WDR44_HUMAN - dbPTM
WDR44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR44_HUMAN
UniProt AC Q5JSH3
Protein Name WD repeat-containing protein 44
Gene Name WDR44
Organism Homo sapiens (Human).
Sequence Length 913
Subcellular Localization Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Colocalized with RAB11 along microtubules oriented toward lamellipodia..
Protein Description Downstream effector for RAB11. May be involved in vesicle recycling (By similarity)..
Protein Sequence MASESDTEEFYDAPEDVHLGGGYPVGSPGKVGLSTFKETENTAYKVGNESPVQELKQDVSKKIIESIIEESQKVLQLEDDSLDSKGKELSDQATASPIVARTDLSNIPGLLAIDQVLPEESQKAESQNTFEETELELKKCFPSDETCEKPVDETTKLTQTSSTEQLNVLETETEVLNKEAVEVKGGGDVLEPVSSDSLSTKDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPPPPSRPAPPPRKRKSELEFETLKTPDIDVPKENITSDSLLTASMASESTVKDSQPSLDLASATSGDKIVTAQENGKAPDGQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDAAQSDDEEKLQSQPTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNVVRIWALKNAFDYFNNMRMKYNTEGRVSPSPSQESLSSSKSDTDTGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKSEGNEKSEDAEVLDATPSGIMKTDNTEVLLSADFTGAIKVFVNKRKNVS
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
2Acetylation------MASESDTEE
------CCCCCCHHC
23.2320068231
3Phosphorylation-----MASESDTEEF
-----CCCCCCHHCH
36.0125159151
5Phosphorylation---MASESDTEEFYD
---CCCCCCHHCHHC
47.5425159151
7Phosphorylation-MASESDTEEFYDAP
-CCCCCCHHCHHCCC
46.8525159151
11PhosphorylationESDTEEFYDAPEDVH
CCCHHCHHCCCCCCC
17.9322115753
23PhosphorylationDVHLGGGYPVGSPGK
CCCCCCCCCCCCCCC
9.6822115753
27PhosphorylationGGGYPVGSPGKVGLS
CCCCCCCCCCCCCCC
30.6125159151
34PhosphorylationSPGKVGLSTFKETEN
CCCCCCCCCCCCCCC
26.3526074081
35PhosphorylationPGKVGLSTFKETENT
CCCCCCCCCCCCCCC
43.7126074081
39PhosphorylationGLSTFKETENTAYKV
CCCCCCCCCCCCEEC
34.8223403867
42PhosphorylationTFKETENTAYKVGNE
CCCCCCCCCEECCCC
25.7323403867
44PhosphorylationKETENTAYKVGNESP
CCCCCCCEECCCCCH
12.2723403867
45 (in isoform 3)Ubiquitination-41.0021890473
50PhosphorylationAYKVGNESPVQELKQ
CEECCCCCHHHHHHH
34.0819664994
60PhosphorylationQELKQDVSKKIIESI
HHHHHHHHHHHHHHH
36.2023403867
66PhosphorylationVSKKIIESIIEESQK
HHHHHHHHHHHHHHH
20.6123186163
71PhosphorylationIESIIEESQKVLQLE
HHHHHHHHHHHHCCC
23.6329970186
81PhosphorylationVLQLEDDSLDSKGKE
HHCCCCCCCCCCCHH
46.5323401153
84PhosphorylationLEDDSLDSKGKELSD
CCCCCCCCCCHHHCH
48.9130266825
852-HydroxyisobutyrylationEDDSLDSKGKELSDQ
CCCCCCCCCHHHCHH
73.92-
87AcetylationDSLDSKGKELSDQAT
CCCCCCCHHHCHHHC
60.2523954790
90PhosphorylationDSKGKELSDQATASP
CCCCHHHCHHHCCCC
28.8625159151
94PhosphorylationKELSDQATASPIVAR
HHHCHHHCCCCCEEC
23.2625159151
96PhosphorylationLSDQATASPIVARTD
HCHHHCCCCCEECCC
15.7119664994
102PhosphorylationASPIVARTDLSNIPG
CCCCEECCCHHCCCH
31.3929514088
105PhosphorylationIVARTDLSNIPGLLA
CEECCCHHCCCHHHH
35.2129514088
126PhosphorylationEESQKAESQNTFEET
HHHHHHHHCCCHHHH
33.3223663014
129PhosphorylationQKAESQNTFEETELE
HHHHHCCCHHHHHHH
25.4523663014
143PhosphorylationELKKCFPSDETCEKP
HHHHHCCCCCCCCCC
28.0328060719
146PhosphorylationKCFPSDETCEKPVDE
