SMRC1_HUMAN - dbPTM
SMRC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRC1_HUMAN
UniProt AC Q92922
Protein Name SWI/SNF complex subunit SMARCC1
Gene Name SMARCC1
Organism Homo sapiens (Human).
Sequence Length 1105
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex. [PubMed: 10078207 Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity]
Protein Sequence MAAAAGGGGPGTAVGATGSGIAAAAAGLAVYRRKDGGPATKFWESPETVSQLDSVRVWLGKHYKKYVHADAPTNKTLAGLVVQLLQFQEDAFGKHVTNPAFTKLPAKCFMDFKAGGALCHILGAAYKYKNEQGWRRFDLQNPSRMDRNVEMFMNIEKTLVQNNCLTRPNIYLIPDIDLKLANKLKDIIKRHQGTFTDEKSKASHHIYPYSSSQDDEEWLRPVMRKEKQVLVHWGFYPDSYDTWVHSNDVDAEIEDPPIPEKPWKVHVKWILDTDIFNEWMNEEDYEVDENRKPVSFRQRISTKNEEPVRSPERRDRKASANARKRKHSPSPPPPTPTESRKKSGKKGQASLYGKRRSQKEEDEQEDLTKDMEDPTPVPNIEEVVLPKNVNLKKDSENTPVKGGTVADLDEQDEETVTAGGKEDEDPAKGDQSRSVDLGEDNVTEQTNHIIIPSYASWFDYNCIHVIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLTGDVCAVMRVHAFLEQWGLVNYQVDPESRPMAMGPPPTPHFNVLADTPSGLVPLHLRSPQVPAAQQMLNFPEKNKEKPVDLQNFGLRTDIYSKKTLAKSKGASAGREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLENSDASLGPLAYQPVPFSQSGNPVMSTVAFLASVVDPRVASAAAKAALEEFSRVREEVPLELVEAHVKKVQEAARASGKVDPTYGLESSCIAGTGPDEPEKLEGAEEEKMEADPDGQQPEKAENKVENETDEGDKAQDGENEKNSEKEQDSEVSEDTKSEEKETEENKELTDTCKERESDTGKKKVEHEISEGNVATAAAAALASAATKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREKEALEQQRQQLLTERQNFHMEQLKYAELRARQQMEQQQHGQNPQQAHQHSGGPGLAPLGAAGHPGMMPHQQPPPYPLMHHQMPPPHPPQPGQIPGPGSMMPGQHMPGRMIPTVAANIHPSGSGPTPPGMPPMPGNILGPRVPLTAPNGMYPPPPQQQPPPPPPADGVPPPPAPGPPASAAP
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------MAAAAGGGG
------CCCCCCCCC		19.6722814378
12PhosphorylationAGGGGPGTAVGATGS
CCCCCCCCCCCCHHH		22.7024043423
17PhosphorylationPGTAVGATGSGIAAA
CCCCCCCHHHHHHHH		26.4224043423
19PhosphorylationTAVGATGSGIAAAAA
CCCCCHHHHHHHHHH		23.7524043423
31PhosphorylationAAAGLAVYRRKDGGP
HHHHHEEEECCCCCC		10.0922210691
40PhosphorylationRKDGGPATKFWESPE
CCCCCCCCCCCCCCC		29.8823898821
41AcetylationKDGGPATKFWESPET
CCCCCCCCCCCCCCH		51.0625953088
41UbiquitinationKDGGPATKFWESPET
CCCCCCCCCCCCCCH		51.06-
45PhosphorylationPATKFWESPETVSQL
CCCCCCCCCCHHHHH		20.7323898821
48PhosphorylationKFWESPETVSQLDSV
CCCCCCCHHHHHHHH		28.9223898821
50PhosphorylationWESPETVSQLDSVRV
CCCCCHHHHHHHHHH		32.2323898821
54PhosphorylationETVSQLDSVRVWLGK
CHHHHHHHHHHHCHH		22.0323898821
56MethylationVSQLDSVRVWLGKHY
HHHHHHHHHHCHHHH		20.18115917193
61AcetylationSVRVWLGKHYKKYVH
HHHHHCHHHHHHEEC		41.4125953088
65AcetylationWLGKHYKKYVHADAP
HCHHHHHHEECCCCC		45.3927452117
65UbiquitinationWLGKHYKKYVHADAP
HCHHHHHHEECCCCC		45.39-
66NitrationLGKHYKKYVHADAPT
CHHHHHHEECCCCCC		8.04-
66PhosphorylationLGKHYKKYVHADAPT
CHHHHHHEECCCCCC		8.0428152594
107AcetylationAFTKLPAKCFMDFKA
HHCCCCCHHHCCCCH		26.5126051181
