UniProt ID | CTR9_HUMAN | |
---|---|---|
UniProt AC | Q6PD62 | |
Protein Name | RNA polymerase-associated protein CTR9 homolog | |
Gene Name | CTR9 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1173 | |
Subcellular Localization | Nucleus speckle. Found in speckles.. | |
Protein Description | Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).. | |
Protein Sequence | MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPSTQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAATEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPISKKKKRRKGSGSEQEGEDEEGGERKKKKRRRHPKGEEGSDDDETENGPKPKKRRPPKAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSNSDSDEDEQRKKCASSESDSDENQNKSGSEAGSPRRPRRQRSDQDSDSDQPSRKRRPSGSEQSDNESVQSGRSHSGVSENDSRPASPSAESDHESERGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MSRGSIEIPLRD ---CCCCCEEEECCC | 18.88 | 23312004 | |
32 | Phosphorylation | PEGDEVISILKQEHT CCCCCHHHHHCHHHH | 27.35 | 24719451 | |
39 | Phosphorylation | SILKQEHTQLHIWIA HHHCHHHHHHHHHHH | 31.88 | 24043423 | |
51 | Phosphorylation | WIALALEYYKQGKTE HHHHHHHHHHCCCHH | 19.47 | 24043423 | |
52 | Phosphorylation | IALALEYYKQGKTEE HHHHHHHHHCCCHHH | 6.35 | 24043423 | |
62 | 2-Hydroxyisobutyrylation | GKTEEFVKLLEAARI CCHHHHHHHHHHHCC | 53.31 | - | |
62 | Ubiquitination | GKTEEFVKLLEAARI CCHHHHHHHHHHHCC | 53.31 | 21906983 | |
80 | Ubiquitination | LDYRDHEKDQMTCLD CCCCCCHHHHHHHHH | 50.25 | 29967540 | |
92 | Phosphorylation | CLDTLAAYYVQQARK HHHHHHHHHHHHHHH | 9.88 | - | |
93 | Phosphorylation | LDTLAAYYVQQARKE HHHHHHHHHHHHHHH | 6.25 | - | |
111 | Phosphorylation | DNKKDLITQATLLYT CCHHHHHHHHHHHHH | 21.32 | 20068231 | |
114 | Phosphorylation | KDLITQATLLYTMAD HHHHHHHHHHHHHHH | 13.89 | 20068231 | |
117 | Phosphorylation | ITQATLLYTMADKII HHHHHHHHHHHHHHH | 9.51 | 20068231 | |
118 | Phosphorylation | TQATLLYTMADKIIM HHHHHHHHHHHHHHH | 13.07 | 20068231 | |
159 | Phosphorylation | FHFVLNQSPNNIPAL EEEHHCCCCCCHHHH | 28.64 | 25159151 | |
176 | Acetylation | KACISFNKKDYRGAL HHHHHCCCCCHHHHH | 45.04 | 26051181 | |
177 | Ubiquitination | ACISFNKKDYRGALA HHHHCCCCCHHHHHH | 62.18 | - | |
187 | Acetylation | RGALAYYKKALRTNP HHHHHHHHHHHHHCC | 20.92 | 26051181 | |
188 | Ubiquitination | GALAYYKKALRTNPG HHHHHHHHHHHHCCC | 36.21 | - | |
210 | Acetylation | GMGHCFVKLNKLEKA CCCCCEEEHHHHHHH | 26.53 | 25953088 | |
210 | Ubiquitination | GMGHCFVKLNKLEKA CCCCCEEEHHHHHHH | 26.53 | 29967540 | |
252 | Acetylation | NKEADSIKNGVQLLS CCHHHHHHHHHHHHH | 52.15 | 26051181 | |
