UniProt ID | CBL_HUMAN | |
---|---|---|
UniProt AC | P22681 | |
Protein Name | E3 ubiquitin-protein ligase CBL | |
Gene Name | CBL | |
Organism | Homo sapiens (Human). | |
Sequence Length | 906 | |
Subcellular Localization | Cytoplasm. Cell membrane. Colocalizes with FGFR2 in lipid rafts at the cell membrane. | |
Protein Description | Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3.. | |
Protein Sequence | MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDTLFMMKELAGAKVERPPSPFSMAPQASLPPVPPRLDLLPQRVCVPSSASALGTASKAASGSLHKDKPLPVPPTLRDLPPPPPPDRPYSVGAESRPQRRPLPCTPGDCPSRDKLPPVPSSRLGDSWLPRPIPKVPVSAPSSSDPWTGRELTNRHSLPFSLPSQMEPRPDVPRLGSTFSLDTSMSMNSSPLVGPECDHPKIKPSSSANAIYSLAARPLPVPKLPPGEQCEGEEDTEYMTPSSRPLRPLDTSQSSRACDCDQQIDSCTYEAMYNIQSQAPSITESSTFGEGNLAAAHANTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNVTEGSQVPERPPKPFPRRINSERKAGSCQQGSGPAASAATASPQLSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFVSISSPAHVAT | |
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 | Ubiquitination | -MAGNVKKSSGAGGG -CCCCCCCCCCCCCC | 45.64 | - | |
8 | Phosphorylation | MAGNVKKSSGAGGGS CCCCCCCCCCCCCCC | 28.43 | 25262027 | |
9 | Phosphorylation | AGNVKKSSGAGGGSG CCCCCCCCCCCCCCC | 41.35 | 25262027 | |
15 | Phosphorylation | SSGAGGGSGSGGSGS CCCCCCCCCCCCCCC | 32.82 | 25627689 | |
17 | Phosphorylation | GAGGGSGSGGSGSGG CCCCCCCCCCCCCCC | 41.50 | 25262027 | |
20 | Phosphorylation | GGSGSGGSGSGGLIG CCCCCCCCCCCCHHH | 33.05 | 25262027 | |
22 | Phosphorylation | SGSGGSGSGGLIGLM CCCCCCCCCCHHHHH | 31.24 | 25627689 | |
43 | Ubiquitination | HHHHHHHLSPHPPGT CCCCCCCCCCCCCCC | 8.07 | 22505724 | |
58 | Ubiquitination | VDKKMVEKCWKLMDK CCHHHHHHHHHHHHH | 33.70 | 29967540 | |
61 | Acetylation | KMVEKCWKLMDKVVR HHHHHHHHHHHHHHH | 43.32 | 25953088 | |
65 | Acetylation | KCWKLMDKVVRLCQN HHHHHHHHHHHHHCC | 28.76 | 25953088 | |
74 | Ubiquitination | VRLCQNPKLALKNSP HHHHCCHHHHHCCCC | 54.67 | 29967540 | |
74 | Acetylation | VRLCQNPKLALKNSP HHHHCCHHHHHCCCC | 54.67 | 25953088 | |
105 | Ubiquitination | ILSRYEGKMETLGEN HHHHHCCCCCCCCCC | 22.94 | 24816145 | |
126 | Phosphorylation | MENLMKKTKQTISLF HHHHHHHHHHHHHHH | 23.90 | 30576142 | |
129 | Phosphorylation | LMKKTKQTISLFKEG HHHHHHHHHHHHHHH | 17.68 | 21406692 | |
131 | Phosphorylation | KKTKQTISLFKEGKE HHHHHHHHHHHHHHH | 31.01 | 24719451 | |
134 | Acetylation | KQTISLFKEGKERMY HHHHHHHHHHHHHHH | 71.50 | 25953088 | |
141 | Phosphorylation | KEGKERMYEENSQPR HHHHHHHHHCCCCCC | 26.72 | 19534553 | |
183 | Ubiquitination | GDTFRITKADAAEFW CCEEEEEHHHHHHHH | 41.73 | - | |
197 | Acetylation | WRKAFGEKTIVPWKS HHHHHCCCCEECHHH | 43.88 | 19608861 | |
203 | Ubiquitination | EKTIVPWKSFRQALH CCCEECHHHHHHHHH | 33.38 | 22505724 | |
203 | Acetylation | EKTIVPWKSFRQALH CCCEECHHHHHHHHH | 33.38 | 25953088 | |
216 | Phosphorylation | LHEVHPISSGLEAMA HHHHCCCCCHHHHHH | 23.86 | 28857561 | |