107UbiquitinationAFTKLPAKCFMDFKA
HHCCCCCHHHCCCCH		26.51-
127AcetylationHILGAAYKYKNEQGW
HHHHHHHCCCCCCCC		45.0523749302
129AcetylationLGAAYKYKNEQGWRR
HHHHHCCCCCCCCCC		50.2726051181
129UbiquitinationLGAAYKYKNEQGWRR
HHHHHCCCCCCCCCC		50.27-
171PhosphorylationCLTRPNIYLIPDIDL
CCCCCCEEECCCCCH		12.7617360941
179AcetylationLIPDIDLKLANKLKD
ECCCCCHHHHHHHHH		41.6326051181
179SumoylationLIPDIDLKLANKLKD
ECCCCCHHHHHHHHH		41.6328112733
179UbiquitinationLIPDIDLKLANKLKD
ECCCCCHHHHHHHHH		41.63-
183UbiquitinationIDLKLANKLKDIIKR
CCHHHHHHHHHHHHH		51.84-
185UbiquitinationLKLANKLKDIIKRHQ
HHHHHHHHHHHHHCC		48.79-
189UbiquitinationNKLKDIIKRHQGTFT
HHHHHHHHHCCCCCC		44.13-
199AcetylationQGTFTDEKSKASHHI
CCCCCCCCCCCCCCC		61.1325953088
199UbiquitinationQGTFTDEKSKASHHI
CCCCCCCCCCCCCCC		61.13-
201UbiquitinationTFTDEKSKASHHIYP
CCCCCCCCCCCCCCC		66.04-
211PhosphorylationHHIYPYSSSQDDEEW
CCCCCCCCCCCCHHH		26.6128464451
212PhosphorylationHIYPYSSSQDDEEWL
CCCCCCCCCCCHHHH		31.52-
295PhosphorylationDENRKPVSFRQRIST
CCCCCCCCHHHHHCC		24.2026074081
301PhosphorylationVSFRQRISTKNEEPV
CCHHHHHCCCCCCCC		35.2026074081
302PhosphorylationSFRQRISTKNEEPVR
CHHHHHCCCCCCCCC		35.2024732914
303AcetylationFRQRISTKNEEPVRS
HHHHHCCCCCCCCCC		56.4225953088
310PhosphorylationKNEEPVRSPERRDRK
CCCCCCCCHHHHHHH		31.2029255136
319PhosphorylationERRDRKASANARKRK
HHHHHHHHHHHHHHC		25.709744861
328PhosphorylationNARKRKHSPSPPPPT
HHHHHCCCCCCCCCC		30.0629255136
330PhosphorylationRKRKHSPSPPPPTPT
HHHCCCCCCCCCCCC		53.7229255136
335PhosphorylationSPSPPPPTPTESRKK
CCCCCCCCCCHHHHH		48.9222167270
337PhosphorylationSPPPPTPTESRKKSG
CCCCCCCCHHHHHCC		49.4222167270
339PhosphorylationPPPTPTESRKKSGKK
CCCCCCHHHHHCCCC		52.4522167270
345AcetylationESRKKSGKKGQASLY
HHHHHCCCCCCHHHH		61.9019608861
346AcetylationSRKKSGKKGQASLYG
HHHHCCCCCCHHHHC		60.8319608861
350PhosphorylationSGKKGQASLYGKRRS
CCCCCCHHHHCHHHC		17.7823401153
352PhosphorylationKKGQASLYGKRRSQK
CCCCHHHHCHHHCCC		20.3626074081
354AcetylationGQASLYGKRRSQKEE
CCHHHHCHHHCCCHH		30.9519608861
357PhosphorylationSLYGKRRSQKEEDEQ
HHHCHHHCCCHHHHH		50.0323401153
359SumoylationYGKRRSQKEEDEQED
HCHHHCCCHHHHHHH		65.40-
359AcetylationYGKRRSQKEEDEQED
HCHHHCCCHHHHHHH		65.4019608861
359SumoylationYGKRRSQKEEDEQED
HCHHHCCCHHHHHHH		65.4028112733
368PhosphorylationEDEQEDLTKDMEDPT
HHHHHHHHHCCCCCC		37.0021815630
369AcetylationDEQEDLTKDMEDPTP
HHHHHHHHCCCCCCC		63.4826051181
375PhosphorylationTKDMEDPTPVPNIEE
HHCCCCCCCCCCCCE		49.6029978859
387AcetylationIEEVVLPKNVNLKKD
CCEEECCCCCCCCCC		70.1723236377
395PhosphorylationNVNLKKDSENTPVKG
CCCCCCCCCCCCCCC		41.4423401153
398PhosphorylationLKKDSENTPVKGGTV
CCCCCCCCCCCCCEE		25.9630266825
401AcetylationDSENTPVKGGTVADL
CCCCCCCCCCEECCC		53.4826051181
404PhosphorylationNTPVKGGTVADLDEQ
CCCCCCCEECCCCCC		22.6130266825
