LAS1L_HUMAN - dbPTM
LAS1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAS1L_HUMAN
UniProt AC Q9Y4W2
Protein Name Ribosomal biogenesis protein LAS1L
Gene Name LAS1L
Organism Homo sapiens (Human).
Sequence Length 734
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm. Cytoplasm. Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Localizes mainly to the granular component, the region implicated in the later
Protein Description Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes..
Protein Sequence MSWESGAGPGLGSQGMDLVWSAWYGKCVKGKGSLPLSAHGIVVAWLSRAEWDQVTVYLFCDDHKLQRYALNRITVWRSRSGNELPLAVASTADLIRCKLLDVTGGLGTDELRLLYGMALVRFVNLISERKTKFAKVPLKCLAQEVNIPDWIVDLRHELTHKKMPHINDCRRGCYFVLDWLQKTYWCRQLENSLRETWELEEFREGIEEEDQEEDKNIVVDDITEQKPEPQDDGKSTESDVKADGDSKGSEEVDSHCKKALSHKELYERARELLVSYEEEQFTVLEKFRYLPKAIKAWNNPSPRVECVLAELKGVTCENREAVLDAFLDDGFLVPTFEQLAALQIEYEDGQTEVQRGEGTDPKSHKNVDLNDVLVPKPFSQFWQPLLRGLHSQNFTQALLERMLSELPALGISGIRPTYILRWTVELIVANTKTGRNARRFSAGQWEARRGWRLFNCSASLDWPRMVESCLGSPCWASPQLLRIIFKAMGQGLPDEEQEKLLRICSIYTQSGENSLVQEGSEASPIGKSPYTLDSLYWSVKPASSSFGSEAKAQQQEEQGSVNDVKEEEKEEKEVLPDQVEEEEENDDQEEEEEDEDDEDDEEEDRMEVGPFSTGQESPTAENARLLAQKRGALQGSAWQVSSEDVRWDTFPLGRMPGQTEDPAELMLENYDTMYLLDQPVLEQRLEPSTCKTDTLGLSCGVGSGNCSNSSSSNFEGLLWSQGQLHGLKTGLQLF
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
2Phosphorylation------MSWESGAGP
------CCCCCCCCC
39.2828348404
5Phosphorylation---MSWESGAGPGLG
---CCCCCCCCCCCC
27.9028348404
13PhosphorylationGAGPGLGSQGMDLVW
CCCCCCCHHCCHHHH
28.7128348404
21PhosphorylationQGMDLVWSAWYGKCV
HCCHHHHHEECCCCC
11.0528674151
24PhosphorylationDLVWSAWYGKCVKGK
HHHHHEECCCCCCCC
13.3628674151
31AcetylationYGKCVKGKGSLPLSA
CCCCCCCCCCCCCCC
39.3426051181
31UbiquitinationYGKCVKGKGSLPLSA
CCCCCCCCCCCCCCC
39.34-
60UbiquitinationQVTVYLFCDDHKLQR
EEEEEEEECCHHHHH
5.7722817900
63UbiquitinationVYLFCDDHKLQRYAL
EEEEECCHHHHHHHH
21.3421890473
64UbiquitinationYLFCDDHKLQRYALN
EEEECCHHHHHHHHH
54.0021963094
80PhosphorylationITVWRSRSGNELPLA
EEEEECCCCCCCCEE
47.4120068231
90PhosphorylationELPLAVASTADLIRC
CCCEEEEHHHHHHHC
19.9620068231
91PhosphorylationLPLAVASTADLIRCK
CCEEEEHHHHHHHCE
17.9120068231
93UbiquitinationLAVASTADLIRCKLL
EEEEHHHHHHHCEEC
42.5929901268
97UbiquitinationSTADLIRCKLLDVTG
HHHHHHHCEECCCCC
2.6321963094
97 (in isoform 3)Ubiquitination-2.6321890473
98UbiquitinationTADLIRCKLLDVTGG
HHHHHHCEECCCCCC
42.0821963094
115PhosphorylationTDELRLLYGMALVRF
HHHHHHHHHHHHHHH
14.94-
