LRRF1_HUMAN - dbPTM
LRRF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRF1_HUMAN
UniProt AC Q32MZ4
Protein Name Leucine-rich repeat flightless-interacting protein 1
Gene Name LRRFIP1
Organism Homo sapiens (Human).
Sequence Length 808
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding..
Protein Sequence MTSPAAAQSREIDCLSPEAQKLAEARLAAKRAARAEAREIRMKELERQQKEEDSERYSRRSRRNTSASDEDERMSVGSRGSLRVEERPEKDFTEKGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALKSTGDGTLGRASEVEVKNEIVANVGKREILHNTEKEQHTEDTVKDCVDIEVFPAGENTEDQKSSEDTAPFLGTLAGATYEEQVQSQILESSSLPENTVQVESNEVMGAPDDRTRTPLEPSNCWSDLDGGNHTENVGEAAVTQVEEQAGTVASCPLGHSDDTVYHDDKCMVEVPQELETSTGHSLEKEFTNQEAAEPKEVPAHSTEVGRDHNEEEGEETGLRDEKPIKTEVPGSPAGTEGNCQEATGPSTVDTQNEPLDMKEPDEEKSDQQGEALDSSQKKTKNKKKKNKKKKSPVPVETLKDVKKELTYQNTDLSEIKEEEQVKSTDRKSAVEAQNEVTENPKQKIAAESSENVDCPENPKIKLDGKLDQEGDDVQTAAEEVLADGDTLDFEDDTVQSSGPRAGGEELDEGVAKDNAKIDGATQSSPAEPKSEDADRCTLPEHESPSQDISDACEAESTERCEMSEHPSQTVRKALDSNSLENDDLSAPGREPGHFNPESREDTRGGNEKGKSKEDCTMS
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------MTSPAAAQS
------CCCHHHHHC
43.3420068231
2Phosphorylation------MTSPAAAQS
------CCCHHHHHC
43.3429255136
2 (in isoform 2)Acetylation-43.34-
2 (in isoform 2)Phosphorylation-43.34-
3Phosphorylation-----MTSPAAAQSR
-----CCCHHHHHCC
15.9629255136
3 (in isoform 2)Phosphorylation-15.96-
5 (in isoform 4)Phosphorylation-18.3928348404
8 (in isoform 4)Phosphorylation-37.9928348404
9PhosphorylationTSPAAAQSREIDCLS
CCHHHHHCCCCCCCC
27.4426074081
14CarbamidationAQSREIDCLSPEAQK
HHCCCCCCCCHHHHH
5.0717322306
16PhosphorylationSREIDCLSPEAQKLA
CCCCCCCCHHHHHHH
27.3329255136
16 (in isoform 2)Phosphorylation-27.3324719451
20 (in isoform 4)Phosphorylation-39.3728348404
21UbiquitinationCLSPEAQKLAEARLA
CCCHHHHHHHHHHHH
57.63-
57PhosphorylationKEEDSERYSRRSRRN
HHHHHHHHHHHHHCC
11.5028258704
58PhosphorylationEEDSERYSRRSRRNT
HHHHHHHHHHHHCCC
27.6928258704
65PhosphorylationSRRSRRNTSASDEDE
HHHHHCCCCCCCHHH
24.6925159151
66PhosphorylationRRSRRNTSASDEDER
HHHHCCCCCCCHHHH
29.3525159151
66 (in isoform 2)Phosphorylation-29.3524719451
68PhosphorylationSRRNTSASDEDERMS
HHCCCCCCCHHHHCC
41.1028355574
68 (in isoform 2)Phosphorylation-41.1024719451
75PhosphorylationSDEDERMSVGSRGSL
CCHHHHCCCCCCCCC
29.5530108239
78PhosphorylationDERMSVGSRGSLRVE
HHHCCCCCCCCCCCC
31.1728450419
81PhosphorylationMSVGSRGSLRVEERP
CCCCCCCCCCCCCCC
16.3427251275
88 (in isoform 3)Phosphorylation-57.1628258704
90 (in isoform 4)Phosphorylation-61.91-
91 (in isoform 3)Phosphorylation-54.7825849741
92 (in isoform 3)Phosphorylation-16.4028258704
97PhosphorylationKDFTEKGSRNMPGLS
