ERC6L_HUMAN - dbPTM
ERC6L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERC6L_HUMAN
UniProt AC Q2NKX8
Protein Name DNA excision repair protein ERCC-6-like
Gene Name ERCC6L
Organism Homo sapiens (Human).
Sequence Length 1250
Subcellular Localization Chromosome, centromere . Chromosome, centromere, kinetochore . Chromosome . Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between
Protein Description DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. [PubMed: 17218258 Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase]
Protein Sequence MEASRRFPEAEALSPEQAAHYLRYVKEAKEATKNGDLEEAFKLFNLAKDIFPNEKVLSRIQKIQEALEELAEQGDDEFTDVCNSGLLLYRELHNQLFEHQKEGIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKTFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRRTKEDVQKKKSSNPEARLNEKNPDVDAICEMPSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMETRSPLAELGVLKKLCDHPRLLSARACCLLNLGTFSAQDGNEGEDSPDVDHIDQVTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTVTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTGEKKNPFRYFSKQELRELFTIEDLQNSVTQLQLQSLHAAQRKSDIKLDEHIAYLQSLGIAGISDHDLMYTCDLSVKEELDVVEESHYIQQRVQKAQFLVEFESQNKEFLMEQQRTRNEGAWLREPVFPSSTKKKCPKLNKPQPQPSPLLSTHHTQEEDISSKMASVVIDDLPKEGEKQDLSSIKVNVTTLQDGKGTGSADSIATLPKGFGSVEELCTNSSLGMEKSFATKNEAVQKETLQEGPKQEALQEDPLESFNYVLSKSTKADIGPNLDQLKDDEILRHCNPWPIISITNESQNAESNVSIIEIADDLSASHSALQDAQASEAKLEEEPSASSPQYACDFNLFLEDSADNRQNFSSQSLEHVEKENSLCGSAPNSRAGFVHSKTCLSWEFSEKDDEPEEVVVKAKIRSKARRIVSDGEDEDDSFKDTSSINPFNTSLFQFSSVKQFDASTPKNDISPPGRFFSSQIPSSVNKSMNSRRSLASRRSLINMVLDHVEDMEERLDDSSEAKGPEDYPEEGVEESSGEASKYTEEDPSGETLSSENKSSWLMTSKPSALAQETSLGAPEPLSGEQLVGSPQDKAAEATNDYETLVKRGKELKECGKIQEALNCLVKALDIKSADPEVMLLTLSLYKQLNNN
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
4Phosphorylation----MEASRRFPEAE
----CCHHHCCCHHH
27.5526074081
14PhosphorylationFPEAEALSPEQAAHY
CCHHHHCCHHHHHHH
33.1825159151
21PhosphorylationSPEQAAHYLRYVKEA
CHHHHHHHHHHHHHH
6.5323403867
26UbiquitinationAHYLRYVKEAKEATK
HHHHHHHHHHHHHHC
42.9127667366
33UbiquitinationKEAKEATKNGDLEEA
HHHHHHHCCCCHHHH
67.0129967540
42UbiquitinationGDLEEAFKLFNLAKD
CCHHHHHHHHHHHHH
60.2529967540
48MethylationFKLFNLAKDIFPNEK
HHHHHHHHHHCCCHH
55.3023644510
48UbiquitinationFKLFNLAKDIFPNEK
HHHHHHHHHHCCCHH
55.3029967540
55MethylationKDIFPNEKVLSRIQK
HHHCCCHHHHHHHHH
55.9323644510
55UbiquitinationKDIFPNEKVLSRIQK
HHHCCCHHHHHHHHH
