| UniProt ID | SQSTM_HUMAN | |
|---|---|---|
| UniProt AC | Q13501 | |
| Protein Name | Sequestosome-1 | |
| Gene Name | SQSTM1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 440 | |
| Subcellular Localization | Cytoplasm, cytosol . Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Nucleus, PML body . Cytoplasm, myofibril, sarcomere. In cardiac muscle, localizes to the sarcomeric band (By similarity). Commonly found | |
| Protein Description | Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. [PubMed: 16286508] | |
| Protein Sequence | MASLTVKAYLLGKEDAAREIRRFSFCCSPEPEAEAEAAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPGNWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MASLTVKAY ------CCCCHHHHH | 17.16 | 22814378 | |
| 2 (in isoform 2) | Acetylation | - | 17.16 | 22814378 | |
| 7 | Ubiquitination | -MASLTVKAYLLGKE -CCCCHHHHHHHCCH | 26.52 | 23000965 | |
| 9 | Phosphorylation | ASLTVKAYLLGKEDA CCCHHHHHHHCCHHH | 9.20 | 28152594 | |
| 13 | 2-Hydroxyisobutyrylation | VKAYLLGKEDAAREI HHHHHHCCHHHHHHH | 53.01 | - | |
| 13 | Acetylation | VKAYLLGKEDAAREI HHHHHHCCHHHHHHH | 53.01 | 26051181 | |
| 13 | Malonylation | VKAYLLGKEDAAREI HHHHHHCCHHHHHHH | 53.01 | 26320211 | |
| 13 | Ubiquitination | VKAYLLGKEDAAREI HHHHHHCCHHHHHHH | 53.01 | 23000965 | |
| 13 (in isoform 1) | Ubiquitination | - | 53.01 | 21890473 | |
| 24 | Phosphorylation | AREIRRFSFCCSPEP HHHHHHHCCCCCCCH | 18.63 | 29255136 | |
| 28 | Phosphorylation | RRFSFCCSPEPEAEA HHHCCCCCCCHHHHH | 33.22 | 29255136 | |
| 49 | Phosphorylation | GPCERLLSRVAALFP CHHHHHHHHHHHHHH | 29.33 | - | |
| 57 | Ubiquitination | RVAALFPALRPGGFQ HHHHHHHHHCCCCEE | 14.63 | 21963094 | |
| 57 (in isoform 2) | Ubiquitination | - | 14.63 | 21890473 | |
| 67 | Phosphorylation | PGGFQAHYRDEDGDL CCCEEEEEECCCCCE | 23.83 | - | |
| 73 | Ubiquitination | HYRDEDGDLVAFSSD EEECCCCCEEEECCC | 50.74 | 21963094 | |
| 73 (in isoform 2) | Ubiquitination | - | 50.74 | 21890473 | |
| 81 | Ubiquitination | LVAFSSDEELTMAMS EEEECCCHHHHHHHH | 57.78 | 21963094 | |
| 81 (in isoform 2) | Ubiquitination | - | 57.78 | 21890473 | |
| 88 | Phosphorylation | EELTMAMSYVKDDIF HHHHHHHHHHHHCHH | 19.75 | 20068231 | |
| 89 | Phosphorylation | ELTMAMSYVKDDIFR HHHHHHHHHHHCHHH | 9.83 | 20068231 | |
| 91 | Ubiquitination | TMAMSYVKDDIFRIY HHHHHHHHHCHHHEE | 41.26 | 29901268 | |
| 103 | Ubiquitination | RIYIKEKKECRRDHR HEEECCHHHHCCCCC | 64.24 | 22817900 | |
| 105 | Ubiquitination | YIKEKKECRRDHRPP EECCHHHHCCCCCCC | 6.25 | 21963094 | |
| 105 (in isoform 2) | Ubiquitination | - | 6.25 | 21890473 | |
| 138 | Phosphorylation | CNGPVVGTRYKCSVC CCCCCCCCCEEEEEC | 21.15 | 28857561 | |
| 141 | Acetylation | PVVGTRYKCSVCPDY CCCCCCEEEEECCCC | 19.42 | 26051181 | |
