NU188_HUMAN - dbPTM
NU188_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU188_HUMAN
UniProt AC Q5SRE5
Protein Name Nucleoporin NUP188 homolog
Gene Name NUP188
Organism Homo sapiens (Human).
Sequence Length 1749
Subcellular Localization Nucleus, nuclear pore complex .
Protein Description May function as a component of the nuclear pore complex (NPC)..
Protein Sequence MAAAAGGPCVRSSRELWTILLGRSALRELSQIEAELNKHWRRLLEGLSYYKPPSPSSAEKVKANKDVASPLKELGLRISKFLGLDEEQSVQLLQCYLQEDYRGTRDSVKTVLQDERQSQALILKIADYYYEERTCILRCVLHLLTYFQDERHPYRVEYADCVDKLEKELVSKYRQQFEELYKTEAPTWETHGNLMTERQVSRWFVQCLREQSMLLEIIFLYYAYFEMAPSDLLVLTKMFKEQGFGSRQTNRHLVDETMDPFVDRIGYFSALILVEGMDIESLHKCALDDRRELHQFAQDGLICQDMDCLMLTFGDIPHHAPVLLAWALLRHTLNPEETSSVVRKIGGTAIQLNVFQYLTRLLQSLASGGNDCTTSTACMCVYGLLSFVLTSLELHTLGNQQDIIDTACEVLADPSLPELFWGTEPTSGLGIILDSVCGMFPHLLSPLLQLLRALVSGKSTAKKVYSFLDKMSFYNELYKHKPHDVISHEDGTLWRRQTPKLLYPLGGQTNLRIPQGTVGQVMLDDRAYLVRWEYSYSSWTLFTCEIEMLLHVVSTADVIQHCQRVKPIIDLVHKVISTDLSIADCLLPITSRIYMLLQRLTTVISPPVDVIASCVNCLTVLAARNPAKVWTDLRHTGFLPFVAHPVSSLSQMISAEGMNAGGYGNLLMNSEQPQGEYGVTIAFLRLITTLVKGQLGSTQSQGLVPCVMFVLKEMLPSYHKWRYNSHGVREQIGCLILELIHAILNLCHETDLHSSHTPSLQFLCICSLAYTEAGQTVINIMGIGVDTIDMVMAAQPRSDGAEGQGQGQLLIKTVKLAFSVTNNVIRLKPPSNVVSPLEQALSQHGAHGNNLIAVLAKYIYHKHDPALPRLAIQLLKRLATVAPMSVYACLGNDAAAIRDAFLTRLQSKIEDMRIKVMILEFLTVAVETQPGLIELFLNLEVKDGSDGSKEFSLGMWSCLHAVLELIDSQQQDRYWCPPLLHRAAIAFLHALWQDRRDSAMLVLRTKPKFWENLTSPLFGTLSPPSETSEPSILETCALIMKIICLEIYYVVKGSLDQSLKDTLKKFSIEKRFAYWSGYVKSLAVHVAETEGSSCTSLLEYQMLVSAWRMLLIIATTHADIMHLTDSVVRRQLFLDVLDGTKALLLVPASVNCLRLGSMKCTLLLILLRQWKRELGSVDEILGPLTEILEGVLQADQQLMEKTKAKVFSAFITVLQMKEMKVSDIPQYSQLVLNVCETLQEEVIALFDQTRHSLALGSATEDKDSMETDDCSRSRHRDQRDGVCVLGLHLAKELCEVDEDGDSWLQVTRRLPILPTLLTTLEVSLRMKQNLHFTEATLHLLLTLARTQQGATAVAGAGITQSICLPLLSVYQLSTNGTAQTPSASRKSLDAPSWPGVYRLSMSLMEQLLKTLRYNFLPEALDFVGVHQERTLQCLNAVRTVQSLACLEEADHTVGFILQLSNFMKEWHFHLPQLMRDIQVNLGYLCQACTSLLHSRKMLQHYLQNKNGDGLPSAVAQRVQRPPSAASAAPSSSKQPAADTEASEQQALHTVQYGLLKILSKTLAALRHFTPDVCQILLDQSLDLAEYNFLFALSFTTPTFDSEVAPSFGTLLATVNVALNMLGELDKKKEPLTQAVGLSTQAEGTRTLKSLLMFTMENCFYLLISQAMRYLRDPAVHPRDKQRMKQELSSELSTLLSSLSRYFRRGAPSSPATGVLPSPQGKSTSLSKASPESQEPLIQLVQAFVRHMQR
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------MAAAAGGPC
------CCCCCCCCC
19.6719413330
13PhosphorylationGGPCVRSSRELWTIL
CCCCCCCHHHHHHHH
21.14-
18PhosphorylationRSSRELWTILLGRSA
CCHHHHHHHHHCHHH
