ACACA_MOUSE - dbPTM
ACACA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACACA_MOUSE
UniProt AC Q5SWU9
Protein Name Acetyl-CoA carboxylase 1
Gene Name Acaca {ECO:0000312|MGI:MGI:108451}
Organism Mus musculus (Mouse).
Sequence Length 2345
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase..
Protein Sequence MDEPSPLAKTLELNQHSRFIIGSVSEDNSEDEISNLVKLDLEEKEGSLSPASVSSDTLSDLGISGLQDGLAFHMRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLFRIKDIRMMYGVSPWGDAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSISNFLHSLERGQVLPAHTLLNTVDVELIYEGIKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVIAKMQLDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSRVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPLNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASNLNHYGMTHVASVSDVLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEIMGCFCDSPPQSPTFPESGHTSLYDEDKVPRDEPIHILNVAIKTDGDIEDDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDFRKQVNCEVDQRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDILTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMSLKSPEYPDGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGARIGLAEEIRHMFHVAWVDPEDPYKGYKYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEVITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEFVPTKAPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECSQPVMVYIPPQAELRGGSWVVIDPTINPRHMEMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRRVDPVYIRLAERLGTPELSPTERKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRTFFYWRLRRLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLVEWLEKQLTEEDGVRSVIEENIKYISRDYVLKQIRSLVQANPEVAMDSIVHMTQHISPTQRAEVVRILSTMDSPST
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MDEPSPLA
-------CCCCCHHH
51.90-
5Phosphorylation---MDEPSPLAKTLE
---CCCCCHHHHHEE
30.428545395
9UbiquitinationDEPSPLAKTLELNQH
CCCCHHHHHEECCCC
62.4222790023
9 (in isoform 2)Ubiquitination-62.4222790023
10PhosphorylationEPSPLAKTLELNQHS
CCCHHHHHEECCCCC
21.6222817900
17PhosphorylationTLELNQHSRFIIGSV
HEECCCCCCEEEEEC
21.0822817900
21 (in isoform 2)Phosphorylation-2.8625159016
23PhosphorylationHSRFIIGSVSEDNSE
CCCEEEEECCCCCCH
16.4424925903
24 (in isoform 2)Phosphorylation-6.4825159016
25PhosphorylationRFIIGSVSEDNSEDE
CEEEEECCCCCCHHH
40.7125521595
29PhosphorylationGSVSEDNSEDEISNL
EECCCCCCHHHHHHH
59.7624925903
34PhosphorylationDNSEDEISNLVKLDL
CCCHHHHHHHEECCH
23.2824925903
47PhosphorylationDLEEKEGSLSPASVS
CHHHCCCCCCCCCCC
27.1127818261
47 (in isoform 2)Ubiquitination-27.11-
49PhosphorylationEEKEGSLSPASVSSD
HHCCCCCCCCCCCCC
21.8121082442
52PhosphorylationEGSLSPASVSSDTLS
CCCCCCCCCCCCCHH
26.3926239621
54PhosphorylationSLSPASVSSDTLSDL
CCCCCCCCCCCHHHH
21.7221082442
55PhosphorylationLSPASVSSDTLSDLG
CCCCCCCCCCHHHHC
32.2426239621
57PhosphorylationPASVSSDTLSDLGIS
CCCCCCCCHHHHCCC
30.0626239621
59PhosphorylationSVSSDTLSDLGISGL
CCCCCCHHHHCCCCC
32.6427180971
64PhosphorylationTLSDLGISGLQDGLA
CHHHHCCCCCCCCCC
31.4923984901
76PhosphorylationGLAFHMRSSMSGLHL
CCCHHHHHHHCCCCH
23.8727742792
77PhosphorylationLAFHMRSSMSGLHLV
CCHHHHHHHCCCCHH
13.4525521595
79PhosphorylationFHMRSSMSGLHLVKQ
HHHHHHHCCCCHHHC
