RBM26_HUMAN - dbPTM
RBM26_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM26_HUMAN
UniProt AC Q5T8P6
Protein Name RNA-binding protein 26
Gene Name RBM26
Organism Homo sapiens (Human).
Sequence Length 1007
Subcellular Localization
Protein Description
Protein Sequence MVSKMIIENFEALKSWLSKTLEPICDADPSALAKYVLALVKKDKSEKELKALCIDQLDVFLQKETQIFVEKLFDAVNTKSYLPPPEQPSSGSLKVEFFPHQEKDIKKEEITKEEEREKKFSRRLNHSPPQSSSRYRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYNRRRGRSRSYSRSRSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTDPLENNYTPVSSVPSISSGHYPVPTLSSTITVIAPTHHGNNTTESWSEFHEDQVDHNSYVRPPMPKKRCRDYDEKGFCMRGDMCPFDHGSDPVVVEDVNLPGMLPFPAQPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGMDAPPNSATSSVPTVVTTGIHHQPPPAPPSLFTADTYDTDGYNPEAPSITNTSRPMYRHRVHAQRPNLIGLTSGDMDLPPREKPPNKSSMRIVVDSESRKRTIGSGEPGVPTKKTWFDKPNFNRTNSPGFQKKVQFGNENTKLELRKVPPELNNISKLNEHFSRFGTLVNLQVAYNGDPEGALIQFATYEEAKKAISSTEAVLNNRFIKVYWHREGSTQQLQTTSPKVMQPLVQQPILPVVKQSVKERLGPVPSSTIEPAEAQSASSDLPQNVTKLSVKDRLGFVSKPSVSATEKVLSTSTGLTKTVYNPAALKAAQKTLLVSTSAVDNNEAQKKKQEALKLQQDVRKRKQEILEKHIETQKMLISKLEKNKTMKSEDKAEIMKTLEVLTKNITKLKDEVKAASPGRCLPKSIKTKTQMQKELLDTELDLYKKMQAGEEVTELRRKYTELQLEAAKRGILSSGRGRGIHSRGRGAVHGRGRGRGRGRGVPGHAVVDHRPRALEISAFTESDREDLLPHFAQYGEIEDCQIDDSSLHAVITFKTRAEAEAAAVHGARFKGQDLKLAWNKPVTNISAVETEEVEPDEEEFQEESLVDDSLLQDDDEEEEDNESRSWRR
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
3Phosphorylation-----MVSKMIIENF
-----CCCCHHHHCH
28.50-
4Acetylation----MVSKMIIENFE
----CCCCHHHHCHH
39.0325953088
14AcetylationIENFEALKSWLSKTL
HHCHHHHHHHHHHCC
46.7830591811
15PhosphorylationENFEALKSWLSKTLE
HCHHHHHHHHHHCCH
33.81-
18PhosphorylationEALKSWLSKTLEPIC
HHHHHHHHHCCHHHC
19.82-
19AcetylationALKSWLSKTLEPICD
HHHHHHHHCCHHHCC
55.7630591817
19UbiquitinationALKSWLSKTLEPICD
HHHHHHHHCCHHHCC
55.76-
25GlutathionylationSKTLEPICDADPSAL
HHCCHHHCCCCHHHH
5.3022555962
30PhosphorylationPICDADPSALAKYVL
HHCCCCHHHHHHHHH
36.14-
41AcetylationKYVLALVKKDKSEKE
HHHHHHHHCCCCHHH
56.9825953088
50UbiquitinationDKSEKELKALCIDQL
CCCHHHHHHHHHHHH
40.16-
53GlutathionylationEKELKALCIDQLDVF
HHHHHHHHHHHHHHH
3.7322555962
63UbiquitinationQLDVFLQKETQIFVE
HHHHHHHHHHHHHHH
65.95-
64 (in isoform 4)Ubiquitination-32.7421890473
64 (in isoform 5)Ubiquitination-32.7421890473
71UbiquitinationETQIFVEKLFDAVNT
HHHHHHHHHHHHCCC
49.5021890473
71 (in isoform 1)Ubiquitination-49.5021890473
71 (in isoform 2)Ubiquitination-49.5021890473
71 (in isoform 3)Ubiquitination-49.5021890473
71 (in isoform 6)Ubiquitination-49.5021890473
78O-linked_GlycosylationKLFDAVNTKSYLPPP
HHHHHCCCCCCCCCC
18.1230059200
80PhosphorylationFDAVNTKSYLPPPEQ
HHHCCCCCCCCCCCC
29.8423663014
81PhosphorylationDAVNTKSYLPPPEQP
HHCCCCCCCCCCCCC
25.4523663014