217 | Phosphorylation | HEVHPISSGLEAMAL HHHCCCCCHHHHHHH | 48.38 | 28857561 | |
245 | O-linked_Glycosylation | VFEFDIFTRLFQPWS EEEHHHHHHHHHHHH | 27.14 | 30059200 | |
253 | Phosphorylation | RLFQPWSSLLRNWNS HHHHHHHHHHHHHHH | 27.79 | 24719451 | |
337 | Phosphorylation | DGFREGFYLFPDGRN HHHHCEEEECCCCCC | 20.49 | 10608804 | |
364 | Phosphorylation | PQDHIKVTQEQYELY CCHHEEECHHHHHHH | 22.76 | 28442448 | |
368 | Phosphorylation | IKVTQEQYELYCEMG EEECHHHHHHHHHCC | 13.72 | 24927040 | |
370 | Phosphorylation | VTQEQYELYCEMGST ECHHHHHHHHHCCCH | 5.16 | 17016520 | |
371 | Phosphorylation | TQEQYELYCEMGSTF CHHHHHHHHHCCCHH | 3.71 | 10635327 | |
376 | Phosphorylation | ELYCEMGSTFQLCKI HHHHHCCCHHHHHHH | 25.41 | 28442448 | |
377 | Phosphorylation | LYCEMGSTFQLCKIC HHHHCCCHHHHHHHH | 15.07 | 28442448 | |
389 | Acetylation | KICAENDKDVKIEPC HHHHCCCCCCEEEEC | 75.82 | 25953088 | |
424 | Ubiquitination | PFCRCEIKGTEPIVV CCCEEEECCCCCEEE | 37.17 | 29967540 | |
439 | Phosphorylation | DPFDPRGSGSLLRQG CCCCCCCCCHHHCCC | 26.87 | 25159151 | |
441 | Phosphorylation | FDPRGSGSLLRQGAE CCCCCCCHHHCCCCC | 26.40 | 25159151 | |
452 | Phosphorylation | QGAEGAPSPNYDDDD CCCCCCCCCCCCCCC | 25.83 | 23927012 | |
454 | Phosphorylation | AEGAPSPNYDDDDDE CCCCCCCCCCCCCCH | 58.15 | 17016520 | |
455 | Phosphorylation | EGAPSPNYDDDDDER CCCCCCCCCCCCCHH | 24.92 | 23927012 | |
466 | Phosphorylation | DDERADDTLFMMKEL CCHHHHHHHHHHHHH | 23.57 | 23403867 | |
483 | Phosphorylation | AKVERPPSPFSMAPQ CCCCCCCCCCCCCCC | 41.06 | 29255136 | |
486 | Phosphorylation | ERPPSPFSMAPQASL CCCCCCCCCCCCCCC | 19.88 | 30266825 | |
492 | Phosphorylation | FSMAPQASLPPVPPR CCCCCCCCCCCCCCC | 35.84 | 23927012 | |
511 | Phosphorylation | PQRVCVPSSASALGT CCCEECCCCCHHHHH | 20.38 | 28555341 | |
512 | Phosphorylation | QRVCVPSSASALGTA CCEECCCCCHHHHHC | 21.85 | 28555341 | |
514 | Phosphorylation | VCVPSSASALGTASK EECCCCCHHHHHCCH | 26.44 | - | |
518 | Phosphorylation | SSASALGTASKAASG CCCHHHHHCCHHHCC | 28.71 | 28555341 | |
520 | Phosphorylation | ASALGTASKAASGSL CHHHHHCCHHHCCCC | 23.75 | - | |
521 | Ubiquitination | SALGTASKAASGSLH HHHHHCCHHHCCCCC | 45.57 | 29967540 | |
524 | Phosphorylation | GTASKAASGSLHKDK HHCCHHHCCCCCCCC | 33.50 | 24719451 | |
526 | Phosphorylation | ASKAASGSLHKDKPL CCHHHCCCCCCCCCC | 25.46 | 28348404 | |
531 | Ubiquitination | SGSLHKDKPLPVPPT CCCCCCCCCCCCCCC | 53.94 | 29967540 | |
538 | Phosphorylation | KPLPVPPTLRDLPPP CCCCCCCCCCCCCCC | 28.49 | 29978859 | |
551 | Phosphorylation | PPPPPDRPYSVGAES CCCCCCCCCCCCCCC | 32.88 | 17016520 | |
552 | Phosphorylation | PPPPDRPYSVGAESR CCCCCCCCCCCCCCC | 19.51 | 28064214 | |
553 | Phosphorylation | PPPDRPYSVGAESRP CCCCCCCCCCCCCCC | 19.43 | 30257219 | |
558 | Phosphorylation | PYSVGAESRPQRRPL CCCCCCCCCCCCCCC | 49.04 | 30257219 | |
568 | Phosphorylation | QRRPLPCTPGDCPSR CCCCCCCCCCCCCCC | 28.50 | 28985074 | |
574 | Phosphorylation | CTPGDCPSRDKLPPV CCCCCCCCCCCCCCC | 60.48 | 27251275 | |
