ARIP4_HUMAN - dbPTM
ARIP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARIP4_HUMAN
UniProt AC Q9Y4B4
Protein Name Helicase ARIP4
Gene Name RAD54L2
Organism Homo sapiens (Human).
Sequence Length 1467
Subcellular Localization Nucleus. Localizes in speckle-like nuclear compartments..
Protein Description DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro (By similarity)..
Protein Sequence MSDESASGSDPDLDPDVELEDAEEEEEEEEVAVEECDRDDEEDLLDDPSLEGMCGTEHAQLGEDGQQPPRCTSTTSSQSEPSEQLRRHQGKNLASEDPKKKRAQKPSHMRRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSSGSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALGRVLVNLNHPPEEENVFLAPQLARAVKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALPADNKPEEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTLKKSFATGRPKKTKKRSHPVIIDLDEEDRQQEFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRDLYTQFMDRFRDCGSSGWLGLNPLKAFCVCCKIWNHPDVLYEALQKESLANEQDLDVEELGSAGTSARCPPQGTKGKGEDSTLASSMGEATNSKFLQGVGFNPFQERGNNIVTYEWAKDLLTNYQTGVLENSPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKREVPCPPGTEGQGAQKWVRNISYFRLDGSTPAFERERLINQFNDPSNLTTWLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVDDLNPMLNFTRKEVENLLHFVEKEPAPQVSLNVKGIKESVLQLACLKYPHLITKEPFEHESLLLNRKDHKLTKAEKKAAKKSYEEDKRTSVPYTRPSYAQYYPASDQSLTSIPAFSQRNWQPTLKGDEKPVASVRPVQSTPIPMMPRHVPLGGSVSSASSTNPSMNFPINYLQRAGVLVQKVVTTTDIVIPGLNSSTDVQARINAGESIHIIRGTKGTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQGPSCESTSNGRHSASSPKAPDPEGLARPVSPDSPEIISELQQYADVAAARESRQSSPSTNAALPGPPAQLMDSSAVPGTALGTEPRLGGHCLNSSLLVTGQPCGDRHPVLDLRGHKRKLATPPAAQESSRRRSRKGHLPAPVQPYEHGYPVSGGFAMPPVSLNHNLTTPFTSQAGENSLFMGSTPSYYQLSNLLADARLVFPVTTDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGILPSYSLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMSIYPGYMSPHAGYPAGGLLRSQVPPFDSHEVAEVGFSSNDDEDKDDDVIEVTGK
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
72PhosphorylationGQQPPRCTSTTSSQS
CCCCCCCCCCCCCCC
30.3225884760
73PhosphorylationQQPPRCTSTTSSQSE
CCCCCCCCCCCCCCC
33.0625850435
74PhosphorylationQPPRCTSTTSSQSEP
CCCCCCCCCCCCCCH
16.7325850435
75PhosphorylationPPRCTSTTSSQSEPS
CCCCCCCCCCCCCHH
26.5825850435
76PhosphorylationPRCTSTTSSQSEPSE
CCCCCCCCCCCCHHH
26.8630257219
77PhosphorylationRCTSTTSSQSEPSEQ
CCCCCCCCCCCHHHH
35.3223312004
79PhosphorylationTSTTSSQSEPSEQLR
CCCCCCCCCHHHHHH
54.1222817900
82PhosphorylationTSSQSEPSEQLRRHQ
CCCCCCHHHHHHHHC
33.6423312004
115SumoylationHMRRNIRKLLREDQL
HHHHHHHHHHHHHCC
48.34-
115SumoylationHMRRNIRKLLREDQL
HHHHHHHHHHHHHCC
48.3428112733