17.8623186163
24PhosphorylationWTILLGRSALRELSQ
HHHHHCHHHHHHHHH
29.83-
30PhosphorylationRSALRELSQIEAELN
HHHHHHHHHHHHHHH
25.1029449344
38AcetylationQIEAELNKHWRRLLE
HHHHHHHHHHHHHHH
58.1123749302
38MalonylationQIEAELNKHWRRLLE
HHHHHHHHHHHHHHH
58.1126320211
38UbiquitinationQIEAELNKHWRRLLE
HHHHHHHHHHHHHHH
58.1119608861
48PhosphorylationRRLLEGLSYYKPPSP
HHHHHHHCCCCCCCC
36.9523186163
49PhosphorylationRLLEGLSYYKPPSPS
HHHHHHCCCCCCCCC
22.1323186163
50PhosphorylationLLEGLSYYKPPSPSS
HHHHHCCCCCCCCCH
17.4023186163
51UbiquitinationLEGLSYYKPPSPSSA
HHHHCCCCCCCCCHH
42.07-
54PhosphorylationLSYYKPPSPSSAEKV
HCCCCCCCCCHHHHH
46.0423917254
56PhosphorylationYYKPPSPSSAEKVKA
CCCCCCCCHHHHHHC
46.6623186163
57PhosphorylationYKPPSPSSAEKVKAN
CCCCCCCHHHHHHCC
43.7823186163
62UbiquitinationPSSAEKVKANKDVAS
CCHHHHHHCCCCCCH
58.2627667366
65UbiquitinationAEKVKANKDVASPLK
HHHHHCCCCCCHHHH
59.4427667366
69PhosphorylationKANKDVASPLKELGL
HCCCCCCHHHHHHCC
30.5220873877
722-HydroxyisobutyrylationKDVASPLKELGLRIS
CCCCHHHHHHCCHHH
55.03-
72UbiquitinationKDVASPLKELGLRIS
CCCCHHHHHHCCHHH
55.0327667366
80UbiquitinationELGLRISKFLGLDEE
HHCCHHHHHHCCCHH
42.0921963094
109UbiquitinationRGTRDSVKTVLQDER
CCCHHHHHHHHCCHH
36.5521906983
109 (in isoform 1)Ubiquitination-36.5521890473
128PhosphorylationLILKIADYYYEERTC
HHHHHHHHHHHHHHH
10.0220860994
129PhosphorylationILKIADYYYEERTCI
HHHHHHHHHHHHHHH
12.6320860994
129 (in isoform 2)Ubiquitination-12.6321890473
164AcetylationEYADCVDKLEKELVS
CHHHHHHHHHHHHHH
37.8426051181
164UbiquitinationEYADCVDKLEKELVS
CHHHHHHHHHHHHHH
37.8429901268
167UbiquitinationDCVDKLEKELVSKYR
HHHHHHHHHHHHHHH
67.7829967540
172UbiquitinationLEKELVSKYRQQFEE
HHHHHHHHHHHHHHH
36.6527667366
181PhosphorylationRQQFEELYKTEAPTW
HHHHHHHHCCCCCCC
21.1028851738
182UbiquitinationQQFEELYKTEAPTWE
HHHHHHHCCCCCCCC
53.1422817900
182 (in isoform 1)Ubiquitination-53.1421890473
233 (in isoform 2)Ubiquitination-3.3921890473
237UbiquitinationSDLLVLTKMFKEQGF
HHHHHHHHHHHHCCC
37.8722817900
2402-HydroxyisobutyrylationLVLTKMFKEQGFGSR
HHHHHHHHHCCCCCC
45.70-
240UbiquitinationLVLTKMFKEQGFGSR
HHHHHHHHHCCCCCC
45.7022817900
240 (in isoform 1)Ubiquitination-45.7021890473
338PhosphorylationHTLNPEETSSVVRKI
HCCCHHHHHHHHHHH
25.3325999147
339PhosphorylationTLNPEETSSVVRKIG
CCCHHHHHHHHHHHC
25.1525999147
340PhosphorylationLNPEETSSVVRKIGG
CCHHHHHHHHHHHCC
31.8620860994
344UbiquitinationETSSVVRKIGGTAIQ