| 141 | Malonylation | PVVGTRYKCSVCPDY CCCCCCEEEEECCCC | 19.42 | 26320211 | |
| 141 | Ubiquitination | PVVGTRYKCSVCPDY CCCCCCEEEEECCCC | 19.42 | 21963094 | |
| 141 (in isoform 1) | Ubiquitination | - | 19.42 | 21890473 | |
| 143 | Phosphorylation | VGTRYKCSVCPDYDL CCCCEEEEECCCCCC | 23.70 | 28857561 | |
| 148 | Phosphorylation | KCSVCPDYDLCSVCE EEEECCCCCCCCEEC | 8.92 | 25159151 | |
| 152 | Phosphorylation | CPDYDLCSVCEGKGL CCCCCCCCEECCCCC | 36.78 | 25159151 | |
| 154 | Ubiquitination | DYDLCSVCEGKGLHR CCCCCCEECCCCCCC | 3.07 | 33845483 | |
| 157 | Acetylation | LCSVCEGKGLHRGHT CCCEECCCCCCCCCC | 35.69 | 26051181 | |
| 157 | Ubiquitination | LCSVCEGKGLHRGHT CCCEECCCCCCCCCC | 35.69 | 21963094 | |
| 157 (in isoform 1) | Ubiquitination | - | 35.69 | 21890473 | |
| 164 | Phosphorylation | KGLHRGHTKLAFPSP CCCCCCCCCEECCCC | 30.49 | 27080861 | |
| 165 | Ubiquitination | GLHRGHTKLAFPSPF CCCCCCCCEECCCCC | 31.95 | 21906983 | |
| 165 (in isoform 1) | Ubiquitination | - | 31.95 | 21890473 | |
| 170 | Phosphorylation | HTKLAFPSPFGHLSE CCCEECCCCCCCCCC | 26.80 | 29255136 | |
| 176 | Phosphorylation | PSPFGHLSEGFSHSR CCCCCCCCCCCCCHH | 29.96 | 25159151 | |
| 180 | Phosphorylation | GHLSEGFSHSRWLRK CCCCCCCCCHHHHHH | 31.26 | 25159151 | |
| 180 | Ubiquitination | GHLSEGFSHSRWLRK CCCCCCCCCHHHHHH | 31.26 | 21963094 | |
| 180 (in isoform 2) | Ubiquitination | - | 31.26 | 21890473 | |
| 182 | Phosphorylation | LSEGFSHSRWLRKVK CCCCCCCHHHHHHHC | 24.77 | 25159151 | |
| 183 | Methylation | SEGFSHSRWLRKVKH CCCCCCHHHHHHHCC | 30.90 | 82797321 | |
| 185 | Phosphorylation | GFSHSRWLRKVKHGH CCCCHHHHHHHCCCC | 3.55 | 32645325 | |
| 187 | Ubiquitination | SHSRWLRKVKHGHFG CCHHHHHHHCCCCCC | 54.16 | 22817900 | |
| 189 | Ubiquitination | SRWLRKVKHGHFGWP HHHHHHHCCCCCCCC | 47.07 | 1890473 | |
| 189 (in isoform 1) | Ubiquitination | - | 47.07 | 21890473 | |
| 197 | Ubiquitination | HGHFGWPGWEMGPPG CCCCCCCCCCCCCCC | 26.85 | 27667366 | |
| 197 (in isoform 2) | Ubiquitination | - | 26.85 | 21890473 | |
| 207 | Phosphorylation | MGPPGNWSPRPPRAG CCCCCCCCCCCCCCC | 18.28 | 25159151 | |
| 211 | Ubiquitination | GNWSPRPPRAGEARP CCCCCCCCCCCCCCC | 39.78 | 27667366 | |
| 211 (in isoform 2) | Ubiquitination | - | 39.78 | 21890473 | |
| 221 | Phosphorylation | GEARPGPTAESASGP CCCCCCCCCCCCCCC | 49.31 | 20068231 | |
| 224 | Phosphorylation | RPGPTAESASGPSED CCCCCCCCCCCCCCC | 25.85 | 25159151 | |
| 226 | Phosphorylation | GPTAESASGPSEDPS CCCCCCCCCCCCCCC | 61.59 | 25159151 | |
| 229 | Phosphorylation | AESASGPSEDPSVNF CCCCCCCCCCCCHHH | 59.15 | 30242111 | |
| 229 | Ubiquitination | AESASGPSEDPSVNF CCCCCCCCCCCCHHH | 59.15 | 21963094 | |
| 233 | Phosphorylation | SGPSEDPSVNFLKNV CCCCCCCCHHHHHHH | 41.85 | 29255136 | |
