FKB15_HUMAN - dbPTM
FKB15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKB15_HUMAN
UniProt AC Q5T1M5
Protein Name FK506-binding protein 15
Gene Name FKBP15
Organism Homo sapiens (Human).
Sequence Length 1219
Subcellular Localization Cytoplasm . Cell projection, axon . Early endosome . Present in axons and neuronal growth cones.
Protein Description May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement..
Protein Sequence MFGAGDEDDTDFLSPSGGARLASLFGLDQAAAGHGNEFFQYTAPKQPKKGQGTAATGNQATPKTAPATMSTPTILVATAVHAYRYTNGQYVKQGKFGAAVLGNHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVEFNKQVCIAKCNSTSSLDAVLSQDLIVADGPAVEVGDSLEVAYTGWLFQNHVLGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGWTQATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSNSLSEQLAINTSPDAVKAKLISRMAKMGQPMLPILPPQLDSNDSEIEDVNTLQGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQAPSAALMQVSSLDSHSAVSGNAQSFQPYAGMQAYAYPQASAVTSQLQPVRPLYPAPLSQPPHFQGSGDMASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTILGTIMNTIKMVTLQLLNQQEQEKEESSSEEEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGHRRKGDSEAEALSEIKDGSLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPEEGDPLALGPESPGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLSGDEEDELFKGATLKALRPKAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDIDWLG
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-------MFGAGDED
-------CCCCCCCC
32.8222814378
10PhosphorylationGAGDEDDTDFLSPSG
CCCCCCCCCCCCCCH
40.7625850435
14PhosphorylationEDDTDFLSPSGGARL
CCCCCCCCCCHHHHH
19.6025159151
16PhosphorylationDTDFLSPSGGARLAS
CCCCCCCCHHHHHHH
46.6230108239
23PhosphorylationSGGARLASLFGLDQA
CHHHHHHHHHCCCHH
28.9028857561
24UbiquitinationGGARLASLFGLDQAA
HHHHHHHHHCCCHHH
3.0827667366
41PhosphorylationHGNEFFQYTAPKQPK
CCCCCCEECCCCCCC
10.3423917254
42PhosphorylationGNEFFQYTAPKQPKK
CCCCCEECCCCCCCC
26.2125159151
53PhosphorylationQPKKGQGTAATGNQA
CCCCCCCCCCCCCCC
12.7729759185
56PhosphorylationKGQGTAATGNQATPK
CCCCCCCCCCCCCCC
33.9125159151
61PhosphorylationAATGNQATPKTAPAT
CCCCCCCCCCCCCCC
18.6325849741
64PhosphorylationGNQATPKTAPATMST
CCCCCCCCCCCCCCC
38.7928555341
68PhosphorylationTPKTAPATMSTPTIL
CCCCCCCCCCCCEEE
15.5924719451
92AcetylationYTNGQYVKQGKFGAA
CCCCCEEECCCCCEE
48.6919608861
92UbiquitinationYTNGQYVKQGKFGAA
CCCCCEEECCCCCEE
48.6927667366
122PhosphorylationISQQQPVTVARIHVN
EECCCCEEEEEEEEE
18.3529888752
156PhosphorylationNWSIMFESEKAAVEF
CEEEEEECHHHHHHC
32.8827732954
231AcetylationKDKLLRLKLGSGKVI
HHHEEEEECCCCCEE
44.3525953088
295PhosphorylationRVKFARDSGSDGHSV
EEEEECCCCCCCCCC
34.3425159151
297PhosphorylationKFARDSGSDGHSVSS
EEECCCCCCCCCCCC
44.3525849741
301PhosphorylationDSGSDGHSVSSRDSA
CCCCCCCCCCCCCCC
29.2621955146
303PhosphorylationGSDGHSVSSRDSAAP
CCCCCCCCCCCCCCC
23.7525849741
304PhosphorylationSDGHSVSSRDSAAPS
CCCCCCCCCCCCCCC
37.6420873877
307PhosphorylationHSVSSRDSAAPSPIP
CCCCCCCCCCCCCCC
25.8129255136
311PhosphorylationSRDSAAPSPIPGADN
CCCCCCCCCCCCCCC
30.6329255136
320PhosphorylationIPGADNLSADPVVSP
CCCCCCCCCCCCCCC
36.5629255136
