UniProt ID | CFTR_HUMAN | |
---|---|---|
UniProt AC | P13569 | |
Protein Name | Cystic fibrosis transmembrane conductance regulator | |
Gene Name | CFTR | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1480 | |
Subcellular Localization |
Apical cell membrane Multi-pass membrane protein . Early endosome membrane Multi-pass membrane protein . Cell membrane Multi-pass membrane protein . Recycling endosome membrane Multi-pass membrane protein . Endoplasmic reticulum membrane Multi-p |
|
Protein Description | Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. [PubMed: 26823428 Mediates the transport of chloride ions across the cell membrane] | |
Protein Sequence | MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MQRSPLEKASV ----CCCCHHHHHHH | 33.28 | 24719451 | |
45 | Phosphorylation | YQIPSVDSADNLSEK CCCCCCCCCCCHHHH | 35.05 | - | |
50 | Phosphorylation | VDSADNLSEKLEREW CCCCCCHHHHHHHHH | 38.65 | - | |
94 | Phosphorylation | FLYLGEVTKAVQPLL HHHHHHHHHHHHHHH | 14.69 | - | |
256 | Phosphorylation | DQRAGKISERLVITS HHCCCCCCCEEEECH | 21.83 | - | |
291 | Phosphorylation | MIENLRQTELKLTRK HHHHHHHHHHHHHHH | 36.53 | 20068231 | |
420 | Ubiquitination | KQNNNNRKTSNGDDS HHCCCCCCCCCCCCC | 59.43 | - | |
421 | Phosphorylation | QNNNNRKTSNGDDSL HCCCCCCCCCCCCCC | 24.96 | 24719451 | |
422 | Phosphorylation | NNNNRKTSNGDDSLF CCCCCCCCCCCCCCC | 41.68 | 21930781 | |
427 | Phosphorylation | KTSNGDDSLFFSNFS CCCCCCCCCCCCCCC | 31.64 | - | |
447 | Sumoylation | VLKDINFKIERGQLL CCCCCCEEEECCCEE | 38.89 | - | |
447 | Sumoylation | VLKDINFKIERGQLL CCCCCCEEEECCCEE | 38.89 | - | |
466 | Phosphorylation | STGAGKTSLLMVIMG CCCCCHHHEEEEEEC | 24.00 | 26657352 | |
489 | Phosphorylation | IKHSGRISFCSQFSW CCCCCCEEEEECCCC | 20.88 | 30631047 | |
492 | Phosphorylation | SGRISFCSQFSWIMP CCCEEEEECCCCCCC | 32.05 | 30631047 | |
501 | Phosphorylation | FSWIMPGTIKENIIF CCCCCCCCCCCCEEE | 24.01 | 30631047 | |
511 | Phosphorylation | ENIIFGVSYDEYRYR CCEEEEECCCHHHHH | 27.52 | 21930781 | |
512 | Phosphorylation | NIIFGVSYDEYRYRS CEEEEECCCHHHHHH | 15.47 | 21807898 | |
515 | Phosphorylation | FGVSYDEYRYRSVIK EEECCCHHHHHHHHH | 15.28 | 17053785 | |
524 | S-palmitoylation | YRSVIKACQLEEDIS HHHHHHHHCCHHHHH | 3.94 | 22119790 | |
547 | Phosphorylation | VLGEGGITLSGGQRA EEECCCEECCCHHHH | 20.39 | 25278378 | |
549 | Phosphorylation | GEGGITLSGGQRARI ECCCEECCCHHHHHH | 32.02 | 20068231 | |
582 | Phosphorylation | FGYLDVLTEKEIFES CCCCCCCCHHHHHHH | 44.88 | 22817900 | |
604 | Phosphorylation | NKTRILVTSKMEHLK CCCEEEEECCHHHHH | 21.13 | 22817900 | |
605 | Phosphorylation | KTRILVTSKMEHLKK CCEEEEECCHHHHHH | 23.64 | - | |
641 | Phosphorylation | QNLQPDFSSKLMGCD HHCCCCCCHHHCCCC | 33.66 | 22817900 | |
660 | Phosphorylation | FSAERRNSILTETLH CCHHHHHHHHHHHHH | 19.70 | 1716180 | |
670 | Phosphorylation | TETLHRFSLEGDAPV HHHHHHHCCCCCCCC | 26.01 | 25330774 | |
682 | Phosphorylation | APVSWTETKKQSFKQ CCCCCCHHCCHHHHC | 35.85 | 22817900 | |
686 | Phosphorylation | WTETKKQSFKQTGEF CCHHCCHHHHCCCCC | 43.20 | 22817900 | |
688 | Ubiquitination | ETKKQSFKQTGEFGE HHCCHHHHCCCCCCH | 52.80 | 22119790 | |
700 | Phosphorylation | FGEKRKNSILNPINS CCHHHCCCCCCHHHH | 31.33 | 22817900 | |
707 | Phosphorylation | SILNPINSIRKFSIV CCCCHHHHHHCCEEE | 25.21 | 22817900 | |
712 | Phosphorylation | INSIRKFSIVQKTPL HHHHHCCEEEECCCC | 25.53 | 22817900 | |
717 | Phosphorylation | KFSIVQKTPLQMNGI CCEEEECCCCCCCCC | 16.49 | 22119790 | |
728 | Phosphorylation | MNGIEEDSDEPLERR CCCCCCCCCCCHHHH | 47.34 | 23879269 | |
737 | Phosphorylation | EPLERRLSLVPDSEQ CCHHHHHCCCCCHHH | 26.05 | 21455600 | |
753 | Phosphorylation | EAILPRISVISTGPT CEECCCEEEEECCCC | 18.06 | 22817900 | |
768 | Phosphorylation | LQARRRQSVLNLMTH HHHHHHHHHHHHHHC | 27.10 | 21455600 | |
774 | Phosphorylation | QSVLNLMTHSVNQGQ HHHHHHHHCCCCCCC | 17.73 | 23312004 | |
776 | Phosphorylation | VLNLMTHSVNQGQNI HHHHHHCCCCCCCCC | 17.38 | 23312004 | |
790 | Phosphorylation | IHRKTTASTRKVSLA CCCCCCCCCCCCCCC | 27.01 | 22817900 | |
795 | Phosphorylation | TASTRKVSLAPQANL CCCCCCCCCCCCCCC | 23.11 | 1716180 | |
803 | Phosphorylation | LAPQANLTELDIYSR CCCCCCCCHHHHHHH | 34.02 | 24719451 | |
808 | Phosphorylation | NLTELDIYSRRLSQE CCCHHHHHHHHHHHH | 8.87 | 28442448 | |
809 | Phosphorylation | LTELDIYSRRLSQET CCHHHHHHHHHHHHH | 15.97 | 22817900 | |
813 | Phosphorylation | DIYSRRLSQETGLEI HHHHHHHHHHHCCCC | 24.94 | 21455600 | |
816 | Phosphorylation | SRRLSQETGLEISEE HHHHHHHHCCCCCHH | 39.16 | - | |
894 | N-linked_Glycosylation | TPLQDKGNSTHSRNN CCCCCCCCCCCCCCC | 49.85 | 7518437 | |