39.9026824392
95PhosphorylationRDRKKIDSQRDFTVA
CCCCCCCCCCCCEEC
30.5027180971
100PhosphorylationIDSQRDFTVASPAEF
CCCCCCCEECCHHHH
21.3228066266
103PhosphorylationQRDFTVASPAEFVTR
CCCCEECCHHHHHHH
21.9527180971
109PhosphorylationASPAEFVTRFGGNKV
CCHHHHHHHCCCCCE
26.1228066266
119UbiquitinationGGNKVIEKVLIANNG
CCCCEEEEEEEECCC
31.0822790023
119 (in isoform 2)Ubiquitination-31.0822790023
157PhosphorylationIRFVVMVTPEDLKAN
EEEEEECCHHHHHHC
11.6730351877
157 (in isoform 2)Ubiquitination-11.67-
275UbiquitinationWQENDFSKRILNVPQ
CCCCCHHHHHCCCCH
43.3722790023
275 (in isoform 2)Ubiquitination-43.3722790023
287UbiquitinationVPQDLYEKGYVKDVD
CCHHHHHCCCCCCHH
41.8222790023
287 (in isoform 2)Ubiquitination-41.8222790023
312PhosphorylationYPVMIKASEGGGGKG
CCEEEEECCCCCCCC
31.60-
313 (in isoform 2)Ubiquitination-67.71-
322MalonylationGGGKGIRKVNNADDF
CCCCCCEECCCCCCC
47.6026320211
325 (in isoform 2)Ubiquitination-47.97-
360 (in isoform 2)Malonylation-18.6626320211
519AcetylationENPDEGFKPSSGTVQ
CCCCCCCCCCCCCEE
55.6423954790
519UbiquitinationENPDEGFKPSSGTVQ
CCCCCCCCCCCCCEE
55.6422790023
519 (in isoform 2)Ubiquitination-55.6422790023
557 (in isoform 2)Ubiquitination-14.71-
581PhosphorylationVVALKELSIRGDFRT
HHHHHHHCCCCCHHH
16.0118779572
609PhosphorylationFQLNRIDTGWLDRLI
CCCCCCCCCHHHHHH
28.0822817900
648PhosphorylationVSLRNSISNFLHSLE
HHHHHHHHHHHHHHH
22.73-
655UbiquitinationSNFLHSLERGQVLPA
HHHHHHHHCCCCCCH
58.7527667366
733PhosphorylationMKEEVDRYRITIGNK
EHHHCCEEEEEECCE
11.2522802335
736PhosphorylationEVDRYRITIGNKTCV
HCCEEEEEECCEEEE
17.5222802335
746AcetylationNKTCVFEKENDPSVM
CEEEEEEECCCCCHH
50.8022826441
785N6-biotinyllysineYAEIEVMKMVMTLTA
EEHHHHHCHHHHHHH
33.25-
785BiotinylationYAEIEVMKMVMTLTA
EEHHHHHCHHHHHHH
33.25-
789PhosphorylationEVMKMVMTLTAVESG
HHHCHHHHHHHHHHC
15.0025521595
812S-nitrosylationGAALDPGCVIAKMQL
CCCCCCCCEEEEEEC
2.1422178444
824UbiquitinationMQLDNPSKVQQAELH
EECCCHHHHEEEEHH
45.3722790023
824 (in isoform 2)Ubiquitination-45.3722790023
834PhosphorylationQAELHTGSLPQIQST
EEEHHCCCCCHHHHH
37.72-
862UbiquitinationVLDNLVNVMNGYCLP
HHHHHHHHHCCCCCC
2.1627667366
862 (in isoform 2)Ubiquitination-2.16-
915MalonylationRIPLNVEKSIKKEMA
CCCCCHHHHHHHHHH
53.8826320211
915UbiquitinationRIPLNVEKSIKKEMA
CCCCCHHHHHHHHHH
53.88-
915 (in isoform 2)Ubiquitination-53.8822790023
953 (in isoform 2)Malonylation-47.1726320211
953 (in isoform 2)Ubiquitination-47.17-
966O-linked_GlycosylationVFFMNTQSIVQLVQR
EEEECHHHHHHHHHH
23.7631010828
1101PhosphorylationLRHNQVESIFLSAID
CCCCHHHHHHHHHHH
21.5622802335
1105PhosphorylationQVESIFLSAIDMYGH
HHHHHHHHHHHHHCH
16.6622802335
1110PhosphorylationFLSAIDMYGHQFCIE
HHHHHHHHCHHHHHH
14.0122802335
1195PhosphorylationPNRGNIPTLNRMSFA
CCCCCCCCCCCCCCH
32.6322817900
1200PhosphorylationIPTLNRMSFASNLNH
CCCCCCCCCHHCCCC
17.9029472430
1203PhosphorylationLNRMSFASNLNHYGM
CCCCCCHHCCCCCCC
39.5819060867
1208PhosphorylationFASNLNHYGMTHVAS
CHHCCCCCCCCCEEE
13.9119060867
1211PhosphorylationNLNHYGMTHVASVSD
CCCCCCCCCEEEHHH
14.6119060867
1215PhosphorylationYGMTHVASVSDVLLD
CCCCCEEEHHHHHHH
22.5122817900
1217PhosphorylationMTHVASVSDVLLDNA
CCCEEEHHHHHHHCC
21.3622817900