115UbiquitinationHMRRNIRKLLREDQL
HHHHHHHHHHHHHCC
48.34-
127SumoylationDQLEPVTKAAQQEEL
HCCHHHHHHHHHHHH
41.79-
127SumoylationDQLEPVTKAAQQEEL
HCCHHHHHHHHHHHH
41.7928112733
127UbiquitinationDQLEPVTKAAQQEEL
HCCHHHHHHHHHHHH
41.79-
147PhosphorylationLEQQRKDYAAPIPTV
HHHHHHHHCCCCCCC
14.01-
187PhosphorylationQEVICLDSSSGSEDE
EEEEEECCCCCCCCC
17.2922817900
188PhosphorylationEVICLDSSSGSEDEK
EEEEECCCCCCCCCC
38.0822817900
189PhosphorylationVICLDSSSGSEDEKS
EEEECCCCCCCCCCC
50.7422817900
191PhosphorylationCLDSSSGSEDEKSSR
EECCCCCCCCCCCCH
43.7722817900
272SumoylationPQLARAVKPHQIGGI
HHHHHHCCHHHCCCC
35.48-
272SumoylationPQLARAVKPHQIGGI
HHHHHHCCHHHCCCC
35.4828112733
272UbiquitinationPQLARAVKPHQIGGI
HHHHHHCCHHHCCCC
35.48-
372UbiquitinationEVQPRFFKVHILNDE
HHCCCEEEEEECCHH
30.14-
381UbiquitinationHILNDEHKTMASRAK
EECCHHHCHHHHHHH
37.64-
395PhosphorylationKVMADWVSEGGVLLM
HHHHHHHHHCCEEEE
26.6925332170
404PhosphorylationGGVLLMGYEMYRLLT
CCEEEEEHHHHHHHH
5.42-
407PhosphorylationLLMGYEMYRLLTLKK
EEEEHHHHHHHHHHH
6.03-
411PhosphorylationYEMYRLLTLKKSFAT
HHHHHHHHHHHHHHC
40.9221964256
414UbiquitinationYRLLTLKKSFATGRP
HHHHHHHHHHHCCCC
54.65-
418PhosphorylationTLKKSFATGRPKKTK
HHHHHHHCCCCCCCC
31.5428787133
428PhosphorylationPKKTKKRSHPVIIDL
CCCCCCCCCCEEEEC
40.8128555341
450UbiquitinationEFRREFEKALCRPGP
HHHHHHHHHHCCCCC
52.56-
469SumoylationCDEGHRIKNCQASTS
CCCCCCCCCCCCCHH
52.18-
469SumoylationCDEGHRIKNCQASTS
CCCCCCCCCCCCCHH
52.18-
469UbiquitinationCDEGHRIKNCQASTS
CCCCCCCCCCCCCHH
52.18-
480AcetylationASTSQALKNIRSRRR
CCHHHHHHHHHHCCC
54.0325953088
480UbiquitinationASTSQALKNIRSRRR
CCHHHHHHHHHHCCC
54.03-
483DimethylationSQALKNIRSRRRVVL
HHHHHHHHHCCCEEE
33.24-
483MethylationSQALKNIRSRRRVVL
HHHHHHHHHCCCEEE
33.2424380133
574UbiquitinationLKIHLPAKEENVILV
EEEECCCCCCCEEEE
64.72-
613UbiquitinationWLGLNPLKAFCVCCK
CCCCCHHHHHHHHHH
40.45-
620AcetylationKAFCVCCKIWNHPDV
HHHHHHHHHHCCHHH
45.7025953088
620UbiquitinationKAFCVCCKIWNHPDV
HHHHHHHHHHCCHHH
45.70-
634UbiquitinationVLYEALQKESLANEQ
HHHHHHHHHHHCCCC
50.55-
636PhosphorylationYEALQKESLANEQDL
HHHHHHHHHCCCCCC
39.5621406692
650PhosphorylationLDVEELGSAGTSARC
CCHHHHHCCCCCCCC
35.8321406692
653PhosphorylationEELGSAGTSARCPPQ
HHHHCCCCCCCCCCC
20.9421406692
654PhosphorylationELGSAGTSARCPPQG
HHHCCCCCCCCCCCC
16.8821406692
662PhosphorylationARCPPQGTKGKGEDS
CCCCCCCCCCCCCCC
31.2321406692
663UbiquitinationRCPPQGTKGKGEDST
CCCCCCCCCCCCCCC
66.50-
665SumoylationPPQGTKGKGEDSTLA
CCCCCCCCCCCCCHH
61.76-
665SumoylationPPQGTKGKGEDSTLA
CCCCCCCCCCCCCHH
61.7628112733
665UbiquitinationPPQGTKGKGEDSTLA