119UbiquitinationRLLYGMALVRFVNLI
HHHHHHHHHHHHHHH
1.7929967540
120UbiquitinationLLYGMALVRFVNLIS
HHHHHHHHHHHHHHC
3.0327667366
127O-linked_GlycosylationVRFVNLISERKTKFA
HHHHHHHCCCCCCCC
34.2230379171
127PhosphorylationVRFVNLISERKTKFA
HHHHHHHCCCCCCCC
34.2220068231
135AcetylationERKTKFAKVPLKCLA
CCCCCCCCCCHHHHH
47.7426051181
135UbiquitinationERKTKFAKVPLKCLA
CCCCCCCCCCHHHHH
47.7427667366
139MethylationKFAKVPLKCLAQEVN
CCCCCCHHHHHHHCC
22.5730783411
139UbiquitinationKFAKVPLKCLAQEVN
CCCCCCHHHHHHHCC
22.5721906983
139 (in isoform 1)Ubiquitination-22.5721890473
139 (in isoform 2)Ubiquitination-22.5721890473
139 (in isoform 4)Ubiquitination-22.5721890473
140GlutathionylationFAKVPLKCLAQEVNI
CCCCCHHHHHHHCCC
5.1222555962
161UbiquitinationLRHELTHKKMPHIND
HHHHHHCCCCCCHHH
45.6029967540
162UbiquitinationRHELTHKKMPHINDC
HHHHHCCCCCCHHHH
50.4927667366
167UbiquitinationHKKMPHINDCRRGCY
CCCCCCHHHHHHCHH
39.0227667366
173UbiquitinationINDCRRGCYFVLDWL
HHHHHHCHHHHHHHH
1.9529967540
180UbiquitinationCYFVLDWLQKTYWCR
HHHHHHHHHHHHHHH
3.6021963094
184UbiquitinationLDWLQKTYWCRQLEN
HHHHHHHHHHHHHHH
15.0027667366
184 (in isoform 3)Ubiquitination-15.0021890473
192UbiquitinationWCRQLENSLRETWEL
HHHHHHHHHHHHCHH
21.3029967540
197UbiquitinationENSLRETWELEEFRE
HHHHHHHCHHHHHHH
11.9221890473
199UbiquitinationSLRETWELEEFREGI
HHHHHCHHHHHHHCC
6.0333845483
199 (in isoform 3)Ubiquitination-6.0321890473
205UbiquitinationELEEFREGIEEEDQE
HHHHHHHCCCHHHHH
28.4927667366
215SumoylationEEDQEEDKNIVVDDI
HHHHHHHCCCEEEEH
52.4328112733
215UbiquitinationEEDQEEDKNIVVDDI
HHHHHHHCCCEEEEH
52.4329967540
215 (in isoform 3)Ubiquitination-52.4321890473
216UbiquitinationEDQEEDKNIVVDDIT
HHHHHHCCCEEEEHH
44.6122817900
221UbiquitinationDKNIVVDDITEQKPE
HCCCEEEEHHCCCCC
37.7927667366
221 (in isoform 3)Ubiquitination-37.7921890473
223PhosphorylationNIVVDDITEQKPEPQ
CCEEEEHHCCCCCCC
39.0830576142
226SumoylationVDDITEQKPEPQDDG
EEEHHCCCCCCCCCC
45.15-
226SumoylationVDDITEQKPEPQDDG
EEEHHCCCCCCCCCC
45.1528112733
226UbiquitinationVDDITEQKPEPQDDG
EEEHHCCCCCCCCCC
45.1521906983
226 (in isoform 1)Ubiquitination-45.1521890473
226 (in isoform 2)Ubiquitination-45.1521890473
226 (in isoform 4)Ubiquitination-45.1521890473
234UbiquitinationPEPQDDGKSTESDVK
CCCCCCCCCCHHHHH
62.2929967540
235PhosphorylationEPQDDGKSTESDVKA
CCCCCCCCCHHHHHC
42.8323927012
236PhosphorylationPQDDGKSTESDVKAD
CCCCCCCCHHHHHCC
42.8925159151
238PhosphorylationDDGKSTESDVKADGD
CCCCCCHHHHHCCCC
