UniProt ID | DHE3_MOUSE | |
---|---|---|
UniProt AC | P26443 | |
Protein Name | Glutamate dehydrogenase 1, mitochondrial | |
Gene Name | Glud1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 558 | |
Subcellular Localization | Mitochondrion matrix. | |
Protein Description | Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.. | |
Protein Sequence | MYRRLGEALLLSRAGPAALGSAAADSAALLGWARGQPSAAPQPGLTPVARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCVGVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKVYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT | |
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 |
---|---|---|---|---|---|
21 | Phosphorylation | AGPAALGSAAADSAA CCHHHHCHHHHHHHH | 18.65 | 22817900 | |
68 | Acetylation | EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH | 37.59 | 23954790 | |
68 | Succinylation | EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH | 37.59 | - | |
68 | Succinylation | EDDPNFFKMVEGFFD CCCCCHHHHHHCHHH | 37.59 | 23806337 | |
79 | Phosphorylation | GFFDRGASIVEDKLV CHHHCCCHHHHHHHH | 29.95 | 25521595 | |
84 | Acetylation | GASIVEDKLVEDLKT CCHHHHHHHHHHHHC | 40.71 | 23806337 | |
84 | Glutarylation | GASIVEDKLVEDLKT CCHHHHHHHHHHHHC | 40.71 | 24703693 | |
84 | Malonylation | GASIVEDKLVEDLKT CCHHHHHHHHHHHHC | 40.71 | 26320211 | |
84 | Succinylation | GASIVEDKLVEDLKT CCHHHHHHHHHHHHC | 40.71 | - | |
84 | Succinylation | GASIVEDKLVEDLKT CCHHHHHHHHHHHHC | 40.71 | 23806337 | |
90 | Acetylation | DKLVEDLKTRESEEQ HHHHHHHHCCCCHHH | 58.83 | 23576753 | |
90 | Glutarylation | DKLVEDLKTRESEEQ HHHHHHHHCCCCHHH | 58.83 | 24703693 | |
90 | Malonylation | DKLVEDLKTRESEEQ HHHHHHHHCCCCHHH | 58.83 | 26073543 | |
90 | Succinylation | DKLVEDLKTRESEEQ HHHHHHHHCCCCHHH | 58.83 | - | |
90 | Ubiquitination | DKLVEDLKTRESEEQ HHHHHHHHCCCCHHH | 58.83 | - | |
94 | Phosphorylation | EDLKTRESEEQKRNR HHHHCCCCHHHHHHH | 43.04 | 23140645 | |
98 | Acetylation | TRESEEQKRNRVRGI CCCCHHHHHHHHHHH | 55.72 | 23864654 | |
110 | Acetylation | RGILRIIKPCNHVLS HHHHHHHHCCCEEEE | 40.94 | 23576753 | |
110 | Succinylation | RGILRIIKPCNHVLS HHHHHHHHCCCEEEE | 40.94 | - | |
110 | Succinylation | RGILRIIKPCNHVLS HHHHHHHHCCCEEEE | 40.94 | 24315375 | |
112 | S-nitrosocysteine | ILRIIKPCNHVLSLS HHHHHHCCCEEEEEE | 4.70 | - | |
112 | S-nitrosylation | ILRIIKPCNHVLSLS HHHHHHCCCEEEEEE | 4.70 | 22178444 | |
112 | S-palmitoylation | ILRIIKPCNHVLSLS HHHHHHCCCEEEEEE | 4.70 | 28526873 | |
117 | Phosphorylation | KPCNHVLSLSFPIRR HCCCEEEEEECEEEC | 22.37 | 23140645 | |
128 | Phosphorylation | PIRRDDGSWEVIEGY EEECCCCCEEEEEEE | 27.36 | 25521595 | |
135 | Phosphorylation | SWEVIEGYRAQHSQH CEEEEEEEECCCCCC | 7.03 | 25619855 | |
147 | Acetylation | SQHRTPCKGGIRYST CCCCCCCCCCCCCCC | 62.47 | 23806337 | |
147 | Malonylation | SQHRTPCKGGIRYST CCCCCCCCCCCCCCC | 62.47 | 26320211 | |