CCCCCCCCCCCCCHH
61.7621906983
669PhosphorylationTKGKGEDSTLASSMG
CCCCCCCCCHHHHHC
22.4823312004
670PhosphorylationKGKGEDSTLASSMGE
CCCCCCCCHHHHHCH
38.3723312004
673PhosphorylationGEDSTLASSMGEATN
CCCCCHHHHHCHHHC
24.7828450419
674PhosphorylationEDSTLASSMGEATNS
CCCCHHHHHCHHHCC
25.7928450419
679PhosphorylationASSMGEATNSKFLQG
HHHHCHHHCCHHCCC
35.4023312004
681PhosphorylationSMGEATNSKFLQGVG
HHCHHHCCHHCCCCC
22.0423312004
682SumoylationMGEATNSKFLQGVGF
HCHHHCCHHCCCCCC
52.7628112733
682UbiquitinationMGEATNSKFLQGVGF
HCHHHCCHHCCCCCC
52.7621906983
706UbiquitinationIVTYEWAKDLLTNYQ
CEEHHHHHHHHHHHC
50.40-
759SumoylationLIEEFLGKREVPCPP
HHHHHHCCCCCCCCC
47.75-
759SumoylationLIEEFLGKREVPCPP
HHHHHHCCCCCCCCC
47.7528112733
775UbiquitinationTEGQGAQKWVRNISY
CCCCCHHHHHHEEEE
47.31-
781PhosphorylationQKWVRNISYFRLDGS
HHHHHEEEEEEECCC
23.0522210691
782PhosphorylationKWVRNISYFRLDGST
HHHHEEEEEEECCCC
6.7422210691
788PhosphorylationSYFRLDGSTPAFERE
EEEEECCCCCHHHHH
30.7722210691
789PhosphorylationYFRLDGSTPAFERER
EEEECCCCCHHHHHH
24.9422210691
856UbiquitinationRVYRYGQKKPCYIYR
HHHHCCCCCCEEEEE
55.08-
857UbiquitinationVYRYGQKKPCYIYRL
HHHCCCCCCEEEEEE
32.22-
872UbiquitinationVADYTLEKKIYDRQI
CCCCCHHHHHHCHHH
47.81-
873UbiquitinationADYTLEKKIYDRQIS
CCCCHHHHHHCHHHH
36.80-
875PhosphorylationYTLEKKIYDRQISKQ
CCHHHHHHCHHHHHC
17.6024719451
880PhosphorylationKIYDRQISKQGMSDR
HHHCHHHHHCCCCHH
15.5824719451
881AcetylationIYDRQISKQGMSDRV
HHCHHHHHCCCCHHH
53.1225953088
881UbiquitinationIYDRQISKQGMSDRV
HHCHHHHHCCCCHHH
53.12-
885PhosphorylationQISKQGMSDRVVDDL
HHHHCCCCHHHHHCC
29.1424719451
899PhosphorylationLNPMLNFTRKEVENL
CHHHHCCCHHHHHHH
39.49-
901SumoylationPMLNFTRKEVENLLH
HHHCCCHHHHHHHHH
64.15-
901SumoylationPMLNFTRKEVENLLH
HHHCCCHHHHHHHHH
64.1528112733
901UbiquitinationPMLNFTRKEVENLLH
HHHCCCHHHHHHHHH
64.15-
912UbiquitinationNLLHFVEKEPAPQVS
HHHHHHHCCCCCCEE
64.79-
923UbiquitinationPQVSLNVKGIKESVL
CCEEECCCCHHHHHH
54.57-
926SumoylationSLNVKGIKESVLQLA
EECCCCHHHHHHHHH
53.24-
926SumoylationSLNVKGIKESVLQLA
EECCCCHHHHHHHHH
53.24-
926UbiquitinationSLNVKGIKESVLQLA
EECCCCHHHHHHHHH
53.24-
936UbiquitinationVLQLACLKYPHLITK
HHHHHHHHCCCCCCC
57.53-
943UbiquitinationKYPHLITKEPFEHES
HCCCCCCCCCCCCHH
57.29-
956UbiquitinationESLLLNRKDHKLTKA
HHHHHHHHCHHCHHH
64.21-
971PhosphorylationEKKAAKKSYEEDKRT
HHHHHHHHHHHHHCC
36.7520068231
972PhosphorylationKKAAKKSYEEDKRTS
HHHHHHHHHHHHCCC
32.0222817900
982PhosphorylationDKRTSVPYTRPSYAQ
HHCCCCCCCCCCHHH
17.1522817900
1014SumoylationRNWQPTLKGDEKPVA
CCCCCCCCCCCCCCC
67.79-
1014SumoylationRNWQPTLKGDEKPVA