48.0323401153
238UbiquitinationDDGKSTESDVKADGD
CCCCCCHHHHHCCCC
48.0321963094
241PhosphorylationKSTESDVKADGDSKG
CCCHHHHHCCCCCCC
45.8332142685
241UbiquitinationKSTESDVKADGDSKG
CCCHHHHHCCCCCCC
45.8321906983
241 (in isoform 1)Ubiquitination-45.8321890473
241 (in isoform 2)Ubiquitination-45.8321890473
241 (in isoform 4)Ubiquitination-45.8321890473
244UbiquitinationESDVKADGDSKGSEE
HHHHHCCCCCCCHHH
46.0521963094
244 (in isoform 3)Ubiquitination-46.0521890473
246PhosphorylationDVKADGDSKGSEEVD
HHHCCCCCCCHHHHH
44.4328985074
246UbiquitinationDVKADGDSKGSEEVD
HHHCCCCCCCHHHHH
44.4327667366
247UbiquitinationVKADGDSKGSEEVDS
HHCCCCCCCHHHHHH
71.8027667366
249PhosphorylationADGDSKGSEEVDSHC
CCCCCCCHHHHHHHH
34.0325849741
250UbiquitinationDGDSKGSEEVDSHCK
CCCCCCHHHHHHHHH
71.3729901268
253UbiquitinationSKGSEEVDSHCKKAL
CCCHHHHHHHHHHHH
35.6221963094
253 (in isoform 3)Ubiquitination-35.6221890473
254PhosphorylationKGSEEVDSHCKKALS
CCHHHHHHHHHHHHC
35.6428985074
257UbiquitinationEEVDSHCKKALSHKE
HHHHHHHHHHHCHHH
35.3421906983
257 (in isoform 1)Ubiquitination-35.3421890473
257 (in isoform 2)Ubiquitination-35.3421890473
257 (in isoform 4)Ubiquitination-35.3421890473
258UbiquitinationEVDSHCKKALSHKEL
HHHHHHHHHHCHHHH
61.0122817900
261PhosphorylationSHCKKALSHKELYER
HHHHHHHCHHHHHHH
37.06-
263UbiquitinationCKKALSHKELYERAR
HHHHHCHHHHHHHHH
46.1421890473
263AcetylationCKKALSHKELYERAR
HHHHHCHHHHHHHHH
46.1426051181
263UbiquitinationCKKALSHKELYERAR
HHHHHCHHHHHHHHH
46.1427667366
263 (in isoform 1)Ubiquitination-46.1421890473
263 (in isoform 2)Ubiquitination-46.1421890473
263 (in isoform 4)Ubiquitination-46.1421890473
270UbiquitinationKELYERARELLVSYE
HHHHHHHHHHHHCCC
41.1221963094
270 (in isoform 3)Ubiquitination-41.1221890473
286UbiquitinationEQFTVLEKFRYLPKA
HHHHHHHHHCCHHHH
30.8621906983
286 (in isoform 1)Ubiquitination-30.8621890473
286 (in isoform 2)Ubiquitination-30.8621890473
292MalonylationEKFRYLPKAIKAWNN
HHHCCHHHHHHHHCC
61.2132601280
292UbiquitinationEKFRYLPKAIKAWNN
HHHCCHHHHHHHHCC
61.2129901268
295SumoylationRYLPKAIKAWNNPSP
CCHHHHHHHHCCCCH
52.81-
295MalonylationRYLPKAIKAWNNPSP
CCHHHHHHHHCCCCH
52.8126320211
295SumoylationRYLPKAIKAWNNPSP
CCHHHHHHHHCCCCH
52.81-
295UbiquitinationRYLPKAIKAWNNPSP
CCHHHHHHHHCCCCH
52.8121906983
295 (in isoform 1)Ubiquitination-52.8121890473
295 (in isoform 2)Ubiquitination-52.8121890473
298PhosphorylationPKAIKAWNNPSPRVE
HHHHHHHCCCCHHHH
56.2333259812