326PhosphorylationLSADPVVSPPTSIPF
CCCCCCCCCCCCCCC
25.9529255136
329PhosphorylationDPVVSPPTSIPFKSG
CCCCCCCCCCCCCCC
42.5530278072
330PhosphorylationPVVSPPTSIPFKSGE
CCCCCCCCCCCCCCC
33.7530278072
342PhosphorylationSGEPALRTKSNSLSE
CCCCCCCCCCCCHHH
39.4130108239
344PhosphorylationEPALRTKSNSLSEQL
CCCCCCCCCCHHHHH
30.9129255136
346PhosphorylationALRTKSNSLSEQLAI
CCCCCCCCHHHHHHC
40.1229255136
348PhosphorylationRTKSNSLSEQLAINT
CCCCCCHHHHHHCCC
24.1030266825
355PhosphorylationSEQLAINTSPDAVKA
HHHHHCCCCHHHHHH
35.2130266825
356PhosphorylationEQLAINTSPDAVKAK
HHHHCCCCHHHHHHH
19.1225159151
520MethylationRQHNTEIRMAVSKVA
HHCCHHHHHHHHHHH
10.77-
526UbiquitinationIRMAVSKVADKMDHL
HHHHHHHHHHHHHHH
6.9324816145
544PhosphorylationVEELQKHSAGNSMLI
HHHHHHHCCCCCCEE
44.9323401153
547UbiquitinationLQKHSAGNSMLIPSM
HHHHCCCCCCEECCC
24.7824816145
555PhosphorylationSMLIPSMSVTMETSM
CCEECCCCCHHHHHH
20.8322210691
561PhosphorylationMSVTMETSMIMSNIQ
CCCHHHHHHHHHHHH
7.9422210691
594UbiquitinationRIEEQNDKISELIER
HHHHHHHHHHHHHHH
56.5324816145
605PhosphorylationLIERNQRYVEQSNLM
HHHHHHHHHHHHHHH
9.8920068231
615UbiquitinationQSNLMMEKRNNSLQT
HHHHHHHHHCCCCCH
42.3924816145
619PhosphorylationMMEKRNNSLQTATEN
HHHHHCCCCCHHHHH
25.9629255136
622PhosphorylationKRNNSLQTATENTQA
HHCCCCCHHHHHHHH
40.6223312004
660PhosphorylationSHLQLKMTAHQKKET
HHHHHHCHHHHHHHH
21.28-
667PhosphorylationTAHQKKETELQMQLT
HHHHHHHHHHHHHHH
51.3723403867
669UbiquitinationHQKKETELQMQLTES
HHHHHHHHHHHHHHH
7.2022817900
670UbiquitinationQKKETELQMQLTESL
HHHHHHHHHHHHHHH
16.0222817900
671UbiquitinationKKETELQMQLTESLK
HHHHHHHHHHHHHHH
5.7222817900
674PhosphorylationTELQMQLTESLKETD
HHHHHHHHHHHHHHH
13.4623403867
676PhosphorylationLQMQLTESLKETDLL
HHHHHHHHHHHHHHH
39.2323403867
679UbiquitinationQLTESLKETDLLRGQ
HHHHHHHHHHHHHHH
53.5022817900
680UbiquitinationLTESLKETDLLRGQL
HHHHHHHHHHHHHHH
30.2922817900
681UbiquitinationTESLKETDLLRGQLT
HHHHHHHHHHHHHHH
44.8122817900
688UbiquitinationDLLRGQLTKVQAKLS
HHHHHHHHHHHHHHH
22.6824816145
689AcetylationLLRGQLTKVQAKLSE
HHHHHHHHHHHHHHH
40.7325953088
693AcetylationQLTKVQAKLSELQET
HHHHHHHHHHHHHHH
35.1426051181
696UbiquitinationKVQAKLSELQETSEQ
HHHHHHHHHHHHHHH
65.9821890473
698UbiquitinationQAKLSELQETSEQAQ
HHHHHHHHHHHHHHH
48.1224816145
703UbiquitinationELQETSEQAQSKFKS
HHHHHHHHHHHHHHH
44.4624816145
706UbiquitinationETSEQAQSKFKSEKQ
HHHHHHHHHHHHHHH
42.9721890473
707AcetylationTSEQAQSKFKSEKQN
HHHHHHHHHHHHHHH
44.7425953088
707MalonylationTSEQAQSKFKSEKQN
HHHHHHHHHHHHHHH
44.7426320211
713UbiquitinationSKFKSEKQNRKQLEL
HHHHHHHHHHHHHHH
51.4024816145
723PhosphorylationKQLELKVTSLEEELT
HHHHHEEEHHHHHHH
26.4628348404
724PhosphorylationQLELKVTSLEEELTD
HHHHEEEHHHHHHHH
36.4528348404
737UbiquitinationTDLRVEKESLEKNLS
HHHHHHHHHHHHHHH
47.2322817900
738UbiquitinationDLRVEKESLEKNLSE
HHHHHHHHHHHHHHH
53.5522817900
739UbiquitinationLRVEKESLEKNLSER
HHHHHHHHHHHHHHH
13.0922817900
747UbiquitinationEKNLSERKKKSAQER
HHHHHHHHHHHHHHH
61.5722817900
748UbiquitinationKNLSERKKKSAQERS
HHHHHHHHHHHHHHH
59.1722817900