| 234 (in isoform 2) | Phosphorylation | - | 7.75 | 21406692 | |
| 238 | Ubiquitination | DPSVNFLKNVGESVA CCCHHHHHHHHHHHH | 45.51 | 33845483 | |
| 243 | Phosphorylation | FLKNVGESVAAALSP HHHHHHHHHHHHHCC | 15.89 | 25850435 | |
| 244 (in isoform 2) | Phosphorylation | - | 3.51 | 21406692 | |
| 248 (in isoform 2) | Phosphorylation | - | 4.67 | 21406692 | |
| 249 | Phosphorylation | ESVAAALSPLGIEVD HHHHHHHCCCCEEEE | 17.22 | 25159151 | |
| 260 | Ubiquitination | IEVDIDVEHGGKRSR EEEEEECCCCCEEEC | 32.82 | 29967540 | |
| 264 | Ubiquitination | IDVEHGGKRSRLTPV EECCCCCEEECEEEC | 52.36 | 21906983 | |
| 264 (in isoform 1) | Ubiquitination | - | 52.36 | 21890473 | |
| 266 | Phosphorylation | VEHGGKRSRLTPVSP CCCCCEEECEEECCC | 34.82 | 22167270 | |
| 269 | Phosphorylation | GGKRSRLTPVSPESS CCEEECEEECCCCCC | 22.12 | 19664994 | |
| 272 | Phosphorylation | RSRLTPVSPESSSTE EECEEECCCCCCCCC | 24.93 | 19664994 | |
| 275 | Phosphorylation | LTPVSPESSSTEEKS EEECCCCCCCCCCCC | 32.73 | 23927012 | |
| 276 | Phosphorylation | TPVSPESSSTEEKSS EECCCCCCCCCCCCC | 39.35 | 25159151 | |
| 277 | Phosphorylation | PVSPESSSTEEKSSS ECCCCCCCCCCCCCC | 49.47 | 23927012 | |
| 278 | Phosphorylation | VSPESSSTEEKSSSQ CCCCCCCCCCCCCCC | 50.54 | 23927012 | |
| 281 | Ubiquitination | ESSSTEEKSSSQPSS CCCCCCCCCCCCCCC | 49.78 | 21906983 | |
| 281 (in isoform 1) | Ubiquitination | - | 49.78 | 21890473 | |
| 282 | Phosphorylation | SSSTEEKSSSQPSSC CCCCCCCCCCCCCCC | 38.20 | 30278072 | |
| 283 | Phosphorylation | SSTEEKSSSQPSSCC CCCCCCCCCCCCCCC | 44.02 | 30278072 | |
| 284 | Phosphorylation | STEEKSSSQPSSCCS CCCCCCCCCCCCCCC | 53.88 | 30278072 | |
| 287 | Phosphorylation | EKSSSQPSSCCSDPS CCCCCCCCCCCCCCC | 28.50 | 30278072 | |
| 288 | Phosphorylation | KSSSQPSSCCSDPSK CCCCCCCCCCCCCCC | 26.31 | 30278072 | |
| 291 | Phosphorylation | SQPSSCCSDPSKPGG CCCCCCCCCCCCCCC | 57.81 | 30278072 | |
| 294 | Phosphorylation | SSCCSDPSKPGGNVE CCCCCCCCCCCCCCC | 57.37 | 23927012 | |
| 294 | Ubiquitination | SSCCSDPSKPGGNVE CCCCCCCCCCCCCCC | 57.37 | 33845483 | |
| 294 (in isoform 2) | Ubiquitination | - | 57.37 | - | |
| 295 | Acetylation | SCCSDPSKPGGNVEG CCCCCCCCCCCCCCH | 53.74 | 26051181 | |
| 295 | Ubiquitination | SCCSDPSKPGGNVEG CCCCCCCCCCCCCCH | 53.74 | 21906983 | |
| 295 (in isoform 1) | Ubiquitination | - | 53.74 | 21890473 | |
| 304 | Phosphorylation | GGNVEGATQSLAEQM CCCCCHHHHHHHHHH | 29.55 | 23927012 | |
| 306 | Phosphorylation | NVEGATQSLAEQMRK CCCHHHHHHHHHHHH | 25.78 | 25159151 | |
| 313 | Ubiquitination | SLAEQMRKIALESEG HHHHHHHHHHHHCCC | 27.30 | 21963094 | |
| 318 | Phosphorylation | MRKIALESEGRPEEQ HHHHHHHCCCCHHHH | 46.32 | 22167270 | |
| 328 | Phosphorylation | RPEEQMESDNCSGGD CHHHHHCCCCCCCCC | 28.87 | 22167270 | |