HHHHHHHHHCCHHHH
33.8122053931
344 (in isoform 1)Ubiquitination-33.8121890473
359 (in isoform 2)Ubiquitination-17.8421890473
368 (in isoform 2)Ubiquitination-33.0621890473
370 (in isoform 2)Ubiquitination-44.7121890473
389 (in isoform 2)Ubiquitination-2.2521890473
455 (in isoform 2)Ubiquitination-7.4721890473
456PhosphorylationQLLRALVSGKSTAKK
HHHHHHHCCCCHHHH
41.1622817900
458UbiquitinationLRALVSGKSTAKKVY
HHHHHCCCCHHHHHH
36.8127667366
463AcetylationSGKSTAKKVYSFLDK
CCCCHHHHHHHHHHH
43.8926051181
463UbiquitinationSGKSTAKKVYSFLDK
CCCCHHHHHHHHHHH
43.8929967540
465PhosphorylationKSTAKKVYSFLDKMS
CCHHHHHHHHHHHHH
11.5523312004
466PhosphorylationSTAKKVYSFLDKMSF
CHHHHHHHHHHHHHH
23.4823312004
470UbiquitinationKVYSFLDKMSFYNEL
HHHHHHHHHHHHHHH
38.2922817900
470 (in isoform 1)Ubiquitination-38.2921890473
479UbiquitinationSFYNELYKHKPHDVI
HHHHHHHHCCCCCEE
58.7533845483
479 (in isoform 1)Ubiquitination-58.7521890473
481UbiquitinationYNELYKHKPHDVISH
HHHHHHCCCCCEEEC
39.6422817900
481 (in isoform 1)Ubiquitination-39.6421890473
487PhosphorylationHKPHDVISHEDGTLW
CCCCCEEECCCCCCE
22.2230622161
500UbiquitinationLWRRQTPKLLYPLGG
CEECCCCCEEEECCC
55.2923000965
500 (in isoform 1)Ubiquitination-55.2921890473
503PhosphorylationRQTPKLLYPLGGQTN
CCCCCEEEECCCCCC
13.5728152594
517 (in isoform 2)Ubiquitination-19.0621890473
522SulfoxidationQGTVGQVMLDDRAYL
CCCCEEEEECCCEEE
2.3321406390
526MethylationGQVMLDDRAYLVRWE
EEEEECCCEEEEEEE
25.46115485829
566AcetylationIQHCQRVKPIIDLVH
HHHHHHHHHHHHHHH
32.4626051181
566UbiquitinationIQHCQRVKPIIDLVH
HHHHHHHHHHHHHHH
32.4621906983
566 (in isoform 1)Ubiquitination-32.4621890473
605PhosphorylationQRLTTVISPPVDVIA
HHHHHCCCCCHHHHH
20.8620068231
609 (in isoform 2)Ubiquitination-31.7021890473
628UbiquitinationLAARNPAKVWTDLRH
HHHCCHHHHHHCCCC
39.2921906983
628 (in isoform 1)Ubiquitination-39.2921890473
688PhosphorylationIAFLRLITTLVKGQL
HHHHHHHHHHHHCCC
20.7627251275
689PhosphorylationAFLRLITTLVKGQLG
HHHHHHHHHHHCCCC
23.6627251275
697PhosphorylationLVKGQLGSTQSQGLV
HHHCCCCCCCCCCHH
31.6827251275
698PhosphorylationVKGQLGSTQSQGLVP
HHCCCCCCCCCCHHH
30.3727251275
700PhosphorylationGQLGSTQSQGLVPCV
CCCCCCCCCCHHHHH
26.7227251275
701 (in isoform 2)Ubiquitination-39.1521890473
718PhosphorylationLKEMLPSYHKWRYNS
HHHHCHHHHHCCCCC
12.89-
720UbiquitinationEMLPSYHKWRYNSHG
HHCHHHHHCCCCCCC
25.7421890473
720 (in isoform 1)Ubiquitination-25.7421890473