415PhosphorylationLDEQDEETVTAGGKE
CCCCCCCCCCCCCCC		22.5530266825
417PhosphorylationEQDEETVTAGGKEDE
CCCCCCCCCCCCCCC		27.3130266825
421AcetylationETVTAGGKEDEDPAK
CCCCCCCCCCCCCCC		62.1626051181
421UbiquitinationETVTAGGKEDEDPAK
CCCCCCCCCCCCCCC		62.1621906983
428AcetylationKEDEDPAKGDQSRSV
CCCCCCCCCCCCCCC		69.2926051181
428UbiquitinationKEDEDPAKGDQSRSV
CCCCCCCCCCCCCCC		69.2921906983
432PhosphorylationDPAKGDQSRSVDLGE
CCCCCCCCCCCCCCC		31.1230576142
434PhosphorylationAKGDQSRSVDLGEDN
CCCCCCCCCCCCCCC		25.8228348404
478UbiquitinationLPEFFNGKNKSKTPE
CHHHHCCCCCCCCCH		63.41-
480UbiquitinationEFFNGKNKSKTPEIY
HHHCCCCCCCCCHHH		57.74-
481PhosphorylationFFNGKNKSKTPEIYL
HHCCCCCCCCCHHHH		51.6721406692
482UbiquitinationFNGKNKSKTPEIYLA
HCCCCCCCCCHHHHE		70.48-
483PhosphorylationNGKNKSKTPEIYLAY
CCCCCCCCCHHHHEE		32.9921406692
487PhosphorylationKSKTPEIYLAYRNFM
CCCCCHHHHEECCCC		5.4321406692
490PhosphorylationTPEIYLAYRNFMIDT
CCHHHHEECCCCEEE		11.9620068231
505PhosphorylationYRLNPQEYLTSTACR
CCCCHHHHHHHHHHH		15.2728152594
507PhosphorylationLNPQEYLTSTACRRN
CCHHHHHHHHHHHCC		24.1128152594
508PhosphorylationNPQEYLTSTACRRNL
CHHHHHHHHHHHCCC		16.0628152594
509PhosphorylationPQEYLTSTACRRNLT
HHHHHHHHHHHCCCC		25.2528152594
511GlutathionylationEYLTSTACRRNLTGD
HHHHHHHHHCCCCHH		4.2122555962
520GlutathionylationRNLTGDVCAVMRVHA
CCCCHHHHHHHHHHH		2.5522555962
523SulfoxidationTGDVCAVMRVHAFLE
CHHHHHHHHHHHHHH		1.6521406390
543PhosphorylationNYQVDPESRPMAMGP
EEEECCCCCCCCCCC		47.26-
553PhosphorylationMAMGPPPTPHFNVLA
CCCCCCCCCCCEEEC		34.8629255136
562PhosphorylationHFNVLADTPSGLVPL
CCEEECCCCCCCEEE		17.4726074081
564PhosphorylationNVLADTPSGLVPLHL
EEECCCCCCCEEEEC		47.0226074081
573PhosphorylationLVPLHLRSPQVPAAQ
CEEEECCCCCCCHHH		26.5023401153
582SulfoxidationQVPAAQQMLNFPEKN
CCCHHHHHHCCCHHH		1.8821406390
588AcetylationQMLNFPEKNKEKPVD
HHHCCCHHHCCCCCC		73.8223749302
588UbiquitinationQMLNFPEKNKEKPVD
HHHCCCHHHCCCCCC		73.8221906983
590UbiquitinationLNFPEKNKEKPVDLQ
HCCCHHHCCCCCCHH		77.51-
592AcetylationFPEKNKEKPVDLQNF
CCHHHCCCCCCHHHC		52.5325953088
592SumoylationFPEKNKEKPVDLQNF
CCHHHCCCCCCHHHC		52.5328112733
592UbiquitinationFPEKNKEKPVDLQNF
CCHHHCCCCCCHHHC		52.5321906983
606PhosphorylationFGLRTDIYSKKTLAK
CCCCCCCCCHHHHHH		19.76-
608AcetylationLRTDIYSKKTLAKSK
CCCCCCCHHHHHHCC		32.5719608861
624PhosphorylationASAGREWTEQETLLL
CCCCCCCCHHHHHHH		24.0423532336
644UbiquitinationMYKDDWNKVSEHVGS
HHHHCHHHHHHHHCC		42.77-
657GlutathionylationGSRTQDECILHFLRL
CCCCHHHHHHHHHCC		5.5822555962
716UbiquitinationRVASAAAKAALEEFS
HHHHHHHHHHHHHHH		29.4821906983
723PhosphorylationKAALEEFSRVREEVP
HHHHHHHHHHHCCCC		32.9024670416
739AcetylationELVEAHVKKVQEAAR
HHHHHHHHHHHHHHH		37.0425953088
739SumoylationELVEAHVKKVQEAAR
HHHHHHHHHHHHHHH		37.0428112733
739UbiquitinationELVEAHVKKVQEAAR
