VIME_MOUSE - dbPTM
VIME_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIME_MOUSE
UniProt AC P20152
Protein Name Vimentin
Gene Name Vim
Organism Mus musculus (Mouse).
Sequence Length 466
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Nucleus matrix .
Protein Description Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.; Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2..
Protein Sequence MSTRSVSSSSYRRMFGGSGTSSRPSSNRSYVTTSTRTYSLGSALRPSTSRSLYSSSPGGAYVTRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPTFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
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------MSTRSVSSS
------CCCCCCCCH
32.31-
2Phosphorylation------MSTRSVSSS
------CCCCCCCCH
32.3126745281
3Phosphorylation-----MSTRSVSSSS
-----CCCCCCCCHH
26.1826745281
5Phosphorylation---MSTRSVSSSSYR
---CCCCCCCCHHCH
26.8327087446
7Phosphorylation-MSTRSVSSSSYRRM
-CCCCCCCCHHCHHH
26.2527087446
7O-linked_Glycosylation-MSTRSVSSSSYRRM
-CCCCCCCCHHCHHH
26.25-
8PhosphorylationMSTRSVSSSSYRRMF
CCCCCCCCHHCHHHC
22.5823684622
9PhosphorylationSTRSVSSSSYRRMFG
CCCCCCCHHCHHHCC
24.7123684622
10PhosphorylationTRSVSSSSYRRMFGG
CCCCCCHHCHHHCCC
25.3027149854
11Nitrated tyrosineRSVSSSSYRRMFGGS
CCCCCHHCHHHCCCC
12.27-
11PhosphorylationRSVSSSSYRRMFGGS
CCCCCHHCHHHCCCC
12.2724899341
18PhosphorylationYRRMFGGSGTSSRPS
CHHHCCCCCCCCCCC
39.0026824392
20PhosphorylationRMFGGSGTSSRPSSN
HHCCCCCCCCCCCCC
25.8123684622
21PhosphorylationMFGGSGTSSRPSSNR
HCCCCCCCCCCCCCC
28.0723684622
21O-linked_GlycosylationMFGGSGTSSRPSSNR
HCCCCCCCCCCCCCC
28.0721540332
22PhosphorylationFGGSGTSSRPSSNRS
CCCCCCCCCCCCCCC
48.3124899341
25PhosphorylationSGTSSRPSSNRSYVT
CCCCCCCCCCCCEEE
38.8522942356
26PhosphorylationGTSSRPSSNRSYVTT
CCCCCCCCCCCEEEE
38.667530295
29PhosphorylationSRPSSNRSYVTTSTR
CCCCCCCCEEEEECC
28.3625263469
30PhosphorylationRPSSNRSYVTTSTRT
CCCCCCCEEEEECCE
9.8926160508
32O-linked_GlycosylationSSNRSYVTTSTRTYS
CCCCCEEEEECCEEE
13.5421540332
32PhosphorylationSSNRSYVTTSTRTYS
CCCCCEEEEECCEEE
13.5424453211
33PhosphorylationSNRSYVTTSTRTYSL
CCCCEEEEECCEEEC
20.3226160508
33O-linked_GlycosylationSNRSYVTTSTRTYSL
CCCCEEEEECCEEEC
20.32-
34PhosphorylationNRSYVTTSTRTYSLG
CCCEEEEECCEEECC
13.4127149854
34O-linked_GlycosylationNRSYVTTSTRTYSLG
CCCEEEEECCEEECC
13.4121540332
35PhosphorylationRSYVTTSTRTYSLGS
CCEEEEECCEEECCC
25.5726160508
37PhosphorylationYVTTSTRTYSLGSAL
EEEEECCEEECCCCC
19.9727087446
38PhosphorylationVTTSTRTYSLGSALR
EEEECCEEECCCCCC
9.9026060331
39PhosphorylationTTSTRTYSLGSALRP
EEECCEEECCCCCCC
26.1627087446
39O-linked_GlycosylationTTSTRTYSLGSALRP
