UniProt ID | SKI_HUMAN | |
---|---|---|
UniProt AC | P12755 | |
Protein Name | Ski oncogene | |
Gene Name | SKI | |
Organism | Homo sapiens (Human). | |
Sequence Length | 728 | |
Subcellular Localization | Nucleus. | |
Protein Description | May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling.. | |
Protein Sequence | MEAAAGGRGCFQPHPGLQKTLEQFHLSSMSSLGGPAAFSARWAQEAYKKESAKEAGAAAVPAPVPAATEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYGNKYKRRVPRVSSEPPASIRPKTDDTSSQSPAPSEKDKPSSWLRTLAGSSNKSLGCVHPRQRLSAFRPWSPAVSASEKELSPHLPALIRDSFYSYKSFETAVAPNVALAPPAQQKVVSSPPCAAAVSRAPEPLATCTQPRKRKLTVDTPGAPETLAPVAAPEEDKDSEAEVEVESREEFTSSLSSLSSPSFTSSSSAKDLGSPGARALPSAVPDAAAPADAPSGLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLSAALQAKRSLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRLRLKRELEQARQARVCDKGCEAGRLRAKYSAQIEDLQVKLQHAEADREQLRADLLREREAREHLEKVVKELQEQLWPRARPEAAGSEGAAELEP | |
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 |
---|---|---|---|---|---|
103 | Phosphorylation | RSTERCETVLEGETI CCCCCCCCHHCCCEE | 33.73 | 22817900 | |
119 | Ubiquitination | CFVVGGEKRLCLPQI EEEECCCEEECHHHH | 54.68 | 22817900 | |
170 | Phosphorylation | VMGILPFSAPSCGLI HHCCCCCCCCCCCCC | 37.01 | 23403867 | |
173 | Phosphorylation | ILPFSAPSCGLITKT CCCCCCCCCCCCCHH | 22.12 | 23403867 | |
214 | Phosphorylation | LALGLELSERSVRVY HHHCHHCHHHHHHHH | 22.91 | 23532336 | |
227 | Ubiquitination | VYHECFGKCKGLLVP HHHHHHCCCCCCCCC | 16.72 | - | |
245 | Ubiquitination | SSPSAACIQCLDCRL CCCCHHHHHHHCCCC | 2.51 | 22817900 | |
258 | Ubiquitination | RLMYPPHKFVVHSHK CCCCCCCEEEEECCC | 45.70 | 29967540 | |
294 | Ubiquitination | LSQDYTGKEEQARLG ECCCCCCHHHHHHHC | 50.72 | 21906983 | |
316 | Ubiquitination | EKFDYGNKYKRRVPR HHCCCCCCCCCCCCC | 48.03 | 29967540 | |
318 | Acetylation | FDYGNKYKRRVPRVS CCCCCCCCCCCCCCC | 35.02 | 20167786 | |
325 | Phosphorylation | KRRVPRVSSEPPASI CCCCCCCCCCCCCCC | 30.20 | 23312004 | |
326 | Phosphorylation | RRVPRVSSEPPASIR CCCCCCCCCCCCCCC | 51.79 | 30624053 | |
335 | Acetylation | PPASIRPKTDDTSSQ CCCCCCCCCCCCCCC | 55.53 | 20167786 | |
339 | Phosphorylation | IRPKTDDTSSQSPAP CCCCCCCCCCCCCCC | 32.84 | 29396449 | |
340 | Phosphorylation | RPKTDDTSSQSPAPS CCCCCCCCCCCCCCC | 33.12 | 29396449 | |
341 | Phosphorylation | PKTDDTSSQSPAPSE CCCCCCCCCCCCCCC | 36.45 | 25262027 | |
343 | Phosphorylation | TDDTSSQSPAPSEKD CCCCCCCCCCCCCCC | 25.61 | 25627689 | |
347 | Phosphorylation | SSQSPAPSEKDKPSS CCCCCCCCCCCCCCH | 60.42 | 25072903 | |
349 | Acetylation | QSPAPSEKDKPSSWL CCCCCCCCCCCCHHH | 75.33 | 25953088 | |
349 | Ubiquitination | QSPAPSEKDKPSSWL CCCCCCCCCCCCHHH | 75.33 | 29967540 | |
351 | Acetylation | PAPSEKDKPSSWLRT CCCCCCCCCCHHHHH | 58.84 | 25953088 | |
351 | Ubiquitination | PAPSEKDKPSSWLRT CCCCCCCCCCHHHHH | 58.84 | 29967540 | |
354 | Phosphorylation | SEKDKPSSWLRTLAG CCCCCCCHHHHHHHC | 38.36 | 25159151 | |
365 | Ubiquitination | TLAGSSNKSLGCVHP HHHCCCCCCCCCCCH | 49.35 | 32015554 | |
366 | Phosphorylation | LAGSSNKSLGCVHPR HHCCCCCCCCCCCHH | 33.95 | 25159151 | |
377 | Phosphorylation | VHPRQRLSAFRPWSP CCHHHHHHHCCCCCC | 27.79 | 23403867 | |
383 | Phosphorylation | LSAFRPWSPAVSASE HHHCCCCCCCCCCCC | 12.98 | 23401153 | |
387 | O-linked_Glycosylation | RPWSPAVSASEKELS CCCCCCCCCCCCHHC | 28.34 | 28657654 | |
387 | Phosphorylation | RPWSPAVSASEKELS CCCCCCCCCCCCHHC | 28.34 | 23403867 | |
