BIG2_HUMAN - dbPTM
BIG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BIG2_HUMAN
UniProt AC Q9Y6D5
Protein Name Brefeldin A-inhibited guanine nucleotide-exchange protein 2
Gene Name ARFGEF2
Organism Homo sapiens (Human).
Sequence Length 1785
Subcellular Localization Cytoplasm. Membrane. Golgi apparatus. Cytoplasm, perinuclear region. Golgi apparatus, trans-Golgi network. Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, dendrite. Cytoplasmic vesicle. Cell junction, synapse
Protein Description Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways..
Protein Sequence MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAEIEKQRLGTAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICSCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPIQSKPQSPVIQAAAVSPKFVRLKHSQAQSKPTTPEKTDLTNGEHARSDSGKVSTENGDAPRERGSSLSGTDDGAQEVVKDILEDVVTSAIKEAAEKHGLTEPERVLGELECQECAIPPGVDENSQTNGIADDRQSLSSADNLESDAQGHQVAARFSHVLQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRTHEMFINAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQTSLGQERLTDQEIGDGKGLDMARRCSVTSMESTVSSGTQTTVQDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGTSVEDIAQFLHQEERLDSTQVGDFLGDSARFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYEEIEGKKIAMKETKELTIATKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAIRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHTLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMAIRCIAQMVNSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTCHIVTTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFEKHWWQDLFRIVFRIFDNMKLPEQLSEKSEWMTTTCNHALYAICDVFTQFYEALNEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPEVWDETCNCMLDIFKTTIPHVLLTWRPVGMEEDSSEKHLDVDLDRQSLSSIDKNPSERGQSQLSNPTDDSWKGRPYANQKLFASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDADIHIETEDQGMYKYMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWEEIQQRLLTVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKINDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFLRIGVVYKIWIPEEPSQVPAALSPVW
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-------MQESQTKS
-------CCHHHHHH		43.2522814378
4O-linked_Glycosylation----MQESQTKSMFV
----CCHHHHHHHHH		42.7430379171
6Phosphorylation--MQESQTKSMFVSR
--CCHHHHHHHHHHH		34.0722798277
8PhosphorylationMQESQTKSMFVSRAL
CCHHHHHHHHHHHHH		22.3522798277
12PhosphorylationQTKSMFVSRALEKIL
HHHHHHHHHHHHHHH		10.6922798277
17AcetylationFVSRALEKILADKEV
HHHHHHHHHHCCCCC		43.8220167786
22AcetylationLEKILADKEVKRPQH
HHHHHCCCCCCCCCH		59.8220167786
22UbiquitinationLEKILADKEVKRPQH
HHHHHCCCCCCCCCH		59.82-
25AcetylationILADKEVKRPQHSQL
HHCCCCCCCCCHHHH		60.4920167786
59UbiquitinationLGTAAPPKANFIEAD
CCCCCCCCCCCCCCC		55.70-
68PhosphorylationNFIEADKYFLPFELA
CCCCCCCCCHHHHHH		15.7622798277
78PhosphorylationPFELACQSKSPRVVS
HHHHHHCCCCCCCEE		34.6822798277
80PhosphorylationELACQSKSPRVVSTS
HHHHCCCCCCCEECH		24.1622798277
101PhosphorylationLIAYGHITGNAPDSG
HHHCCCCCCCCCCCC		20.7820071362
107PhosphorylationITGNAPDSGAPGKRL