55.9322817900
116UbiquitinationSLYRDGRKGGILADD
HHHHCCCCCCCEECC
68.0029967540
166UbiquitinationTWVKEFIKWTPGMRV
HHHHHHHHCCCCCCE
50.7929967540
175PhosphorylationTPGMRVKTFHGPSKD
CCCCCEEECCCCCCC
20.29-
180PhosphorylationVKTFHGPSKDERTRN
EEECCCCCCCHHHHH
58.28-
185PhosphorylationGPSKDERTRNLNRIQ
CCCCCHHHHHHHHHH
23.1227174698
232AcetylationVILDEAHKIKTSSTK
EEEECHHHCCCCCCC
53.6025953088
235PhosphorylationDEAHKIKTSSTKSAI
ECHHHCCCCCCCHHH
31.2327461979
236PhosphorylationEAHKIKTSSTKSAIC
CHHHCCCCCCCHHHH
30.8927461979
237PhosphorylationAHKIKTSSTKSAICA
HHHCCCCCCCHHHHH
45.1227461979
238PhosphorylationHKIKTSSTKSAICAR
HHCCCCCCCHHHHHH
28.8727461979
239UbiquitinationKIKTSSTKSAICARA
HCCCCCCCHHHHHHH
39.5829967540
240PhosphorylationIKTSSTKSAICARAI
CCCCCCCHHHHHHHC
23.9727461979
287UbiquitinationLGTLKTFKMEYENPI
HHHHHHHCEEECCCC
35.7329967540
307UbiquitinationKDATPGEKALGFKIS
CCCCCCCHHHCCCCC
55.6229967540
312UbiquitinationGEKALGFKISENLMA
CCHHHCCCCCHHHHH
43.45-
322UbiquitinationENLMAIIKPYFLRRT
HHHHHHHHHHHHHHC
27.79-
324PhosphorylationLMAIIKPYFLRRTKE
HHHHHHHHHHHHCHH
15.3920049867
329PhosphorylationKPYFLRRTKEDVQKK
HHHHHHHCHHHHHHH
32.1424719451
336UbiquitinationTKEDVQKKKSSNPEA
CHHHHHHHHCCCCCH
40.5724816145
337UbiquitinationKEDVQKKKSSNPEAR
HHHHHHHHCCCCCHH
67.1824816145
339PhosphorylationDVQKKKSSNPEARLN
HHHHHHCCCCCHHHH
66.3426546556
348UbiquitinationPEARLNEKNPDVDAI
CCHHHHCCCCCHHHH
73.1129967540
362PhosphorylationICEMPSLSRKNDLII
HHCCCCCCCCCCEEE
45.6124260401
383UbiquitinationLQEEIYRKFVSLDHI
CCHHHHHHHCCHHHH
32.9022505724
391UbiquitinationFVSLDHIKELLMETR
HCCHHHHHHHHHHCC
38.6029967540
399PhosphorylationELLMETRSPLAELGV
HHHHHCCCHHHHHHH
31.5225159151
408UbiquitinationLAELGVLKKLCDHPR
HHHHHHHHHHCCCHH
41.0929967540
409UbiquitinationAELGVLKKLCDHPRL
HHHHHHHHHCCCHHH
50.6229967540
418PhosphorylationCDHPRLLSARACCLL
CCCHHHHHHHHHHHH
21.9424719451
470UbiquitinationIFLMDLLKRLRDEGH
HHHHHHHHHHHHCCC
57.60-
479PhosphorylationLRDEGHQTLVFSQSR
HHHCCCCEEEEECHH
21.1529083192
483PhosphorylationGHQTLVFSQSRQILN
CCCEEEEECHHHHHH
21.5529083192
485PhosphorylationQTLVFSQSRQILNII
CEEEEECHHHHHHHH
25.5929083192
503PhosphorylationLKNRHFKTLRIDGTV
HHCCCCCEEEECCHH
21.96-
511PhosphorylationLRIDGTVTHLLEREK
EEECCHHHHHHHHHH
13.4723403867
576UbiquitinationRVYRIGQKENVVVYR
HHHHCCCCCCEEEEE
46.15-
593UbiquitinationTCGTVEEKIYRRQVF
ECCCHHHHHHHHHHH
31.3729967540
601UbiquitinationIYRRQVFKDSLIRQT
