UniProt ID | MSD2_HUMAN | |
---|---|---|
UniProt AC | Q6P1R3 | |
Protein Name | Myb/SANT-like DNA-binding domain-containing protein 2 | |
Gene Name | MSANTD2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 559 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MAAPCGSELPANSPLKIPKMEVLSPASPGGLSDGNPSLSDPSTPRGASPLGPGSAAGSGAAASGGLGLGLGGRSAASSSVSFSPGGGGGGAAAAAAAACRGMSWTPAETNALIAVWGNERLVEARYQQLEGAGTVFGSKAPGPAMYERVSRALAELGYERTPSQCRERIKTLRRCYSRVKEHGVGKRKSSYTFEQLEQVFGQGGWDAQPCQPVLINSSGLYQELESDGSTMEDYSQEDWGNHSQDLHGYPTDQELDEIPVTKRTLKIKQESSEEAQKRDIMQNIVQILESVQLKWELFQSWTDFSRLHLSNKLAIFGIGYNTRWKEDIRYHYAEISSQVPLGKRLREYFNSEKPEGRIIMTRVQKMNWKNVYYKFLEITISEARCLELHMEIDWIPIAHSKPTGGNVVQYLLPGGIPKSPGLYAIGYEECIERPLSPHMEQSSLDPGKEGRVDLETLSAQASLQVEIEPTRIIYCYLGIAEVRTLQQCLFLHFQANTKTFSKDWVGINGFLSQNCIVDPGVSPKSIYIKFVEVERDFLSAGSLVECLEKAIGYPLKFNN | |
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 |
---|---|---|---|---|---|
7 | Phosphorylation | -MAAPCGSELPANSP -CCCCCCCCCCCCCC | 42.55 | 29255136 | |
13 | Phosphorylation | GSELPANSPLKIPKM CCCCCCCCCCCCCCE | 33.44 | 29255136 | |
24 | Phosphorylation | IPKMEVLSPASPGGL CCCEEEECCCCCCCC | 24.48 | 29255136 | |
27 | Phosphorylation | MEVLSPASPGGLSDG EEEECCCCCCCCCCC | 27.71 | 29255136 | |
32 | Phosphorylation | PASPGGLSDGNPSLS CCCCCCCCCCCCCCC | 46.90 | 29255136 | |
37 | Phosphorylation | GLSDGNPSLSDPSTP CCCCCCCCCCCCCCC | 44.50 | 28450419 | |
39 | Phosphorylation | SDGNPSLSDPSTPRG CCCCCCCCCCCCCCC | 52.38 | 28450419 | |
42 | Phosphorylation | NPSLSDPSTPRGASP CCCCCCCCCCCCCCC | 56.91 | 28450419 | |
43 | Phosphorylation | PSLSDPSTPRGASPL CCCCCCCCCCCCCCC | 23.53 | 28450419 | |
48 | Phosphorylation | PSTPRGASPLGPGSA CCCCCCCCCCCCCCC | 24.39 | 29255136 | |
54 | Phosphorylation | ASPLGPGSAAGSGAA CCCCCCCCCCCCCCH | 20.34 | 23927012 | |
58 | Phosphorylation | GPGSAAGSGAAASGG CCCCCCCCCCHHCCC | 22.11 | 30278072 | |
63 | Phosphorylation | AGSGAAASGGLGLGL CCCCCHHCCCCCCCC | 28.77 | 23403867 | |
74 | Phosphorylation | GLGLGGRSAASSSVS CCCCCCCCCCCCEEE | 31.31 | 26552605 | |
77 | Phosphorylation | LGGRSAASSSVSFSP CCCCCCCCCEEEECC | 23.90 | 26552605 | |
78 | Phosphorylation | GGRSAASSSVSFSPG CCCCCCCCEEEECCC | 29.99 | 26552605 | |
79 | Phosphorylation | GRSAASSSVSFSPGG CCCCCCCEEEECCCC | 21.20 | 26552605 | |
81 | Phosphorylation | SAASSSVSFSPGGGG CCCCCEEEECCCCCC | 23.19 | 26552605 | |
83 | Phosphorylation | ASSSVSFSPGGGGGG CCCEEEECCCCCCHH | 18.35 | 28985074 | |
161 | Phosphorylation | AELGYERTPSQCRER HHCCCCCCHHHHHHH | 18.49 | 28555341 | |
268 | Sumoylation | TKRTLKIKQESSEEA CCCEEEECCCCCHHH | 46.56 | 28112733 | |
268 | Ubiquitination | TKRTLKIKQESSEEA CCCEEEECCCCCHHH | 46.56 | - | |
268 | Sumoylation | TKRTLKIKQESSEEA CCCEEEECCCCCHHH | 46.56 | - | |
300 | Phosphorylation | LKWELFQSWTDFSRL HHHHHHHCCCHHHHH | 25.30 | 27174698 | |
302 | Phosphorylation | WELFQSWTDFSRLHL HHHHHCCCHHHHHHH | 32.20 | 27174698 | |
305 | Phosphorylation | FQSWTDFSRLHLSNK HHCCCHHHHHHHCCC | 36.42 | 27174698 | |
323 | Methylation | FGIGYNTRWKEDIRY EEECCCCCCHHHHHH | 38.54 | 115483855 | |
325 | Ubiquitination | IGYNTRWKEDIRYHY ECCCCCCHHHHHHHH | 42.07 | - | |
330 | Phosphorylation | RWKEDIRYHYAEISS CCHHHHHHHHHHHHC | 10.26 | 28270605 | |
332 | Phosphorylation | KEDIRYHYAEISSQV HHHHHHHHHHHHCCC | 9.30 | 28270605 | |
336 | Phosphorylation | RYHYAEISSQVPLGK HHHHHHHHCCCCHHH | 13.26 | 28270605 | |
337 | Phosphorylation | YHYAEISSQVPLGKR HHHHHHHCCCCHHHH | 40.64 | 28270605 | |
343 | Sumoylation | SSQVPLGKRLREYFN HCCCCHHHHHHHHHC | 56.81 | 28112733 | |
348 | Phosphorylation | LGKRLREYFNSEKPE HHHHHHHHHCCCCCC | 11.13 | - | |
384 | Phosphorylation | EITISEARCLELHME EEEECHHHHHHHCEE | 22.85 | 27251275 | |
419 | Phosphorylation | LPGGIPKSPGLYAIG ECCCCCCCCCEEEEC | 20.88 | 26434776 | |
423 | Phosphorylation | IPKSPGLYAIGYEEC CCCCCCEEEECHHHH | 11.33 | 26434776 | |
427 | Phosphorylation | PGLYAIGYEECIERP CCEEEECHHHHHCCC | 11.48 | 25159151 | |
436 | Phosphorylation | ECIERPLSPHMEQSS HHHCCCCCCCCCHHC | 18.55 | 25159151 | |
442 | Phosphorylation | LSPHMEQSSLDPGKE CCCCCCHHCCCCCCC | 21.40 | 29978859 | |
443 | Phosphorylation | SPHMEQSSLDPGKEG CCCCCHHCCCCCCCC | 36.16 | 29978859 |
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 MSD2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MSD2_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 MSD2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ERCC3_HUMAN | ERCC3 | physical | 21988832 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-48, 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-48 AND SER-54, AND MASSSPECTROMETRY. | |
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY. |