UniProt ID | SURF2_HUMAN | |
---|---|---|
UniProt AC | Q15527 | |
Protein Name | Surfeit locus protein 2 | |
Gene Name | SURF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 256 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MSELPGDVRAFLREHPSLRLQTDARKVRCILTGHELPCRLPELQVYTRGKKYQRLVRASPAFDYAEFEPHIVPSTKNPHQLFCKLTLRHINKCPEHVLRHTQGRRYQRALCKYEECQKQGVEYVPACLVHRRRRREDQMDGDGPRPREAFWEPTSSDEGGAASDDSMTDLYPPELFTRKDLGSTEDGDGTDDFLTDKEDEKAKPPREKATDESRRETTVYRGLVQKRGKKQLGSLKKKFKSHHRKPKSFSSCKQPG | |
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 |
---|---|---|---|---|---|
9 | Methylation | SELPGDVRAFLREHP CCCCHHHHHHHHHCC | 25.10 | 115918041 | |
17 | Phosphorylation | AFLREHPSLRLQTDA HHHHHCCCCCCCCCC | 28.20 | 24719451 | |
29 | S-nitrosocysteine | TDARKVRCILTGHEL CCCCCEEEEHHCCCC | 3.15 | - | |
29 | S-nitrosylation | TDARKVRCILTGHEL CCCCCEEEEHHCCCC | 3.15 | 19483679 | |
38 | S-nitrosocysteine | LTGHELPCRLPELQV HHCCCCCCCCCCCEE | 12.48 | - | |
38 | S-nitrosylation | LTGHELPCRLPELQV HHCCCCCCCCCCCEE | 12.48 | 19483679 | |
59 | Phosphorylation | YQRLVRASPAFDYAE HHHHHHCCCCCCHHH | 13.24 | 30576142 | |
64 | Phosphorylation | RASPAFDYAEFEPHI HCCCCCCHHHCCCCC | 11.11 | 23312004 | |
74 | Phosphorylation | FEPHIVPSTKNPHQL CCCCCCCCCCCHHHH | 40.91 | 28348404 | |
75 | Phosphorylation | EPHIVPSTKNPHQLF CCCCCCCCCCHHHHH | 28.86 | 28348404 | |
84 | Acetylation | NPHQLFCKLTLRHIN CHHHHHHHHHHHHHH | 36.85 | 23749302 | |
112 | Acetylation | RYQRALCKYEECQKQ HHHHHHHCHHHHHHC | 57.45 | 25953088 | |
118 | Ubiquitination | CKYEECQKQGVEYVP HCHHHHHHCCCCCCC | 61.76 | 29967540 | |
145 | Phosphorylation | QMDGDGPRPREAFWE CCCCCCCCCHHHCCC | 48.73 | 32645325 | |
154 | Phosphorylation | REAFWEPTSSDEGGA HHHCCCCCCCCCCCC | 29.37 | 25849741 | |
155 | Phosphorylation | EAFWEPTSSDEGGAA HHCCCCCCCCCCCCC | 46.65 | 25849741 | |
156 | Phosphorylation | AFWEPTSSDEGGAAS HCCCCCCCCCCCCCC | 42.00 | 22115753 | |
163 | Phosphorylation | SDEGGAASDDSMTDL CCCCCCCCCCCCCCC | 41.22 | 22617229 | |
166 | Phosphorylation | GGAASDDSMTDLYPP CCCCCCCCCCCCCCH | 28.68 | 23663014 | |
168 | Phosphorylation | AASDDSMTDLYPPEL CCCCCCCCCCCCHHH | 27.14 | 23663014 | |
171 | Phosphorylation | DDSMTDLYPPELFTR CCCCCCCCCHHHCCC | 21.39 | 23663014 | |
177 | Phosphorylation | LYPPELFTRKDLGST CCCHHHCCCCCCCCC | 49.81 | 20068231 | |
183 | Phosphorylation | FTRKDLGSTEDGDGT CCCCCCCCCCCCCCC | 35.60 | 30266825 | |
184 | Phosphorylation | TRKDLGSTEDGDGTD CCCCCCCCCCCCCCC | 35.98 | 30266825 | |
190 | Phosphorylation | STEDGDGTDDFLTDK CCCCCCCCCCCCCCH | 36.82 | 29255136 | |
195 | Phosphorylation | DGTDDFLTDKEDEKA CCCCCCCCCHHHHCC | 45.05 | 29255136 | |
197 | Ubiquitination | TDDFLTDKEDEKAKP CCCCCCCHHHHCCCC | 62.93 | 24816145 | |
217 | Phosphorylation | TDESRRETTVYRGLV CHHHHHHHHHHHHHH | 21.54 | 29209046 | |
218 | Phosphorylation | DESRRETTVYRGLVQ HHHHHHHHHHHHHHH | 15.70 | 29209046 | |
220 | Phosphorylation | SRRETTVYRGLVQKR HHHHHHHHHHHHHHH | 9.25 | 29209046 | |
221 | Methylation | RRETTVYRGLVQKRG HHHHHHHHHHHHHHC | 27.86 | 115918037 | |
234 | Phosphorylation | RGKKQLGSLKKKFKS HCHHHHHHHHHHHHH | 45.68 | 28355574 | |
248 | Phosphorylation | SHHRKPKSFSSCKQP HCCCCCCCHHHCCCC | 38.60 | 22210691 | |
250 | Phosphorylation | HRKPKSFSSCKQPG- CCCCCCHHHCCCCC- | 41.75 | 21712546 | |
251 | Phosphorylation | RKPKSFSSCKQPG-- CCCCCHHHCCCCC-- | 24.27 | 21712546 |
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 SURF2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SURF2_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 SURF2_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. |
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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 THR-154; SER-155; SER-156;SER-163; THR-190 AND THR-195, AND MASS SPECTROMETRY. | |
"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 THR-190 AND THR-195, ANDMASS SPECTROMETRY. | |
"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 THR-190 AND THR-195, ANDMASS SPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190 AND THR-195, ANDMASS SPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195, AND MASSSPECTROMETRY. |