577 | Ubiquitination | GDCPSRDKLPPVPSS CCCCCCCCCCCCCHH | 62.88 | 29967540 | |
583 | Phosphorylation | DKLPPVPSSRLGDSW CCCCCCCHHHCCCCC | 28.46 | 24275569 | |
584 | Phosphorylation | KLPPVPSSRLGDSWL CCCCCCHHHCCCCCC | 26.00 | 24275569 | |
589 | Phosphorylation | PSSRLGDSWLPRPIP CHHHCCCCCCCCCCC | 28.81 | 27251275 | |
589 | O-linked_Glycosylation | PSSRLGDSWLPRPIP CHHHCCCCCCCCCCC | 28.81 | 30059200 | |
601 | Phosphorylation | PIPKVPVSAPSSSDP CCCCCCCCCCCCCCC | 28.52 | - | |
601 | O-linked_Glycosylation | PIPKVPVSAPSSSDP CCCCCCCCCCCCCCC | 28.52 | 30059200 | |
604 | O-linked_Glycosylation | KVPVSAPSSSDPWTG CCCCCCCCCCCCCCC | 42.04 | 30059200 | |
604 | Phosphorylation | KVPVSAPSSSDPWTG CCCCCCCCCCCCCCC | 42.04 | 29978859 | |
605 | O-linked_Glycosylation | VPVSAPSSSDPWTGR CCCCCCCCCCCCCCC | 37.39 | 30059200 | |
605 | Phosphorylation | VPVSAPSSSDPWTGR CCCCCCCCCCCCCCC | 37.39 | 29978859 | |
606 | O-linked_Glycosylation | PVSAPSSSDPWTGRE CCCCCCCCCCCCCCC | 52.62 | 30059200 | |
606 | Phosphorylation | PVSAPSSSDPWTGRE CCCCCCCCCCCCCCC | 52.62 | 29978859 | |
610 | O-linked_Glycosylation | PSSSDPWTGRELTNR CCCCCCCCCCCCCCC | 31.58 | 30059200 | |
610 | Phosphorylation | PSSSDPWTGRELTNR CCCCCCCCCCCCCCC | 31.58 | 29978859 | |
615 | Phosphorylation | PWTGRELTNRHSLPF CCCCCCCCCCCCCCC | 26.00 | 23401153 | |
619 | Phosphorylation | RELTNRHSLPFSLPS CCCCCCCCCCCCCCC | 34.20 | 23401153 | |
623 | Phosphorylation | NRHSLPFSLPSQMEP CCCCCCCCCCCCCCC | 37.11 | 29255136 | |
626 | O-linked_Glycosylation | SLPFSLPSQMEPRPD CCCCCCCCCCCCCCC | 47.67 | 30059200 | |
626 | Phosphorylation | SLPFSLPSQMEPRPD CCCCCCCCCCCCCCC | 47.67 | 28450419 | |
639 | Phosphorylation | PDVPRLGSTFSLDTS CCCCCCCCCEEECCC | 30.76 | 11024037 | |
640 | Phosphorylation | DVPRLGSTFSLDTSM CCCCCCCCEEECCCC | 18.55 | 28464451 | |
642 | Phosphorylation | PRLGSTFSLDTSMSM CCCCCCEEECCCCCC | 25.98 | 21712546 | |
645 | Phosphorylation | GSTFSLDTSMSMNSS CCCEEECCCCCCCCC | 31.46 | 28450419 | |
646 | Phosphorylation | STFSLDTSMSMNSSP CCEEECCCCCCCCCC | 14.45 | 28450419 | |
648 | Phosphorylation | FSLDTSMSMNSSPLV EEECCCCCCCCCCCC | 17.99 | 28464451 | |
651 | Phosphorylation | DTSMSMNSSPLVGPE CCCCCCCCCCCCCCC | 25.37 | 28450419 | |
652 | Phosphorylation | TSMSMNSSPLVGPEC CCCCCCCCCCCCCCC | 19.76 | 28464451 | |
667 | Phosphorylation | DHPKIKPSSSANAIY CCCCCCCCCHHHHHH | 31.74 | 23401153 | |
668 | Phosphorylation | HPKIKPSSSANAIYS CCCCCCCCHHHHHHH | 41.83 | 21945579 | |
669 | Phosphorylation | PKIKPSSSANAIYSL CCCCCCCHHHHHHHH | 29.85 | 25159151 | |
674 | Phosphorylation | SSSANAIYSLAARPL CCHHHHHHHHHCCCC | 8.67 | 25159151 | |
675 | Phosphorylation | SSANAIYSLAARPLP CHHHHHHHHHCCCCC | 12.86 | 21945579 | |
698 | Phosphorylation | QCEGEEDTEYMTPSS CCCCCCCCCCCCCCC | 32.09 | 30576142 | |
699 | Phosphorylation | CEGEEDTEYMTPSSR CCCCCCCCCCCCCCC | 45.70 | 17016520 | |
700 | Phosphorylation | EGEEDTEYMTPSSRP CCCCCCCCCCCCCCC | 14.37 | 9525940 | |