CCCCCCCCCCCCCCC
67.7928112733
1018SumoylationPTLKGDEKPVASVRP
CCCCCCCCCCCEEEC
49.92-
1018AcetylationPTLKGDEKPVASVRP
CCCCCCCCCCCEEEC
49.9225953088
1018SumoylationPTLKGDEKPVASVRP
CCCCCCCCCCCEEEC
49.9228112733
1022PhosphorylationGDEKPVASVRPVQST
CCCCCCCEEECCCCC
20.9224719451
1028PhosphorylationASVRPVQSTPIPMMP
CEEECCCCCCCCCCC
36.0626074081
1029PhosphorylationSVRPVQSTPIPMMPR
EEECCCCCCCCCCCC
14.2429507054
1049PhosphorylationGSVSSASSTNPSMNF
CCCCCCCCCCCCCCC
31.7428555341
1073O-linked_GlycosylationVLVQKVVTTTDIVIP
CEEEEEEECCCEEEC
27.2823301498
1074O-linked_GlycosylationLVQKVVTTTDIVIPG
EEEEEEECCCEEECC
15.7423301498
1075O-linked_GlycosylationVQKVVTTTDIVIPGL
EEEEEECCCEEECCC
17.8623301498
1085O-linked_GlycosylationVIPGLNSSTDVQARI
EECCCCCCCCHHHHH
27.7923301498
1105UbiquitinationIHIIRGTKGTYIRTS
EEEEECCCCEEEECC
52.67-
1107PhosphorylationIIRGTKGTYIRTSDG
EEECCCCEEEECCCC
19.8223532336
1108PhosphorylationIRGTKGTYIRTSDGR
EECCCCEEEECCCCC
9.3223532336
1124UbiquitinationFAVRATGKPKVPEDG
EEEEECCCCCCCCCC
36.9921906983
1126UbiquitinationVRATGKPKVPEDGRM
EEECCCCCCCCCCCC
74.1221906983
1136PhosphorylationEDGRMAASGSQGPSC
CCCCCCCCCCCCCCC
29.46-
1138PhosphorylationGRMAASGSQGPSCES
CCCCCCCCCCCCCCC
29.4817525332
1142PhosphorylationASGSQGPSCESTSNG
CCCCCCCCCCCCCCC
37.0229449344
1145PhosphorylationSQGPSCESTSNGRHS
CCCCCCCCCCCCCCC
41.2727251789
1146PhosphorylationQGPSCESTSNGRHSA
CCCCCCCCCCCCCCC
12.1529449344
1147PhosphorylationGPSCESTSNGRHSAS
CCCCCCCCCCCCCCC
46.7129449344
1152PhosphorylationSTSNGRHSASSPKAP
CCCCCCCCCCCCCCC
28.6023898821
1154PhosphorylationSNGRHSASSPKAPDP
CCCCCCCCCCCCCCC
50.6328348404
1155PhosphorylationNGRHSASSPKAPDPE
CCCCCCCCCCCCCCC
30.0923898821
1169PhosphorylationEGLARPVSPDSPEII
CCCCCCCCCCCHHHH
26.1826503892
1172PhosphorylationARPVSPDSPEIISEL
CCCCCCCCHHHHHHH
28.0226503892
1177PhosphorylationPDSPEIISELQQYAD
CCCHHHHHHHHHHHH
37.6021955146
1182PhosphorylationIISELQQYADVAAAR
HHHHHHHHHHHHHHH
7.5720068231
1191PhosphorylationDVAAARESRQSSPST
HHHHHHHHHHCCCCC
30.0226074081
1194PhosphorylationAARESRQSSPSTNAA
HHHHHHHCCCCCCCC
43.0130108239
1195PhosphorylationARESRQSSPSTNAAL
HHHHHHCCCCCCCCC
17.9630108239
1197PhosphorylationESRQSSPSTNAALPG
HHHHCCCCCCCCCCC
35.9225022875
1198PhosphorylationSRQSSPSTNAALPGP
HHHCCCCCCCCCCCC
32.0625022875
1212PhosphorylationPPAQLMDSSAVPGTA
CCHHHCCCCCCCCCC
13.2628450419
1213PhosphorylationPAQLMDSSAVPGTAL
CHHHCCCCCCCCCCC
29.0819690332
1218PhosphorylationDSSAVPGTALGTEPR
CCCCCCCCCCCCCCC
16.7928450419
1222PhosphorylationVPGTALGTEPRLGGH
CCCCCCCCCCCCCCC