89PhosphorylationLPPPEQPSSGSLKVE
CCCCCCCCCCCCEEE
47.2023663014
90PhosphorylationPPPEQPSSGSLKVEF
CCCCCCCCCCCEEEE
38.8023663014
92PhosphorylationPEQPSSGSLKVEFFP
CCCCCCCCCEEEECC
27.2823663014
94SumoylationQPSSGSLKVEFFPHQ
CCCCCCCEEEECCCC
41.2228112733
94UbiquitinationQPSSGSLKVEFFPHQ
CCCCCCCEEEECCCC
41.22-
103UbiquitinationEFFPHQEKDIKKEEI
EECCCCCCCCCHHHC
59.17-
106SumoylationPHQEKDIKKEEITKE
CCCCCCCCHHHCCHH
65.3525114211
111PhosphorylationDIKKEEITKEEEREK
CCCHHHCCHHHHHHH
35.3725690035
112SumoylationIKKEEITKEEEREKK
CCHHHCCHHHHHHHH
69.64-
112SumoylationIKKEEITKEEEREKK
CCHHHCCHHHHHHHH
69.64-
121PhosphorylationEEREKKFSRRLNHSP
HHHHHHHHHHHCCCC
25.93-
127PhosphorylationFSRRLNHSPPQSSSR
HHHHHCCCCCCCHHH
36.8829255136
127 (in isoform 3)Phosphorylation-36.8818220336
131PhosphorylationLNHSPPQSSSRYREN
HCCCCCCCHHHHHHH
35.7320201521
132PhosphorylationNHSPPQSSSRYRENR
CCCCCCCHHHHHHHC
17.3720201521
133PhosphorylationHSPPQSSSRYRENRS
CCCCCCHHHHHHHCC
38.2820201521
162 (in isoform 4)Phosphorylation-42.8925022875
162 (in isoform 5)Phosphorylation-42.8925022875
163 (in isoform 4)Phosphorylation-51.8330631047
163 (in isoform 5)Phosphorylation-51.8330631047
164PhosphorylationRNPPRRDSYRDRYNR
CCCCCCCHHHHHHHH
21.9123828894
168 (in isoform 4)Phosphorylation-22.9425159151
168 (in isoform 5)Phosphorylation-22.9425159151
169 (in isoform 4)Phosphorylation-19.8125022875
169 (in isoform 5)Phosphorylation-19.8125022875
170 (in isoform 4)Phosphorylation-31.6925159151
170 (in isoform 5)Phosphorylation-31.6925159151
176PhosphorylationYNRRRGRSRSYSRSR
HHHHHCCCCCHHHHH
28.5320068231
178PhosphorylationRRRGRSRSYSRSRSR
HHHCCCCCHHHHHCC
28.8020068231
179PhosphorylationRRGRSRSYSRSRSRS
HHCCCCCHHHHHCCC
13.6420068231
180PhosphorylationRGRSRSYSRSRSRSW
HCCCCCHHHHHCCCC
25.6520068231
182PhosphorylationRSRSYSRSRSRSWSK
CCCCHHHHHCCCCCH
28.7721406692
184PhosphorylationRSYSRSRSRSWSKER
CCHHHHHCCCCCHHH
31.7324144214
186PhosphorylationYSRSRSRSWSKERLR
HHHHHCCCCCHHHHH
36.6326055452
188PhosphorylationRSRSRSWSKERLRER
HHHCCCCCHHHHHHH
26.3626055452
196 (in isoform 5)Phosphorylation-52.6724173317
197 (in isoform 5)Phosphorylation-47.6821406692
198 (in isoform 5)Phosphorylation-58.1421406692
206 (in isoform 5)Phosphorylation-38.9721406692
208 (in isoform 5)Phosphorylation-33.9521406692
209 (in isoform 5)Phosphorylation-32.3821406692
216 (in isoform 5)Phosphorylation-13.4521406692
217 (in isoform 5)Phosphorylation-42.9921406692
218 (in isoform 5)Phosphorylation-32.7221406692
219 (in isoform 5)Phosphorylation-45.7521406692
222 (in isoform 5)Phosphorylation-4.3321406692
236 (in isoform 5)Ubiquitination-27.1621890473
260 (in isoform 4)Ubiquitination-22.5721890473
463PhosphorylationRPNLIGLTSGDMDLP
CCCEEECCCCCCCCC