1226PhosphorylationVLLDNAFTPPCQRMG
HHHHCCCCCCCCCCC
24.7422817900
1258PhosphorylationIMGCFCDSPPQSPTF
HHCCCCCCCCCCCCC
39.3926824392
1262PhosphorylationFCDSPPQSPTFPESG
CCCCCCCCCCCCCCC
31.5121082442
1264PhosphorylationDSPPQSPTFPESGHT
CCCCCCCCCCCCCCC
58.0021082442
1268PhosphorylationQSPTFPESGHTSLYD
CCCCCCCCCCCCCCC
35.7925619855
1271PhosphorylationTFPESGHTSLYDEDK
CCCCCCCCCCCCCCC
24.7725619855
1272PhosphorylationFPESGHTSLYDEDKV
CCCCCCCCCCCCCCC
21.1825619855
1274PhosphorylationESGHTSLYDEDKVPR
CCCCCCCCCCCCCCC
19.6325619855
1315UbiquitinationREFTQQNKATLVEHG
HHHHHHHHHHHHHHH
38.1122790023
1315 (in isoform 2)Ubiquitination-38.1122790023
1333AcetylationLTFLVAQKDFRKQVN
HHHHHCCHHHHHHCC
49.44-
1337MalonylationVAQKDFRKQVNCEVD
HCCHHHHHHCCCCHH
59.6026320211
1337UbiquitinationVAQKDFRKQVNCEVD
HCCHHHHHHCCCCHH
59.60-
1337 (in isoform 2)Ubiquitination-59.6022790023
1353 (in isoform 2)Ubiquitination-59.43-
1369PhosphorylationKFEEDRIYRHLEPAL
CCCHHHHHHHHHHHH
7.9017242355
1375 (in isoform 2)Malonylation-11.3526320211
1375 (in isoform 2)Ubiquitination-11.35-
1416UbiquitinationVEVGTEVTDYRFFVR
EECCCCCCCHHHHHH
22.5327667366
1497UbiquitinationSVRSMVMRYGSRLWK
HHHHHHHHHHHHHHH
22.6527667366
1552PhosphorylationKEVTDSRTAQIMFQA
EECCCCCCEEEEEHH
27.1929109428
1576PhosphorylationGMLINTPYVTKDLLQ
EEEECCCCCCHHHHH
20.7929109428
1577UbiquitinationMLINTPYVTKDLLQS
EEECCCCCCHHHHHC
5.8927667366
1579AcetylationINTPYVTKDLLQSKR
ECCCCCCHHHHHCCC
36.0123236377
1579UbiquitinationINTPYVTKDLLQSKR
ECCCCCCHHHHHCCC
36.0127667366
1584PhosphorylationVTKDLLQSKRFQAQS
CCHHHHHCCCCCCHH
26.2629109428
1585UbiquitinationTKDLLQSKRFQAQSL
CHHHHHCCCCCCHHC
44.2527667366
1611UbiquitinationFRQSLIKLWESMSTQ
HHHHHHHHHHHHCCC
4.9327667366
1623UbiquitinationSTQAFLPSPPLPSDI
CCCCCCCCCCCCHHH
41.1027667366
1658UbiquitinationPGGNEIGMVAWKMSL
CCCCCHHCEEEEHHC
1.9827667366
1662UbiquitinationEIGMVAWKMSLKSPE
CHHCEEEEHHCCCCC
14.6322790023
1662 (in isoform 2)Ubiquitination-14.6322790023
1666UbiquitinationVAWKMSLKSPEYPDG
EEEEHHCCCCCCCCC
57.5722790023
1666 (in isoform 2)Ubiquitination-57.5722790023
1700 (in isoform 2)Ubiquitination-28.82-
1704UbiquitinationLFLRASELARAEGIP
HHHCHHHHHHHCCCC
3.4627667366
1704 (in isoform 2)Ubiquitination-3.46-
1740UbiquitinationFHVAWVDPEDPYKGY
HEEEECCCCCCCCCC
37.9727667366
1748UbiquitinationEDPYKGYKYLYLTPQ
CCCCCCCEEEEECHH
37.1322790023
1748 (in isoform 2)Ubiquitination-37.1322790023
1753PhosphorylationGYKYLYLTPQDYKRV
CCEEEEECHHHHHHH
12.8328576409
1758AcetylationYLTPQDYKRVSALNS
EECHHHHHHHHHCCC
55.3923954790
1758SuccinylationYLTPQDYKRVSALNS
EECHHHHHHHHHCCC
55.3923954790
1758UbiquitinationYLTPQDYKRVSALNS
EECHHHHHHHHHCCC
55.39-
1758 (in isoform 2)Ubiquitination-55.3922790023
1759UbiquitinationLTPQDYKRVSALNSV
ECHHHHHHHHHCCCE
22.7627667366
1772UbiquitinationSVHCEHVEDEGESRY
CEECEECCCCCCCCE
52.8627667366
1780UbiquitinationDEGESRYKITDIIGK
CCCCCCEEEEECCCC
37.7122790023
1780 (in isoform 2)Ubiquitination-37.7122790023
1786UbiquitinationYKITDIIGKEEGLGA
EEEEECCCCCCCCCC
31.4927667366
1786 (in isoform 2)Ubiquitination-31.49-
1787UbiquitinationKITDIIGKEEGLGAE
EEEECCCCCCCCCCC
42.0322790023
1787 (in isoform 2)Ubiquitination-42.0322790023