EEECCEEECCCCCCC
26.1621540332
42PhosphorylationTRTYSLGSALRPSTS
CCEEECCCCCCCCCC
29.4428725479
47PhosphorylationLGSALRPSTSRSLYS
CCCCCCCCCCCCCCC
32.3622942356
48PhosphorylationGSALRPSTSRSLYSS
CCCCCCCCCCCCCCC
30.7322942356
48O-linked_GlycosylationGSALRPSTSRSLYSS
CCCCCCCCCCCCCCC
30.7321540332
49PhosphorylationSALRPSTSRSLYSSS
CCCCCCCCCCCCCCC
24.9822942356
49O-linked_GlycosylationSALRPSTSRSLYSSS
CCCCCCCCCCCCCCC
24.9821540332
51PhosphorylationLRPSTSRSLYSSSPG
CCCCCCCCCCCCCCC
31.2727087446
53PhosphorylationPSTSRSLYSSSPGGA
CCCCCCCCCCCCCCE
14.0428725479
54PhosphorylationSTSRSLYSSSPGGAY
CCCCCCCCCCCCCEE
29.6323527152
54O-linked_GlycosylationSTSRSLYSSSPGGAY
CCCCCCCCCCCCCEE
29.6321540332
55PhosphorylationTSRSLYSSSPGGAYV
CCCCCCCCCCCCEEE
27.3127087446
55O-linked_GlycosylationTSRSLYSSSPGGAYV
CCCCCCCCCCCCEEE
27.3121540332
56PhosphorylationSRSLYSSSPGGAYVT
CCCCCCCCCCCEEEE
22.9427087446
61PhosphorylationSSSPGGAYVTRSSAV
CCCCCCEEEECCCCC
12.9627149854
63PhosphorylationSPGGAYVTRSSAVRL
CCCCEEEECCCCCCC
16.5027742792
65PhosphorylationGGAYVTRSSAVRLRS
CCEEEECCCCCCCCC
17.1821454597
66PhosphorylationGAYVTRSSAVRLRSS
CEEEECCCCCCCCCC
27.747530295
72PhosphorylationSSAVRLRSSVPGVRL
CCCCCCCCCCCCCHH
40.037530295
73PhosphorylationSAVRLRSSVPGVRLL
CCCCCCCCCCCCHHC
26.3726824392
83PhosphorylationGVRLLQDSVDFSLAD
CCHHCCCCCCHHHHH
15.6015140879
87PhosphorylationLQDSVDFSLADAINT
CCCCCCHHHHHHHCC
20.4126824392
94PhosphorylationSLADAINTEFKNTRT
HHHHHHCCCCCCCCC
36.3629119230
97UbiquitinationDAINTEFKNTRTNEK
HHHCCCCCCCCCCCC
51.70-
104UbiquitinationKNTRTNEKVELQELN
CCCCCCCCEEHHHHH
42.98-
104AcetylationKNTRTNEKVELQELN
CCCCCCCCEEHHHHH
42.9823806337
104SuccinylationKNTRTNEKVELQELN
CCCCCCCCEEHHHHH
42.9823806337
117PhosphorylationLNDRFANYIDKVRFL
HHHHHHHHHHHHHHH
13.6826824392
120MethylationRFANYIDKVRFLEQQ
HHHHHHHHHHHHHHH
26.25-
120AcetylationRFANYIDKVRFLEQQ
HHHHHHHHHHHHHHH
26.2523806337
120SuccinylationRFANYIDKVRFLEQQ
HHHHHHHHHHHHHHH
26.25-
120UbiquitinationRFANYIDKVRFLEQQ
HHHHHHHHHHHHHHH
26.25-
120SuccinylationRFANYIDKVRFLEQQ
HHHHHHHHHHHHHHH
26.2523806337
129AcetylationRFLEQQNKILLAELE
HHHHHHCHHHHHHHH
30.3223806337
129SuccinylationRFLEQQNKILLAELE
HHHHHHCHHHHHHHH
30.32-
129SuccinylationRFLEQQNKILLAELE
HHHHHHCHHHHHHHH
30.3223806337
139AcetylationLAELEQLKGQGKSRL
HHHHHHHCCCCCCCH
49.2123806337
139UbiquitinationLAELEQLKGQGKSRL
HHHHHHHCCCCCCCH
49.21-
139SuccinylationLAELEQLKGQGKSRL
HHHHHHHCCCCCCCH
49.2123806337
143UbiquitinationEQLKGQGKSRLGDLY
HHHCCCCCCCHHHHH
25.2322790023
144PhosphorylationQLKGQGKSRLGDLYE
HHCCCCCCCHHHHHH
39.2926824392