HHHHHHHHHHHHHCC
47.7724816145
603PhosphorylationRRQVFKDSLIRQTTG
HHHHHHHHHHHCCCC
26.7024719451
612UbiquitinationIRQTTGEKKNPFRYF
HHCCCCCCCCCCCCC
60.2329967540
618PhosphorylationEKKNPFRYFSKQELR
CCCCCCCCCCHHHHH
16.75-
621UbiquitinationNPFRYFSKQELRELF
CCCCCCCHHHHHHHC
37.5822505724
651UbiquitinationSLHAAQRKSDIKLDE
HHHHHHHHHCCCHHH
40.1629967540
694PhosphorylationELDVVEESHYIQQRV
HHHHHHHHHHHHHHH
14.2128796482
696PhosphorylationDVVEESHYIQQRVQK
HHHHHHHHHHHHHHH
15.0928796482
703UbiquitinationYIQQRVQKAQFLVEF
HHHHHHHHHHHHHEH
41.1029967540
712PhosphorylationQFLVEFESQNKEFLM
HHHHEHHHHCHHHHH
44.3628555341
738PhosphorylationLREPVFPSSTKKKCP
CCCCCCCCCCCCCCC
38.8922199227
739PhosphorylationREPVFPSSTKKKCPK
CCCCCCCCCCCCCCC
44.4722199227
740PhosphorylationEPVFPSSTKKKCPKL
CCCCCCCCCCCCCCC
51.7421815630
741UbiquitinationPVFPSSTKKKCPKLN
CCCCCCCCCCCCCCC
52.7829967540
749MalonylationKKCPKLNKPQPQPSP
CCCCCCCCCCCCCCC
56.3026320211
749UbiquitinationKKCPKLNKPQPQPSP
CCCCCCCCCCCCCCC
56.3029967540
755PhosphorylationNKPQPQPSPLLSTHH
CCCCCCCCCCCCCCC
23.9625159151
759PhosphorylationPQPSPLLSTHHTQEE
CCCCCCCCCCCCCHH
33.1224732914
760PhosphorylationQPSPLLSTHHTQEED
CCCCCCCCCCCCHHH
20.0428555341
763PhosphorylationPLLSTHHTQEEDISS
CCCCCCCCCHHHHHH
30.0324732914
769PhosphorylationHTQEEDISSKMASVV
CCCHHHHHHHHHHHH
35.9124732914
770PhosphorylationTQEEDISSKMASVVI
CCHHHHHHHHHHHHE
27.1224732914
771UbiquitinationQEEDISSKMASVVID
CHHHHHHHHHHHHEC
31.5329967540
774PhosphorylationDISSKMASVVIDDLP
HHHHHHHHHHECCCC
17.2625159151
790PhosphorylationEGEKQDLSSIKVNVT
CCCCCCHHHCEEEEE
38.0022199227
791PhosphorylationGEKQDLSSIKVNVTT
CCCCCHHHCEEEEEE
33.4521815630
793UbiquitinationKQDLSSIKVNVTTLQ
CCCHHHCEEEEEECC
29.7029967540
797PhosphorylationSSIKVNVTTLQDGKG
HHCEEEEEECCCCCC
19.3130576142
798PhosphorylationSIKVNVTTLQDGKGT
HCEEEEEECCCCCCC
20.3825850435
803UbiquitinationVTTLQDGKGTGSADS
EEECCCCCCCCCCHH
62.6829967540
805PhosphorylationTLQDGKGTGSADSIA
ECCCCCCCCCCHHEE
31.3025159151
807PhosphorylationQDGKGTGSADSIATL
CCCCCCCCCHHEEEC
28.8329255136
810PhosphorylationKGTGSADSIATLPKG
CCCCCCHHEEECCCC
17.5329255136
813PhosphorylationGSADSIATLPKGFGS
CCCHHEEECCCCCCC
41.7625159151
816UbiquitinationDSIATLPKGFGSVEE
HHEEECCCCCCCHHH
70.73-
820PhosphorylationTLPKGFGSVEELCTN
ECCCCCCCHHHHHHC
24.8825159151
826PhosphorylationGSVEELCTNSSLGME
CCHHHHHHCCCCCCC
51.2423927012