CCCCCCCCCCCCCCC
31.3926074081
97 (in isoform 4)Phosphorylation-31.3925159151
98 (in isoform 4)Phosphorylation-52.7329507054
100SulfoxidationTEKGSRNMPGLSAAT
CCCCCCCCCCCCHHH
2.4321406390
104PhosphorylationSRNMPGLSAATLASL
CCCCCCCCHHHHHHC
23.0523927012
107PhosphorylationMPGLSAATLASLGGT
CCCCCHHHHHHCCCC
23.6729255136
107 (in isoform 2)Phosphorylation-23.6724719451
110PhosphorylationLSAATLASLGGTSSR
CCHHHHHHCCCCCCC
30.5729255136
110 (in isoform 2)Phosphorylation-30.5724719451
114PhosphorylationTLASLGGTSSRRGSG
HHHHCCCCCCCCCCC
23.0229255136
114 (in isoform 2)Phosphorylation-23.0221406692
115PhosphorylationLASLGGTSSRRGSGD
HHHCCCCCCCCCCCC
25.7329255136
115 (in isoform 2)Phosphorylation-25.7321406692
116PhosphorylationASLGGTSSRRGSGDT
HHCCCCCCCCCCCCC
26.3229255136
116 (in isoform 2)Phosphorylation-26.32-
120PhosphorylationGTSSRRGSGDTSISI
CCCCCCCCCCCCEEE
31.5119664994
120 (in isoform 2)Phosphorylation-31.5124719451
123PhosphorylationSRRGSGDTSISIDTE
CCCCCCCCCEEECCH
31.3325159151
123 (in isoform 2)Phosphorylation-31.3325849741
124PhosphorylationRRGSGDTSISIDTEA
CCCCCCCCEEECCHH
21.0525159151
124 (in isoform 2)Phosphorylation-21.0528258704
126PhosphorylationGSGDTSISIDTEASI
CCCCCCEEECCHHHH
17.7430278072
126 (in isoform 2)Phosphorylation-17.74-
129PhosphorylationDTSISIDTEASIREI
CCCEEECCHHHHHHH
31.6123927012
132PhosphorylationISIDTEASIREIKEL
EEECCHHHHHHHHHH
18.8823663014
139 (in isoform 4)Phosphorylation-5.2530183078
141 (in isoform 4)Phosphorylation-70.5830183078
170UbiquitinationSLAEVEEKYKKAMVS
HHHHHHHHHHHHHHH
49.19-
173UbiquitinationEVEEKYKKAMVSNAQ
HHHHHHHHHHHHCCC
38.33-
175SulfoxidationEEKYKKAMVSNAQLD
HHHHHHHHHHCCCCC
4.6921406390
185TrimethylationNAQLDNEKTNFMYQV
CCCCCCCCCCCHHHH
55.83-
185MethylationNAQLDNEKTNFMYQV
CCCCCCCCCCCHHHH
55.83-
187 (in isoform 4)Phosphorylation-30.6526437602
197 (in isoform 4)Phosphorylation-35.7526437602
198SulfoxidationQVDTLKDMLLELEEQ
HHHHHHHHHHHHHHH
4.3830846556
204 (in isoform 4)Phosphorylation-64.6222468782
205 (in isoform 4)Phosphorylation-36.2826437602
209 (in isoform 4)Phosphorylation-27.4428387310
228PhosphorylationEREKHAHSILQFQFA
HHHHHHHHHHHHHHH
26.2727251275
271 (in isoform 2)Phosphorylation-31.53-
280SulfoxidationGYQGPTKMTKEELNA
CCCCCCCCCHHHHHH
7.7221406390
289UbiquitinationKEELNALKSTGDGTL
HHHHHHHHHCCCCCC
43.49-
290PhosphorylationEELNALKSTGDGTLG
HHHHHHHHCCCCCCC
38.1729214152
291PhosphorylationELNALKSTGDGTLGR
HHHHHHHCCCCCCCC
37.3929214152
295PhosphorylationLKSTGDGTLGRASEV
HHHCCCCCCCCCCEE
30.6825159151
300PhosphorylationDGTLGRASEVEVKNE
CCCCCCCCEEEECHH
40.5928355574