301PhosphorylationIKAWNNPSPRVECVL
HHHHCCCCHHHHHHH
27.7125159151
310UbiquitinationRVECVLAELKGVTCE
HHHHHHHHHCCCCCC
47.0227667366
312AcetylationECVLAELKGVTCENR
HHHHHHHCCCCCCCH
42.7225953088
312UbiquitinationECVLAELKGVTCENR
HHHHHHHCCCCCCCH
42.7221906983
312 (in isoform 1)Ubiquitination-42.7221890473
312 (in isoform 2)Ubiquitination-42.7221890473
320UbiquitinationGVTCENREAVLDAFL
CCCCCCHHHHHHHHC
55.5022817900
323UbiquitinationCENREAVLDAFLDDG
CCCHHHHHHHHCCCC
5.1821890473
327UbiquitinationEAVLDAFLDDGFLVP
HHHHHHHCCCCCCCC
6.6827667366
362UbiquitinationRGEGTDPKSHKNVDL
CCCCCCCCCCCCCCH
68.9222817900
363PhosphorylationGEGTDPKSHKNVDLN
CCCCCCCCCCCCCHH
45.11-
365UbiquitinationGTDPKSHKNVDLNDV
CCCCCCCCCCCHHHC
66.8021890473
365UbiquitinationGTDPKSHKNVDLNDV
CCCCCCCCCCCHHHC
66.8021890473
365 (in isoform 1)Ubiquitination-66.8021890473
372UbiquitinationKNVDLNDVLVPKPFS
CCCCHHHCCCCCCHH
5.8921963094
373 (in isoform 3)Ubiquitination-6.4321890473
376UbiquitinationLNDVLVPKPFSQFWQ
HHHCCCCCCHHHHHH
51.7433845483
389UbiquitinationWQPLLRGLHSQNFTQ
HHHHHHHHHCCCHHH
2.5821963094
404PhosphorylationALLERMLSELPALGI
HHHHHHHHHCHHHCC
27.9520068231
412PhosphorylationELPALGISGIRPTYI
HCHHHCCCCCCCCEE
26.7720068231
415 (in isoform 2)Ubiquitination-22.4921890473
417PhosphorylationGISGIRPTYILRWTV
CCCCCCCCEEHHEEE
17.2220068231
418PhosphorylationISGIRPTYILRWTVE
CCCCCCCEEHHEEEE
10.7122210691
427UbiquitinationLRWTVELIVANTKTG
HHEEEEEEEEECCCC
1.4127667366
427 (in isoform 3)Ubiquitination-1.4121890473
432UbiquitinationELIVANTKTGRNARR
EEEEEECCCCCCCHH
49.1121906983
432 (in isoform 1)Ubiquitination-49.1121890473
440UbiquitinationTGRNARRFSAGQWEA
CCCCCHHCCCCCCHH
4.9721963094
440 (in isoform 3)Ubiquitination-4.9721890473
441PhosphorylationGRNARRFSAGQWEAR
CCCCHHCCCCCCHHH
29.6728450419
444UbiquitinationARRFSAGQWEARRGW
CHHCCCCCCHHHCCE
34.2627667366
457UbiquitinationGWRLFNCSASLDWPR
CEEEEEEEECCCHHH
23.2321890473
469UbiquitinationWPRMVESCLGSPCWA
HHHHHHHHHCCCCCC
2.9327667366
469 (in isoform 2)Ubiquitination-2.9321890473
477PhosphorylationLGSPCWASPQLLRII
HCCCCCCCHHHHHHH
6.6721815630
481UbiquitinationCWASPQLLRIIFKAM
CCCCHHHHHHHHHHH
2.8821963094
481 (in isoform 3)Ubiquitination-2.8821890473
482UbiquitinationWASPQLLRIIFKAMG
CCCHHHHHHHHHHHC
28.6621963094
482 (in isoform 2)Ubiquitination-28.6621890473
486UbiquitinationQLLRIIFKAMGQGLP
HHHHHHHHHHCCCCC
27.3621890473
486AcetylationQLLRIIFKAMGQGLP
HHHHHHHHHHCCCCC
27.3626051181