252 | Ubiquitination | NKEADSIKNGVQLLS CCHHHHHHHHHHHHH | 52.15 | 21906983 | |
263 | Phosphorylation | QLLSRAYTIDPSNPM HHHHHCEECCCCCHH | 20.23 | - | |
282 | Acetylation | LANHFFFKKDYSKVQ HHHHHCCCCCHHHHH | 39.31 | 25953088 | |
357 | Acetylation | MYIYRGDKENASQCF EEEEECCHHHHHHHH | 56.54 | 26051181 | |
357 | Ubiquitination | MYIYRGDKENASQCF EEEEECCHHHHHHHH | 56.54 | - | |
361 | Phosphorylation | RGDKENASQCFEKVL ECCHHHHHHHHHHHH | 38.78 | - | |
366 | Acetylation | NASQCFEKVLKAYPN HHHHHHHHHHHHCCC | 32.39 | 26051181 | |
366 | Ubiquitination | NASQCFEKVLKAYPN HHHHHHHHHHHHCCC | 32.39 | 22817900 | |
369 | Ubiquitination | QCFEKVLKAYPNNYE HHHHHHHHHCCCCHH | 49.19 | 21906983 | |
379 | Ubiquitination | PNNYETMKILGSLYA CCCHHHHHHHHHHHH | 42.05 | 21906983 | |
393 | 2-Hydroxyisobutyrylation | AASEDQEKRDIAKGH HCCCCHHHHHHHHHH | 50.14 | - | |
393 | Acetylation | AASEDQEKRDIAKGH HCCCCHHHHHHHHHH | 50.14 | 26051181 | |
393 | Ubiquitination | AASEDQEKRDIAKGH HCCCCHHHHHHHHHH | 50.14 | 21906983 | |
398 | Ubiquitination | QEKRDIAKGHLKKVT HHHHHHHHHHHHHHH | 47.39 | 22817900 | |
444 | Ubiquitination | ATRILQEKVQADVPP HHHHHHHHHHCCCCH | 27.04 | - | |
471 | Acetylation | LGNLGEAKKYFLASL CCCHHHHHHHHHHHH | 43.64 | 25953088 | |
471 | Ubiquitination | LGNLGEAKKYFLASL CCCHHHHHHHHHHHH | 43.64 | 22817900 | |
472 | 2-Hydroxyisobutyrylation | GNLGEAKKYFLASLD CCHHHHHHHHHHHHH | 48.56 | - | |
472 | Ubiquitination | GNLGEAKKYFLASLD CCHHHHHHHHHHHHH | 48.56 | 21890473 | |
518 | Acetylation | CEFHEAEKLYKNILR HHHHHHHHHHHHHHH | 65.25 | 26822725 | |
521 | Ubiquitination | HEAEKLYKNILREHP HHHHHHHHHHHHHCC | 48.20 | - | |
544 | Ubiquitination | LGAMARDKGNFYEAS HHCHHHCCCCCCCCC | 50.64 | 21906983 | |
548 | Phosphorylation | ARDKGNFYEASDWFK HHCCCCCCCCCHHHH | 18.00 | 28152594 | |
551 | Phosphorylation | KGNFYEASDWFKEAL CCCCCCCCHHHHHHH | 24.35 | 28152594 | |
578 | Ubiquitination | IGNLHLAKQEWGPGQ HHHHHHHHCCCCCCH | 55.93 | 29967540 | |
637 | Acetylation | DRALAIYKQVLRNDA HHHHHHHHHHHHHHH | 28.02 | 25953088 | |
637 | Malonylation | DRALAIYKQVLRNDA HHHHHHHHHHHHHHH | 28.02 | 32601280 | |
637 | Ubiquitination | DRALAIYKQVLRNDA HHHHHHHHHHHHHHH | 28.02 | 33845483 | |
645 | Ubiquitination | QVLRNDAKNLYAANG HHHHHHHHHHHHHCC | 50.80 | 22817900 | |
660 | Ubiquitination | IGAVLAHKGYFREAR HHHHHHCCCHHHHHH | 50.10 | 23000965 | |
737 | Ubiquitination | CGKLQECKQTLLKAR CCCHHHHHHHHHHHC | 45.63 | 29967540 | |
749 | Phosphorylation | KARHVAPSDTVLMFN HHCCCCCCCCHHHHH | 35.85 | 24719451 | |