HHCCCCCCCCCCCCC
30.8430624053
154PhosphorylationCEKPVDETTKLTQTS
CCCCCCCCCEEEECC
25.4330624053
155PhosphorylationEKPVDETTKLTQTSS
CCCCCCCCEEEECCC
23.2430624053
158PhosphorylationVDETTKLTQTSSTEQ
CCCCCEEEECCCHHH
31.2122167270
160PhosphorylationETTKLTQTSSTEQLN
CCCEEEECCCHHHHC
21.2922167270
161PhosphorylationTTKLTQTSSTEQLNV
CCEEEECCCHHHHCE
25.9922167270
162PhosphorylationTKLTQTSSTEQLNVL
CEEEECCCHHHHCEE
39.0722167270
163PhosphorylationKLTQTSSTEQLNVLE
EEEECCCHHHHCEEE
27.7622167270
171PhosphorylationEQLNVLETETEVLNK
HHHCEEEEEEEECCC
44.0123927012
173PhosphorylationLNVLETETEVLNKEA
HCEEEEEEEECCCHH
38.5223403867
194PhosphorylationGDVLEPVSSDSLSTK
CCCCCCCCCCCCCCC
38.8625159151
195PhosphorylationDVLEPVSSDSLSTKD
CCCCCCCCCCCCCCC
31.3025159151
197PhosphorylationLEPVSSDSLSTKDFA
CCCCCCCCCCCCCCH
26.6023401153
199PhosphorylationPVSSDSLSTKDFAAV
CCCCCCCCCCCCHHH
37.0525159151
200PhosphorylationVSSDSLSTKDFAAVE
CCCCCCCCCCCHHHH
39.6730266825
201UbiquitinationSSDSLSTKDFAAVEE
CCCCCCCCCCHHHHH
47.69-
213UbiquitinationVEEVAPAKPPRHLTP
HHHHCCCCCCCCCCC
55.27-
213AcetylationVEEVAPAKPPRHLTP
HHHHCCCCCCCCCCC
55.2725953088
219PhosphorylationAKPPRHLTPEPDIVA
CCCCCCCCCCCCCCC
21.3423401153
227PhosphorylationPEPDIVASTKKPVPA
CCCCCCCCCCCCCCC
29.8423403867
228PhosphorylationEPDIVASTKKPVPAR
CCCCCCCCCCCCCCC
33.0923403867
251PhosphorylationPPRPPPPSRPAPPPR
CCCCCCCCCCCCCCC
57.5822210691
261UbiquitinationAPPPRKRKSELEFET
CCCCCCCCCHHCEEE
51.85-
262PhosphorylationPPPRKRKSELEFETL
CCCCCCCCHHCEEEC
51.9919664994
268PhosphorylationKSELEFETLKTPDID
CCHHCEEECCCCCCC
38.5822617229
271PhosphorylationLEFETLKTPDIDVPK
HCEEECCCCCCCCCH
29.3429255136
282PhosphorylationDVPKENITSDSLLTA
CCCHHHCCCHHHHHH
37.7526503514
283 (in isoform 3)Ubiquitination-22.7721890473
285PhosphorylationKENITSDSLLTASMA
HHHCCCHHHHHHHHC
25.6628555341
288PhosphorylationITSDSLLTASMASES
CCCHHHHHHHHCCCC
23.2126503514
290PhosphorylationSDSLLTASMASESTV
CHHHHHHHHCCCCCC
15.0526503514
300PhosphorylationSESTVKDSQPSLDLA
CCCCCCCCCCCCCCC
37.9720068231
303PhosphorylationTVKDSQPSLDLASAT
CCCCCCCCCCCCCCC
27.2120068231
308PhosphorylationQPSLDLASATSGDKI
CCCCCCCCCCCCCEE
39.1020068231
310PhosphorylationSLDLASATSGDKIVT
CCCCCCCCCCCEEEE
30.6520068231
311PhosphorylationLDLASATSGDKIVTA
CCCCCCCCCCEEEEE
44.7220068231
329PhosphorylationGKAPDGQTVAGEVMG
CCCCCCCCCCCEECC
20.1826074081
342PhosphorylationMGPQRPRSNSGRELT
CCCCCCCCCCCCCCC
37.7226846344
344PhosphorylationPQRPRSNSGRELTDE
CCCCCCCCCCCCCHH
40.2426846344
349PhosphorylationSNSGRELTDEEILAS
CCCCCCCCHHHHHHH
36.2926846344
356PhosphorylationTDEEILASVMIKNLD
CHHHHHHHHHEECCC
14.5823403867
392PhosphorylationTLHIMRRTKEYVSND
HHHHHHHCHHHHCCC
20.1930266825
395PhosphorylationIMRRTKEYVSNDAAQ
HHHHCHHHHCCCHHC
15.6730266825
397PhosphorylationRRTKEYVSNDAAQSD
HHCHHHHCCCHHCCC
28.2623401153
403PhosphorylationVSNDAAQSDDEEKLQ
HCCCHHCCCCHHHHH
42.1619664994
411PhosphorylationDDEEKLQSQPTDTDG
CCHHHHHHCCCCCCC
48.8730266825
414PhosphorylationEKLQSQPTDTDGGRL
HHHHHCCCCCCCCHH
43.8430266825
416PhosphorylationLQSQPTDTDGGRLKQ
HHHCCCCCCCCHHCH
38.7430266825