486UbiquitinationQLLRIIFKAMGQGLP
HHHHHHHHHHCCCCC
27.3627667366
486 (in isoform 1)Ubiquitination-27.3621890473
492UbiquitinationFKAMGQGLPDEEQEK
HHHHCCCCCHHHHHH
3.5729967540
498UbiquitinationGLPDEEQEKLLRICS
CCCHHHHHHHHHHHH
49.2921963094
499UbiquitinationLPDEEQEKLLRICSI
CCHHHHHHHHHHHHH
53.1421890473
499AcetylationLPDEEQEKLLRICSI
CCHHHHHHHHHHHHH
53.1426051181
499UbiquitinationLPDEEQEKLLRICSI
CCHHHHHHHHHHHHH
53.1421963094
499 (in isoform 1)Ubiquitination-53.1421890473
501PhosphorylationDEEQEKLLRICSIYT
HHHHHHHHHHHHHHC
5.2732142685
505PhosphorylationEKLLRICSIYTQSGE
HHHHHHHHHHCCCCC
19.0929255136
506UbiquitinationKLLRICSIYTQSGEN
HHHHHHHHHCCCCCC
3.6027667366
506 (in isoform 3)Ubiquitination-3.6021890473
507PhosphorylationLLRICSIYTQSGENS
HHHHHHHHCCCCCCC
5.1729255136
508PhosphorylationLRICSIYTQSGENSL
HHHHHHHCCCCCCCC
18.0029255136
510PhosphorylationICSIYTQSGENSLVQ
HHHHHCCCCCCCCCC
40.0329255136
514PhosphorylationYTQSGENSLVQEGSE
HCCCCCCCCCCCCCC
26.1429255136
520PhosphorylationNSLVQEGSEASPIGK
CCCCCCCCCCCCCCC
29.2730266825
523PhosphorylationVQEGSEASPIGKSPY
CCCCCCCCCCCCCCC
17.0129255136
523UbiquitinationVQEGSEASPIGKSPY
CCCCCCCCCCCCCCC
17.0127667366
523 (in isoform 2)Ubiquitination-17.0121890473
528PhosphorylationEASPIGKSPYTLDSL
CCCCCCCCCCCHHHH
20.2321945579
530PhosphorylationSPIGKSPYTLDSLYW
CCCCCCCCCHHHHEE
27.3321945579
531PhosphorylationPIGKSPYTLDSLYWS
CCCCCCCCHHHHEEE
27.7221945579
534PhosphorylationKSPYTLDSLYWSVKP
CCCCCHHHHEEECCC
26.8621945579
534UbiquitinationKSPYTLDSLYWSVKP
CCCCCHHHHEEECCC
26.8629967540
536PhosphorylationPYTLDSLYWSVKPAS
CCCHHHHEEECCCCC
10.2921945579
538PhosphorylationTLDSLYWSVKPASSS
CHHHHEEECCCCCCC
13.5021945579
540AcetylationDSLYWSVKPASSSFG
HHHEEECCCCCCCCC
29.3826051181
540UbiquitinationDSLYWSVKPASSSFG
HHHEEECCCCCCCCC
29.3821906983
540 (in isoform 1)Ubiquitination-29.3821890473
543PhosphorylationYWSVKPASSSFGSEA
EEECCCCCCCCCHHH
34.7325159151
544PhosphorylationWSVKPASSSFGSEAK
EECCCCCCCCCHHHH
31.6226074081
545PhosphorylationSVKPASSSFGSEAKA
ECCCCCCCCCHHHHH
31.0021945579
548PhosphorylationPASSSFGSEAKAQQQ
CCCCCCCHHHHHHHH
32.1625159151
548UbiquitinationPASSSFGSEAKAQQQ
CCCCCCCHHHHHHHH
32.1627667366
548 (in isoform 2)Ubiquitination-32.1621890473
551UbiquitinationSSFGSEAKAQQQEEQ
CCCCHHHHHHHHHHC
42.5529967540
558PhosphorylationKAQQQEEQGSVNDVK
HHHHHHHCCCCCHHH
49.0233259812
560PhosphorylationQQQEEQGSVNDVKEE
HHHHHCCCCCHHHHH
19.9029255136
565SumoylationQGSVNDVKEEEKEEK