766 | Phosphorylation | LVLQRLATSVLKDEK HHHHHHHHHHHCCCC | 24.78 | 24719451 | |
767 | Phosphorylation | VLQRLATSVLKDEKS HHHHHHHHHHCCCCC | 21.61 | 24719451 | |
770 | Acetylation | RLATSVLKDEKSNLK HHHHHHHCCCCCCHH | 62.78 | 25953088 | |
770 | Ubiquitination | RLATSVLKDEKSNLK HHHHHHHCCCCCCHH | 62.78 | 21906983 | |
773 | Ubiquitination | TSVLKDEKSNLKEVL HHHHCCCCCCHHHHH | 55.57 | 22817900 | |
777 | Ubiquitination | KDEKSNLKEVLNAVK CCCCCCHHHHHHHHH | 50.45 | 29967540 | |
784 | Ubiquitination | KEVLNAVKELELAHR HHHHHHHHHHHHHHH | 54.92 | 22817900 | |
798 | 2-Hydroxyisobutyrylation | RYFSYLSKVGDKMRF HHHHHHHHHCHHHHH | 47.87 | - | |
798 | Ubiquitination | RYFSYLSKVGDKMRF HHHHHHHHHCHHHHH | 47.87 | 22817900 | |
802 | Ubiquitination | YLSKVGDKMRFDLAL HHHHHCHHHHHHHHH | 26.50 | 22817900 | |
812 | Phosphorylation | FDLALAATEARQCSD HHHHHHHHHHHHHHH | 25.27 | 21406692 | |
820 | Ubiquitination | EARQCSDLLSQAQYH HHHHHHHHHHHHHHH | 2.59 | 22817900 | |
825 | Ubiquitination | SDLLSQAQYHVARAR HHHHHHHHHHHHHHH | 22.64 | 22817900 | |
831 | Ubiquitination | AQYHVARARKQDEEE HHHHHHHHHHCCHHH | 17.18 | 29967540 | |
839 | Ubiquitination | RKQDEEERELRAKQE HHCCHHHHHHHHHHH | 52.08 | 24816145 | |
844 | "N6,N6-dimethyllysine" | EERELRAKQEQEKEL HHHHHHHHHHHHHHH | 48.19 | - | |
844 | Methylation | EERELRAKQEQEKEL HHHHHHHHHHHHHHH | 48.19 | - | |
844 | Ubiquitination | EERELRAKQEQEKEL HHHHHHHHHHHHHHH | 48.19 | 21906983 | |
849 | Ubiquitination | RAKQEQEKELLRQKL HHHHHHHHHHHHHHH | 54.05 | 21906983 | |
855 | Ubiquitination | EKELLRQKLLKEQEE HHHHHHHHHHHHHHH | 49.72 | 29967540 | |
863 | Ubiquitination | LLKEQEEKRLREKEE HHHHHHHHHHHHHHH | 56.85 | 24816145 | |
873 | Ubiquitination | REKEEQKKLLEQRAQ HHHHHHHHHHHHHHH | 58.98 | 24816145 | |
884 | Acetylation | QRAQYVEKTKNILMF HHHHHHHHHHCEEEE | 55.55 | 23749302 | |
885 | Phosphorylation | RAQYVEKTKNILMFT HHHHHHHHHCEEEEC | 18.80 | 23532336 | |
890 | Sulfoxidation | EKTKNILMFTGETEA HHHHCEEEECCCCHH | 2.21 | 21406390 | |
892 | Phosphorylation | TKNILMFTGETEATK HHCEEEECCCCHHCC | 21.83 | 20068231 | |
895 | Phosphorylation | ILMFTGETEATKEKK EEEECCCCHHCCCCC | 32.06 | 23532336 | |
898 | Phosphorylation | FTGETEATKEKKRGG ECCCCHHCCCCCCCC | 33.24 | 20068231 | |
899 | Acetylation | TGETEATKEKKRGGG CCCCHHCCCCCCCCC | 74.67 | 26051181 | |
901 | Phosphorylation | ETEATKEKKRGGGGG CCHHCCCCCCCCCCC | 49.69 | 32645325 | |
911 | Phosphorylation | GGGGGRRSKKGGEFD CCCCCCCCCCCCCCC | 37.04 | 21712546 | |
925 | Phosphorylation | DEFVNDDTDDDLPIS CHHCCCCCCCCCCCC | 44.16 | 19664994 | |