828PhosphorylationVEELCTNSSLGMEKS
HHHHHHCCCCCCCHH
14.5825159151
829PhosphorylationEELCTNSSLGMEKSF
HHHHHCCCCCCCHHH
30.8925159151
835PhosphorylationSSLGMEKSFATKNEA
CCCCCCHHHHCCCHH
13.5521712546
838PhosphorylationGMEKSFATKNEAVQK
CCCHHHHCCCHHHHH
32.1821712546
847PhosphorylationNEAVQKETLQEGPKQ
CHHHHHHHHCCCCCH
40.5521406692
853UbiquitinationETLQEGPKQEALQED
HHHCCCCCHHHHHCC
72.1829967540
864PhosphorylationLQEDPLESFNYVLSK
HHCCCHHHHHHHHCC
26.8625159151
867PhosphorylationDPLESFNYVLSKSTK
CCHHHHHHHHCCCCC
10.7628796482
870PhosphorylationESFNYVLSKSTKADI
HHHHHHHCCCCCCCC
17.9528796482
871UbiquitinationSFNYVLSKSTKADIG
HHHHHHCCCCCCCCC
58.9729967540
872PhosphorylationFNYVLSKSTKADIGP
HHHHHCCCCCCCCCC
31.5918691976
873PhosphorylationNYVLSKSTKADIGPN
HHHHCCCCCCCCCCC
33.7129214152
874UbiquitinationYVLSKSTKADIGPNL
HHHCCCCCCCCCCCH
51.6729967540
885UbiquitinationGPNLDQLKDDEILRH
CCCHHHCCHHHHHHH
58.4629967540
905PhosphorylationIISITNESQNAESNV
EEEEECCCCCCCCCC
30.7019664994
913PhosphorylationQNAESNVSIIEIADD
CCCCCCCEEEEEHHH
23.3118691976
943PhosphorylationAKLEEEPSASSPQYA
HHHHCCCCCCCCCEE
44.0228731282
945PhosphorylationLEEEPSASSPQYACD
HHCCCCCCCCCEEEE
47.0625850435
946PhosphorylationEEEPSASSPQYACDF
HCCCCCCCCCEEEEE
18.7528731282
949PhosphorylationPSASSPQYACDFNLF
CCCCCCCEEEEEEEE
16.7529496963
968PhosphorylationADNRQNFSSQSLEHV
CCCCCCCCHHHHHHH
34.7130266825
969PhosphorylationDNRQNFSSQSLEHVE
CCCCCCCHHHHHHHH
21.4630266825
971PhosphorylationRQNFSSQSLEHVEKE
CCCCCHHHHHHHHHH
37.3630266825
977UbiquitinationQSLEHVEKENSLCGS
HHHHHHHHHCCCCCC
62.1929967540
980PhosphorylationEHVEKENSLCGSAPN
HHHHHHCCCCCCCCC
26.5729255136
984PhosphorylationKENSLCGSAPNSRAG
HHCCCCCCCCCCCCC
39.2925159151
988PhosphorylationLCGSAPNSRAGFVHS
CCCCCCCCCCCCEEE
23.5822199227
995PhosphorylationSRAGFVHSKTCLSWE
CCCCCEEECEEEEEE
25.1017192257
997PhosphorylationAGFVHSKTCLSWEFS
CCCEEECEEEEEECC
22.9922199227
1000PhosphorylationVHSKTCLSWEFSEKD
EEECEEEEEECCCCC
27.0625159151
1004PhosphorylationTCLSWEFSEKDDEPE
EEEEEECCCCCCCCC
32.0225159151
1016UbiquitinationEPEEVVVKAKIRSKA
CCCEEEEHHHHHHHH
32.1429967540
1028PhosphorylationSKARRIVSDGEDEDD
HHHHHHHCCCCCCCC
37.2119664994
1036PhosphorylationDGEDEDDSFKDTSSI
CCCCCCCCCCCCCCC
46.6623927012
1038UbiquitinationEDEDDSFKDTSSINP
CCCCCCCCCCCCCCC
65.1429967540
1040PhosphorylationEDDSFKDTSSINPFN
CCCCCCCCCCCCCCC
25.6023898821
1041PhosphorylationDDSFKDTSSINPFNT