CCCCCCCCCCCCHHH		35.4820071362
195PhosphorylationQMLNVIFTRMENQVL
HHHHHHHHHHHHHHH		20.2720068231
214PhosphorylationELEKPIQSKPQSPVI
HCCCCCCCCCCCCCC		47.2029255136
218PhosphorylationPIQSKPQSPVIQAAA
CCCCCCCCCCCHHHC		29.6629255136
227PhosphorylationVIQAAAVSPKFVRLK
CCHHHCCCHHHEECC		20.0419664994
236PhosphorylationKFVRLKHSQAQSKPT
HHEECCHHHCCCCCC		26.1423927012
240PhosphorylationLKHSQAQSKPTTPEK
CCHHHCCCCCCCCCC		43.5523927012
243PhosphorylationSQAQSKPTTPEKTDL
HHCCCCCCCCCCCCC		59.7323927012
244PhosphorylationQAQSKPTTPEKTDLT
HCCCCCCCCCCCCCC		37.6725159151
248PhosphorylationKPTTPEKTDLTNGEH
CCCCCCCCCCCCCCC		34.2828450419
251PhosphorylationTPEKTDLTNGEHARS
CCCCCCCCCCCCCCC		43.9423927012
258PhosphorylationTNGEHARSDSGKVST
CCCCCCCCCCCCCCC		36.5923312004
260PhosphorylationGEHARSDSGKVSTEN
CCCCCCCCCCCCCCC		41.5823312004
264PhosphorylationRSDSGKVSTENGDAP
CCCCCCCCCCCCCCC		33.2329514088
265PhosphorylationSDSGKVSTENGDAPR
CCCCCCCCCCCCCCC		36.1429514088
276PhosphorylationDAPRERGSSLSGTDD
CCCCCCCCCCCCCCH		34.0429255136
277PhosphorylationAPRERGSSLSGTDDG
CCCCCCCCCCCCCHH		29.4019664994
279PhosphorylationRERGSSLSGTDDGAQ
CCCCCCCCCCCHHHH		41.4129255136
281PhosphorylationRGSSLSGTDDGAQEV
CCCCCCCCCHHHHHH		27.7830266825
298PhosphorylationDILEDVVTSAIKEAA
HHHHHHHHHHHHHHH		16.5830301811
299PhosphorylationILEDVVTSAIKEAAE
HHHHHHHHHHHHHHH		19.1820071362
302UbiquitinationDVVTSAIKEAAEKHG
HHHHHHHHHHHHHCC		40.80-
335PhosphorylationPPGVDENSQTNGIAD
CCCCCCCCCCCCCCC		36.0125999147
337PhosphorylationGVDENSQTNGIADDR
CCCCCCCCCCCCCCH		34.9225999147
346PhosphorylationGIADDRQSLSSADNL
CCCCCHHHHHCHHCH		30.9830266825
348PhosphorylationADDRQSLSSADNLES
CCCHHHHHCHHCHHH		28.8230266825
349PhosphorylationDDRQSLSSADNLESD
CCHHHHHCHHCHHHH		44.9623401153
355PhosphorylationSSADNLESDAQGHQV
HCHHCHHHHHHHHHH		41.2223663014
383AcetylationLVFRSLCKLSMKPLG
HHHHHHHHHCCCCCC		49.227823411
385PhosphorylationFRSLCKLSMKPLGEG
HHHHHHHCCCCCCCC		15.3925002506
398PhosphorylationEGPPDPKSHELRSKV
CCCCCCCCHHHHHHH		27.8125002506
424PhosphorylationNAGPVFRTHEMFINA
HCCCCCCCHHHHHHH		15.66-
504PhosphorylationWMVIQTLTRICADAQ
HHHHHHHHHHHCCCC		22.7520860994
545PhosphorylationSKIAQGRSGHELGMT
HHHHCCCCCCCCCCC		51.8628348404
552PhosphorylationSGHELGMTPLQELSL
CCCCCCCCHHHHHHH		21.0328348404
558PhosphorylationMTPLQELSLRKKGLE
CCHHHHHHHHHHHHH		25.9424719451
569PhosphorylationKGLECLVSILKCMVE
HHHHHHHHHHHHHHH		14.8424719451
589PhosphorylationYVNPNHQTSLGQERL
CCCCCCCCCCCCCCC		20.5430576142
590PhosphorylationVNPNHQTSLGQERLT
CCCCCCCCCCCCCCC		24.7523312004
614PhosphorylationLDMARRCSVTSMEST
HHHHHHCEEEEEEEE		26.9823401153
616PhosphorylationMARRCSVTSMESTVS
HHHHCEEEEEEEECC		13.1830278072
617PhosphorylationARRCSVTSMESTVSS
HHHCEEEEEEEECCC		20.5630278072
620PhosphorylationCSVTSMESTVSSGTQ
CEEEEEEEECCCCCC		26.0130278072
621PhosphorylationSVTSMESTVSSGTQT
EEEEEEEECCCCCCE		15.8830278072
623PhosphorylationTSMESTVSSGTQTTV
EEEEEECCCCCCEEE		24.1230278072
624PhosphorylationSMESTVSSGTQTTVQ
EEEEECCCCCCEEEC		41.3330278072