749UbiquitinationNLSERKKKSAQERSQ
HHHHHHHHHHHHHHH
54.8022817900
756UbiquitinationKSAQERSQAEEEIDE
HHHHHHHHHHHHHHH
60.0424816145
764UbiquitinationAEEEIDEIRKSYQEE
HHHHHHHHHHHHHHH
6.2821890473
764 (in isoform 2)Ubiquitination-6.2821890473
766UbiquitinationEEIDEIRKSYQEELD
HHHHHHHHHHHHHHH
60.2124816145
767PhosphorylationEIDEIRKSYQEELDK
HHHHHHHHHHHHHHH
23.38-
771UbiquitinationIRKSYQEELDKLRQL
HHHHHHHHHHHHHHH
46.9024816145
774AcetylationSYQEELDKLRQLLKK
HHHHHHHHHHHHHHH
59.1926051181
774UbiquitinationSYQEELDKLRQLLKK
HHHHHHHHHHHHHHH
59.1929967540
774 (in isoform 1)Ubiquitination-59.1921890473
781UbiquitinationKLRQLLKKTRVSTDQ
HHHHHHHHHCCCHHH
41.3424816145
782PhosphorylationLRQLLKKTRVSTDQA
HHHHHHHHCCCHHHH
34.4128348404
785PhosphorylationLLKKTRVSTDQAAAE
HHHHHCCCHHHHHHH
23.9928857561
786PhosphorylationLKKTRVSTDQAAAEQ
HHHHCCCHHHHHHHH
29.3128857561
795PhosphorylationQAAAEQLSLVQAELQ
HHHHHHHHHHHHHHH
26.6224275569
808UbiquitinationLQTQWEAKCEHLLAS
HHHHHHHHHHHHHHH
28.7429967540
837AcetylationQRDAYQQKLVQLQEK
HHHHHHHHHHHHHHH
34.7926051181
837UbiquitinationQRDAYQQKLVQLQEK
HHHHHHHHHHHHHHH
34.7929967540
856O-linked_GlycosylationQAQITALTKQNEQHI
HHHHHHHHHHHHHHH
28.2830379171
873SulfoxidationLEKNKSQMSGVEAAA
HHHCHHHHHHCHHHH
4.9321406390
874PhosphorylationEKNKSQMSGVEAAAS
HHCHHHHHHCHHHHC
31.8625404012
881PhosphorylationSGVEAAASDPSEKVK
HHCHHHHCCHHHHHH
45.3825404012
884PhosphorylationEAAASDPSEKVKKIM
HHHHCCHHHHHHHHH
55.8525404012
897PhosphorylationIMNQVFQSLRREFEL
HHHHHHHHHHHHHCH
16.6324719451
925PhosphorylationMNTIKMVTLQLLNQQ
HHHHHHHHHHHHHHH
12.8023927012
939PhosphorylationQEQEKEESSSEEEEE
HHHHHHHCCCHHHHH
40.0126503892
940PhosphorylationEQEKEESSSEEEEEK
HHHHHHCCCHHHHHH
45.0826503892
941PhosphorylationQEKEESSSEEEEEKA
HHHHHCCCHHHHHHH
59.3026503892
956PhosphorylationEERPRRPSQEQSASA
HHCCCCCCHHHHHCC
44.5329255136
960PhosphorylationRRPSQEQSASASSGQ
CCCCHHHHHCCCCCC
24.3622167270
962PhosphorylationPSQEQSASASSGQPQ
CCHHHHHCCCCCCCC
33.6523927012
964PhosphorylationQEQSASASSGQPQAP
HHHHHCCCCCCCCCC
32.2929209046
965PhosphorylationEQSASASSGQPQAPL
HHHHCCCCCCCCCCC
40.9623927012
979PhosphorylationLNRERPESPMVPSEQ
CCCCCCCCCCCCCHH
22.4529255136
984PhosphorylationPESPMVPSEQVVEEA
CCCCCCCCHHHHHHC
29.2930266825
1000PhosphorylationPLPPQALTTSQDGHR
CCCCCCEECCCCCCC
27.6723927012
1001PhosphorylationLPPQALTTSQDGHRR
CCCCCEECCCCCCCC
25.8223927012
1002PhosphorylationPPQALTTSQDGHRRK
CCCCEECCCCCCCCC
22.4923927012
1012PhosphorylationGHRRKGDSEAEALSE
CCCCCCCHHHHHHHH
47.5830266825
1018PhosphorylationDSEAEALSEIKDGSL
CHHHHHHHHCCCCCC
44.3030266825
1024PhosphorylationLSEIKDGSLPPELSC
HHHCCCCCCCCCCCC
48.0825159151
1030PhosphorylationGSLPPELSCIPSHRV
CCCCCCCCCCCCCCC
14.3430108239
1034PhosphorylationPELSCIPSHRVLGPP
CCCCCCCCCCCCCCC
12.1923312004
1053PhosphorylationPEPLGPVSMDSECEE
CCCCCCCCCCCHHHH
21.7222210691
1056PhosphorylationLGPVSMDSECEESLA
CCCCCCCCHHHHHHC
35.1926074081
1061PhosphorylationMDSECEESLAASPMA
CCCHHHHHHCCCCCC
10.8726074081
1065PhosphorylationCEESLAASPMAAKPD
HHHHHCCCCCCCCCC
15.0326074081
1075PhosphorylationAAKPDNPSGKVCVRE