CCCCCHHHHHHHHHH
63.37-
565SumoylationQGSVNDVKEEEKEEK
CCCCCHHHHHHHHHH
63.37-
565UbiquitinationQGSVNDVKEEEKEEK
CCCCCHHHHHHHHHH
63.3727667366
565 (in isoform 1)Ubiquitination-63.3721890473
570UbiquitinationDVKEEEKEEKEVLPD
HHHHHHHHHHCCCCH
77.0527667366
587UbiquitinationEEEEENDDQEEEEED
HHHHHCCCHHHHHCC
70.1727667366
600PhosphorylationEDEDDEDDEEEDRME
CCCCCCCCCHHHHHC
64.2633259812
612PhosphorylationRMEVGPFSTGQESPT
HHCCCCCCCCCCCCC
34.4622167270
612UbiquitinationRMEVGPFSTGQESPT
HHCCCCCCCCCCCCC
34.4627667366
613PhosphorylationMEVGPFSTGQESPTA
HCCCCCCCCCCCCCH
43.1722167270
617PhosphorylationPFSTGQESPTAENAR
CCCCCCCCCCHHHHH
21.4719664994
619PhosphorylationSTGQESPTAENARLL
CCCCCCCCHHHHHHH
56.7530266825
629UbiquitinationNARLLAQKRGALQGS
HHHHHHHHHCCCCCC
47.3827667366
632UbiquitinationLLAQKRGALQGSAWQ
HHHHHHCCCCCCCEE
10.7621963094
641PhosphorylationQGSAWQVSSEDVRWD
CCCCEECCCCCCCCC
16.9529449344
642PhosphorylationGSAWQVSSEDVRWDT
CCCEECCCCCCCCCC
38.6728985074
649UbiquitinationSEDVRWDTFPLGRMP
CCCCCCCCCCCCCCC
21.8621963094
673UbiquitinationMLENYDTMYLLDQPV
HHHCCCCEEECCCHH
1.7121963094
674UbiquitinationLENYDTMYLLDQPVL
HHCCCCEEECCCHHH
13.2521963094
690UbiquitinationQRLEPSTCKTDTLGL
HHCCCCCCCCCCCCC
5.3921963094
691UbiquitinationRLEPSTCKTDTLGLS
HCCCCCCCCCCCCCC
49.9121963094

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 LAS1L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAS1L_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 LAS1L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PELP1_HUMANPELP1physical
20442285
PELP1_HUMANPELP1physical
22939629
TEX10_HUMANTEX10physical
22939629
PELP1_HUMANPELP1physical
22190735
IPO5_HUMANIPO5physical
22190735
TEX10_HUMANTEX10physical
22190735
NOL9_HUMANNOL9physical
22190735
SENP3_HUMANSENP3physical
22190735
WDR18_HUMANWDR18physical
22190735
NOL9_HUMANNOL9physical
26344197
PELP1_HUMANPELP1physical
26344197
TEX10_HUMANTEX10physical
26344197
WDR18_HUMANWDR18physical
26344197
RAF1_HUMANRAF1physical
27173435

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 LAS1L_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-617, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, 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 SER-523, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND SER-560, 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-523, AND MASSSPECTROMETRY.

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