932 | Phosphorylation | TDDDLPISKKKKRRK CCCCCCCCCCCCCCC | 36.16 | 22167270 | |
941 | Phosphorylation | KKKRRKGSGSEQEGE CCCCCCCCCCCCCCC | 42.03 | 29255136 | |
943 | Phosphorylation | KRRKGSGSEQEGEDE CCCCCCCCCCCCCCC | 37.49 | 29255136 | |
967 | Ubiquitination | RRRHPKGEEGSDDDE CCCCCCCCCCCCCCC | 66.37 | 24816145 | |
970 | Phosphorylation | HPKGEEGSDDDETEN CCCCCCCCCCCCCCC | 40.94 | 29255136 | |
975 | Phosphorylation | EGSDDDETENGPKPK CCCCCCCCCCCCCCC | 41.57 | 22167270 | |
991 | Ubiquitination | RRPPKAEKKKAPKPE CCCCHHHHCCCCCHH | 65.52 | 24816145 | |
1003 | Ubiquitination | KPERLPPSMKGKIKS CHHHCCHHHCCCCCE | 31.05 | 33845483 | |
1005 | Acetylation | ERLPPSMKGKIKSKA HHCCHHHCCCCCEEE | 62.48 | 25953088 | |
1015 | Phosphorylation | IKSKAIISSSDDSSD CCEEEEECCCCCCCC | 20.06 | 25159151 | |
1016 | Phosphorylation | KSKAIISSSDDSSDE CEEEEECCCCCCCCH | 27.64 | 25159151 | |
1017 | Phosphorylation | SKAIISSSDDSSDED EEEEECCCCCCCCHH | 38.35 | 25159151 | |
1020 | Phosphorylation | IISSSDDSSDEDKLK EECCCCCCCCHHHHH | 44.68 | 25159151 | |
1021 | Phosphorylation | ISSSDDSSDEDKLKI ECCCCCCCCHHHHHH | 52.60 | 28355574 | |
1027 | Ubiquitination | SSDEDKLKIADEGHP CCCHHHHHHCCCCCC | 41.40 | 33845483 | |
1037 | Phosphorylation | DEGHPRNSNSNSDSD CCCCCCCCCCCCCCC | 42.80 | 29255136 | |
1039 | Phosphorylation | GHPRNSNSNSDSDED CCCCCCCCCCCCCHH | 37.22 | 29255136 | |
1041 | Phosphorylation | PRNSNSNSDSDEDEQ CCCCCCCCCCCHHHH | 38.01 | 29255136 | |
1043 | Phosphorylation | NSNSNSDSDEDEQRK CCCCCCCCCHHHHHH | 42.60 | 21955146 | |
1044 | Phosphorylation | SNSNSDSDEDEQRKK CCCCCCCCHHHHHHH | 72.81 | 33259812 | |
1054 | Phosphorylation | EQRKKCASSESDSDE HHHHHHHHCCCCCCC | 44.07 | 29083192 | |
1055 | Phosphorylation | QRKKCASSESDSDEN HHHHHHHCCCCCCCC | 23.69 | 25072903 | |
1057 | Phosphorylation | KKCASSESDSDENQN HHHHHCCCCCCCCCC | 44.34 | 25072903 | |
1059 | Phosphorylation | CASSESDSDENQNKS HHHCCCCCCCCCCCC | 56.98 | 28985074 | |
1066 | Phosphorylation | SDENQNKSGSEAGSP CCCCCCCCCCCCCCC | 55.92 | 25159151 | |
1068 | Phosphorylation | ENQNKSGSEAGSPRR CCCCCCCCCCCCCCC | 31.22 | 20363803 | |
1072 | Phosphorylation | KSGSEAGSPRRPRRQ CCCCCCCCCCCCCCC | 23.45 | 25159151 | |
1081 | Phosphorylation | RRPRRQRSDQDSDSD CCCCCCCCCCCCCCC | 31.14 | 27273156 | |
1085 | Phosphorylation | RQRSDQDSDSDQPSR CCCCCCCCCCCCCCC | 33.12 | 27273156 | |
1087 | Phosphorylation | RSDQDSDSDQPSRKR CCCCCCCCCCCCCCC | 41.94 | 27273156 | |
1091 | Phosphorylation | DSDSDQPSRKRRPSG CCCCCCCCCCCCCCC | 44.81 | 25884760 | |