765 (in isoform 2)Ubiquitination-1.6221890473
797 (in isoform 2)Ubiquitination-34.9921890473
798PhosphorylationVMAAQPRSDGAEGQG
EEEECCCCCCCCCCC
47.2623403867
812AcetylationGQGQLLIKTVKLAFS
CCCCEEEEEEEEEEE
47.4326051181
812UbiquitinationGQGQLLIKTVKLAFS
CCCCEEEEEEEEEEE
47.4323000965
812 (in isoform 1)Ubiquitination-47.4321890473
815UbiquitinationQLLIKTVKLAFSVTN
CEEEEEEEEEEEEEC
39.0523000965
862UbiquitinationLAKYIYHKHDPALPR
HHHHHHHCCCCHHHH
32.5033845483
876AcetylationRLAIQLLKRLATVAP
HHHHHHHHHHHCCCC
54.6926051181
876UbiquitinationRLAIQLLKRLATVAP
HHHHHHHHHHHCCCC
54.6923000965
876 (in isoform 1)Ubiquitination-54.6921890473
903PhosphorylationAIRDAFLTRLQSKIE
HHHHHHHHHHHHHHH
23.9128674419
907PhosphorylationAFLTRLQSKIEDMRI
HHHHHHHHHHHHHHH
39.9428674419
908UbiquitinationFLTRLQSKIEDMRIK
HHHHHHHHHHHHHHH
36.8322817900
908 (in isoform 1)Ubiquitination-36.8321890473
998PhosphorylationLWQDRRDSAMLVLRT
HHHCCCCCCEEEEEC
17.4820068231
1000SulfoxidationQDRRDSAMLVLRTKP
HCCCCCCEEEEECCH
2.8521406390
1060UbiquitinationGSLDQSLKDTLKKFS
CCCCHHHHHHHHHCC
54.6429967540
1065AcetylationSLKDTLKKFSIEKRF
HHHHHHHHCCHHHHH
47.6730590949
1070AcetylationLKKFSIEKRFAYWSG
HHHCCHHHHHHHHHH
51.6626051181
1070UbiquitinationLKKFSIEKRFAYWSG
HHHCCHHHHHHHHHH
51.6627667366
1081PhosphorylationYWSGYVKSLAVHVAE
HHHHHHHEEEEEHHH
16.1224043423
1089PhosphorylationLAVHVAETEGSSCTS
EEEEHHHCCCCCCHH
35.5924043423
1092PhosphorylationHVAETEGSSCTSLLE
EHHHCCCCCCHHHHH
18.9324043423
1093PhosphorylationVAETEGSSCTSLLEY
HHHCCCCCCHHHHHH
32.0724043423
1095PhosphorylationETEGSSCTSLLEYQM
HCCCCCCHHHHHHHH
25.1024043423
1096PhosphorylationTEGSSCTSLLEYQML
CCCCCCHHHHHHHHH
34.9724043423
1100PhosphorylationSCTSLLEYQMLVSAW
CCHHHHHHHHHHHHH
10.1324043423
1105PhosphorylationLEYQMLVSAWRMLLI
HHHHHHHHHHHHHHH
20.3924043423
1180 (in isoform 2)Ubiquitination-4.6921890473
1252PhosphorylationLFDQTRHSLALGSAT
HHHHCCHHHHCCCCC
16.4328555341
1257PhosphorylationRHSLALGSATEDKDS
CHHHHCCCCCCCHHC
32.6325849741
1259PhosphorylationSLALGSATEDKDSME
HHHCCCCCCCHHCCC
46.5523312004
1262AcetylationLGSATEDKDSMETDD
CCCCCCCHHCCCCCC
45.5325953088
1262UbiquitinationLGSATEDKDSMETDD
CCCCCCCHHCCCCCC
45.5324816145
1264PhosphorylationSATEDKDSMETDDCS
CCCCCHHCCCCCCCC
25.0229214152
1267PhosphorylationEDKDSMETDDCSRSR
CCHHCCCCCCCCHHH
28.6123312004
1270GlutathionylationDSMETDDCSRSRHRD
HCCCCCCCCHHHCCC
3.9722555962
