UniProt ID | SMAD1_HUMAN | |
---|---|---|
UniProt AC | Q15797 | |
Protein Name | Mothers against decapentaplegic homolog 1 | |
Gene Name | SMAD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 465 | |
Subcellular Localization | Cytoplasm . Nucleus . Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4 (PubMed:15647271). Co-localizes with LEMD3 at the nucleus inner membrane (PubMed:15647271). Exported from the nucleus to the cytoplasm when | |
Protein Description | Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.. | |
Protein Sequence | MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MNVTSLFS -------CCCCCCCC | 9.09 | - | |
5 | Phosphorylation | ---MNVTSLFSFTSP ---CCCCCCCCCCCH | 24.12 | 28348404 | |
8 | Phosphorylation | MNVTSLFSFTSPAVK CCCCCCCCCCCHHHH | 32.67 | 26270265 | |
10 | Phosphorylation | VTSLFSFTSPAVKRL CCCCCCCCCHHHHHH | 32.38 | 22199227 | |
11 | Phosphorylation | TSLFSFTSPAVKRLL CCCCCCCCHHHHHHH | 14.62 | 22199227 | |
21 | Ubiquitination | VKRLLGWKQGDEEEK HHHHHCCCCCCHHHH | 42.47 | 29967540 | |
28 | Ubiquitination | KQGDEEEKWAEKAVD CCCCHHHHHHHHHHH | 55.79 | 27667366 | |
32 | Ubiquitination | EEEKWAEKAVDALVK HHHHHHHHHHHHHHH | 46.06 | 29967540 | |
62 | Phosphorylation | LSCPGQPSNCVTIPR HCCCCCCCCEEEECC | 34.67 | 24400094 | |
78 | Phosphorylation | LDGRLQVSHRKGLPH CCCCEEEECCCCCCE | 12.47 | 26670566 | |
81 | Ubiquitination | RLQVSHRKGLPHVIY CEEEECCCCCCEEEE | 60.42 | 33845483 | |
88 | Phosphorylation | KGLPHVIYCRVWRWP CCCCEEEEEEEEECC | 3.52 | - | |
116 | Ubiquitination | CEFPFGSKQKEVCIN ECCCCCCCCCEEEEC | 66.81 | 22817900 | |
116 | Sumoylation | CEFPFGSKQKEVCIN ECCCCCCCCCEEEEC | 66.81 | - | |
118 | Ubiquitination | FPFGSKQKEVCINPY CCCCCCCCEEEECCC | 56.71 | 22817900 | |
118 | Sumoylation | FPFGSKQKEVCINPY CCCCCCCCEEEECCC | 56.71 | - | |
127 | Phosphorylation | VCINPYHYKRVESPV EEECCCCCCCCCCCC | 8.47 | 12601080 | |
132 | Phosphorylation | YHYKRVESPVLPPVL CCCCCCCCCCCCCEE | 19.90 | 30266825 | |
144 | Phosphorylation | PVLVPRHSEYNPQHS CEECCCCCCCCCCCC | 42.95 | 24719451 | |
146 | Phosphorylation | LVPRHSEYNPQHSLL ECCCCCCCCCCCCHH | 34.85 | 27282143 | |
151 | Phosphorylation | SEYNPQHSLLAQFRN CCCCCCCCHHHHHHH | 21.60 | 29214152 | |
187 | Phosphorylation | NSHPFPHSPNSSYPN CCCCCCCCCCCCCCC | 26.47 | 22817900 | |
195 | Phosphorylation | PNSSYPNSPGSSSST CCCCCCCCCCCCCCC | 26.57 | 22817900 | |
202 | Phosphorylation | SPGSSSSTYPHSPTS CCCCCCCCCCCCCCC | 42.91 | 22817900 | |
206 | Phosphorylation | SSSTYPHSPTSSDPG CCCCCCCCCCCCCCC | 25.93 | 22817900 | |
214 | Phosphorylation | PTSSDPGSPFQMPAD CCCCCCCCCCCCCCC | 28.12 | 22817900 | |
239 | Phosphorylation | DPMTQDGSQPMDTNM CCCCCCCCCCCCCCC | 39.12 | 22588298 | |
265 | Phosphorylation | GDVQAVAYEEPKHWC CCEEEEEECCCCCEE | 17.77 | 27642862 | |
269 | Ubiquitination | AVAYEEPKHWCSIVY EEEECCCCCEEEEEE | 53.68 | 22817900 | |
315 | Phosphorylation | RFCLGLLSNVNRNST CEEHHHHCCCCCCCC | 43.72 | 21712546 | |
321 | Phosphorylation | LSNVNRNSTIENTRR HCCCCCCCCCHHHHH | 27.76 | 28348404 | |
322 | Phosphorylation | SNVNRNSTIENTRRH CCCCCCCCCHHHHHH | 35.54 | 22985185 | |
337 | Phosphorylation | IGKGVHLYYVGGEVY CCCCEEEEEECCEEE | 4.92 | 22468782 | |
338 | Phosphorylation | GKGVHLYYVGGEVYA CCCEEEEEECCEEEE | 10.05 | 22468782 | |
344 | Phosphorylation | YYVGGEVYAECLSDS EEECCEEEEECCCCC | 7.74 | 22468782 | |
418 | Ubiquitination | TIRMSFVKGWGAEYH CEEHHHHCCCCCCHH | 47.11 | 21890473 | |
452 | Phosphorylation | QWLDKVLTQMGSPHN HHHHHHHHHCCCCCC | 21.35 | 25159151 | |
456 | Phosphorylation | KVLTQMGSPHNPISS HHHHHCCCCCCCCCC | 20.04 | 25159151 | |
462 | Phosphorylation | GSPHNPISSVS---- CCCCCCCCCCC---- | 26.41 | 22322096 | |
463 | Phosphorylation | SPHNPISSVS----- CCCCCCCCCC----- | 27.40 | 22322096 | |
465 | 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 |
---|---|---|---|---|---|---|
187 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
187 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
187 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
195 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
195 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
195 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
202 | T | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
206 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
206 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
206 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
206 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
214 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
214 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
214 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
239 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
322 | T | Phosphorylation | Kinase | TNIK | Q9UKE5 | Uniprot |
322 | T | Phosphorylation | Kinase | MINK | Q8N4C8 | PSP |
322 | T | Phosphorylation | Kinase | HGK | O95819 | PSP |
462 | S | Phosphorylation | Kinase | BMR1B | O00238 | PhosphoELM |
463 | S | Phosphorylation | Kinase | BMR1B | O00238 | PhosphoELM |
465 | S | Phosphorylation | Kinase | BMR1B | O00238 | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF1 | Q9HCE7 | PMID:14711801 |
- | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:14701756 |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF2 | Q9HAU4 | PMID:11158580 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMAD1_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 SMAD1_HUMAN !! |
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. |
loading...
Phosphorylation | |
Reference | PubMed |
"The TGF-beta family mediator Smad1 is phosphorylated directly andactivated functionally by the BMP receptor kinase."; Kretzschmar M., Liu F., Hata A., Doody J., Massague J.; Genes Dev. 11:984-995(1997). Cited for: PHOSPHORYLATION AT SER-463 AND SER-465. | |
"Smad inhibition by the Ste20 kinase Misshapen."; Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M.,Kariya K., Mao J., Ip Y.T., Xu L.; Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011). Cited for: PHOSPHORYLATION AT THR-322. |