SMRC2_HUMAN - dbPTM
SMRC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRC2_HUMAN
UniProt AC Q8TAQ2
Protein Name SWI/SNF complex subunit SMARCC2
Gene Name SMARCC2
Organism Homo sapiens (Human).
Sequence Length 1214
Subcellular Localization Nucleus.
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. [PubMed: 11018012 Can stimulate the ATPase activity of the catalytic subunit of these complexes]
Protein Sequence MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIIKRHQGTVTEDKNNASHVVYPVPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVNDDKNPVSRRKKISAKTLTDEVNSPDSDRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQEDESMETTGKDEDENSTGNKGEQTKNPDLHEDNVTEQTHHIIIPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKTPQQTSASQQMLNFPDKGKEKPTDMQNFGLRTDMYTKKNVPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTTSDEPERIEESGNDEARVEGQATDEKKEPKEPREGGGAIEEEAKEKTSEAPKKDEEKGKEGDSEKESEKSDGDPIVDPEKEKEPKEGQEEVLKEVVESEGERKTKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMHQQQQQPPPALPPGSQPIPPTGAAGPPAVHGLAVAPASVVPAPAGSGAPPGSLGPSEQIGQAGSTAGPQQQQPAGAPQPGAVPPGVPPPGPHGPSPFPNQQTPPSMMPGAVPGSGHPGVAGNAPLGLPFGMPPPPPPPAPSIIPFGSLADSISINLPAPPNLHGHHHHLPFAPGTLPPPNLPVSMANPLHPNLPATTTMPSSLPLGPGLGSAAAQSPAIVAAVQGNLLPSASPLPDPGTPLPPDPTAPSPGTVTPVPPPQ
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
13AcetylationKDGGPNVKYYEAADT
CCCCCCCEEEECCCC		49.0726051181
33AcetylationNVRLWLGKNYKKYIQ
CEEEECCCCHHHHHC		55.7425953088
37MalonylationWLGKNYKKYIQAEPP
ECCCCHHHHHCCCCC		36.9126320211
37UbiquitinationWLGKNYKKYIQAEPP
ECCCCHHHHHCCCCC		36.91-
38PhosphorylationLGKNYKKYIQAEPPT
CCCCHHHHHCCCCCC		8.3028152594
69PhosphorylationEVFGKHVSNAPLTKL
HHHCCCCCCCCCCCC		27.3025159151
79AcetylationPLTKLPIKCFLDFKA
CCCCCCEEEEEEECC		19.5926051181
99AcetylationHILAAAYKFKSDQGW
HHHHHHHHCCCCCCC		41.4025953088
101AcetylationLAAAYKFKSDQGWRR
HHHHHHCCCCCCCCC		49.3127452117
102PhosphorylationAAAYKFKSDQGWRRY
HHHHHCCCCCCCCCC		38.0020068231
102 (in isoform 2)Phosphorylation-38.00-
145S-nitrosocysteineSRPNIFLCPEIEPKL
CCCCEEECCCCCHHH		1.66-
145S-nitrosylationSRPNIFLCPEIEPKL
CCCCEEECCCCCHHH		1.6622178444
151AcetylationLCPEIEPKLLGKLKD
ECCCCCHHHHHHHHH		43.4826051181
157UbiquitinationPKLLGKLKDIIKRHQ
HHHHHHHHHHHHHCC		50.82-
161UbiquitinationGKLKDIIKRHQGTVT
HHHHHHHHHCCCCCC		44.13-
175PhosphorylationTEDKNNASHVVYPVP
CCCCCCCCEEEEECC		20.9520860994
179PhosphorylationNNASHVVYPVPGNLE
CCCCEEEEECCCCCC		9.4520860994
230PhosphorylationASVEDAPTPEKPRKV
EECCCCCCCCCCCCC		45.8925159151
275AcetylationRRKKISAKTLTDEVN
HHHCCCCEECCCCCC		36.9623236377
275UbiquitinationRRKKISAKTLTDEVN
HHHCCCCEECCCCCC		36.9621890473
275 (in isoform 1)Ubiquitination-36.9621890473
275 (in isoform 2)Ubiquitination-36.9621890473