626PhosphorylationESTVSSGTQTTVQDD
EEECCCCCCEEECCC		25.3730278072
628PhosphorylationTVSSGTQTTVQDDPE
ECCCCCCEEECCCHH		28.8630278072
629PhosphorylationVSSGTQTTVQDDPEQ
CCCCCCEEECCCHHH		13.3223927012
690PhosphorylationHQEERLDSTQVGDFL
HHHHCCCCCCHHHHH		25.9020068231
691PhosphorylationQEERLDSTQVGDFLG
HHHCCCCCCHHHHHC		27.2620068231
700PhosphorylationVGDFLGDSARFNKEV
HHHHHCCHHHCCHHH		21.3930243723
741UbiquitinationRLPGEAQKIDRLMEK
CCCCHHHHHHHHHHH		54.33-
794AcetylationQVKNKMTKEQYIKMN
HHHCCCCHHHHHHHH		39.047363975
797PhosphorylationNKMTKEQYIKMNRGI
CCCCHHHHHHHHCCC		12.00-
808UbiquitinationNRGINDSKDLPEEYL
HCCCCCCCCCCHHHH		67.17-
819PhosphorylationEEYLSSIYEEIEGKK
HHHHHHHHHHHCCCE		14.9527642862
840UbiquitinationKELTIATKSTKQNVA
CEEEEEECCCCHHHC		47.29-
866PhosphorylationEMEQMAKTAKALMEA
HHHHHHHHHHHHHHH		24.69-
875PhosphorylationKALMEAVSHAKAPFT
HHHHHHHHHCCCCCC		25.44-
882PhosphorylationSHAKAPFTSATHLDH
HHCCCCCCCCCCHHH		19.1820071362
883PhosphorylationHAKAPFTSATHLDHV
HCCCCCCCCCCHHHH		31.3920071362
885PhosphorylationKAPFTSATHLDHVRP
CCCCCCCCCHHHHHH		23.8020071362
952PhosphorylationVQALARFSLLTASSS
HHHHHHHHHHHCCCC		19.5421902226
957PhosphorylationRFSLLTASSSITEMK
HHHHHHCCCCHHHHH		21.2721902226
958PhosphorylationFSLLTASSSITEMKQ
HHHHHCCCCHHHHHH		24.2421902226
1007PhosphorylationELAQLIGTGVKTRYL
HHHHHHCCCCCCEEC		31.63-
1010UbiquitinationQLIGTGVKTRYLSGS
HHHCCCCCCEECCCC		28.73-
1015PhosphorylationGVKTRYLSGSGRERE
CCCCEECCCCCCCCC		23.2130576142
1017PhosphorylationKTRYLSGSGREREGS
CCEECCCCCCCCCCC		31.1626434776
1024PhosphorylationSGREREGSLKGHTLA
CCCCCCCCCCCCCCC		23.3529978859
1029PhosphorylationEGSLKGHTLAGEEFM
CCCCCCCCCCCCCCC		27.2925849741
1045PhosphorylationLGLGNLVSGGVDKRQ
CCCHHHHCCCCCHHH		32.7528122231
1063PhosphorylationFQESVGETSSQSVVV
HHHHCCCCCCCCEEE		27.9624275569
1064PhosphorylationQESVGETSSQSVVVA
HHHCCCCCCCCEEEE		23.2922817900
1067PhosphorylationVGETSSQSVVVAVDR
CCCCCCCCEEEEEEE		20.8722817900
1077PhosphorylationVAVDRIFTGSTRLDG
EEEEEEECCCCCCCC		28.0524275569
1079PhosphorylationVDRIFTGSTRLDGNA
EEEEECCCCCCCCCH		13.8024275569
1080PhosphorylationDRIFTGSTRLDGNAI
EEEECCCCCCCCCHH		36.2724275569
1112PhosphorylationPHHPRMFSLQKIVEI
CCCCCCCCHHHHHEE		22.1323532336
1167UbiquitinationSLRQLSMKFLEKGEL
HHHHHHHHHHHCCCC		43.34-
1171UbiquitinationLSMKFLEKGELANFR
HHHHHHHCCCCCCCC		60.8921890473
1181UbiquitinationLANFRFQKDFLRPFE
CCCCCCCHHHHHHHH		47.97-
1196PhosphorylationHIMKKNRSPTIRDMA
HHHHHCCCHHHHHHH		35.4724719451
1349PhosphorylationRCKLDVRTRGLTVMF
HCCCCHHHCCHHHHH		29.0128270605
1353PhosphorylationDVRTRGLTVMFEIMK
CHHHCCHHHHHHHHH		16.8528270605
1361PhosphorylationVMFEIMKSYGHTFEK
HHHHHHHHHCCCCHH		20.9728270605
1362PhosphorylationMFEIMKSYGHTFEKH
HHHHHHHHCCCCHHH		13.8628270605
1365PhosphorylationIMKSYGHTFEKHWWQ
HHHHHCCCCHHHHHH		29.1828270605
1488PhosphorylationTIPHVLLTWRPVGME
CCCEEEEEECCCCCC		18.4428270605
1498PhosphorylationPVGMEEDSSEKHLDV
CCCCCCCCCCCCCCC		43.6125850435
1499PhosphorylationVGMEEDSSEKHLDVD
CCCCCCCCCCCCCCC		64.0925850435
