLAKFRSASLH HHHHHHHHHHHCCCC | 41.08 | 21890473 | |
| 317 | Phosphorylation | RFCLGLLSNVNRNST CCHHHHHCCCCCCCC | 43.72 | 21712546 | |
| 323 | Phosphorylation | LSNVNRNSTIENTRR HCCCCCCCCCHHHHH | 27.76 | 28348404 | |
| 324 | Phosphorylation | SNVNRNSTIENTRRH CCCCCCCCCHHHHHH | 35.54 | 22985185 | |
| 383 (in isoform 2) | Ubiquitination | - | 28.61 | 21890473 | |
| 420 | Acetylation | TIRMSFVKGWGAEYH EEEHHHHCCCCCCHH | 47.11 | 25953088 | |
| 420 (in isoform 1) | Ubiquitination | - | 47.11 | 21890473 | |
| 420 | Ubiquitination | TIRMSFVKGWGAEYH EEEHHHHCCCCCCHH | 47.11 | 21890473 | |
| 420 | Ubiquitination | TIRMSFVKGWGAEYH EEEHHHHCCCCCCHH | 47.11 | 21890473 | |
| 454 | Phosphorylation | QWLDKVLTQMGSPHN HHHHHHHHHCCCCCC | 21.35 | 25159151 | |
| 458 | Phosphorylation | KVLTQMGSPHNPISS HHHHHCCCCCCCCCC | 20.04 | 25159151 | |
| 464 | Phosphorylation | GSPHNPISSVS---- CCCCCCCCCCC---- | 26.41 | 23911959 | |
| 465 | Phosphorylation | SPHNPISSVS----- CCCCCCCCCC----- | 27.40 | 22322096 | |
| 467 | Phosphorylation | HNPISSVS------- CCCCCCCC------- | 36.13 | 22322096 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 136 | T | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMAD9_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 SMAD9_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 615342 | Pulmonary hypertension, primary, 2 (PPH2) | |||||
| 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 |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND SER-467, ANDMASS SPECTROMETRY. | |