150PhosphorylationKSRLGDLYEEEMREL
CCCHHHHHHHHHHHH
26.4919854140
168AcetylationVDQLTNDKARVEVER
HHHHHCCHHHHHHCC
39.9123806337
168UbiquitinationVDQLTNDKARVEVER
HHHHHCCHHHHHHCC
39.91-
168SuccinylationVDQLTNDKARVEVER
HHHHHCCHHHHHHCC
39.9123806337
188AcetylationDIMRLREKLQEEMLQ
HHHHHHHHHHHHHHH
49.3823806337
188SuccinylationDIMRLREKLQEEMLQ
HHHHHHHHHHHHHHH
49.38-
188UbiquitinationDIMRLREKLQEEMLQ
HHHHHHHHHHHHHHH
49.38-
188SuccinylationDIMRLREKLQEEMLQ
HHHHHHHHHHHHHHH
49.3823806337
201PhosphorylationLQREEAESTLQSFRQ
HHHHHHHHHHHHHHH
41.2726824392
202PhosphorylationQREEAESTLQSFRQD
HHHHHHHHHHHHHHH
21.9626824392
205PhosphorylationEAESTLQSFRQDVDN
HHHHHHHHHHHHHCH
26.0526824392
214PhosphorylationRQDVDNASLARLDLE
HHHHCHHHHHHHHHH
28.9027087446
223AcetylationARLDLERKVESLQEE
HHHHHHHHHHHHHHH
40.7623806337
223UbiquitinationARLDLERKVESLQEE
HHHHHHHHHHHHHHH
40.76-
223SuccinylationARLDLERKVESLQEE
HHHHHHHHHHHHHHH
40.7623806337
226PhosphorylationDLERKVESLQEEIAF
HHHHHHHHHHHHHHH
38.0427180971
235AcetylationQEEIAFLKKLHDEEI
HHHHHHHHHHCHHHH
47.0023806337
235UbiquitinationQEEIAFLKKLHDEEI
HHHHHHHHHHCHHHH
47.00-
235SuccinylationQEEIAFLKKLHDEEI
HHHHHHHHHHCHHHH
47.0023806337
236UbiquitinationEEIAFLKKLHDEEIQ
HHHHHHHHHCHHHHH
53.88-
261PhosphorylationVQIDVDVSKPDLTAA
CEEEECCCCHHHHHH
33.7326824392
276PhosphorylationLRDVRQQYESVAAKN
HHHHHHHHHHHHHHC
11.2222817900
278PhosphorylationDVRQQYESVAAKNLQ
HHHHHHHHHHHHCHH
16.4824899341
282UbiquitinationQYESVAAKNLQEAEE
HHHHHHHHCHHHHHH
48.7522790023
291PhosphorylationLQEAEEWYKSKFADL
HHHHHHHHHHHHHHH
14.5225367039
292AcetylationQEAEEWYKSKFADLS
HHHHHHHHHHHHHHH
48.52134195
292UbiquitinationQEAEEWYKSKFADLS
HHHHHHHHHHHHHHH
48.5222790023
293PhosphorylationEAEEWYKSKFADLSE
HHHHHHHHHHHHHHH
19.8025367039
294AcetylationAEEWYKSKFADLSEA
HHHHHHHHHHHHHHH
40.1823806337
294SuccinylationAEEWYKSKFADLSEA
HHHHHHHHHHHHHHH
40.18-
294UbiquitinationAEEWYKSKFADLSEA
HHHHHHHHHHHHHHH
40.18-
294SuccinylationAEEWYKSKFADLSEA
HHHHHHHHHHHHHHH
40.1823806337
299PhosphorylationKSKFADLSEAANRNN
HHHHHHHHHHHHHCH
26.2426824392
325PhosphorylationEYRRQVQSLTCEVDA
HHHHHHHHHHHHHHH
27.1325521595
327PhosphorylationRRQVQSLTCEVDALK
HHHHHHHHHHHHHHH
16.3327742792
328S-nitrosocysteineRQVQSLTCEVDALKG
HHHHHHHHHHHHHHC
6.10-
328GlutathionylationRQVQSLTCEVDALKG
HHHHHHHHHHHHHHC
6.1024333276
328S-nitrosylationRQVQSLTCEVDALKG
HHHHHHHHHHHHHHC
6.1020925432
328S-palmitoylationRQVQSLTCEVDALKG
HHHHHHHHHHHHHHC
6.1028526873
334UbiquitinationTCEVDALKGTNESLE
HHHHHHHHCCCHHHH
66.4622790023
334AcetylationTCEVDALKGTNESLE
HHHHHHHHCCCHHHH
66.4622826441
336PhosphorylationEVDALKGTNESLERQ