26.0028555341
464PhosphorylationPNLIGLTSGDMDLPP
CCEEECCCCCCCCCC
37.5328555341
487PhosphorylationSMRIVVDSESRKRTI
CCEEEEECHHCCEEC
26.3425159151
492PhosphorylationVDSESRKRTIGSGEP
EECHHCCEECCCCCC
30.39-
493PhosphorylationDSESRKRTIGSGEPG
ECHHCCEECCCCCCC
32.5028985074
496PhosphorylationSRKRTIGSGEPGVPT
HCCEECCCCCCCCCC
35.8121815630
501PhosphorylationIGSGEPGVPTKKTWF
CCCCCCCCCCCCCCC
8.77-
504AcetylationGEPGVPTKKTWFDKP
CCCCCCCCCCCCCCC
41.9825953088
510AcetylationTKKTWFDKPNFNRTN
CCCCCCCCCCCCCCC
32.1819608861
510UbiquitinationTKKTWFDKPNFNRTN
CCCCCCCCCCCCCCC
32.1821890473
510 (in isoform 1)Ubiquitination-32.1821890473
510 (in isoform 2)Ubiquitination-32.1821890473
510 (in isoform 3)Ubiquitination-32.1821890473
515AcetylationFDKPNFNRTNSPGFQ
CCCCCCCCCCCCCHH
31.0119608861
515UbiquitinationFDKPNFNRTNSPGFQ
CCCCCCCCCCCCCHH
31.0119608861
516PhosphorylationDKPNFNRTNSPGFQK
CCCCCCCCCCCCHHH
40.9530266825
518PhosphorylationPNFNRTNSPGFQKKV
CCCCCCCCCCHHHCE
26.2825159151
518 (in isoform 3)Phosphorylation-26.2818669648
521PhosphorylationNRTNSPGFQKKVQFG
CCCCCCCHHHCEECC
12.50-
5232-HydroxyisobutyrylationTNSPGFQKKVQFGNE
CCCCCHHHCEECCCC
53.29-
523PhosphorylationTNSPGFQKKVQFGNE
CCCCCHHHCEECCCC
53.2918669648
524SumoylationNSPGFQKKVQFGNEN
CCCCHHHCEECCCCC
30.41-
529SumoylationQKKVQFGNENTKLEL
HHCEECCCCCCCEEE
40.40-
529UbiquitinationQKKVQFGNENTKLEL
HHCEECCCCCCCEEE
40.40-
547PhosphorylationPPELNNISKLNEHFS
CHHHCCHHHHHHHHH
32.9629449344
585UbiquitinationATYEEAKKAISSTEA
ECHHHHHHHHHCHHH
58.9818655026
588PhosphorylationEEAKKAISSTEAVLN
HHHHHHHHCHHHHHH
35.7529255136
589PhosphorylationEAKKAISSTEAVLNN
HHHHHHHCHHHHHHC
24.9328387310
590PhosphorylationAKKAISSTEAVLNNR
HHHHHHCHHHHHHCC
22.6029255136
590UbiquitinationAKKAISSTEAVLNNR
HHHHHHCHHHHHHCC
22.60-
595PhosphorylationSSTEAVLNNRFIKVY
HCHHHHHHCCEEEEE
30.91-
602PhosphorylationNNRFIKVYWHREGST
HCCEEEEEEECCCCC
7.1817360941
607PhosphorylationKVYWHREGSTQQLQT
EEEEECCCCCCCCCC
35.63-
608PhosphorylationVYWHREGSTQQLQTT
EEEECCCCCCCCCCC
20.4922167270
608 (in isoform 3)Phosphorylation-20.4925022875
609PhosphorylationYWHREGSTQQLQTTS
EEECCCCCCCCCCCC
31.0622167270
609 (in isoform 3)Phosphorylation-31.0630631047
613PhosphorylationEGSTQQLQTTSPKVM
CCCCCCCCCCCCCHH
38.09-
614PhosphorylationGSTQQLQTTSPKVMQ
CCCCCCCCCCCCHHH
37.5230266825
614 (in isoform 3)Phosphorylation-37.5225159151
615PhosphorylationSTQQLQTTSPKVMQP
CCCCCCCCCCCHHHH
30.0330266825
615 (in isoform 3)Phosphorylation-30.0325022875
616PhosphorylationTQQLQTTSPKVMQPL
CCCCCCCCCCHHHHH
26.5529255136
616 (in isoform 3)Phosphorylation-26.5525159151
620SulfoxidationQTTSPKVMQPLVQQP
CCCCCCHHHHHHHCC
4.1921406390
621PhosphorylationTTSPKVMQPLVQQPI
CCCCCHHHHHHHCCC
31.0316964243
633SumoylationQPILPVVKQSVKERL