702 | Phosphorylation | EEDTEYMTPSSRPLR CCCCCCCCCCCCCCC | 21.08 | 30576142 | |
704 | Phosphorylation | DTEYMTPSSRPLRPL CCCCCCCCCCCCCCC | 29.79 | 30576142 | |
705 | Phosphorylation | TEYMTPSSRPLRPLD CCCCCCCCCCCCCCC | 38.84 | 30576142 | |
713 | Phosphorylation | RPLRPLDTSQSSRAC CCCCCCCCCCCCCCC | 36.03 | 26552605 | |
714 | Phosphorylation | PLRPLDTSQSSRACD CCCCCCCCCCCCCCC | 27.94 | 25159151 | |
716 | Phosphorylation | RPLDTSQSSRACDCD CCCCCCCCCCCCCCC | 22.89 | 27050516 | |
717 | Phosphorylation | PLDTSQSSRACDCDQ CCCCCCCCCCCCCCH | 19.09 | 26552605 | |
731 | Phosphorylation | QQIDSCTYEAMYNIQ HHHHHHHHHHHHHHH | 13.15 | 9525940 | |
735 | Phosphorylation | SCTYEAMYNIQSQAP HHHHHHHHHHHHCCC | 19.03 | 22817900 | |
762 | Phosphorylation | LAAAHANTGPEESEN CHHHHCCCCCCCCCC | 55.70 | 26074081 | |
767 | Phosphorylation | ANTGPEESENEDDGY CCCCCCCCCCCCCCC | 44.02 | 26657352 | |
774 | Phosphorylation | SENEDDGYDVPKPPV CCCCCCCCCCCCCCC | 22.29 | 9525940 | |
789 | Phosphorylation | PAVLARRTLSDISNA CHHHHHCCHHHHCCC | 25.67 | 26074081 | |
791 | Phosphorylation | VLARRTLSDISNASS HHHHCCHHHHCCCCC | 32.08 | 28464451 | |
794 | Phosphorylation | RRTLSDISNASSSFG HCCHHHHCCCCCCCC | 31.19 | 26074081 | |
797 | Phosphorylation | LSDISNASSSFGWLS HHHHCCCCCCCCCEE | 30.66 | 26074081 | |
798 | Phosphorylation | SDISNASSSFGWLSL HHHCCCCCCCCCEEC | 27.55 | 26074081 | |
799 | Phosphorylation | DISNASSSFGWLSLD HHCCCCCCCCCEECC | 25.86 | 26074081 | |
804 | Phosphorylation | SSSFGWLSLDGDPTT CCCCCCEECCCCCCC | 20.22 | 28270605 | |
833 | Phosphorylation | PFPRRINSERKAGSC CCCCCCCCCCCCCCC | 36.09 | 28102081 | |
866 | Phosphorylation | SEIENLMSQGYSYQD HHHHHHHHCCCCHHH | 24.50 | - | |
887 | Sulfoxidation | IAQNNIEMAKNILRE HHHHHHHHHHHHHHH | 5.95 | 21406390 | |
897 | Phosphorylation | NILREFVSISSPAHV HHHHHHHHCCCCCCC | 23.29 | 22199227 | |
899 | Phosphorylation | LREFVSISSPAHVAT HHHHHHCCCCCCCCC | 23.82 | 25159151 | |
900 | Phosphorylation | REFVSISSPAHVAT- HHHHHCCCCCCCCC- | 25.16 | 25159151 | |
906 | Phosphorylation | SSPAHVAT------- CCCCCCCC------- | 37.75 | 22199227 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
371 | Y | Phosphorylation | Kinase | EGFR | Q01279 | PSP |
371 | Y | Phosphorylation | Kinase | LYN | P07948 | PSP |
371 | Y | Phosphorylation | Kinase | INSR | P06213 | Uniprot |
371 | Y | Phosphorylation | Kinase | INSR | P15127 | PSP |
700 | Y | Phosphorylation | Kinase | ABL1 | P00520 | GPS |
700 | Y | Phosphorylation | Kinase | FYN | P06241 | PSP |
700 | Y | Phosphorylation | Kinase | INSR | P06213 | PhosphoELM |
700 | Y | Phosphorylation | Kinase | INSR | P15127 | PSP |
700 | Y | Phosphorylation | Kinase | YES1 | P07947 | GPS |
700 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
700 | Y | Phosphorylation | Kinase | ABL1 | P00519 | Uniprot |
700 | Y | Phosphorylation | Kinase | LCK | P06239 | PSP |