276PhosphorylationRKKISAKTLTDEVNS
HHCCCCEECCCCCCC		34.3123927012
278PhosphorylationKISAKTLTDEVNSPD
CCCCEECCCCCCCCC		35.0330278072
283PhosphorylationTLTDEVNSPDSDRRD
ECCCCCCCCCCCCCC		34.9519664994
283 (in isoform 2)Phosphorylation-34.95-
286PhosphorylationDEVNSPDSDRRDKKG
CCCCCCCCCCCCCCC		36.0822167270
286 (in isoform 2)Phosphorylation-36.08-
296PhosphorylationRDKKGGNYKKRKRSP
CCCCCCCCCCCCCCC		22.5917924679
296 (in isoform 2)Phosphorylation-22.59-
302PhosphorylationNYKKRKRSPSPSPTP
CCCCCCCCCCCCCCH		32.5329255136
302 (in isoform 2)Phosphorylation-32.53-
304PhosphorylationKKRKRSPSPSPTPEA
CCCCCCCCCCCCHHH		38.9829255136
304 (in isoform 2)Phosphorylation-38.98-
306PhosphorylationRKRSPSPSPTPEAKK
CCCCCCCCCCHHHHH		45.8229255136
306 (in isoform 2)Phosphorylation-45.82-
308PhosphorylationRSPSPSPTPEAKKKN
CCCCCCCCHHHHHHC		37.7929255136
308 (in isoform 2)Phosphorylation-37.79-
321PhosphorylationKNAKKGPSTPYTKSK
HCCCCCCCCCCCCCC		51.1625159151
321 (in isoform 2)Phosphorylation-51.16-
322PhosphorylationNAKKGPSTPYTKSKR
CCCCCCCCCCCCCCC		24.3723401153
322 (in isoform 2)Phosphorylation-24.37-
324PhosphorylationKKGPSTPYTKSKRGH
CCCCCCCCCCCCCCC		27.2123403867
325PhosphorylationKGPSTPYTKSKRGHR
CCCCCCCCCCCCCCC		30.0023403867
326AcetylationGPSTPYTKSKRGHRE
CCCCCCCCCCCCCCH		48.4119608861
326 (in isoform 2)Acetylation-48.41-
327PhosphorylationPSTPYTKSKRGHREE
CCCCCCCCCCCCCHH		21.5621712546
340PhosphorylationEEEQEDLTKDMDEPS
HHHHHHHHCCCCCCC		37.0021815630
347PhosphorylationTKDMDEPSPVPNVEE
HCCCCCCCCCCCCEE		36.1629255136
347 (in isoform 2)Phosphorylation-36.16-
356PhosphorylationVPNVEEVTLPKTVNT
CCCCEEEECCCEECC		40.3922167270
359AcetylationVEEVTLPKTVNTKKD
CEEEECCCEECCCCC		69.1223236377
360PhosphorylationEEVTLPKTVNTKKDS
EEEECCCEECCCCCC		19.6326074081
363PhosphorylationTLPKTVNTKKDSESA
ECCCEECCCCCCCCC		34.8226074081
367PhosphorylationTVNTKKDSESAPVKG
EECCCCCCCCCCCCC		42.1829396449
369PhosphorylationNTKKDSESAPVKGGT
CCCCCCCCCCCCCCC		41.6524247654
373AcetylationDSESAPVKGGTMTDL
CCCCCCCCCCCCCCC		51.0326051181
376PhosphorylationSAPVKGGTMTDLDEQ
CCCCCCCCCCCCHHH		26.0923927012
378PhosphorylationPVKGGTMTDLDEQED
CCCCCCCCCCHHHCC		32.9923927012
387PhosphorylationLDEQEDESMETTGKD
CHHHCCHHHHHCCCC		33.9530278072
390PhosphorylationQEDESMETTGKDEDE
HCCHHHHHCCCCCCC		32.0130278072
391PhosphorylationEDESMETTGKDEDEN
CCHHHHHCCCCCCCC		29.0030576142
399PhosphorylationGKDEDENSTGNKGEQ
CCCCCCCCCCCCCCC		35.3330278072
399 (in isoform 2)Phosphorylation-35.33-
400PhosphorylationKDEDENSTGNKGEQT
CCCCCCCCCCCCCCC		57.2530278072
407PhosphorylationTGNKGEQTKNPDLHE
CCCCCCCCCCCCCCC		28.6130278072
453AcetylationLPEFFNGKNKSKTPE
CHHHHCCCCCCCCCH		63.4126051181
453UbiquitinationLPEFFNGKNKSKTPE
CHHHHCCCCCCCCCH		63.41-