305SumoylationRASEVEVKNEIVANV
CCCEEEECHHHEEEC
35.0425114211
314AcetylationEIVANVGKREILHNT
HHEEECCHHHHHCCC
42.4425953088
314UbiquitinationEIVANVGKREILHNT
HHEEECCHHHHHCCC
42.44-
321PhosphorylationKREILHNTEKEQHTE
HHHHHCCCCCCCCCC
37.3729514088
3232-HydroxyisobutyrylationEILHNTEKEQHTEDT
HHHCCCCCCCCCCCH
61.71-
366PhosphorylationLGTLAGATYEEQVQS
HHHHCCCCHHHHHHH
30.4627251275
367PhosphorylationGTLAGATYEEQVQSQ
HHHCCCCHHHHHHHH
19.5527251275
373PhosphorylationTYEEQVQSQILESSS
CHHHHHHHHHHHCCC
21.9727251275
378PhosphorylationVQSQILESSSLPENT
HHHHHHHCCCCCCCE
23.0627251275
379PhosphorylationQSQILESSSLPENTV
HHHHHHCCCCCCCEE
26.9027251275
380PhosphorylationSQILESSSLPENTVQ
HHHHHCCCCCCCEEE
58.1727251275
394 (in isoform 4)Phosphorylation-2.8620068231
399 (in isoform 4)Phosphorylation-53.4420068231
401PhosphorylationMGAPDDRTRTPLEPS
CCCCCCCCCCCCCCC
45.9826074081
403PhosphorylationAPDDRTRTPLEPSNC
CCCCCCCCCCCCCCC
31.4526074081
408PhosphorylationTRTPLEPSNCWSDLD
CCCCCCCCCCCCCCC
34.9326074081
412PhosphorylationLEPSNCWSDLDGGNH
CCCCCCCCCCCCCCC
30.4226074081
451PhosphorylationGHSDDTVYHDDKCMV
CCCCCCCCCCCEEEE
11.13-
466PhosphorylationEVPQELETSTGHSLE
ECCCHHHHCCCCCHH
44.1825159151
467PhosphorylationVPQELETSTGHSLEK
CCCHHHHCCCCCHHH
24.0225159151
468PhosphorylationPQELETSTGHSLEKE
CCHHHHCCCCCHHHH
46.4625159151
471PhosphorylationLETSTGHSLEKEFTN
HHHCCCCCHHHHHCC
39.3025159151
477O-linked_GlycosylationHSLEKEFTNQEAAEP
CCHHHHHCCCCCCCC
36.7623301498
491PhosphorylationPKEVPAHSTEVGRDH
CCCCCCCCCCCCCCC
28.5025627689
497 (in isoform 2)Phosphorylation-42.93-
506PhosphorylationNEEEGEETGLRDEKP
CHHHCCCCCCCCCCC
36.8926074081
516PhosphorylationRDEKPIKTEVPGSPA
CCCCCCEEECCCCCC
42.8223927012
521PhosphorylationIKTEVPGSPAGTEGN
CEEECCCCCCCCCCC
12.9028355574
525PhosphorylationVPGSPAGTEGNCQEA
CCCCCCCCCCCCCCC
42.7123927012
531 (in isoform 2)Phosphorylation-50.8521406692
533PhosphorylationEGNCQEATGPSTVDT
CCCCCCCCCCCCCCC
49.2025159151
536PhosphorylationCQEATGPSTVDTQNE
CCCCCCCCCCCCCCC
42.2722199227
537PhosphorylationQEATGPSTVDTQNEP
CCCCCCCCCCCCCCC
26.0721815630
540PhosphorylationTGPSTVDTQNEPLDM
CCCCCCCCCCCCCCC
29.0222199227
540 (in isoform 2)Phosphorylation-29.02-
541 (in isoform 2)Phosphorylation-48.07-
555PhosphorylationKEPDEEKSDQQGEAL
CCCCHHHCHHHHHHH
43.8819664994
557 (in isoform 2)Phosphorylation-61.3424719451
559 (in isoform 4)Phosphorylation-19.26-
563 (in isoform 2)Phosphorylation-53.98-
564PhosphorylationQQGEALDSSQKKTKN
HHHHHHHHHHHHHHC
35.2023401153
565PhosphorylationQGEALDSSQKKTKNK
HHHHHHHHHHHHHCH
45.7625159151
568AcetylationALDSSQKKTKNKKKK
HHHHHHHHHHCHHHC
58.03130861