1271PhosphorylationSMETDDCSRSRHRDQ
CCCCCCCCHHHCCCC
40.0423312004
1275 (in isoform 2)Ubiquitination-38.6321890473
1291UbiquitinationVLGLHLAKELCEVDE
EEHHHHHHHHCCCCC
58.5422817900
1291 (in isoform 1)Ubiquitination-58.5421890473
1298 (in isoform 2)Ubiquitination-69.90-
1342PhosphorylationATLHLLLTLARTQQG
HHHHHHHHHHHHHCC
20.5224719451
1386MalonylationQTPSASRKSLDAPSW
CCCCCCCCCCCCCCC
53.5326320211
1386UbiquitinationQTPSASRKSLDAPSW
CCCCCCCCCCCCCCC
53.5322817900
1386 (in isoform 1)Ubiquitination-53.5321890473
1387PhosphorylationTPSASRKSLDAPSWP
CCCCCCCCCCCCCCC
30.3027134283
1400PhosphorylationWPGVYRLSMSLMEQL
CCHHHHHHHHHHHHH
9.4221406692
1402PhosphorylationGVYRLSMSLMEQLLK
HHHHHHHHHHHHHHH
22.6121406692
1409AcetylationSLMEQLLKTLRYNFL
HHHHHHHHHHHHCCC
54.8520167786
1409UbiquitinationSLMEQLLKTLRYNFL
HHHHHHHHHHHHCCC
54.8523503661
1413PhosphorylationQLLKTLRYNFLPEAL
HHHHHHHHCCCHHHH
17.2422798277
1422 (in isoform 2)Ubiquitination-5.5421890473
1430PhosphorylationVGVHQERTLQCLNAV
CCCCHHHHHHHHHHH
22.0420068231
1496UbiquitinationTSLLHSRKMLQHYLQ
HHHHHHHHHHHHHHH
47.1523000965
1505AcetylationLQHYLQNKNGDGLPS
HHHHHHCCCCCCCCH
49.7126051181
1505UbiquitinationLQHYLQNKNGDGLPS
HHHHHHCCCCCCCCH
49.7129967540
1512PhosphorylationKNGDGLPSAVAQRVQ
CCCCCCCHHHHHHCC
40.1826074081
1523PhosphorylationQRVQRPPSAASAAPS
HHCCCCCCHHHCCCC
38.8729255136
1526PhosphorylationQRPPSAASAAPSSSK
CCCCCHHHCCCCCCC
25.3630266825
1530PhosphorylationSAASAAPSSSKQPAA
CHHHCCCCCCCCCCC
42.3823403867
1531PhosphorylationAASAAPSSSKQPAAD
HHHCCCCCCCCCCCC
40.2623403867
1532PhosphorylationASAAPSSSKQPAADT
HHCCCCCCCCCCCCC
39.3823403867
1533UbiquitinationSAAPSSSKQPAADTE
HCCCCCCCCCCCCCC
63.3521906983
1533 (in isoform 1)Ubiquitination-63.3521890473
1598PhosphorylationALSFTTPTFDSEVAP
EEECCCCCCCCCCCC
37.6719369195
1606PhosphorylationFDSEVAPSFGTLLAT
CCCCCCCCHHHHHHH
26.9417494752
1610 (in isoform 2)Ubiquitination-2.9121890473
1616 (in isoform 2)Ubiquitination-5.80-
1627UbiquitinationMLGELDKKKEPLTQA
HHCCHHCCCCCCHHH
63.1329967540
1628UbiquitinationLGELDKKKEPLTQAV
HCCHHCCCCCCHHHH
71.0129967540
1632PhosphorylationDKKKEPLTQAVGLST
HCCCCCCHHHHCCCC
25.7920860994
1638PhosphorylationLTQAVGLSTQAEGTR
CHHHHCCCCCCCCHH
16.7323532336
1639PhosphorylationTQAVGLSTQAEGTRT
HHHHCCCCCCCCHHH
36.5227251789
1644PhosphorylationLSTQAEGTRTLKSLL
CCCCCCCHHHHHHHH
16.4023532336
1646PhosphorylationTQAEGTRTLKSLLMF