43.6026074081
1233PhosphorylationLGGHCLNSSLLVTGQ
CCCCCCCCCEEEECC
14.9324247654
1245MethylationTGQPCGDRHPVLDLR
ECCCCCCCCCEECCC
22.69115490147
1252MethylationRHPVLDLRGHKRKLA
CCCEECCCCCCCCCC
44.85115490139
1260PhosphorylationGHKRKLATPPAAQES
CCCCCCCCCHHHHHH
40.0029255136
1267PhosphorylationTPPAAQESSRRRSRK
CCHHHHHHHHHHCCC
19.6423882029
1268PhosphorylationPPAAQESSRRRSRKG
CHHHHHHHHHHCCCC
29.1122210691
1272PhosphorylationQESSRRRSRKGHLPA
HHHHHHHCCCCCCCC
36.2123882029
1395MethylationQPLLSEPRMFAPFPS
CCCCCCCCEECCCCC
28.8883108711
1414PhosphorylationSNLSRGMSIYPGYMS
CCCCCCCCCCCCCCC
23.0728450419
1416PhosphorylationLSRGMSIYPGYMSPH
CCCCCCCCCCCCCCC
5.3629978859
1419PhosphorylationGMSIYPGYMSPHAGY
CCCCCCCCCCCCCCC
7.0128450419
1421PhosphorylationSIYPGYMSPHAGYPA
CCCCCCCCCCCCCCC
12.6822115753
1426PhosphorylationYMSPHAGYPAGGLLR
CCCCCCCCCCCCCHH
7.2422199227
1433MethylationYPAGGLLRSQVPPFD
CCCCCCHHCCCCCCC
30.0481424337
1434PhosphorylationPAGGLLRSQVPPFDS
CCCCCHHCCCCCCCC
35.1829449344
1441PhosphorylationSQVPPFDSHEVAEVG
CCCCCCCCCCCCEEC
23.1729449344
1450PhosphorylationEVAEVGFSSNDDEDK
CCCEECCCCCCCCCC
23.4629523821
1451PhosphorylationVAEVGFSSNDDEDKD
CCEECCCCCCCCCCC
41.8529523821
1465PhosphorylationDDDVIEVTGK-----
CCCCEEECCC-----
26.8529449344

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 ARIP4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARIP4_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 ARIP4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANDR_HUMANARphysical
16212558
UBC9_HUMANUBE2Iphysical
16212558
STF1_HUMANNR5A1physical
19692572
NR5A2_HUMANNR5A2physical
19692572
ANDR_HUMANARphysical
19692572
PIAS1_HUMANPIAS1physical
19692572
GCR_HUMANNR3C1physical
19692572
PPARG_HUMANPPARGphysical
19692572
RXRA_HUMANRXRAphysical
19692572
FUBP2_HUMANKHSRPphysical
26344197
CNOT7_HUMANCNOT7physical
21516116
TAXB1_HUMANTAX1BP1physical
21516116
DYR1A_HUMANDYRK1Aphysical
26412716
SQSTM_HUMANSQSTM1physical
26412716
DCAF7_HUMANDCAF7physical
26412716

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 ARIP4_HUMAN

loading...

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-1169 AND SER-1172, ANDMASS 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-1169 AND SER-1172, ANDMASS SPECTROMETRY.
"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-1138, 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-187; SER-188; SER-189;SER-191; SER-1169 AND SER-1172, 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 THR-1260, AND MASSSPECTROMETRY.

TOP