422UbiquitinationDTDGGRLKQKTTQLK
CCCCCHHCHHHHHHH
48.68-
426PhosphorylationGRLKQKTTQLKKFLG
CHHCHHHHHHHHHHC
38.6518077418
434AcetylationQLKKFLGKSVKRAKH
HHHHHHCHHHHHHHH
54.987213989
434UbiquitinationQLKKFLGKSVKRAKH
HHHHHHCHHHHHHHH
54.98-
435PhosphorylationLKKFLGKSVKRAKHL
HHHHHCHHHHHHHHH
30.9523401153
437AcetylationKFLGKSVKRAKHLAE
HHHCHHHHHHHHHHH
54.457213999
440UbiquitinationGKSVKRAKHLAEEYG
CHHHHHHHHHHHHHH
43.0921906983
440 (in isoform 1)Ubiquitination-43.0921890473
440 (in isoform 2)Ubiquitination-43.0921890473
446PhosphorylationAKHLAEEYGERAINK
HHHHHHHHHHHHHHH
18.7828674419
456PhosphorylationRAINKVKSVRDEVFH
HHHHHHHHHHHHCCC
25.9320068231
464PhosphorylationVRDEVFHTDQDDPSS
HHHHCCCCCCCCCCC
24.7221955146
470PhosphorylationHTDQDDPSSSDDEGM
CCCCCCCCCCCCCCC
49.8521955146
471PhosphorylationTDQDDPSSSDDEGMP
CCCCCCCCCCCCCCC
43.0825159151
472PhosphorylationDQDDPSSSDDEGMPY
CCCCCCCCCCCCCCC
54.1125159151
479PhosphorylationSDDEGMPYTRPVKFK
CCCCCCCCCCCCEEE
13.3925072903
480PhosphorylationDDEGMPYTRPVKFKA
CCCCCCCCCCCEEEE
23.7221601212
486UbiquitinationYTRPVKFKAAHGFKG
CCCCCEEEECCCCCC
38.66-
492UbiquitinationFKAAHGFKGPYDFDQ
EEECCCCCCCCCHHH
64.66-
493UbiquitinationKAAHGFKGPYDFDQI
EECCCCCCCCCHHHE
24.6021890473
495PhosphorylationAHGFKGPYDFDQIKV
CCCCCCCCCHHHEEE
37.60-
507PhosphorylationIKVVQDLSGEHMGAV
EEEEEECCCCCCCEE
50.8826503892
516PhosphorylationEHMGAVWTMKFSHCG
CCCCEEEEEEECHHH
12.1326503892
518UbiquitinationMGAVWTMKFSHCGRL
CCEEEEEEECHHHHH
36.0221890473
518 (in isoform 1)Ubiquitination-36.0221890473
518 (in isoform 2)Ubiquitination-36.0221890473
528PhosphorylationHCGRLLASAGQDNVV
HHHHHHHHCCCCHHH
32.66-
546PhosphorylationALKNAFDYFNNMRMK
EHHHHHHHHHCCCCE
11.1826503514
554PhosphorylationFNNMRMKYNTEGRVS
HHCCCCEECCCCCCC
20.2723927012
556PhosphorylationNMRMKYNTEGRVSPS
CCCCEECCCCCCCCC
36.4123927012
561PhosphorylationYNTEGRVSPSPSQES
ECCCCCCCCCCCHHH
20.4919664994
563PhosphorylationTEGRVSPSPSQESLS
CCCCCCCCCCHHHHH
29.6723927012
565PhosphorylationGRVSPSPSQESLSSS
CCCCCCCCHHHHHCC
51.4129255136
568PhosphorylationSPSPSQESLSSSKSD
CCCCCHHHHHCCCCC
26.3917525332
570PhosphorylationSPSQESLSSSKSDTD
CCCHHHHHCCCCCCC
41.6729255136
571PhosphorylationPSQESLSSSKSDTDT
CCHHHHHCCCCCCCC
47.2629255136
572PhosphorylationSQESLSSSKSDTDTG
CHHHHHCCCCCCCCC
32.5729255136
574PhosphorylationESLSSSKSDTDTGVC
HHHHCCCCCCCCCCC
47.9223927012
576PhosphorylationLSSSKSDTDTGVCSG
HHCCCCCCCCCCCCC
42.4230278072
578PhosphorylationSSKSDTDTGVCSGTD
CCCCCCCCCCCCCCC
33.3423927012
582PhosphorylationDTDTGVCSGTDEDPD
CCCCCCCCCCCCCCC
42.1723401153
584PhosphorylationDTGVCSGTDEDPDDK
CCCCCCCCCCCCCCC
21.6623927012
614PhosphorylationTADLLDLSWSKNYFL
CCEECCCCCCCCEEE
29.0419664995
619PhosphorylationDLSWSKNYFLLSSSM
CCCCCCCEEEECCCC
10.1929759185
662PhosphorylationFHPRDDRYFLSGSLD
CCCCCCCEEEEEECC
18.8323186163
665PhosphorylationRDDRYFLSGSLDGKL
CCCCEEEEEECCCEE
19.2123186163
667PhosphorylationDRYFLSGSLDGKLRL
CCEEEEEECCCEEEE
21.6623186163
667UbiquitinationDRYFLSGSLDGKLRL
CCEEEEEECCCEEEE
21.6621890473
671UbiquitinationLSGSLDGKLRLWNIP
EEEECCCEEEEEECC