CCCHHHHHHHHHHHH
36.77-
635PhosphorylationILPVVKQSVKERLGP
CHHHHHHHHHHHHCC
29.4626074081
635SumoylationILPVVKQSVKERLGP
CHHHHHHHHHHHHCC
29.46-
637PhosphorylationPVVKQSVKERLGPVP
HHHHHHHHHHHCCCC
42.22-
642 (in isoform 3)Phosphorylation-39.1624173317
643 (in isoform 3)Phosphorylation-7.3421406692
644 (in isoform 3)Phosphorylation-26.2021406692
645 (in isoform 2)Phosphorylation-40.1124173317
646 (in isoform 2)Phosphorylation-27.6021406692
647 (in isoform 2)Phosphorylation-33.4321406692
652 (in isoform 3)Phosphorylation-58.9421406692
654 (in isoform 3)Phosphorylation-30.9121406692
655 (in isoform 2)Phosphorylation-36.8521406692
655 (in isoform 3)Phosphorylation-36.8521406692
657 (in isoform 2)Phosphorylation-29.6321406692
658 (in isoform 2)Phosphorylation-42.7721406692
662 (in isoform 3)Phosphorylation-65.4121406692
663 (in isoform 3)Phosphorylation-41.3021406692
664 (in isoform 3)Phosphorylation-4.1521406692
665 (in isoform 2)Phosphorylation-33.5421406692
665 (in isoform 3)Phosphorylation-33.5421406692
666 (in isoform 2)Phosphorylation-34.1921406692
667 (in isoform 2)Phosphorylation-5.3421406692
668 (in isoform 2)Phosphorylation-28.7721406692
668 (in isoform 3)Phosphorylation-28.7721406692
671 (in isoform 2)Phosphorylation-49.2121406692
678AcetylationDRLGFVSKPSVSATE
HHCCCCCCCCCCCCC
35.6923236377
680AcetylationLGFVSKPSVSATEKV
CCCCCCCCCCCCCHH
32.23-
682 (in isoform 3)Ubiquitination-33.5421890473
685 (in isoform 2)Ubiquitination-40.6621890473
689O-linked_GlycosylationSATEKVLSTSTGLTK
CCCCHHHHCCCCCCC
24.2530059200
689PhosphorylationSATEKVLSTSTGLTK
CCCCHHHHCCCCCCC
24.2524505115
690O-linked_GlycosylationATEKVLSTSTGLTKT
CCCHHHHCCCCCCCC
26.5830059200
690PhosphorylationATEKVLSTSTGLTKT
CCCHHHHCCCCCCCC
26.5824505115
691O-linked_GlycosylationTEKVLSTSTGLTKTV
CCHHHHCCCCCCCCC
19.6630059200
691PhosphorylationTEKVLSTSTGLTKTV
CCHHHHCCCCCCCCC
19.6624505115
692O-linked_GlycosylationEKVLSTSTGLTKTVY
CHHHHCCCCCCCCCC
35.9830059200
692PhosphorylationEKVLSTSTGLTKTVY
CHHHHCCCCCCCCCC
35.9824505115
695O-linked_GlycosylationLSTSTGLTKTVYNPA
HHCCCCCCCCCCCHH
26.4730059200
695PhosphorylationLSTSTGLTKTVYNPA
HHCCCCCCCCCCCHH
26.4724505115
697O-linked_GlycosylationTSTGLTKTVYNPAAL
CCCCCCCCCCCHHHH
24.0030059200
705AcetylationVYNPAALKAAQKTLL
CCCHHHHHHHHHHHE
36.6325953088
705MethylationVYNPAALKAAQKTLL
CCCHHHHHHHHHHHE
36.63115976411
707MethylationNPAALKAAQKTLLVS
CHHHHHHHHHHHEEE
15.15-
707UbiquitinationNPAALKAAQKTLLVS
CHHHHHHHHHHHEEE
15.15-
709AcetylationAALKAAQKTLLVSTS
HHHHHHHHHHEEECH
36.0925953088
709UbiquitinationAALKAAQKTLLVSTS
HHHHHHHHHHEEECH
36.0921890473
709 (in isoform 1)Ubiquitination-36.0921890473
711UbiquitinationLKAAQKTLLVSTSAV
HHHHHHHHEEECHHC
5.99-