900 | N-linked_Glycosylation | GNSTHSRNNSYAVII CCCCCCCCCEEEEEE | 44.83 | 7518437 | |
1014 | Phosphorylation | VVAVLQPYIFVATVP HHHHHHCCHHHHHHH | 8.27 | - | |
1019 | Phosphorylation | QPYIFVATVPVIVAF HCCHHHHHHHHHHHH | 21.75 | - | |
1045 | Phosphorylation | QQLKQLESEGRSPIF HHHHHHHHCCCCHHH | 54.68 | - | |
1171 | Phosphorylation | FKFIDMPTEGKPTKS HHHCCCCCCCCCCCC | 51.21 | 28509920 | |
1176 | Phosphorylation | MPTEGKPTKSTKPYK CCCCCCCCCCCCCCC | 40.90 | 19413330 | |
1246 | Phosphorylation | RVGLLGRTGSGKSTL EEEEECCCCCCHHHH | 33.62 | 28258704 | |
1248 | Phosphorylation | GLLGRTGSGKSTLLS EEECCCCCCHHHHHH | 42.29 | 28258704 | |
1255 | Phosphorylation | SGKSTLLSAFLRLLN CCHHHHHHHHHHHHC | 21.78 | 22210691 | |
1344 | Glutathionylation | FVLVDGGCVLSHGHK EEEEECCEEECCHHH | 3.21 | 22833525 | |
1359 | Phosphorylation | QLMCLARSVLSKAKI HHHHHHHHHHHHCEE | 23.08 | 20068231 | |
1362 | Phosphorylation | CLARSVLSKAKILLL HHHHHHHHHCEEHHH | 28.54 | 20068231 | |
1395 | S-palmitoylation | LKQAFADCTVILCEH HHHHHCCCEEEEECH | 2.69 | 22119790 | |
1424 | Phosphorylation | EENKVRQYDSIQKLL ECCCHHCHHHHHHHH | 10.90 | 26270265 | |
1426 | Phosphorylation | NKVRQYDSIQKLLNE CCHHCHHHHHHHHHH | 23.22 | 26270265 | |
1444 | Phosphorylation | FRQAISPSDRVKLFP HHHCCCHHHHCCCCC | 31.12 | 22119790 | |
1455 | Phosphorylation | KLFPHRNSSKCKSKP CCCCCCCCHHCCCCH | 31.00 | 24670416 | |
1456 | Phosphorylation | LFPHRNSSKCKSKPQ CCCCCCCHHCCCCHH | 45.69 | 7680525 | |
1471 | Phosphorylation | IAALKEETEEEVQDT HHHHHHHHHHHHHHH | 50.19 | 21930781 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
421 | T | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
422 | S | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
422 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
427 | S | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
511 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
511 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
512 | Y | Phosphorylation | Kinase | SYK | P43405 | PSP |
604 | T | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
641 | S | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
641 | S | Phosphorylation | Kinase | PKCA | P17252 | PSP |
660 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
660 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
660 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
660 | S | Phosphorylation | Kinase | PRKG1 | P00516 | GPS |
660 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
660 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
660 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
660 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
660 | S | Phosphorylation | Kinase | PRKACA | P00517 | GPS |
670 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
670 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
682 | T | Phosphorylation | Kinase | PKCA | P17252 | PSP |
682 | T | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
686 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
686 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
686 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
686 | S | Phosphorylation | Kinase | KPCA | P17252 | PhosphoELM |
686 | S | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
700 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
700 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
700 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
700 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
700 | S | Phosphorylation | Kinase | PRKACA | P00517 | GPS |
700 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
700 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
700 | S | Phosphorylation | Kinase | PRKG1 | P00516 | GPS |
707 | S | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
712 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
712 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
712 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
737 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
737 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
737 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
737 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
737 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
737 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
737 | S | Phosphorylation | Kinase | LMTK2 | Q8IWU2 | GPS |
737 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
737 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
753 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