| 332 | Phosphorylation | QMESDNCSGGDDDWT HHCCCCCCCCCCCCH | 52.65 | 22167270 | |
| 336 | Ubiquitination | DNCSGGDDDWTHLSS CCCCCCCCCCHHHCC | 57.53 | 21963094 | |
| 336 (in isoform 2) | Ubiquitination | - | 57.53 | 21890473 | |
| 339 | Phosphorylation | SGGDDDWTHLSSKEV CCCCCCCHHHCCCEE | 21.67 | 22167270 | |
| 342 | Phosphorylation | DDDWTHLSSKEVDPS CCCCHHHCCCEECCC | 31.59 | 23927012 | |
| 343 | Phosphorylation | DDWTHLSSKEVDPST CCCHHHCCCEECCCC | 38.91 | 25159151 | |
| 344 | Acetylation | DWTHLSSKEVDPSTG CCHHHCCCEECCCCC | 59.38 | 18530509 | |
| 344 | Ubiquitination | DWTHLSSKEVDPSTG CCHHHCCCEECCCCC | 59.38 | 29967540 | |
| 349 | Phosphorylation | SSKEVDPSTGELQSL CCCEECCCCCCCCCC | 44.58 | 30278072 | |
| 350 | Phosphorylation | SKEVDPSTGELQSLQ CCEECCCCCCCCCCC | 39.81 | 30278072 | |
| 351 | Ubiquitination | KEVDPSTGELQSLQM CEECCCCCCCCCCCC | 37.64 | 23000965 | |
| 351 (in isoform 2) | Ubiquitination | - | 37.64 | 21890473 | |
| 355 | Phosphorylation | PSTGELQSLQMPESE CCCCCCCCCCCCCCC | 32.94 | 28355574 | |
| 361 | Phosphorylation | QSLQMPESEGPSSLD CCCCCCCCCCCCCCC | 41.82 | 25159151 | |
| 365 | Phosphorylation | MPESEGPSSLDPSQE CCCCCCCCCCCCCCC | 55.15 | 26846344 | |
| 366 | Phosphorylation | PESEGPSSLDPSQEG CCCCCCCCCCCCCCC | 39.67 | 26846344 | |
| 370 | Phosphorylation | GPSSLDPSQEGPTGL CCCCCCCCCCCCCCC | 40.30 | 26846344 | |
| 375 | Phosphorylation | DPSQEGPTGLKEAAL CCCCCCCCCCHHHHH | 67.03 | 26846344 | |
| 378 | Acetylation | QEGPTGLKEAALYPH CCCCCCCHHHHHCCC | 46.80 | 18529093 | |
| 378 | Ubiquitination | QEGPTGLKEAALYPH CCCCCCCHHHHHCCC | 46.80 | 33845483 | |
| 383 | Phosphorylation | GLKEAALYPHLPPEA CCHHHHHCCCCCCCC | 5.49 | 25394399 | |
| 397 | Phosphorylation | ADPRLIESLSQMLSM CCHHHHHHHHHHHHC | 26.74 | 24275569 | |
| 403 | Phosphorylation | ESLSQMLSMGFSDEG HHHHHHHHCCCCCCC | 16.12 | 15125799 | |
| 407 | Phosphorylation | QMLSMGFSDEGGWLT HHHHCCCCCCCCHHH | 29.08 | - | |
| 420 | Ubiquitination | LTRLLQTKNYDIGAA HHHHHHCCCCCHHHH | 40.32 | 21906983 | |
| 420 (in isoform 1) | Ubiquitination | - | 40.32 | 21890473 | |
| 422 | Phosphorylation | RLLQTKNYDIGAALD HHHHCCCCCHHHHHH | 15.53 | 21945579 | |
| 430 | Phosphorylation | DIGAALDTIQYSKHP CHHHHHHHHHHCCCC | 15.72 | 21945579 | |
| 433 | Phosphorylation | AALDTIQYSKHPPPL HHHHHHHHCCCCCCC | 18.81 | 21945579 | |
| 434 | Phosphorylation | ALDTIQYSKHPPPL- HHHHHHHCCCCCCC- | 14.22 | 21945579 | |
| 435 | Acetylation | LDTIQYSKHPPPL-- HHHHHHCCCCCCC-- | 56.02 | 21466224 | |
| 435 | Sumoylation | LDTIQYSKHPPPL-- HHHHHHCCCCCCC-- | 56.02 | 28112733 | |
| 435 | Ubiquitination | LDTIQYSKHPPPL-- HHHHHHCCCCCCC-- | 56.02 | 23000965 | |
| 435 (in isoform 1) | Ubiquitination | - | 56.02 | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 138 | T | Phosphorylation | Kinase | LRRK2 | Q5S007 | PSP |