456PhosphorylationFFNGKNKSKTPEIYL
HHCCCCCCCCCHHHH		51.6721406692
457MalonylationFNGKNKSKTPEIYLA
HCCCCCCCCCHHHHE		70.4826320211
457UbiquitinationFNGKNKSKTPEIYLA
HCCCCCCCCCHHHHE		70.48-
458PhosphorylationNGKNKSKTPEIYLAY
CCCCCCCCCHHHHEE		32.9921406692
462PhosphorylationKSKTPEIYLAYRNFM
CCCCCHHHHEECCCC		5.4321406692
465PhosphorylationTPEIYLAYRNFMIDT
CCHHHHEECCCCEEE		11.9620068231
465 (in isoform 2)Phosphorylation-11.96-
480PhosphorylationYRLNPQEYLTSTACR
CCCCHHHHHHHHHHH		15.2728152594
482PhosphorylationLNPQEYLTSTACRRN
CCHHHHHHHHHHHHH		24.1128152594
483PhosphorylationNPQEYLTSTACRRNL
CHHHHHHHHHHHHHC		16.0628152594
484PhosphorylationPQEYLTSTACRRNLA
HHHHHHHHHHHHHCC		25.2528152594
548PhosphorylationLVPLQPKTPQQTSAS
CCCCCCCCCCCCCHH		32.7729255136
552PhosphorylationQPKTPQQTSASQQML
CCCCCCCCCHHHHHH		22.4825159151
553PhosphorylationPKTPQQTSASQQMLN
CCCCCCCCHHHHHHC		22.9121712546
555PhosphorylationTPQQTSASQQMLNFP
CCCCCCHHHHHHCCC		22.2525159151
564AcetylationQMLNFPDKGKEKPTD
HHHCCCCCCCCCCCC		72.6023236377
564SumoylationQMLNFPDKGKEKPTD
HHHCCCCCCCCCCCC		72.6028112733
564UbiquitinationQMLNFPDKGKEKPTD
HHHCCCCCCCCCCCC		72.6021890473
564 (in isoform 1)Ubiquitination-72.6021890473
566SumoylationLNFPDKGKEKPTDMQ
HCCCCCCCCCCCCHH		69.2028112733
566UbiquitinationLNFPDKGKEKPTDMQ
HCCCCCCCCCCCCHH		69.20-
568AcetylationFPDKGKEKPTDMQNF
CCCCCCCCCCCHHHC		57.6225953088
568SumoylationFPDKGKEKPTDMQNF
CCCCCCCCCCCHHHC		57.6228112733
568UbiquitinationFPDKGKEKPTDMQNF
CCCCCCCCCCCHHHC		57.6221890473
568 (in isoform 1)Ubiquitination-57.6221890473
579PhosphorylationMQNFGLRTDMYTKKN
HHHCCCCCCCCCCCC		30.11-
582PhosphorylationFGLRTDMYTKKNVPS
CCCCCCCCCCCCCCC		20.44-
583PhosphorylationGLRTDMYTKKNVPSK
CCCCCCCCCCCCCCH		28.98-
583 (in isoform 2)Phosphorylation-28.9826714015
583 (in isoform 3)Phosphorylation-28.9826714015
584AcetylationLRTDMYTKKNVPSKS
CCCCCCCCCCCCCHH		25.5125953088
584 (in isoform 2)Phosphorylation-25.5126714015
584 (in isoform 3)Phosphorylation-25.5126714015
586 (in isoform 2)Phosphorylation-53.1125159151
586 (in isoform 3)Phosphorylation-53.1125159151
589PhosphorylationYTKKNVPSKSKAAAS
CCCCCCCCHHHHHHH		45.3223898821
591PhosphorylationKKNVPSKSKAAASAT
CCCCCCHHHHHHHHC		31.6823898821
592SumoylationKNVPSKSKAAASATR
CCCCCHHHHHHHHCC		45.8628112733
596PhosphorylationSKSKAAASATREWTE
CHHHHHHHHCCHHHH		26.0022210691
598PhosphorylationSKAAASATREWTEQE
HHHHHHHCCHHHHHH		26.9922210691
599 (in isoform 2)Ubiquitination-36.8521890473
622UbiquitinationMYKDDWNKVSEHVGS
HHHHCHHHHHHHHCC		42.77-
694UbiquitinationRVASAAAKSALEEFS
HHHHHHHHHHHHHHH		31.3821890473
694 (in isoform 1)Ubiquitination-31.3821890473
695PhosphorylationVASAAAKSALEEFSK
HHHHHHHHHHHHHHH		33.10-
702UbiquitinationSALEEFSKMKEEVPT