570AcetylationDSSQKKTKNKKKKNK
HHHHHHHHCHHHCCC
75.54130863
575 (in isoform 4)Phosphorylation-80.85-
578 (in isoform 4)Phosphorylation-74.87-
581PhosphorylationKKNKKKKSPVPVETL
HCCCCCCCCCCHHHH
39.7525159151
587PhosphorylationKSPVPVETLKDVKKE
CCCCCHHHHHHHHHH
39.0622199227
589UbiquitinationPVPVETLKDVKKELT
CCCHHHHHHHHHHHH
68.82-
592AcetylationVETLKDVKKELTYQN
HHHHHHHHHHHHCCC
51.1425953088
593UbiquitinationETLKDVKKELTYQNT
HHHHHHHHHHHCCCC
58.78-
594 (in isoform 2)Phosphorylation-40.4024719451
596PhosphorylationKDVKKELTYQNTDLS
HHHHHHHHCCCCCHH
24.9326356563
597PhosphorylationDVKKELTYQNTDLSE
HHHHHHHCCCCCHHH
16.6425159151
600PhosphorylationKELTYQNTDLSEIKE
HHHHCCCCCHHHHHH
23.8526356563
603PhosphorylationTYQNTDLSEIKEEEQ
HCCCCCHHHHHHHHH
39.8321815630
606SumoylationNTDLSEIKEEEQVKS
CCCHHHHHHHHHHCC
55.8328112733
606UbiquitinationNTDLSEIKEEEQVKS
CCCHHHHHHHHHHCC
55.83-
613PhosphorylationKEEEQVKSTDRKSAV
HHHHHHCCCCHHHHH
36.3623403867
614PhosphorylationEEEQVKSTDRKSAVE
HHHHHCCCCHHHHHH
33.8223403867
614 (in isoform 2)Phosphorylation-33.8224719451
618PhosphorylationVKSTDRKSAVEAQNE
HCCCCHHHHHHHHHH
38.1429255136
627PhosphorylationVEAQNEVTENPKQKI
HHHHHHHCCCHHHHH
24.7027251275
633UbiquitinationVTENPKQKIAAESSE
HCCCHHHHHHHHCCC
40.20-
634 (in isoform 4)Phosphorylation-3.9922199227
638PhosphorylationKQKIAAESSENVDCP
HHHHHHHCCCCCCCC
37.9230278072
639PhosphorylationQKIAAESSENVDCPE
HHHHHHCCCCCCCCC
25.3730278072
644GlutathionylationESSENVDCPENPKIK
HCCCCCCCCCCCCCE
3.8722555962
649UbiquitinationVDCPENPKIKLDGKL
CCCCCCCCCEECCCC
65.14-
652 (in isoform 2)Phosphorylation-13.79-
663 (in isoform 2)Phosphorylation-6.92-
665PhosphorylationQEGDDVQTAAEEVLA
CCCCHHHHHHHHHHC
27.9027499020
676PhosphorylationEVLADGDTLDFEDDT
HHHCCCCEECCCCCC
33.4818669648
687PhosphorylationEDDTVQSSGPRAGGE
CCCCCCCCCCCCCCC
35.4118669648
687 (in isoform 2)Phosphorylation-35.4121406692
689 (in isoform 2)Phosphorylation-25.5421406692
690 (in isoform 2)Phosphorylation-49.7624719451
709 (in isoform 2)Phosphorylation-33.7124719451
711PhosphorylationNAKIDGATQSSPAEP
CCCCCCCCCCCCCCC
34.2223927012
711 (in isoform 2)Phosphorylation-34.2224719451
713PhosphorylationKIDGATQSSPAEPKS
CCCCCCCCCCCCCCC
33.6529255136
714PhosphorylationIDGATQSSPAEPKSE
CCCCCCCCCCCCCCC
20.5019664994
720PhosphorylationSSPAEPKSEDADRCT
CCCCCCCCCCCCCCC
51.9623401153
725MethylationPKSEDADRCTLPEHE
CCCCCCCCCCCCCCC
19.62115482327
726CarbamidationKSEDADRCTLPEHES
CCCCCCCCCCCCCCC
4.7617322306
727PhosphorylationSEDADRCTLPEHESP
CCCCCCCCCCCCCCC
46.3630266825
733PhosphorylationCTLPEHESPSQDISD
CCCCCCCCCCCCHHH
31.5829255136