30.05-
681UbiquitinationLWNIPDKKVALWNEV
EEECCCCEEEEEEEC
39.87-
696PhosphorylationDGQTKLITAANFCQN
CCCEEEEEEEHHHHC
30.1021406692
744UbiquitinationGRNKVGRKITGIEPL
CCCCCCCEECCCCCC
38.40-
756UbiquitinationEPLPGENKILVTSND
CCCCCCCCEEEECCC
32.8721890473
756 (in isoform 1)Ubiquitination-32.8721890473
756 (in isoform 2)Ubiquitination-32.8721890473
777PhosphorylationDLRDLSLSMKYKGYV
EHHHCCEEEEECEEC
15.1724719451
779AcetylationRDLSLSMKYKGYVNS
HHCCEEEEECEECCC
40.2019813317
781AcetylationLSLSMKYKGYVNSSS
CCEEEEECEECCCCH
37.9419813325
781UbiquitinationLSLSMKYKGYVNSSS
CCEEEEECEECCCCH
37.94-
783PhosphorylationLSMKYKGYVNSSSQI
EEEEECEECCCCHHE
7.7222817900
799PhosphorylationASFSHDFTYLVSGSE
EEECCCEEEEEECCC
23.2322817900
800PhosphorylationSFSHDFTYLVSGSED
EECCCEEEEEECCCC
12.7122817900
803PhosphorylationHDFTYLVSGSEDKYV
CCEEEEEECCCCCEE
33.72-
809PhosphorylationVSGSEDKYVYIWSTY
EECCCCCEEEEEEEE
15.7127251275
823PhosphorylationYHDLSKFTSVRRDRN
ECCHHHHHHCCCCCC
30.0125332170
870UbiquitinationEKSEGNEKSEDAEVL
CCCCCCCCCCCCCHH
64.24-
871PhosphorylationKSEGNEKSEDAEVLD
CCCCCCCCCCCCHHH
34.2325159151
880PhosphorylationDAEVLDATPSGIMKT
CCCHHHCCCCCEECC
20.0421815630
882PhosphorylationEVLDATPSGIMKTDN
CHHHCCCCCEECCCC
36.2721815630
885SulfoxidationDATPSGIMKTDNTEV
HCCCCCEECCCCCEE
4.3321406390

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 WDR44_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR44_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 WDR44_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATH_HUMANATP6V1Hphysical
22863883
OSB11_HUMANOSBPL11physical
22863883
PRP39_HUMANPRPF39physical
22863883
VAPB_HUMANVAPBphysical
24885147
ACSF2_HUMANACSF2physical
28514442
ASML_HUMANASMTLphysical
28514442
PDP1_HUMANPDP1physical
28514442

Drug and Disease Associations
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.
Regulatory Network of WDR44_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5; SER-50; SER-90; SER-96; THR-158; SER-161;SER-162; THR-163; SER-403; SER-561; SER-563 AND SER-565, AND MASSSPECTROMETRY.
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-50; SER-96 AND SER-403,AND MASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5; SER-50; SER-90; SER-96; THR-158; SER-161;SER-162; THR-163; SER-403; SER-561; SER-563 AND SER-565, AND MASSSPECTROMETRY.
"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-50; SER-96; THR-219;SER-262; SER-403; SER-470; SER-471 AND SER-472, AND MASS 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-470; SER-471; SER-472AND SER-561, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, 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-561; SER-565 ANDSER-568, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-262; THR-271;TYR-783; THR-799 AND TYR-800, AND MASS 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-50 AND SER-96, AND MASSSPECTROMETRY.
"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-5; SER-27; SER-262 ANDSER-403, AND MASS SPECTROMETRY.

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