HHHHHHCCCHHHHHH
33.9425619855
339PhosphorylationALKGTNESLERQMRE
HHHCCCHHHHHHHHH
37.2927087446
358PhosphorylationFALEAANYQDTIGRL
HHHHHHHHHHHHHHH
11.7530635358
361PhosphorylationEAANYQDTIGRLQDE
HHHHHHHHHHHHHHH
15.1430635358
373AcetylationQDEIQNMKEEMARHL
HHHHHHHHHHHHHHH
59.0623806337
373UbiquitinationQDEIQNMKEEMARHL
HHHHHHHHHHHHHHH
59.06-
373SuccinylationQDEIQNMKEEMARHL
HHHHHHHHHHHHHHH
59.0623806337
383Nitrated tyrosineMARHLREYQDLLNVK
HHHHHHHHHHHHCHH
10.82-
383PhosphorylationMARHLREYQDLLNVK
HHHHHHHHHHHHCHH
10.8225367039
402UbiquitinationIEIATYRKLLEGEES
HHHHHHHHHHCCCCC
47.1922790023
409PhosphorylationKLLEGEESRISLPLP
HHHCCCCCCCCCCCC
30.5224899341
412PhosphorylationEGEESRISLPLPTFS
CCCCCCCCCCCCCCC
23.877530295
417PhosphorylationRISLPLPTFSSLNLR
CCCCCCCCCCCCCCC
43.7826824392
419PhosphorylationSLPLPTFSSLNLRET
CCCCCCCCCCCCCCC
36.0727087446
420PhosphorylationLPLPTFSSLNLRETN
CCCCCCCCCCCCCCC
19.6527087446
426PhosphorylationSSLNLRETNLESLPL
CCCCCCCCCCHHCCC
38.3726824392
430PhosphorylationLRETNLESLPLVDTH
CCCCCCHHCCCCCCC
38.1525521595
436PhosphorylationESLPLVDTHSKRTLL
HHCCCCCCCCCCEEE
22.1425521595
438PhosphorylationLPLVDTHSKRTLLIK
CCCCCCCCCCEEEEE
26.4026824392
439AcetylationPLVDTHSKRTLLIKT
CCCCCCCCCEEEEEE
41.6223806337
439UbiquitinationPLVDTHSKRTLLIKT
CCCCCCCCCEEEEEE
41.62-
439SuccinylationPLVDTHSKRTLLIKT
CCCCCCCCCEEEEEE
41.6223806337
441PhosphorylationVDTHSKRTLLIKTVE
CCCCCCCEEEEEEEE
29.6529514104
445AcetylationSKRTLLIKTVETRDG
CCCEEEEEEEECCCC
46.6223806337
445SuccinylationSKRTLLIKTVETRDG
CCCEEEEEEEECCCC
46.62-
445UbiquitinationSKRTLLIKTVETRDG
CCCEEEEEEEECCCC
46.62-
445SuccinylationSKRTLLIKTVETRDG
CCCEEEEEEEECCCC
46.6223806337
446PhosphorylationKRTLLIKTVETRDGQ
CCEEEEEEEECCCCC
19.3126824392
449PhosphorylationLLIKTVETRDGQVIN
EEEEEEECCCCCEEC
29.7129550500
458PhosphorylationDGQVINETSQHHDDL
CCCEECCCCCCCCCC
29.2427087446
459PhosphorylationGQVINETSQHHDDLE
CCEECCCCCCCCCCC
22.7225521595

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
5SPhosphorylationKinasePKC-FAMILY-GPS
5SPhosphorylationKinasePKC_GROUP-PhosphoELM
5SPhosphorylationKinasePKA_GROUP-PhosphoELM
5SPhosphorylationKinasePKA-FAMILY-GPS
7SPhosphorylationKinasePRKCAP20444
GPS
7SPhosphorylationKinasePRKACAP05132
GPS
7SPhosphorylationKinaseAURKBO70126
GPS
7SPhosphorylationKinasePKC-Uniprot
7SPhosphorylationKinasePKA-Uniprot
7SPhosphorylationKinasePKC-FAMILY-GPS
7SPhosphorylationKinasePKA-FAMILY-GPS
8SPhosphorylationKinasePKC_GROUP-PhosphoELM
8SPhosphorylationKinasePKC-FAMILY-GPS
9SPhosphorylationKinasePKC-Uniprot
9SPhosphorylationKinasePKC-FAMILY-GPS