CCCCCCCCCCCCCCC
39.0830175587
1042PhosphorylationDSFKDTSSINPFNTS
CCCCCCCCCCCCCCC
28.6023898821
1048PhosphorylationSSINPFNTSLFQFSS
CCCCCCCCCCCCCCC
27.4726074081
1049PhosphorylationSINPFNTSLFQFSSV
CCCCCCCCCCCCCCC
28.4327050516
1054PhosphorylationNTSLFQFSSVKQFDA
CCCCCCCCCCCEECC
24.3626074081
1055PhosphorylationTSLFQFSSVKQFDAS
CCCCCCCCCCEECCC
34.3226074081
1062PhosphorylationSVKQFDASTPKNDIS
CCCEECCCCCCCCCC
47.2721712546
1063PhosphorylationVKQFDASTPKNDISP
CCEECCCCCCCCCCC
39.7521712546
1065UbiquitinationQFDASTPKNDISPPG
EECCCCCCCCCCCCC
68.3029967540
1069PhosphorylationSTPKNDISPPGRFFS
CCCCCCCCCCCCCCC
28.1029255136
1076PhosphorylationSPPGRFFSSQIPSSV
CCCCCCCCCCCCHHH
20.7220068231
1077PhosphorylationPPGRFFSSQIPSSVN
CCCCCCCCCCCHHHC
27.2925159151
1081PhosphorylationFFSSQIPSSVNKSMN
CCCCCCCHHHCHHHH
48.8525159151
1082PhosphorylationFSSQIPSSVNKSMNS
CCCCCCHHHCHHHHH
25.1025159151
1085AcetylationQIPSSVNKSMNSRRS
CCCHHHCHHHHHCHH
49.2625953088
1085UbiquitinationQIPSSVNKSMNSRRS
CCCHHHCHHHHHCHH
49.2629967540
1086PhosphorylationIPSSVNKSMNSRRSL
CCHHHCHHHHHCHHH
20.2826055452
1089PhosphorylationSVNKSMNSRRSLASR
HHCHHHHHCHHHHHH
22.0421712546
1098PhosphorylationRSLASRRSLINMVLD
HHHHHHHHHHHHHHH
32.2725159151
1102UbiquitinationSRRSLINMVLDHVED
HHHHHHHHHHHHHHH
2.2232015554
1117PhosphorylationMEERLDDSSEAKGPE
HHHHCCCCCCCCCCC
29.7329978859
1118PhosphorylationEERLDDSSEAKGPED
HHHCCCCCCCCCCCC
48.8729978859
1126PhosphorylationEAKGPEDYPEEGVEE
CCCCCCCCCCCCCCC
15.7530576142
1134PhosphorylationPEEGVEESSGEASKY
CCCCCCCCCCCHHHC
30.0925159151
1135PhosphorylationEEGVEESSGEASKYT
CCCCCCCCCCHHHCC
43.8825159151
1139PhosphorylationEESSGEASKYTEEDP
CCCCCCHHHCCCCCC
23.1523663014
1141PhosphorylationSSGEASKYTEEDPSG
CCCCHHHCCCCCCCC
19.5230576142
1142PhosphorylationSGEASKYTEEDPSGE
CCCHHHCCCCCCCCC
36.3121406692
1147PhosphorylationKYTEEDPSGETLSSE
HCCCCCCCCCCCCCC
62.6821406692
1150PhosphorylationEEDPSGETLSSENKS
CCCCCCCCCCCCCCC
35.1530576142
1152PhosphorylationDPSGETLSSENKSSW
CCCCCCCCCCCCCCC
42.9225159151
1153PhosphorylationPSGETLSSENKSSWL
CCCCCCCCCCCCCCC
48.5825159151
1156MethylationETLSSENKSSWLMTS
CCCCCCCCCCCCCCC
41.64-
1158PhosphorylationLSSENKSSWLMTSKP
CCCCCCCCCCCCCCH
26.3227251275
1166PhosphorylationWLMTSKPSALAQETS
CCCCCCHHHHHHCCC
39.3826074081
1172PhosphorylationPSALAQETSLGAPEP
HHHHHHCCCCCCCCC
19.7118691976
1173PhosphorylationSALAQETSLGAPEPL