700 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
731 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
731 | Y | Phosphorylation | Kinase | SRC | P12931 | Uniprot |
731 | Y | Phosphorylation | Kinase | LCK | P06239 | PSP |
731 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
731 | Y | Phosphorylation | Kinase | FYN | P06241 | PSP |
731 | Y | Phosphorylation | Kinase | YES1 | P07947 | GPS |
774 | Y | Phosphorylation | Kinase | YES1 | P07947 | GPS |
774 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
774 | Y | Phosphorylation | Kinase | SYK | Q15046 | PhosphoELM |
774 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
774 | Y | Phosphorylation | Kinase | LCK | P06239 | PSP |
774 | Y | Phosphorylation | Kinase | INSR | P15127 | PSP |
774 | Y | Phosphorylation | Kinase | FYN | P06241 | PSP |
774 | Y | Phosphorylation | Kinase | ABL1 | P00520 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | ITCH | Q96J02 | PMID:12226085 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CBL_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 CBL_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00523 | Noonan syndrome and related disorders, including: Noonan syndrome (NS); Leopard syndrome (LS); Noona | |||||
OMIM Disease | ||||||
613563 | Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND MASS SPECTROMETRY. | |
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-452, AND MASSSPECTROMETRY. | |
"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 SER-900, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-675, ANDMASS SPECTROMETRY. | |
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669 AND TYR-674, ANDMASS SPECTROMETRY. | |
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141; TYR-674 ANDTYR-774, AND MASS SPECTROMETRY. | |
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-455; TYR-552 ANDTYR-700, AND MASS 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-674, AND MASSSPECTROMETRY. | |
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371 AND TYR-552, ANDMASS SPECTROMETRY. | |
"Src kinase activity is essential for osteoclast function."; Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.; J. Biol. Chem. 279:17660-17666(2004). Cited for: FUNCTION, PHOSPHORYLATION AT TYR-731, AND MUTAGENESIS OF TYR-731. | |
"Catalytic domains of tyrosine kinases determine the phosphorylationsites within c-Cbl."; Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S.,Deininger M.W., Druker B.J.; FEBS Lett. 577:555-562(2004). Cited for: PHOSPHORYLATION AT TYR-700. | |
"APS facilitates c-Cbl tyrosine phosphorylation and GLUT4translocation in response to insulin in 3T3-L1 adipocytes."; Liu J., Kimura A., Baumann C.A., Saltiel A.R.; Mol. Cell. Biol. 22:3599-3609(2002). Cited for: INTERACTION WITH SH2B2, MUTAGENESIS OF TYR-371; TYR-700; TYR-731 ANDTYR-774, AND PHOSPHORYLATION AT TYR-371; TYR-700 AND TYR-774. |