IPO5_HUMAN - dbPTM
IPO5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO5_HUMAN
UniProt AC O00410
Protein Name Importin-5
Gene Name IPO5
Organism Homo sapiens (Human).
Sequence Length 1097
Subcellular Localization Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus
nuclear rim. Found particularly in the nuclear rim and nucleolus.
Protein Description Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation (By similarity). In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev..
Protein Sequence MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA
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------MAAAAAEQQ
------CCHHHHHHH
19.6719413330
20PhosphorylationLLLGNLLSPDNVVRK
HHHHHCCCCCHHHHH
33.1120068231
27UbiquitinationSPDNVVRKQAEETYE
CCCHHHHHHHHHHHH
42.10-
32PhosphorylationVRKQAEETYENIPGQ
HHHHHHHHHHCCCCH
27.8628152594
33PhosphorylationRKQAEETYENIPGQS
HHHHHHHHHCCCCHH
15.4028152594
38PhosphorylationETYENIPGQSKITFL
HHHHCCCCHHHHHHH
40.3720068231
40PhosphorylationYENIPGQSKITFLLQ
HHCCCCHHHHHHHHH
31.7528152594
41UbiquitinationENIPGQSKITFLLQA
HCCCCHHHHHHHHHH
37.57-
45UbiquitinationGQSKITFLLQAIRNT
CHHHHHHHHHHHHCC
2.31-
45 (in isoform 3)Ubiquitination-2.31-
47 (in isoform 2)Ubiquitination-36.57-
48 (in isoform 2)Ubiquitination-11.59-
51PhosphorylationFLLQAIRNTTAAEEA
HHHHHHHCCCHHHHH
35.35-
51 (in isoform 3)Phosphorylation-35.3527642862
61SulfoxidationAAEEARQMAAVLLRR
HHHHHHHHHHHHHHH
1.8428183972
71PhosphorylationVLLRRLLSSAFDEVY
HHHHHHHHHHHHHHH
24.9818452278
72PhosphorylationLLRRLLSSAFDEVYP
HHHHHHHHHHHHHHC
32.69-
74 (in isoform 2)Ubiquitination-9.94-
78PhosphorylationSSAFDEVYPALPSDV
HHHHHHHHCCCCHHH
4.83-
83PhosphorylationEVYPALPSDVQTAIK
HHHCCCCHHHHHHHH
51.7918452278
89PhosphorylationPSDVQTAIKSELLMI
CHHHHHHHHHHHHHH
5.9918452278
95SulfoxidationAIKSELLMIIQMETQ
HHHHHHHHHHHHHCC
3.8728465586
96PhosphorylationIKSELLMIIQMETQS
HHHHHHHHHHHHCCH
1.67-
99SulfoxidationELLMIIQMETQSSMR
HHHHHHHHHCCHHHH
4.1928465586
101PhosphorylationLMIIQMETQSSMRKK
HHHHHHHCCHHHHHH
28.5418452278
108UbiquitinationTQSSMRKKVCDIAAE
CCHHHHHHHHHHHHH
37.42-
110GlutathionylationSSMRKKVCDIAAELA
HHHHHHHHHHHHHHH
4.2622555962
125 (in isoform 3)Ubiquitination-32.70-
126UbiquitinationNLIDEDGNNQWPEGL
HHCCCCCCCCCCCHH
50.25-
126 (in isoform 3)Ubiquitination-50.25-
139PhosphorylationGLKFLFDSVSSQNVG
HHHHHHHHHCCCCCC
19.3021406692
141PhosphorylationKFLFDSVSSQNVGLR
HHHHHHHCCCCCCHH
30.1121406692
142PhosphorylationFLFDSVSSQNVGLRE
HHHHHHCCCCCCHHH
24.5021406692
188PhosphorylationMQDQEHPSIRTLSAR
HCCCCCCCHHHHHHH
26.9824719451
238UbiquitinationQNDDSVLKSLVEIAD
CCCHHHHHHHHHHHH
39.32-
239PhosphorylationNDDSVLKSLVEIADT
CCHHHHHHHHHHHHH
33.2223911959
256UbiquitinationKYLRPHLEATLQLSL
HHHHHHHHHHHHHHH
36.25-
257PhosphorylationYLRPHLEATLQLSLK
HHHHHHHHHHHHHHH
21.70-
258PhosphorylationLRPHLEATLQLSLKL
HHHHHHHHHHHHHHH
12.9820068231
274SulfoxidationGDTSLNNMQRQLALE