147 | Succinylation | SQHRTPCKGGIRYST CCCCCCCCCCCCCCC | 62.47 | - | |
147 | Ubiquitination | SQHRTPCKGGIRYST CCCCCCCCCCCCCCC | 62.47 | - | |
152 | Phosphorylation | PCKGGIRYSTDVSVD CCCCCCCCCCCCCHH | 17.63 | 23984901 | |
153 | Phosphorylation | CKGGIRYSTDVSVDE CCCCCCCCCCCCHHH | 14.32 | 25521595 | |
154 | Phosphorylation | KGGIRYSTDVSVDEV CCCCCCCCCCCHHHH | 31.33 | 23140645 | |
157 | Phosphorylation | IRYSTDVSVDEVKAL CCCCCCCCHHHHHHH | 27.02 | 25521595 | |
162 | Acetylation | DVSVDEVKALASLMT CCCHHHHHHHHHHHH | 35.32 | 23576753 | |
162 | Succinylation | DVSVDEVKALASLMT CCCHHHHHHHHHHHH | 35.32 | - | |
162 | Succinylation | DVSVDEVKALASLMT CCCHHHHHHHHHHHH | 35.32 | 23806337 | |
162 | Ubiquitination | DVSVDEVKALASLMT CCCHHHHHHHHHHHH | 35.32 | - | |
171 | Acetylation | LASLMTYKCAVVDVP HHHHHHCEEEEEECC | 13.42 | 23576753 | |
171 | Ubiquitination | LASLMTYKCAVVDVP HHHHHHCEEEEEECC | 13.42 | 22790023 | |
172 | ADP-ribosylation | ASLMTYKCAVVDVPF HHHHHCEEEEEECCC | 2.15 | - | |
172 | ADP-ribosylation | ASLMTYKCAVVDVPF HHHHHCEEEEEECCC | 2.15 | - | |
172 | S-nitrosylation | ASLMTYKCAVVDVPF HHHHHCEEEEEECCC | 2.15 | 22178444 | |
172 | S-palmitoylation | ASLMTYKCAVVDVPF HHHHHCEEEEEECCC | 2.15 | 28526873 | |
183 | Acetylation | DVPFGGAKAGVKINP ECCCCCCCCCCCCCC | 49.28 | 23806337 | |
183 | Succinylation | DVPFGGAKAGVKINP ECCCCCCCCCCCCCC | 49.28 | - | |
183 | Succinylation | DVPFGGAKAGVKINP ECCCCCCCCCCCCCC | 49.28 | 23806337 | |
183 | Ubiquitination | DVPFGGAKAGVKINP ECCCCCCCCCCCCCC | 49.28 | - | |
187 | Acetylation | GGAKAGVKINPKNYT CCCCCCCCCCCCCCC | 35.53 | 23576753 | |
187 | Malonylation | GGAKAGVKINPKNYT CCCCCCCCCCCCCCC | 35.53 | 26320211 | |
187 | Succinylation | GGAKAGVKINPKNYT CCCCCCCCCCCCCCC | 35.53 | 23806337 | |
191 | Acetylation | AGVKINPKNYTDNEL CCCCCCCCCCCHHHH | 59.09 | 23576753 | |
191 | Malonylation | AGVKINPKNYTDNEL CCCCCCCCCCCHHHH | 59.09 | 26320211 | |
191 | Succinylation | AGVKINPKNYTDNEL CCCCCCCCCCCHHHH | 59.09 | - | |
191 | Succinylation | AGVKINPKNYTDNEL CCCCCCCCCCCHHHH | 59.09 | 23806337 | |
191 | Ubiquitination | AGVKINPKNYTDNEL CCCCCCCCCCCHHHH | 59.09 | - | |
193 | Phosphorylation | VKINPKNYTDNELEK CCCCCCCCCHHHHHH | 22.92 | 25195567 | |
200 | Acetylation | YTDNELEKITRRFTM CCHHHHHHHHHHHHH | 63.10 | 23864654 | |
200 | Succinylation | YTDNELEKITRRFTM CCHHHHHHHHHHHHH | 63.10 | - | |
200 | Succinylation | YTDNELEKITRRFTM CCHHHHHHHHHHHHH | 63.10 | 23806337 | |
200 | Ubiquitination | YTDNELEKITRRFTM CCHHHHHHHHHHHHH | 63.10 | - | |
211 | Acetylation | RFTMELAKKGFIGPG HHHHHHHHCCCCCCC | 67.08 | 23576753 | |
211 | Succinylation | RFTMELAKKGFIGPG HHHHHHHHCCCCCCC | 67.08 | 23806337 | |
212 | Ubiquitination | FTMELAKKGFIGPGI HHHHHHHCCCCCCCC | 54.14 | 22790023 | |
226 | Oxidation | IDVPAPDMSTGEREM CCCCCCCCCCCHHHH | 3.63 | 17242355 | |