| 269 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 269 | T | Phosphorylation | Kinase | MAPK13 | O15264 | GPS |
| 272 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 272 | S | Phosphorylation | Kinase | MAPK13 | O15264 | GPS |
| 294 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
| 349 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
| 349 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
| 366 | S | Phosphorylation | Kinase | TBK1 | Q9UHD2 | PSP |
| 403 | S | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
| 403 | S | Phosphorylation | Kinase | TBK1 | Q9UHD2 | Uniprot |
| 403 | S | Phosphorylation | Kinase | ULK1 | O75385 | Uniprot |
| 433 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | PRKN | O60260 | PMID:26746706 |
| - | K | Ubiquitination | E3 ubiquitin ligase | RNF26 | Q9BY78 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | KEAP1 | Q14145 | PMID:28380357 |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:29021346 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM32 | Q13049 | PMID:31685529 |
* 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 SQSTM_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 602080 | Paget disease of bone (PDB) | |||||
| Note=In a cell model for Huntington disease (HD), appears to form a shell surrounding aggregates of mutant HTT that may protect cells from apoptosis, possibly by recruiting autophagosomal components to the polyubiquitinated protein aggregates. | ||||||
| 616437 | ||||||
| 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 |
| "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-272; SER-355 ANDSER-361, AND MASS SPECTROMETRY. | |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, 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 THR-269; SER-272; SER-277;SER-366 AND SER-370, AND MASS 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 SER-170; SER-207; THR-269;SER-272; SER-276; SER-328; SER-332; SER-355 AND SER-366, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, ANDMASS SPECTROMETRY. | |
| "Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-266; SER-272AND SER-366, AND MASS 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-269; SER-361; SER-365AND SER-366, AND MASS SPECTROMETRY. | |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, ANDMASS SPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, ANDMASS SPECTROMETRY. | |
| "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-269; SER-272 ANDSER-332, AND MASS SPECTROMETRY. | |
| "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, ANDMASS SPECTROMETRY. | |
| "Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-148, AND MASSSPECTROMETRY. | |