1511PhosphorylationDVDLDRQSLSSIDKN
CCCCCHHHHHHCCCC		30.9829255136
1513PhosphorylationDLDRQSLSSIDKNPS
CCCHHHHHHCCCCHH		30.4125159151
1514PhosphorylationLDRQSLSSIDKNPSE
CCHHHHHHCCCCHHH		39.8523927012
1517UbiquitinationQSLSSIDKNPSERGQ
HHHHHCCCCHHHHCC		69.92-
1520PhosphorylationSSIDKNPSERGQSQL
HHCCCCHHHHCCCCC		49.6830278072
1525PhosphorylationNPSERGQSQLSNPTD
CHHHHCCCCCCCCCC		35.5917525332
1528PhosphorylationERGQSQLSNPTDDSW
HHCCCCCCCCCCCCC		32.8819664994
1531PhosphorylationQSQLSNPTDDSWKGR
CCCCCCCCCCCCCCC		57.6030266825
1534PhosphorylationLSNPTDDSWKGRPYA
CCCCCCCCCCCCCCC		33.2322167270
1536UbiquitinationNPTDDSWKGRPYANQ
CCCCCCCCCCCCCCH		49.33-
1540PhosphorylationDSWKGRPYANQKLFA
CCCCCCCCCCHHHHH		19.4723663014
1621PhosphorylationLLDCLQESHSFSKAF
HHHHHHHHHCHHHHH		16.0920873877
1623PhosphorylationDCLQESHSFSKAFNS
HHHHHHHCHHHHHCC		40.2624719451
1625PhosphorylationLQESHSFSKAFNSNY
HHHHHCHHHHHCCCH		26.5320873877
1630PhosphorylationSFSKAFNSNYEQRTV
CHHHHHCCCHHHCHH		34.0428857561
1632PhosphorylationSKAFNSNYEQRTVLW
HHHHCCCHHHCHHHH		17.1728857561
1636PhosphorylationNSNYEQRTVLWRAGF
CCCHHHCHHHHHCCC		21.4628857561
1727UbiquitinationTLKINDEKFKAHASM
HCCCCHHHHHHHHHH		55.84-
1775PhosphorylationIWIPEEPSQVPAALS
EECCCCHHCCCCCCC		47.2720873877
1782PhosphorylationSQVPAALSPVW----
HCCCCCCCCCC----		16.8125159151
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

Oops, there are no upstream regulatory protein records of BIG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BIG2_HUMAN !!
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 BIG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAP0_HUMANPRKAR1Aphysical
12571360
KAP2_HUMANPRKAR2Aphysical
12571360
BIG1_HUMANARFGEF1physical
10716990
RSP5_YEASTRSP5physical
18832381
ITCH_MOUSEItchphysical
18832381
PLPL2_HUMANPNPLA2physical
21789191
NUP88_HUMANNUP88physical
22863883
PAF1_HUMANPAF1physical
22863883
Drug and Disease Associations
Kegg Disease
H00270 Periventricular nodular heterotopia (PVNH)
OMIM Disease
608097Periventricular nodular heterotopia 2 (PVNH2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BIG2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-218; SER-227; SER-277;SER-1525 AND SER-1528, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-1528, ANDMASS SPECTROMETRY.
"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 SER-218; SER-227; SER-240AND THR-244, AND MASS 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 SER-614 AND THR-616, ANDMASS SPECTROMETRY.
"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 SER-218; SER-227; THR-244;SER-614; THR-621; SER-1511; SER-1513; SER-1514; SER-1525; SER-1528 ANDSER-1782, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1525 AND SER-1528, 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 SER-218; SER-227; SER-1511;SER-1513; SER-1514; SER-1525 AND SER-1528, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-690 AND THR-691, ANDMASS SPECTROMETRY.

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