227 | Phosphorylation | DVPAPDMSTGEREMS CCCCCCCCCCHHHHH | 40.41 | 22324799 | |
228 | Phosphorylation | VPAPDMSTGEREMSW CCCCCCCCCHHHHHH | 36.10 | 22817900 | |
254 | S-nitrosylation | YDINAHACVTGKPIS CEECCCEEEECCCCC | 1.70 | 22178444 | |
261 | Phosphorylation | CVTGKPISQGGIHGR EEECCCCCCCCCCCC | 31.16 | 22324799 | |
270 | Phosphorylation | GGIHGRISATGRGVF CCCCCCCCCCCCCHH | 20.58 | 29899451 | |
272 | Phosphorylation | IHGRISATGRGVFHG CCCCCCCCCCCHHHC | 22.18 | 22324799 | |
326 | Acetylation | YLHRFGAKCVGVGES HHHHCCCEEEEECCC | 29.81 | 23576753 | |
326 | Succinylation | YLHRFGAKCVGVGES HHHHCCCEEEEECCC | 29.81 | 23806337 | |
326 | Ubiquitination | YLHRFGAKCVGVGES HHHHCCCEEEEECCC | 29.81 | - | |
327 | S-nitrosocysteine | LHRFGAKCVGVGESD HHHCCCEEEEECCCC | 2.97 | - | |
327 | S-nitrosylation | LHRFGAKCVGVGESD HHHCCCEEEEECCCC | 2.97 | 24895380 | |
333 | Phosphorylation | KCVGVGESDGSIWNP EEEEECCCCCCCCCC | 41.15 | 23984901 | |
336 | Phosphorylation | GVGESDGSIWNPDGI EECCCCCCCCCCCCC | 29.44 | 23140645 | |
346 | Acetylation | NPDGIDPKELEDFKL CCCCCCHHHHHHCCC | 71.79 | 23576753 | |
346 | Malonylation | NPDGIDPKELEDFKL CCCCCCHHHHHHCCC | 71.79 | 26073543 | |
346 | Succinylation | NPDGIDPKELEDFKL CCCCCCHHHHHHCCC | 71.79 | - | |
346 | Succinylation | NPDGIDPKELEDFKL CCCCCCHHHHHHCCC | 71.79 | 23806337 | |
352 | Acetylation | PKELEDFKLQHGSIL HHHHHHCCCCCCCCC | 60.61 | 23576753 | |
352 | Succinylation | PKELEDFKLQHGSIL HHHHHHCCCCCCCCC | 60.61 | - | |
352 | Succinylation | PKELEDFKLQHGSIL HHHHHHCCCCCCCCC | 60.61 | 23806337 | |
352 | Ubiquitination | PKELEDFKLQHGSIL HHHHHHCCCCCCCCC | 60.61 | - | |
357 | Phosphorylation | DFKLQHGSILGFPKA HCCCCCCCCCCCCCC | 16.71 | 23140645 | |
363 | Acetylation | GSILGFPKAKVYEGS CCCCCCCCCEEECCC | 59.59 | 23576753 | |
363 | Glutarylation | GSILGFPKAKVYEGS CCCCCCCCCEEECCC | 59.59 | 24703693 | |
363 | Succinylation | GSILGFPKAKVYEGS CCCCCCCCCEEECCC | 59.59 | - | |
363 | Succinylation | GSILGFPKAKVYEGS CCCCCCCCCEEECCC | 59.59 | 23806337 | |
363 | Ubiquitination | GSILGFPKAKVYEGS CCCCCCCCCEEECCC | 59.59 | - | |
365 | Acetylation | ILGFPKAKVYEGSIL CCCCCCCEEECCCCE | 52.02 | 23576753 | |
365 | Succinylation | ILGFPKAKVYEGSIL CCCCCCCEEECCCCE | 52.02 | - | |
365 | Succinylation | ILGFPKAKVYEGSIL CCCCCCCEEECCCCE | 52.02 | 23806337 | |
367 | Phosphorylation | GFPKAKVYEGSILEA CCCCCEEECCCCEEE | 17.54 | 23984901 | |
370 | Phosphorylation | KAKVYEGSILEADCD CCEEECCCCEEECCC | 16.44 | 19060867 | |
376 | Glutathionylation | GSILEADCDILIPAA CCCEEECCCEEEECC | 4.52 | 24333276 | |
376 | S-nitrosylation | GSILEADCDILIPAA CCCEEECCCEEEECC | 4.52 | 22588120 | |
384 | Phosphorylation | DILIPAASEKQLTKS CEEEECCCHHHCCCC | 47.64 | 23140645 | |
386 | Acetylation | LIPAASEKQLTKSNA EEECCCHHHCCCCCC | 48.38 | 23864654 | |
389 | Phosphorylation | AASEKQLTKSNAPRV CCCHHHCCCCCCCHH | 29.90 | 29550500 | |