CCCCCCCCCCEEEEE
58.4626074081
1092PhosphorylationPDGPLQESSTRLSLT
CCCCCCCCCCEEEEC
24.8530278072
1093PhosphorylationDGPLQESSTRLSLTS
CCCCCCCCCEEEECC
19.4530278072
1094PhosphorylationGPLQESSTRLSLTSD
CCCCCCCCEEEECCC
44.9330278072
1097PhosphorylationQESSTRLSLTSDPEE
CCCCCEEEECCCCCC
26.7230278072
1099PhosphorylationSSTRLSLTSDPEEGD
CCCEEEECCCCCCCC
27.9230278072
1100PhosphorylationSTRLSLTSDPEEGDP
CCEEEECCCCCCCCC
57.3630278072
1114PhosphorylationPLALGPESPGEPQPP
CCCCCCCCCCCCCCC
41.1423927012
1129PhosphorylationQLKKDDVTSSTGPHK
CCCCCCCCCCCCCCC
24.7726074081
1130PhosphorylationLKKDDVTSSTGPHKE
CCCCCCCCCCCCCCC
26.2525159151
1131PhosphorylationKKDDVTSSTGPHKEL
CCCCCCCCCCCCCCC
28.1925849741
1132PhosphorylationKDDVTSSTGPHKELS
CCCCCCCCCCCCCCC
55.2725159151
1139PhosphorylationTGPHKELSSTEAGST
CCCCCCCCCCCCCCC
35.9825159151
1140PhosphorylationGPHKELSSTEAGSTV
CCCCCCCCCCCCCCC
42.7823312004
1141PhosphorylationPHKELSSTEAGSTVA
CCCCCCCCCCCCCCC
26.8630177828
1145PhosphorylationLSSTEAGSTVAGAAL
CCCCCCCCCCCCHHC
27.1020873877
1146PhosphorylationSSTEAGSTVAGAALR
CCCCCCCCCCCHHCC
17.2930108239
1155PhosphorylationAGAALRPSHHSQRSS
CCHHCCCCCCCCCCC
27.6529255136
1158PhosphorylationALRPSHHSQRSSLSG
HCCCCCCCCCCCCCC
23.1229255136
1161PhosphorylationPSHHSQRSSLSGDEE
CCCCCCCCCCCCCCC
28.1729255136
1162PhosphorylationSHHSQRSSLSGDEED
CCCCCCCCCCCCCCH
28.8329255136
1164PhosphorylationHSQRSSLSGDEEDEL
CCCCCCCCCCCCHHH
46.2619664994
1173UbiquitinationDEEDELFKGATLKAL
CCCHHHHHHCHHHHH
61.3332015554
1176PhosphorylationDELFKGATLKALRPK
HHHHHHCHHHHHCCC
37.1423927012
1195PhosphorylationEEDEDEVSMKGRPPP
CCCCCCCCCCCCCCC
16.8423401153
1203PhosphorylationMKGRPPPTPLFGDDD
CCCCCCCCCCCCCCC
38.109734811

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 FKB15_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKB15_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 FKB15_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WASC5_HUMANKIAA0196physical
20376207
WASC4_HUMANKIAA1033physical
20376207
TTBK2_HUMANTTBK2physical
20376207
UBC_HUMANUBCphysical
20376207
AIPL1_HUMANAIPL1physical
27173435
PDE5A_HUMANPDE5Aphysical
27173435

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 FKB15_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND MASS SPECTROMETRY.
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-326; SER-356; SER-1114AND SER-1164, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-1162AND SER-1164, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161; SER-1162 ANDSER-1164, 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-344; SER-346; SER-356;SER-939; SER-940; SER-941; SER-956; SER-979; THR-1094; SER-1097;SER-1114; SER-1162 AND SER-1164, 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-1161; SER-1162 ANDSER-1164, AND MASS 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-311 AND SER-956, ANDMASS 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-1114 AND SER-1164, ANDMASS SPECTROMETRY.

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