735PhosphorylationLPEHESPSQDISDAC
CCCCCCCCCCHHHHH
50.1729255136
739PhosphorylationESPSQDISDACEAES
CCCCCCHHHHHHHHH
27.6930266825
742CarbamidationSQDISDACEAESTER
CCCHHHHHHHHHCCC
6.4617322306
742 (in isoform 2)Phosphorylation-6.4624719451
744 (in isoform 2)Phosphorylation-18.8724719451
746PhosphorylationSDACEAESTERCEMS
HHHHHHHHCCCCCCC
42.4923927012
747PhosphorylationDACEAESTERCEMSE
HHHHHHHCCCCCCCC
20.9624702127
753PhosphorylationSTERCEMSEHPSQTV
HCCCCCCCCCHHHHH
15.51-
757PhosphorylationCEMSEHPSQTVRKAL
CCCCCCHHHHHHHHH
40.1520068231
759PhosphorylationMSEHPSQTVRKALDS
CCCCHHHHHHHHHHC
26.9820068231
762UbiquitinationHPSQTVRKALDSNSL
CHHHHHHHHHHCCCC
49.30-
766PhosphorylationTVRKALDSNSLENDD
HHHHHHHCCCCCCCC
29.2129255136
768PhosphorylationRKALDSNSLENDDLS
HHHHHCCCCCCCCCC
40.8029255136
775PhosphorylationSLENDDLSAPGREPG
CCCCCCCCCCCCCCC
39.1423927012
788PhosphorylationPGHFNPESREDTRGG
CCCCCCCCCCCCCCC
42.0820873877

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 LRRF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRF1_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 LRRF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLII_HUMANFLIIphysical
9525888
FLII_HUMANFLIIphysical
19265123
CN166_HUMANC14orf166physical
22863883
RTCB_HUMANRTCBphysical
22863883
DDX1_HUMANDDX1physical
22863883
DHX9_HUMANDHX9physical
22863883
SYEP_HUMANEPRSphysical
22863883
FLII_HUMANFLIIphysical
22863883
MRE11_HUMANMRE11Aphysical
22863883
PRKDC_HUMANPRKDCphysical
22863883
RFC2_HUMANRFC2physical
22863883
MED4_HUMANMED4physical
25416956
CEP44_HUMANCEP44physical
25416956
TMOD3_HUMANTMOD3physical
28514442
TMOD1_HUMANTMOD1physical
28514442
FLII_HUMANFLIIphysical
28514442
TFR2_HUMANTFR2physical
28514442
CCNB1_HUMANCCNB1physical
28514442
TCAL2_HUMANTCEAL2physical
28514442
MCTS1_HUMANMCTS1physical
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 LRRF1_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-115; SER-120 ANDSER-618, 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-116; SER-638; THR-711;SER-713 AND SER-714, 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-16; SER-120; SER-124;SER-581; SER-618; THR-676; SER-714 AND SER-733, 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-714, 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-16, 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-733, AND MASSSPECTROMETRY.
"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-521 AND SER-714, ANDMASS 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 THR-295, AND MASSSPECTROMETRY.

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