390 | Acetylation | ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE | 50.75 | 23576753 | |
390 | Glutarylation | ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE | 50.75 | 24703693 | |
390 | Malonylation | ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE | 50.75 | 26320211 | |
390 | Succinylation | ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE | 50.75 | - | |
390 | Succinylation | ASEKQLTKSNAPRVK CCHHHCCCCCCCHHE | 50.75 | 23806337 | |
391 | Phosphorylation | SEKQLTKSNAPRVKA CHHHCCCCCCCHHEE | 32.75 | 29550500 | |
397 | Acetylation | KSNAPRVKAKIIAEG CCCCCHHEEEEEECC | 45.29 | 23201123 | |
399 | Acetylation | NAPRVKAKIIAEGAN CCCHHEEEEEECCCC | 29.00 | 23576753 | |
399 | Glutarylation | NAPRVKAKIIAEGAN CCCHHEEEEEECCCC | 29.00 | 24703693 | |
399 | Malonylation | NAPRVKAKIIAEGAN CCCHHEEEEEECCCC | 29.00 | 26320211 | |
399 | Ubiquitination | NAPRVKAKIIAEGAN CCCHHEEEEEECCCC | 29.00 | - | |
409 | Phosphorylation | AEGANGPTTPEADKI ECCCCCCCCHHHHHH | 57.28 | 21082442 | |
410 | Phosphorylation | EGANGPTTPEADKIF CCCCCCCCHHHHHHH | 23.43 | 25521595 | |
415 | Acetylation | PTTPEADKIFLERNI CCCHHHHHHHHHCCE | 42.26 | 23576753 | |
415 | Succinylation | PTTPEADKIFLERNI CCCHHHHHHHHHCCE | 42.26 | - | |
415 | Succinylation | PTTPEADKIFLERNI CCCHHHHHHHHHCCE | 42.26 | 23806337 | |
415 | Ubiquitination | PTTPEADKIFLERNI CCCHHHHHHHHHCCE | 42.26 | - | |
444 | Acetylation | VSYFEWLKNLNHVSY EEHHHHHHCCCCCEE | 61.53 | 23576753 | |
450 | Phosphorylation | LKNLNHVSYGRLTFK HHCCCCCEEEEEEEE | 17.83 | 26824392 | |
451 | Phosphorylation | KNLNHVSYGRLTFKY HCCCCCEEEEEEEEE | 12.74 | 26032504 | |
457 | N6-malonyllysine | SYGRLTFKYERDSNY EEEEEEEEEECCCCC | 40.75 | - | |
457 | Acetylation | SYGRLTFKYERDSNY EEEEEEEEEECCCCC | 40.75 | 23576753 | |
457 | Malonylation | SYGRLTFKYERDSNY EEEEEEEEEECCCCC | 40.75 | 26320211 | |
457 | Succinylation | SYGRLTFKYERDSNY EEEEEEEEEECCCCC | 40.75 | - | |
457 | Ubiquitination | SYGRLTFKYERDSNY EEEEEEEEEECCCCC | 40.75 | - | |
473 | Phosphorylation | LLMSVQESLERKFGK EEEEHHHHHHHHHHC | 20.59 | 22942356 | |
477 | Acetylation | VQESLERKFGKHGGT HHHHHHHHHHCCCCC | 49.44 | 23576753 | |
477 | Succinylation | VQESLERKFGKHGGT HHHHHHHHHHCCCCC | 49.44 | - | |
477 | Succinylation | VQESLERKFGKHGGT HHHHHHHHHHCCCCC | 49.44 | 23806337 | |
477 | Ubiquitination | VQESLERKFGKHGGT HHHHHHHHHHCCCCC | 49.44 | - | |
480 | Acetylation | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | 23576753 | |
480 | Glutarylation | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | 24703693 | |
480 | Malonylation | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | 26320211 | |
480 | Succinylation | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | - | |
480 | Succinylation | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | 23806337 | |