HHHHHHHHHHHHHHH		37.04-
740UbiquitinationLVEAHVKKVQEAARA
HHHHHHHHHHHHHHH		48.32-
748PhosphorylationVQEAARASGKVDPTY
HHHHHHHCCCCCCCC		33.3328555341
750AcetylationEAARASGKVDPTYGL
HHHHHCCCCCCCCCC		40.7525953088
750UbiquitinationEAARASGKVDPTYGL
HHHHHCCCCCCCCCC		40.75-
760PhosphorylationPTYGLESSCIAGTGP
CCCCCCCHHCCCCCC		10.5228555341
792AcetylationPDGQQPEKAENKVEN
CCCCCCHHHHHHCCC		68.6222424773
796AcetylationQPEKAENKVENETDE
CCHHHHHHCCCCCCC		42.2922424773
796SumoylationQPEKAENKVENETDE
CCHHHHHHCCCCCCC		42.2928112733
801PhosphorylationENKVENETDEGDKAQ
HHHCCCCCCCCCCCC		51.4330576142
816PhosphorylationDGENEKNSEKEQDSE
CCCCCCCCHHHHHHH		62.2029255136
822PhosphorylationNSEKEQDSEVSEDTK
CCHHHHHHHCCCCHH		39.3229255136
825PhosphorylationKEQDSEVSEDTKSEE
HHHHHHCCCCHHHHH		26.2125159151
828PhosphorylationDSEVSEDTKSEEKET
HHHCCCCHHHHHHHH		32.2130576142
829SumoylationSEVSEDTKSEEKETE
HHCCCCHHHHHHHHH		69.0928112733
829UbiquitinationSEVSEDTKSEEKETE
HHCCCCHHHHHHHHH		69.0921906983
830PhosphorylationEVSEDTKSEEKETEE
HCCCCHHHHHHHHHH		53.7525159151
835PhosphorylationTKSEEKETEENKELT
HHHHHHHHHHHHHHH		60.7227251275
846UbiquitinationKELTDTCKERESDTG
HHHHHHHHHHCCHHC		63.00-
856AcetylationESDTGKKKVEHEISE
CCHHCCHHEEEECHH		57.2326051181
856SumoylationESDTGKKKVEHEISE
CCHHCCHHEEEECHH		57.2328112733
856UbiquitinationESDTGKKKVEHEISE
CCHHCCHHEEEECHH		57.23-
876PhosphorylationAAAAALASAATKAKH
HHHHHHHHHHHHHHH		21.2021712546
879PhosphorylationAALASAATKAKHLAA
HHHHHHHHHHHHHHH		31.11-
880UbiquitinationALASAATKAKHLAAV
HHHHHHHHHHHHHHH		51.1921906983
882UbiquitinationASAATKAKHLAAVEE
HHHHHHHHHHHHHHH		40.4821906983
893UbiquitinationAVEERKIKSLVALLV
HHHHHHHHHHHHHHH		40.5521906983
894PhosphorylationVEERKIKSLVALLVE
HHHHHHHHHHHHHHH		31.3928348404
905UbiquitinationLLVETQMKKLEIKLR
HHHHHHHHHHHHHHH		44.3721906983
906UbiquitinationLVETQMKKLEIKLRH
HHHHHHHHHHHHHHH		46.1121906983
910UbiquitinationQMKKLEIKLRHFEEL
HHHHHHHHHHHHHHH		30.0521906983
919PhosphorylationRHFEELETIMDREKE
HHHHHHHHHHHHHHH		33.9428857561
925UbiquitinationETIMDREKEALEQQR
HHHHHHHHHHHHHHH		49.5421906983
948AcetylationNFHMEQLKYAELRAR
HHCHHHHHHHHHHHH		41.9519608861
948UbiquitinationNFHMEQLKYAELRAR
HHCHHHHHHHHHHHH		41.9521906983
1064Asymmetric dimethylargininePGNILGPRVPLTAPN
CCCCCCCCCCCCCCC		40.67-
1064MethylationPGNILGPRVPLTAPN
CCCCCCCCCCCCCCC		40.67-
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 SMRC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRC1_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 SMRC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PB1_HUMANPBRM1physical
19650111
ARI1A_HUMANARID1Aphysical
19650111
SMRC2_HUMANSMARCC2physical
19650111
SNF5_HUMANSMARCB1physical
18809673
SMCA4_HUMANSMARCA4physical
18809673
SMCE1_HUMANSMARCE1physical