CCCCCHHHHHHHHHH
38.0723898821
1660PhosphorylationFTMENCFYLLISQAM
HHHHHHHHHHHHHHH
11.64-
1684UbiquitinationPRDKQRMKQELSSEL
HHHHHHHHHHHHHHH
42.69-
1688PhosphorylationQRMKQELSSELSTLL
HHHHHHHHHHHHHHH
22.4821406692
1689PhosphorylationRMKQELSSELSTLLS
HHHHHHHHHHHHHHH
56.0021406692
1692PhosphorylationQELSSELSTLLSSLS
HHHHHHHHHHHHHHH
16.9821406692
1693PhosphorylationELSSELSTLLSSLSR
HHHHHHHHHHHHHHH
44.3221406692
1696PhosphorylationSELSTLLSSLSRYFR
HHHHHHHHHHHHHHH
32.1420068231
1697PhosphorylationELSTLLSSLSRYFRR
HHHHHHHHHHHHHHC
30.2720068231
1699PhosphorylationSTLLSSLSRYFRRGA
HHHHHHHHHHHHCCC
27.2121406692
1701PhosphorylationLLSSLSRYFRRGAPS
HHHHHHHHHHCCCCC
9.6921406692
1708PhosphorylationYFRRGAPSSPATGVL
HHHCCCCCCCCCCCC
48.7129255136
1709PhosphorylationFRRGAPSSPATGVLP
HHCCCCCCCCCCCCC
19.9329255136
1712PhosphorylationGAPSSPATGVLPSPQ
CCCCCCCCCCCCCCC
31.0729255136
1717PhosphorylationPATGVLPSPQGKSTS
CCCCCCCCCCCCCCC
26.2029255136
1721UbiquitinationVLPSPQGKSTSLSKA
CCCCCCCCCCCCCCC
45.3622817900
1721 (in isoform 1)Ubiquitination-45.3621890473
1726PhosphorylationQGKSTSLSKASPESQ
CCCCCCCCCCCHHHC
26.4122468782
1727UbiquitinationGKSTSLSKASPESQE
CCCCCCCCCCHHHCH
59.1721987572
1729PhosphorylationSTSLSKASPESQEPL
CCCCCCCCHHHCHHH
32.7025627689

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 NU188_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU188_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 NU188_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUP93_HUMANNUP93physical
26344197

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 NU188_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-1708; SER-1709; THR-1712 AND SER-1717, AND MASSSPECTROMETRY.
"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-38, 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-1709; THR-1712 ANDSER-1717, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1708, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-1708; SER-1709; THR-1712 AND SER-1717, 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-1708; SER-1709 ANDSER-1717, 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-1708; SER-1709 ANDSER-1717, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1709 AND SER-1717, ANDMASS 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-1717, AND MASSSPECTROMETRY.

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