1097 | Phosphorylation | PSRKRRPSGSEQSDN CCCCCCCCCCCCCCC | 53.81 | 23401153 | |
1099 | Phosphorylation | RKRRPSGSEQSDNES CCCCCCCCCCCCCCC | 36.48 | 29255136 | |
1102 | Phosphorylation | RPSGSEQSDNESVQS CCCCCCCCCCCCCCC | 38.05 | 29255136 | |
1106 | Phosphorylation | SEQSDNESVQSGRSH CCCCCCCCCCCCCCC | 31.54 | 23663014 | |
1109 | Phosphorylation | SDNESVQSGRSHSGV CCCCCCCCCCCCCCC | 33.74 | 23663014 | |
1112 | Phosphorylation | ESVQSGRSHSGVSEN CCCCCCCCCCCCCCC | 26.06 | 20363803 | |
1114 | Phosphorylation | VQSGRSHSGVSENDS CCCCCCCCCCCCCCC | 41.98 | 23312004 | |
1117 | Phosphorylation | GRSHSGVSENDSRPA CCCCCCCCCCCCCCC | 33.92 | 20363803 | |
1121 | Phosphorylation | SGVSENDSRPASPSA CCCCCCCCCCCCCCC | 52.31 | 20363803 | |
1125 | Phosphorylation | ENDSRPASPSAESDH CCCCCCCCCCCCCCC | 23.28 | 23312004 | |
1127 | Phosphorylation | DSRPASPSAESDHES CCCCCCCCCCCCCCC | 42.02 | 20363803 | |
1130 | Phosphorylation | PASPSAESDHESERG CCCCCCCCCCCCCCC | 43.94 | 25849741 | |
1138 | Phosphorylation | DHESERGSDNEGSGQ CCCCCCCCCCCCCCC | 43.41 | 20873877 | |
1143 | Phosphorylation | RGSDNEGSGQGSGNE CCCCCCCCCCCCCCC | 23.05 | 20873877 | |
1147 | Phosphorylation | NEGSGQGSGNESEPE CCCCCCCCCCCCCCC | 30.47 | 21815630 | |
1151 | Phosphorylation | GQGSGNESEPEGSNN CCCCCCCCCCCCCCC | 63.55 | 20873877 | |
1156 | Phosphorylation | NESEPEGSNNEASDR CCCCCCCCCCCCCCC | 34.52 | 20873877 | |
1172 | Phosphorylation | SEHGSDDSD------ CCCCCCCCC------ | 50.65 | 30242111 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
1081 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTR9_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 CTR9_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 |
"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-925 AND SER-932, 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-925; SER-970; SER-1015;SER-1016; SER-1017; SER-1020; SER-1021; SER-1037; SER-1039; SER-1041AND SER-1043, AND MASS SPECTROMETRY. | |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1020 AND SER-1021, 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 SER-941 AND SER-943, 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-925; SER-941; SER-943;SER-970; SER-1015; SER-1016; SER-1017; SER-1020 AND SER-1021, 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-925, 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-925, AND MASSSPECTROMETRY. | |
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND MASSSPECTROMETRY. |