1796 (in isoform 2)Ubiquitination-5.02-
1818UbiquitinationDEVITISLVTCRAIG
CCEEEEEEEEHHHHC
3.0627667366
1818 (in isoform 2)Ubiquitination-3.06-
1825 (in isoform 2)Ubiquitination-15.99-
1920UbiquitinationNSKDPIDRIIEFVPT
CCCCCHHHHHHCCCC
32.2927667366
1928UbiquitinationIIEFVPTKAPYDPRW
HHHCCCCCCCCCCCC
41.0922790023
1928 (in isoform 2)Ubiquitination-41.0922790023
1966UbiquitinationFSEIMQPWAQTVVVG
HHHHCHHHHCEEEEE
5.5427667366
1966 (in isoform 2)Ubiquitination-5.54-
1995PhosphorylationETRTVELSIPADPAN
EECEEEEECCCCCCC
17.0221183079
2005PhosphorylationADPANLDSEAKIIQQ
CCCCCCCHHHHHHHH
42.4921183079
2030UbiquitinationFKTYQAIKDFNREGL
HHHHHHHHHCCCCCC
60.3222790023
2030 (in isoform 2)Ubiquitination-60.3222790023
2053UbiquitinationRGFSGGMKDMYDQVL
CCCCCCHHHHHHHHH
42.4922790023
2053 (in isoform 2)Ubiquitination-42.4922790023
2068 (in isoform 2)Ubiquitination-40.63-
2091O-linked_GlycosylationQAELRGGSWVVIDPT
CCHHCCCCEEEECCC
21.3731010828
2091 (in isoform 2)Ubiquitination-21.37-
2126AcetylationPEGTVEIKFRKKDLV
CCCEEEEEEEHHHHH
26.1323954790
2126MalonylationPEGTVEIKFRKKDLV
CCCEEEEEEEHHHHH
26.1326320211
2126UbiquitinationPEGTVEIKFRKKDLV
CCCEEEEEEEHHHHH
26.13-
2126 (in isoform 2)Ubiquitination-26.1322790023
2152PhosphorylationRLAERLGTPELSPTE
HHHHHHCCCCCCHHH
20.4122817900
2156PhosphorylationRLGTPELSPTERKEL
HHCCCCCCHHHHHHH
28.2830352176
2158PhosphorylationGTPELSPTERKELES
CCCCCCHHHHHHHHH
45.0826745281
2164 (in isoform 2)Malonylation-47.0926320211
2164 (in isoform 2)Ubiquitination-47.09-
2230UbiquitinationLEDLVKKKIHNANPE
HHHHHHHHHHCCCCC
43.4022790023
2230 (in isoform 2)Ubiquitination-43.4022790023
2268 (in isoform 2)Ubiquitination-59.06-
2285O-linked_GlycosylationTEEDGVRSVIEENIK
CCCCCHHHHHHHHHH
25.6631010828
2322PhosphorylationMDSIVHMTQHISPTQ
HHHHHHHHCCCCHHH
11.3421183079
2326PhosphorylationVHMTQHISPTQRAEV
HHHHCCCCHHHHHHH
21.5519060867
2328PhosphorylationMTQHISPTQRAEVVR
HHCCCCHHHHHHHHH
24.7326060331
2338PhosphorylationAEVVRILSTMDSPST
HHHHHHHHCCCCCCC
21.2222817900
2339PhosphorylationEVVRILSTMDSPST-
HHHHHHHCCCCCCC-
22.8828066266
2342PhosphorylationRILSTMDSPST----
HHHHCCCCCCC----
15.2125521595
2344PhosphorylationLSTMDSPST------
HHCCCCCCC------
51.1821743459
2345PhosphorylationSTMDSPST-------
HCCCCCCC-------
46.1128066266

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
79SPhosphorylationKinaseAMPKA1Q13131
PSP
79SPhosphorylationKinasePRKAA2Q8BRK8
GPS
79SPhosphorylationKinasePRKAG3-GPS
79SPhosphorylationKinaseAMPK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
79SPhosphorylation

17208939
1262SPhosphorylation

21183079

Disease-associated PTM Sites based on SAP

* 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 ACACA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACACA_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACACA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-29 AND SER-79, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, 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-23; SER-25 AND SER-29,AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

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