CCCCCHHHHHHHHHH
3.1921406390
304PhosphorylationHTNIVAQTIPQMLAM
HHHHHHHHHHHHHHH
25.5317192257
322PhosphorylationLEEDEDWANADELED
CCCCCCCCCCHHCCC
17.4118691976
371UbiquitinationMQMLQNPDWKYRHAG
HHHHHCCCHHHHHHH
63.15-
371 (in isoform 3)Ubiquitination-63.15-
420GlutathionylationPRVRYAACNAVGQMA
HHHHHHHHHHHHHHH
2.2722555962
436AcetylationDFAPGFQKKFHEKVI
CCCCCHHHHHHHHHH
55.9623749302
436UbiquitinationDFAPGFQKKFHEKVI
CCCCCHHHHHHHHHH
55.9622053931
450SulfoxidationIAALLQTMEDQGNQR
HHHHHHHHHHHCCHH
3.2628183972
454AcetylationLQTMEDQGNQRVQAH
HHHHHHHCCHHHHHH
44.55-
455 (in isoform 3)Ubiquitination-22.35-
473GlutathionylationLINFTEDCPKSLLIP
HHHCCCCCCHHHHHH
3.5822555962
476PhosphorylationFTEDCPKSLLIPYLD
CCCCCCHHHHHHHHH
17.3527499020
488 (in isoform 2)Ubiquitination-22.6921890473
491PhosphorylationNLVKHLHSIMVLKLQ
HHHHHHHHHHHHHHH
20.8121060948
494PhosphorylationKHLHSIMVLKLQELI
HHHHHHHHHHHHHHH
3.98-
494 (in isoform 3)Phosphorylation-3.9827251275
505PhosphorylationQELIQKGTKLVLEQV
HHHHHHCCHHHHHHH
28.3922210691
509PhosphorylationQKGTKLVLEQVVTSI
HHCCHHHHHHHHHHH
5.73-
514PhosphorylationLVLEQVVTSIASVAD
HHHHHHHHHHHHHHH
18.6330622161
515PhosphorylationVLEQVVTSIASVADT
HHHHHHHHHHHHHHH
12.4430622161
518PhosphorylationQVVTSIASVADTAEE
HHHHHHHHHHHHHHH
19.0322210691
521UbiquitinationTSIASVADTAEEKFV
HHHHHHHHHHHHHCC
44.27-
521 (in isoform 3)Ubiquitination-44.27-
522PhosphorylationSIASVADTAEEKFVP
HHHHHHHHHHHHCCC
26.6522210691
530PhosphorylationAEEKFVPYYDLFMPS
HHHHCCCHHHHHHHH
12.33-
548AcetylationIVENAVQKELRLLRG
HHHHHHHHHHHHHCC
52.7126051181
548PhosphorylationIVENAVQKELRLLRG
HHHHHHHHHHHHHCC
52.71-
548UbiquitinationIVENAVQKELRLLRG
HHHHHHHHHHHHHCC
52.712189047
548 (in isoform 1)Ubiquitination-52.7121890473
549 (in isoform 3)Phosphorylation-23.2527642862
556UbiquitinationELRLLRGKTIECISL
HHHHHCCCCHHHHHH
39.64-
557PhosphorylationLRLLRGKTIECISLI
HHHHCCCCHHHHHHH
25.4920068231
560GlutathionylationLRGKTIECISLIGLA
HCCCCHHHHHHHHHH
1.9522555962
560S-palmitoylationLRGKTIECISLIGLA
HCCCCHHHHHHHHHH
1.9529575903
562PhosphorylationGKTIECISLIGLAVG
CCCHHHHHHHHHHHC
26.1220068231
566UbiquitinationECISLIGLAVGKEKF
HHHHHHHHHHCHHHH
2.50-
566 (in isoform 3)Ubiquitination-2.5021890473
574SulfoxidationAVGKEKFMQDASDVM
HHCHHHHCCCHHHHH
5.3721406390
574UbiquitinationAVGKEKFMQDASDVM
HHCHHHHCCCHHHHH
5.37-
574 (in isoform 3)Ubiquitination-5.37-
578PhosphorylationEKFMQDASDVMQLLL
HHHCCCHHHHHHHHH
38.7420068231
611 (in isoform 2)Ubiquitination-1.79-
613AcetylationSAWARMCKILGKEFQ
HHHHHHHHHHCHHHH
31.4625953088
613MalonylationSAWARMCKILGKEFQ
HHHHHHHHHHCHHHH
31.4626320211
617UbiquitinationRMCKILGKEFQQYLP
HHHHHHCHHHHHHHH
52.49-
627SulfoxidationQQYLPVVMGPLMKTA
HHHHHHHHCCHHCCC
4.6928465586
630 (in isoform 2)Ubiquitination-4.5621890473
631SulfoxidationPVVMGPLMKTASIKP
HHHHCCHHCCCCCCC
4.0028465586
631UbiquitinationPVVMGPLMKTASIKP
HHHHCCHHCCCCCCC
4.00-