9SPhosphorylationKinasePRKCAP20444
GPS
10SPhosphorylationKinasePRKCAP20444
GPS
10SPhosphorylationKinasePKC-FAMILY-GPS
10SPhosphorylationKinasePKC-Uniprot
21SPhosphorylationKinasePKC-FAMILY-GPS
21SPhosphorylationKinasePKC_GROUP-PhosphoELM
21SPhosphorylationKinasePKC-Uniprot
21SPhosphorylationKinasePRKCAP20444
GPS
25SPhosphorylationKinasePKC-FAMILY-GPS
25SPhosphorylationKinasePKA-FAMILY-GPS
25SPhosphorylationKinasePKA-Uniprot
25SPhosphorylationKinasePRKCAP20444
GPS
25SPhosphorylationKinasePKC-Uniprot
25SPhosphorylationKinaseAURKBO70126
GPS
25SPhosphorylationKinasePRKACAP05132
GPS
26SPhosphorylationKinasePRKCAP20444
GPS
26SPhosphorylationKinasePKC-Uniprot
26SPhosphorylationKinasePKC-FAMILY-GPS
34SPhosphorylationKinasePRKCAP20444
GPS
34SPhosphorylationKinasePKC-FAMILY-GPS
34SPhosphorylationKinasePKC-Uniprot
34SPhosphorylationKinasePKC_GROUP-PhosphoELM
39SPhosphorylationKinasePKC-Uniprot
39SPhosphorylationKinaseAURKBO70126
GPS
39SPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
39SPhosphorylationKinasePRKACAP05132
GPS
39SPhosphorylationKinasePRKCAP20444
GPS
39SPhosphorylationKinasePKC-FAMILY-GPS
39SPhosphorylationKinaseCAMK2AP11275
PSP
39SPhosphorylationKinaseCAMK2BP28652
GPS
39SPhosphorylationKinaseROCK2P70336
Uniprot
39SPhosphorylationKinasePKA-Uniprot
39SPhosphorylationKinaseCAMK2-FAMILY-GPS
39SPhosphorylationKinaseCAMK2-Uniprot
39SPhosphorylationKinasePKA-FAMILY-GPS
42SPhosphorylationKinasePKC_GROUP-PhosphoELM
42SPhosphorylationKinasePRKCAP20444
GPS
42SPhosphorylationKinasePKC-Uniprot
42SPhosphorylationKinasePKC-FAMILY-GPS
47SPhosphorylationKinasePKA-Uniprot
47SPhosphorylationKinaseAURKBO70126
GPS
47SPhosphorylationKinasePKA_GROUP-PhosphoELM
47SPhosphorylationKinasePKA-FAMILY-GPS
47SPhosphorylationKinasePRKACAP05132
GPS
51SPhosphorylationKinasePRKACAP05132
GPS
51SPhosphorylationKinasePKC_GROUP-PhosphoELM
51SPhosphorylationKinasePKC-FAMILY-GPS
51SPhosphorylationKinasePKACAP17612
PSP
51SPhosphorylationKinasePRKCAP20444
GPS
51SPhosphorylationKinasePKC-Uniprot
51SPhosphorylationKinasePKA_GROUP-PhosphoELM
51SPhosphorylationKinasePKA-FAMILY-GPS
51SPhosphorylationKinasePKA-Uniprot
56SPhosphorylationKinaseCDK_GROUP-PhosphoELM
56SPhosphorylationKinaseCDK-FAMILY-GPS
56SPhosphorylationKinaseCDK1P11440
PSP
56SPhosphorylationKinaseCDK1P06493
PSP
65SPhosphorylationKinaseAURKBO70126
GPS
66SPhosphorylationKinasePKC-FAMILY-GPS
66SPhosphorylationKinasePKA-FAMILY-GPS
66SPhosphorylationKinasePRKCAP20444
GPS
66SPhosphorylationKinasePRKACAP05132
GPS
66SPhosphorylationKinasePKA-Uniprot
66SPhosphorylationKinasePKC-Uniprot