716PhosphorylationKTLLVSTSAVDNNEA
HHHEEECHHCCCCHH
20.8428555341
741UbiquitinationQQDVRKRKQEILEKH
HHHHHHHHHHHHHHH
56.15-
743UbiquitinationDVRKRKQEILEKHIE
HHHHHHHHHHHHHHH
53.21-
753UbiquitinationEKHIETQKMLISKLE
HHHHHHHHHHHHHHH
42.99-
784UbiquitinationLEVLTKNITKLKDEV
HHHHHHHHHHHHHHH
3.71-
795PhosphorylationKDEVKAASPGRCLPK
HHHHHHCCCCCCCCH
32.5225159151
797PhosphorylationEVKAASPGRCLPKSI
HHHHCCCCCCCCHHH
30.3632645325
803PhosphorylationPGRCLPKSIKTKTQM
CCCCCCHHHHHHHHH
27.6426074081
806PhosphorylationCLPKSIKTKTQMQKE
CCCHHHHHHHHHHHH
37.3426074081
808PhosphorylationPKSIKTKTQMQKELL
CHHHHHHHHHHHHHH
34.2120044836
810PhosphorylationSIKTKTQMQKELLDT
HHHHHHHHHHHHHHH
8.12-
817PhosphorylationMQKELLDTELDLYKK
HHHHHHHHHHHHHHH
38.1220068231
819PhosphorylationKELLDTELDLYKKMQ
HHHHHHHHHHHHHHH
6.2920068231
822PhosphorylationLDTELDLYKKMQAGE
HHHHHHHHHHHHCCH
14.2920068231
823AcetylationDTELDLYKKMQAGEE
HHHHHHHHHHHCCHH
49.4126051181
8242-HydroxyisobutyrylationTELDLYKKMQAGEEV
HHHHHHHHHHCCHHH
23.76-
824PhosphorylationTELDLYKKMQAGEEV
HHHHHHHHHHCCHHH
23.7620068231
825SulfoxidationELDLYKKMQAGEEVT
HHHHHHHHHCCHHHH
2.6321406390
825UbiquitinationELDLYKKMQAGEEVT
HHHHHHHHHCCHHHH
2.63-
838PhosphorylationVTELRRKYTELQLEA
HHHHHHHHHHHHHHH
12.0218083107
839PhosphorylationTELRRKYTELQLEAA
HHHHHHHHHHHHHHH
33.00-
839UbiquitinationTELRRKYTELQLEAA
HHHHHHHHHHHHHHH
33.00-
841PhosphorylationLRRKYTELQLEAAKR
HHHHHHHHHHHHHHC
5.62-
855MethylationRGILSSGRGRGIHSR
CCHHHCCCCCCCCCC
33.3218961539
857MethylationILSSGRGRGIHSRGR
HHHCCCCCCCCCCCC
39.2618961549
859MethylationSSGRGRGIHSRGRGA
HCCCCCCCCCCCCCC
2.28-
878MethylationGRGRGRGRGVPGHAV
CCCCCCCCCCCCCEE
41.3954558567
880MethylationGRGRGRGVPGHAVVD
CCCCCCCCCCCEEEC
5.03-
896PhosphorylationRPRALEISAFTESDR
CCCEEEEECCCHHHH
14.1426074081
899PhosphorylationALEISAFTESDREDL
EEEEECCCHHHHHHH
34.0126074081
901PhosphorylationEISAFTESDREDLLP
EEECCCHHHHHHHHH
38.6226074081

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
839TPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM26_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 RBM26_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPC9_HUMANCRCPphysical
22939629

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 RBM26_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-510, AND MASS SPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, 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-518 AND SER-616, ANDMASS 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-127, AND MASSSPECTROMETRY.
"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-616, 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-127, AND MASSSPECTROMETRY.

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