631 (in isoform 3)Ubiquitination-4.00-
633PhosphorylationVMGPLMKTASIKPEV
HHCCHHCCCCCCCCE
16.2118669648
635PhosphorylationGPLMKTASIKPEVAL
CCHHCCCCCCCCEEE
36.0528464451
640 (in isoform 3)Phosphorylation-6.5327642862
645PhosphorylationPEVALLDTQDMENMS
CCEEEECCCCCCCCC
26.8328464451
651PhosphorylationDTQDMENMSDDDGWE
CCCCCCCCCCCCCCE
2.7118669648
652PhosphorylationTQDMENMSDDDGWEF
CCCCCCCCCCCCCEE
49.8525159151
663PhosphorylationGWEFVNLGDQQSFGI
CCEEEECCCHHCCCC
26.02-
667PhosphorylationVNLGDQQSFGIKTAG
EECCCHHCCCCCCCC
21.5828176443
670PhosphorylationGDQQSFGIKTAGLEE
CCHHCCCCCCCCCCC
3.1818452278
670 (in isoform 3)Phosphorylation-3.1827251275
671UbiquitinationDQQSFGIKTAGLEEK
CHHCCCCCCCCCCCC
32.47-
678UbiquitinationKTAGLEEKSTACQML
CCCCCCCCCHHHHHH
43.67-
680PhosphorylationAGLEEKSTACQMLVC
CCCCCCCHHHHHHHH
42.3921712546
687GlutathionylationTACQMLVCYAKELKE
HHHHHHHHHHHHHHC
2.1122555962
689UbiquitinationCQMLVCYAKELKEGF
HHHHHHHHHHHHCCH
8.17-
690AcetylationQMLVCYAKELKEGFV
HHHHHHHHHHHCCHH
36.7826051181
690UbiquitinationQMLVCYAKELKEGFV
HHHHHHHHHHHCCHH
36.78-
690 (in isoform 1)Ubiquitination-36.7821890473
693AcetylationVCYAKELKEGFVEYT
HHHHHHHHCCHHHHH
57.8126051181
693UbiquitinationVCYAKELKEGFVEYT
HHHHHHHHCCHHHHH
57.81-
696UbiquitinationAKELKEGFVEYTEQV
HHHHHCCHHHHHHHH
3.86-
696 (in isoform 3)Ubiquitination-3.86-
698PhosphorylationELKEGFVEYTEQVVK
HHHCCHHHHHHHHHH
44.47-
699PhosphorylationLKEGFVEYTEQVVKL
HHCCHHHHHHHHHHH
15.41-
700PhosphorylationKEGFVEYTEQVVKLM
HCCHHHHHHHHHHHH
13.36-
708UbiquitinationEQVVKLMVPLLKFYF
HHHHHHHHHHHHHHC
4.35-
708 (in isoform 3)Ubiquitination-4.3521890473
711UbiquitinationVKLMVPLLKFYFHDG
HHHHHHHHHHHCCCC
2.70-
711 (in isoform 3)Ubiquitination-2.70-
717PhosphorylationLLKFYFHDGVRVAAA
HHHHHCCCCCCHHHH
47.59-
718PhosphorylationLKFYFHDGVRVAAAE
HHHHCCCCCCHHHHH
10.68-
727SulfoxidationRVAAAESMPLLLECA
CHHHHHHHHHHHHHH
1.7221406390
730UbiquitinationAAESMPLLLECARVR
HHHHHHHHHHHHHHH
2.89-
733GlutathionylationSMPLLLECARVRGPE
HHHHHHHHHHHHCHH
2.7122555962
767PhosphorylationEPDSDVLSEIMHSFA
CCCHHHHHHHHHHHH
25.5628348404
793UbiquitinationNNEHFEELGGILKAK
CCHHHHHHHHHHHHH
6.32-
800UbiquitinationLGGILKAKLEEHFKN
HHHHHHHHHHHHHCC
55.64-
806AcetylationAKLEEHFKNQELRQV
HHHHHHHCCHHHHHH
60.6825953088
811MethylationHFKNQELRQVKRQDE
HHCCHHHHHHHHCCC
38.19-
818UbiquitinationRQVKRQDEDYDEQVE
HHHHHCCCCHHHHHH
50.56-
818 (in isoform 3)Ubiquitination-50.56-
820PhosphorylationVKRQDEDYDEQVEES
HHHCCCCHHHHHHHH
21.2323403867
824UbiquitinationDEDYDEQVEESLQDE
CCCHHHHHHHHHCCC
9.19-
824 (in isoform 3)Ubiquitination-9.19-
827PhosphorylationYDEQVEESLQDEDDN
HHHHHHHHHCCCCCC
20.1625159151
829MethylationEQVEESLQDEDDNDV
HHHHHHHCCCCCCCE
62.42-
837PhosphorylationDEDDNDVYILTKVSD
CCCCCCEEEEEHHHH
7.9623663014
838 (in isoform 3)Phosphorylation-3.8527642862
840PhosphorylationDNDVYILTKVSDILH
CCCEEEEEHHHHHHH
21.6029691806
843PhosphorylationVYILTKVSDILHSIF
EEEEEHHHHHHHHHH
22.0829396449