753 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
753 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
753 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
768 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
768 | S | Phosphorylation | Kinase | AMPK-FAMILY | - | GPS |
768 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
768 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
768 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
768 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
768 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
768 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
790 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
790 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
790 | S | Phosphorylation | Kinase | PRKCA | P05696 | GPS |
790 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
795 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
795 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
795 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
795 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
795 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
795 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
795 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
813 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
813 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
813 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
813 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
813 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
813 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
813 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
813 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:11146634 |
- | K | Ubiquitination | E3 ubiquitin ligase | AMFR | Q9UKV5 | PMID:18216283 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF5 | Q99942 | PMID:21148293 |
- | K | Ubiquitination | E3 ubiquitin ligase | RNF185 | Q96GF1 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | CBL | P22681 | PMID:22467879 |
- | K | Ubiquitination | E3 ubiquitin ligase | MARCHF2 | Q9P0N8 | PMID:23818989 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CFTR_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 CFTR_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00218 | Cystic fibrosis (CF) | |||||
H00933 | Hereditary pancreatitis; Hereditary chronic pancreatitis | |||||
H01033 | Congenital bilateral absence of vas deferens | |||||
OMIM Disease | ||||||
219700 | Cystic fibrosis (CF) | |||||
277180 | Congenital bilateral absence of the vas deferens (CBAVD) | |||||
Kegg Drug | ||||||
D00808 | Suramin hexasodium (USAN); Bayer 205 (TN) | |||||
D09916 | Ivacaftor (USAN/INN); Kalydeco (TN) | |||||
D10134 | Lumacaftor (USAN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Mapping of cystic fibrosis transmembrane conductance regulatormembrane topology by glycosylation site insertion."; Chang X.-B., Hou Y.-X., Jensen T.J., Riordan J.R.; J. Biol. Chem. 269:18572-18575(1994). Cited for: GLYCOSYLATION AT ASN-894 AND ASN-900, AND TOPOLOGY. | |
Palmitoylation | |
Reference | PubMed |
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications."; McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.; Protein Eng. Des. Sel. 25:7-14(2012). Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications."; McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.; Protein Eng. Des. Sel. 25:7-14(2012). Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY. | |
"Evidence for phosphorylation of serine 753 in CFTR using a novelmetal-ion affinity resin and matrix-assisted laser desorption massspectrometry."; Neville D.C.A., Rozanas C.R., Rice E.M., Gruis D.B., Verkman A.S.,Townsend R.R.; Protein Sci. 6:2436-2445(1997). Cited for: PHOSPHORYLATION AT SER-660; SER-700; SER-712; SER-737; SER-753;SER-768; SER-795 AND SER-813. | |
"Phosphorylation of the cystic fibrosis transmembrane conductanceregulator."; Picciotto M.R., Cohn J.A., Bertuzzi G., Greenguard P., Nairn A.C.; J. Biol. Chem. 267:12742-12752(1992). Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-737; SER-768;SER-790; SER-795 AND SER-813. | |
"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-1176, AND MASSSPECTROMETRY. | |
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-515, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications."; McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.; Protein Eng. Des. Sel. 25:7-14(2012). Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY. |