480 | Ubiquitination | SLERKFGKHGGTIPV HHHHHHHCCCCCCCC | 42.06 | - | |
484 | Phosphorylation | KFGKHGGTIPVVPTA HHHCCCCCCCCCCCH | 27.05 | - | |
490 | Phosphorylation | GTIPVVPTAEFQDRI CCCCCCCCHHHHHHC | 27.49 | 23140645 | |
498 | Phosphorylation | AEFQDRISGASEKDI HHHHHHCCCCCHHHH | 29.24 | 23140645 | |
501 | Phosphorylation | QDRISGASEKDIVHS HHHCCCCCHHHHCHH | 49.02 | 19060867 | |
503 | N6-malonyllysine | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | - | |
503 | Acetylation | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | 23806337 | |
503 | Glutarylation | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | 24703693 | |
503 | Malonylation | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | 26073543 | |
503 | Phosphoglycerylation | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | - | |
503 | Succinylation | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | 23806337 | |
503 | Ubiquitination | RISGASEKDIVHSGL HCCCCCHHHHCHHHH | 50.70 | - | |
508 | Phosphorylation | SEKDIVHSGLAYTME CHHHHCHHHHHHHHH | 25.30 | 25521595 | |
512 | Phosphorylation | IVHSGLAYTMERSAR HCHHHHHHHHHHHHH | 16.21 | 16873679 | |
513 | Phosphorylation | VHSGLAYTMERSARQ CHHHHHHHHHHHHHH | 13.62 | 22817900 | |
527 | N6-malonyllysine | QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH | 28.64 | - | |
527 | Acetylation | QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH | 28.64 | 23806337 | |
527 | Glutarylation | QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH | 28.64 | 24703693 | |
527 | Malonylation | QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH | 28.64 | 26320211 | |
527 | Succinylation | QIMRTAMKYNLGLDL HHHHHHHHHCCCCCH | 28.64 | 23806337 | |
528 | Phosphorylation | IMRTAMKYNLGLDLR HHHHHHHHCCCCCHH | 11.52 | 29514104 | |
545 | Acetylation | AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH | 47.02 | 23806337 | |
545 | Glutarylation | AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH | 47.02 | 24703693 | |
545 | Succinylation | AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH | 47.02 | - | |
545 | Succinylation | AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH | 47.02 | 23806337 | |
545 | Ubiquitination | AYVNAIEKVFKVYNE HHHHHHHHHHHHHHH | 47.02 | - | |
548 | Acetylation | NAIEKVFKVYNEAGV HHHHHHHHHHHHCCC | 46.96 | 23576753 | |
548 | Succinylation | NAIEKVFKVYNEAGV HHHHHHHHHHHHCCC | 46.96 | 24315375 |
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 DHE3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
84 | K | Acetylation |
| 23806337 |
* 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 DHE3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of DHE3_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASSSPECTROMETRY. | |
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135 AND TYR-512, ANDMASS SPECTROMETRY. |