18809673
AKT1_HUMANAKT1physical
16568092
SNF5_HUMANSMARCB1physical
16568092
SMCA4_HUMANSMARCA4physical
16452305
SMCA2_HUMANSMARCA2physical
16452305
ANM5_HUMANPRMT5physical
14559996
ARI1A_HUMANARID1Aphysical
16230384
ARI1B_HUMANARID1Bphysical
16230384
SMCA4_HUMANSMARCA4physical
16230384
SMCA2_HUMANSMARCA2physical
16230384
SMRC2_HUMANSMARCC2physical
16230384
SMRC1_HUMANSMARCC1physical
16230384
SMCE1_HUMANSMARCE1physical
16199878
ANDR_MOUSEArphysical
15923603
ARI1A_HUMANARID1Aphysical
15170388
ARI1B_HUMANARID1Bphysical
15170388
SMCA4_HUMANSMARCA4physical
9584200
SNF5_HUMANSMARCB1physical
9584200
SNF5_HUMANSMARCB1physical
21520050
SMCA4_HUMANSMARCA4physical
21520050
P53_MOUSETrp53physical
18303029
SMCA4_HUMANSMARCA4physical
18303029
SNF5_HUMANSMARCB1physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
ATL4_HUMANADAMTSL4physical
25416956
ACL6A_HUMANACTL6Aphysical
26344197
ARI1A_HUMANARID1Aphysical
26344197
ARI1B_HUMANARID1Bphysical
26344197
REQU_HUMANDPF2physical
26344197
DPF3_HUMANDPF3physical
26344197
KDM1A_HUMANKDM1Aphysical
26344197
MESD_HUMANMESDC2physical
26344197
MRE11_HUMANMRE11Aphysical
26344197
SAMD9_HUMANSAMD9physical
26344197
SNF5_HUMANSMARCB1physical
26344197
SMRD1_HUMANSMARCD1physical
26344197
SMRD2_HUMANSMARCD2physical
26344197
SMRD3_HUMANSMARCD3physical
26344197
SMCE1_HUMANSMARCE1physical
26344197
SSXT_HUMANSS18physical
26344197
CREST_HUMANSS18L1physical
26344197
TBL1R_HUMANTBL1XR1physical
26344197
NCOA1_HUMANNCOA1physical
15923603
ARI1A_HUMANARID1Aphysical
9584200
SMRC2_HUMANSMARCC2physical
9584200
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 SMRC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-345; LYS-346; LYS-354;LYS-359 AND LYS-948, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-310; SER-328; SER-330;THR-335; THR-337; SER-357 AND SER-573, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-319; SER-328;SER-330; THR-335; THR-337 AND SER-357, AND MASS SPECTROMETRY.
"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-310; SER-328 ANDSER-330, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330 ANDTHR-335, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, ANDMASS SPECTROMETRY.
"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-328; SER-330 ANDSER-573, 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 SER-328; SER-330; THR-335AND SER-339, AND MASS SPECTROMETRY.
"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-310, AND MASSSPECTROMETRY.
"Mitotic inactivation of a human SWI/SNF chromatin remodelingcomplex.";
Sif S., Stukenberg P.T., Kirschner M.W., Kingston R.E.;
Genes Dev. 12:2842-2851(1998).
Cited for: PHOSPHORYLATION AT THE G2/M TRANSITION.

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