389 | O-linked_Glycosylation | WSPAVSASEKELSPH CCCCCCCCCCHHCCC | 41.51 | 28657654 | |
389 | Phosphorylation | WSPAVSASEKELSPH CCCCCCCCCCHHCCC | 41.51 | 23403867 | |
394 | Phosphorylation | SASEKELSPHLPALI CCCCCHHCCCHHHHH | 16.03 | 28188228 | |
404 | Phosphorylation | LPALIRDSFYSYKSF HHHHHHHCCCCCCCC | 19.08 | 25159151 | |
409 | Ubiquitination | RDSFYSYKSFETAVA HHCCCCCCCCCCCCC | 42.61 | 21906983 | |
431 | Phosphorylation | PAQQKVVSSPPCAAA HHHHCCCCCCCCHHH | 39.86 | 23401153 | |
432 | Phosphorylation | AQQKVVSSPPCAAAV HHHCCCCCCCCHHHH | 22.66 | 23401153 | |
440 | O-linked_Glycosylation | PPCAAAVSRAPEPLA CCCHHHHHCCCCCCC | 20.28 | 28657654 | |
440 | Phosphorylation | PPCAAAVSRAPEPLA CCCHHHHHCCCCCCC | 20.28 | 29396449 | |
448 | Phosphorylation | RAPEPLATCTQPRKR CCCCCCCCCCCCCCC | 24.62 | 26074081 | |
450 | Phosphorylation | PEPLATCTQPRKRKL CCCCCCCCCCCCCCC | 36.93 | 26074081 | |
458 | Phosphorylation | QPRKRKLTVDTPGAP CCCCCCCCCCCCCCC | 21.26 | 29978859 | |
461 | Phosphorylation | KRKLTVDTPGAPETL CCCCCCCCCCCCCCC | 21.20 | 29978859 | |
467 | Phosphorylation | DTPGAPETLAPVAAP CCCCCCCCCCCCCCC | 27.45 | 30108239 | |
480 | Phosphorylation | APEEDKDSEAEVEVE CCCCCCCCCCEEEEE | 44.43 | 30266825 | |
488 | Phosphorylation | EAEVEVESREEFTSS CCEEEEECHHHHHHH | 50.60 | 30266825 | |
493 | Phosphorylation | VESREEFTSSLSSLS EECHHHHHHHHHHHC | 22.23 | 29978859 | |
495 | Phosphorylation | SREEFTSSLSSLSSP CHHHHHHHHHHHCCC | 29.25 | 29978859 | |
497 | Phosphorylation | EEFTSSLSSLSSPSF HHHHHHHHHHCCCCC | 31.05 | 29978859 | |
498 | Phosphorylation | EFTSSLSSLSSPSFT HHHHHHHHHCCCCCC | 37.25 | 28348404 | |
500 | Phosphorylation | TSSLSSLSSPSFTSS HHHHHHHCCCCCCCC | 41.99 | 29978859 | |
501 | Phosphorylation | SSLSSLSSPSFTSSS HHHHHHCCCCCCCCC | 29.83 | 28348404 | |
503 | Phosphorylation | LSSLSSPSFTSSSSA HHHHCCCCCCCCCCC | 43.00 | 29978859 | |
505 | Phosphorylation | SLSSPSFTSSSSAKD HHCCCCCCCCCCCHH | 31.85 | 29978859 | |
506 | Phosphorylation | LSSPSFTSSSSAKDL HCCCCCCCCCCCHHH | 26.64 | 29978859 | |
507 | Phosphorylation | SSPSFTSSSSAKDLG CCCCCCCCCCCHHHC | 25.84 | 29978859 | |
508 | Phosphorylation | SPSFTSSSSAKDLGS CCCCCCCCCCHHHCC | 33.80 | 29978859 | |
509 | Phosphorylation | PSFTSSSSAKDLGSP CCCCCCCCCHHHCCC | 41.09 | 29978859 | |
515 | Phosphorylation | SSAKDLGSPGARALP CCCHHHCCCCHHCCC | 27.70 | 28102081 | |
523 | Phosphorylation | PGARALPSAVPDAAA CCHHCCCCCCCCCCC | 42.63 | 26074081 | |
584 | Ubiquitination | LSAALQAKRSLHQEL HHHHHHHHHHHHHHH | 29.56 | 29967540 | |
633 | Phosphorylation | KMKEANESRLRLKRE HHHHHHHHHHHHHHH | 36.10 | 26074081 | |
662 | Ubiquitination | EAGRLRAKYSAQIED HHHHHHHHHHHHHHH | 33.05 | 29967540 | |
673 | Ubiquitination | QIEDLQVKLQHAEAD HHHHHHHHHHHHHHC | 29.48 | 29967540 | |
720 | Phosphorylation | ARPEAAGSEGAAELE CCHHHCCCCCCCCCC | 28.29 | 30576142 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
326 | S | Phosphorylation | Kinase | AURKA | O14965 | GPS |
383 | S | Phosphorylation | Kinase | AURKA | O14965 | GPS |
458 | T | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF111 | Q6ZNA4 | PMID:17510063 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SKI_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 SKI_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
182212 | Shprintzen-Goldberg craniosynostosis syndrome (SGS) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND MASSSPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY. |