66SPhosphorylationKinaseAURKBO70126
GPS
72SPhosphorylationKinaseROCK2P70336
Uniprot
72SPhosphorylationKinaseROCK1P70335
PSP
72SPhosphorylationKinaseROCK1Q13464
PSP
72SPhosphorylationKinaseAURKBO70126
Uniprot
73SPhosphorylationKinaseAURKBO70126
PhosphoELM
83SPhosphorylationKinaseCAMK2-Uniprot
83SPhosphorylationKinaseCAMK2-FAMILY-GPS
83SPhosphorylationKinasePLK1P53350
PSP
83SPhosphorylationKinaseCAMK2BP28652
GPS
83SPhosphorylationKinaseCAMK2AP11275
PSP
83SPhosphorylationKinaseCAMK2AP11798
PSP
83SPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
87SPhosphorylationKinaseAURKBO70126
GPS
459SPhosphorylationKinasePLK1P53350
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
55SPhosphorylation

-
56SPhosphorylation

17242355

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 VIME_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPARG_MOUSEPpargphysical
23297177
RAB7A_HUMANRAB7Aphysical
26496610
PHB2_HUMANPHB2physical
26496610
ZBT11_HUMANZBTB11physical
26496610
CENPJ_HUMANCENPJphysical
26496610
SYNCI_HUMANSYNCphysical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIME_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56;SER-66; SER-419; SER-420; SER-430 AND SER-459, AND MASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-214, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-72; SER-73;SER-144; SER-226; SER-430 AND SER-459, AND MASS SPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-73, AND MASSSPECTROMETRY.
"Phosphorylation of vimentin by Rho-associated kinase at a uniqueamino-terminal site that is specifically phosphorylated duringcytokinesis.";
Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M.,Kaibuchi K., Inagaki M.;
J. Biol. Chem. 273:11728-11736(1998).
Cited for: PHOSPHORYLATION AT SER-39 AND SER-72.
"Evidence that Ser-82 is a unique phosphorylation site on vimentin forCa2(+)-calmodulin-dependent protein kinase II.";
Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.;
Biochem. Biophys. Res. Commun. 175:955-962(1991).
Cited for: PHOSPHORYLATION AT SER-39 AND SER-83.
"Domain- and sequence-specific phosphorylation of vimentin inducesdisassembly of the filament structure.";
Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.;
Biochemistry 28:2974-2979(1989).
Cited for: PROTEIN SEQUENCE OF 5-69, AND PHOSPHORYLATION AT SER-7; SER-9; SER-10;SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 ANDSER-66.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, AND MASSSPECTROMETRY.

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