HHHHHCCCCCCCCCC
24.8525159151
1181PhosphorylationLGAPEPLSGEQLVGS
CCCCCCCCCCCCCCC
51.5025159151
1188PhosphorylationSGEQLVGSPQDKAAE
CCCCCCCCHHHHHHH
16.3525159151
1197PhosphorylationQDKAAEATNDYETLV
HHHHHHHCCHHHHHH
21.8126074081
1200PhosphorylationAAEATNDYETLVKRG
HHHHCCHHHHHHHHC
16.9428796482
1202PhosphorylationEATNDYETLVKRGKE
HHCCHHHHHHHHCHH
30.5328796482
1205UbiquitinationNDYETLVKRGKELKE
CHHHHHHHHCHHHHH
59.5529967540
1225UbiquitinationEALNCLVKALDIKSA
HHHHHHHHHHCCCCC
30.2232015554
1240PhosphorylationDPEVMLLTLSLYKQL
CHHHHHHHHHHHHHH
15.4426270265
1242PhosphorylationEVMLLTLSLYKQLNN
HHHHHHHHHHHHHHC
25.1521712546

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
1063TPhosphorylationKinaseCDK1P06493
PSP
1063TPhosphorylationKinasePLK1P53350
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERC6L_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 ERC6L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBCC1_HUMANRB1CC1physical
17353931
RFA3_HUMANRPA3physical
17353931
IF4B_HUMANEIF4Bphysical
26496610
LDHA_HUMANLDHAphysical
26496610
PLK1_HUMANPLK1physical
26496610
PLK1_HUMANPLK1physical
28514442
SIX1_HUMANSIX1physical
28514442
MIDN_HUMANMIDNphysical
28514442
CHK1_HUMANCHEK1physical
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 ERC6L_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-1028 AND SER-1098, ANDMASS 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-755, 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-820; SER-1028; SER-1135AND SER-1188, 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-14; SER-774; SER-807;SER-810; THR-813; SER-820; SER-1028 AND SER-1069, 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-14; SER-755; SER-774;THR-805; SER-807; SER-810; SER-820; THR-826; SER-828; SER-829;SER-968; SER-969; SER-971; SER-980; SER-984; SER-995; SER-1000;SER-1004; SER-1028; SER-1036; THR-1040; SER-1041; SER-1042; SER-1069;SER-1098; SER-1181 AND SER-1188, AND MASS SPECTROMETRY.
"PICH, a centromere-associated SNF2 family ATPase, is regulated byPlk1 and required for the spindle checkpoint.";
Baumann C., Koerner R., Hofmann K., Nigg E.A.;
Cell 128:101-114(2007).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,PHOSPHORYLATION AT THR-1063, INTERACTION WITH PLK1, AND MUTAGENESIS OF127-GLY--THR-129 AND THR-1063.

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