845PhosphorylationILTKVSDILHSIFSS
EEEHHHHHHHHHHHH
2.6517081983
845 (in isoform 3)Phosphorylation-2.6524719451
848PhosphorylationKVSDILHSIFSSYKE
HHHHHHHHHHHHHHH
23.1429396449
851PhosphorylationDILHSIFSSYKEKVL
HHHHHHHHHHHHHHH
30.9629396449
852PhosphorylationILHSIFSSYKEKVLP
HHHHHHHHHHHHHHH
29.4929396449
853PhosphorylationLHSIFSSYKEKVLPW
HHHHHHHHHHHHHHH
23.2029396449
854SuccinylationHSIFSSYKEKVLPWF
HHHHHHHHHHHHHHH
53.6723954790
855 (in isoform 3)Phosphorylation-39.9227642862
899PhosphorylationIEHCSPASFKYAEYF
HHHCCHHHHHHHHHH
26.1724719451
961AcetylationVIQSADSKTKENVNA
HHHCCCCCCCCCCCC
65.2525953088
963UbiquitinationQSADSKTKENVNATE
HCCCCCCCCCCCCCH
51.53-
972GlutathionylationNVNATENCISAVGKI
CCCCCHHHHHHHHHH
1.8022555962
972S-nitrosylationNVNATENCISAVGKI
CCCCCHHHHHHHHHH
1.802212679
978AcetylationNCISAVGKIMKFKPD
HHHHHHHHHHCCCCC
32.7825953088
981UbiquitinationSAVGKIMKFKPDCVN
HHHHHHHCCCCCCCC
54.42-
981 (in isoform 3)Ubiquitination-54.42-
996UbiquitinationVEEVLPHWLSWLPLH
HHHHHHHHHHCCCCC
7.08-
1040PhosphorylationTNLPKIFSIIAEGEM
CCCCHHHHHHHCCHH
19.29-
1052AcetylationGEMHEAIKHEDPCAK
CHHHHHHHCCCHHHH
48.2525953088

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 IPO5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO5_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 IPO5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU214_HUMANNUP214physical
9114010
NU153_HUMANNUP153physical
9114010
RAN_HUMANRANphysical
9114010
TNPO1_HUMANTNPO1physical
22939629
RL7_HUMANRPL7physical
20828572
MUC1_HUMANMUC1physical
17500061
WASL_HUMANWASLphysical
21988832
HXK2_HUMANHK2physical
22863883
CAND1_HUMANCAND1physical
26344197
CLH1_HUMANCLTCphysical
26344197
XPO2_HUMANCSE1Lphysical
26344197
DCA13_HUMANDCAF13physical
26344197
DDX56_HUMANDDX56physical
26344197
FBRL_HUMANFBLphysical
26344197
DHB12_HUMANHSD17B12physical
26344197
IPO7_HUMANIPO7physical
26344197
IPO9_HUMANIPO9physical
26344197
IMA5_HUMANKPNA1physical
26344197
IMA6_HUMANKPNA5physical
26344197
IMB1_HUMANKPNB1physical
26344197
MCM7_HUMANMCM7physical
26344197
RAN_HUMANRANphysical
26344197
RPN1_HUMANRPN1physical
26344197
RPN2_HUMANRPN2physical
26344197
SCAM3_HUMANSCAMP3physical
26344197
S61A1_HUMANSEC61A1physical
26344197
1433S_HUMANSFNphysical
26344197
TNPO1_HUMANTNPO1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
XPO1_HUMANXPO1physical
26344197
IMA5_HUMANKPNA1physical
12861017

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 IPO5_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, 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-827, 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-827, AND MASSSPECTROMETRY.
"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 THR-304; SER-652 ANDSER-827, 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-827, AND MASSSPECTROMETRY.

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