HHHHHHHHHHHHCCH		60.3521890473
702 (in isoform 1)Ubiquitination-60.3521890473
704SumoylationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.23-
7042-HydroxyisobutyrylationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.23-
704AcetylationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.2326051181
704SumoylationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.2328112733
704UbiquitinationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.23-
724UbiquitinationRKVEEAAKVTGKADP
HHHHHHHHHHCCCCC		47.58-
725 (in isoform 2)Ubiquitination-7.9621890473
726PhosphorylationVEEAAKVTGKADPAF
HHHHHHHHCCCCCCC		32.05-
728AcetylationEAAKVTGKADPAFGL
HHHHHHCCCCCCCCC		40.0126051181
728UbiquitinationEAAKVTGKADPAFGL
HHHHHHCCCCCCCCC		40.01-
733 (in isoform 2)Ubiquitination-16.2721890473
737PhosphorylationDPAFGLESSGIAGTT
CCCCCCCCCCCCCCC		38.6227732954
738PhosphorylationPAFGLESSGIAGTTS
CCCCCCCCCCCCCCC		25.5021815630
743PhosphorylationESSGIAGTTSDEPER
CCCCCCCCCCCCHHH		17.6927732954
744PhosphorylationSSGIAGTTSDEPERI
CCCCCCCCCCCHHHH		33.0127732954
745PhosphorylationSGIAGTTSDEPERIE
CCCCCCCCCCHHHHH		39.5530108239
754PhosphorylationEPERIEESGNDEARV
CHHHHHHCCCCCCCE		30.0630108239
766PhosphorylationARVEGQATDEKKEPK
CCEECCCCCCCCCCC		36.4826074081
769AcetylationEGQATDEKKEPKEPR
ECCCCCCCCCCCCCC		66.3123749302
787AcetylationGAIEEEAKEKTSEAP
CHHHHHHHHHHCCCC		64.1226051181
787SumoylationGAIEEEAKEKTSEAP
CHHHHHHHHHHCCCC		64.1228112733
795AcetylationEKTSEAPKKDEEKGK
HHHCCCCHHHHHCCC		78.787711389
806PhosphorylationEKGKEGDSEKESEKS
HCCCCCCCHHHHHCC		62.5227362937
810PhosphorylationEGDSEKESEKSDGDP
CCCCHHHHHCCCCCC		62.4829255136
813PhosphorylationSEKESEKSDGDPIVD
CHHHHHCCCCCCCCC		42.6529255136
836UbiquitinationEGQEEVLKEVVESEG
CCHHHHHHHHHHCCC		54.35-
837 (in isoform 2)Phosphorylation-47.86-
841PhosphorylationVLKEVVESEGERKTK
HHHHHHHCCCCCCCC		39.0125159151
841 (in isoform 2)Phosphorylation-39.01-
844 (in isoform 2)Phosphorylation-47.13-
848SumoylationSEGERKTKVERDIGE
CCCCCCCCCEEECCC		45.1728112733
859PhosphorylationDIGEGNLSTAAAAAL
ECCCCCHHHHHHHHH		21.7222210691
860PhosphorylationIGEGNLSTAAAAALA
CCCCCHHHHHHHHHH		24.3922210691
872AcetylationALAAAAVKAKHLAAV
HHHHHHHHHHHHHHH		47.1725953088
872UbiquitinationALAAAAVKAKHLAAV
HHHHHHHHHHHHHHH		47.1721890473
872 (in isoform 1)Ubiquitination-47.1721890473
872 (in isoform 2)Phosphorylation-47.17-
8742-HydroxyisobutyrylationAAAAVKAKHLAAVEE
HHHHHHHHHHHHHHH		33.17-
874UbiquitinationAAAAVKAKHLAAVEE
HHHHHHHHHHHHHHH		33.1721890473
874 (in isoform 1)Ubiquitination-33.1721890473
885UbiquitinationAVEERKIKSLVALLV
HHHHHHHHHHHHHHH		40.5521890473
885 (in isoform 1)Ubiquitination-40.5521890473
886PhosphorylationVEERKIKSLVALLVE
HHHHHHHHHHHHHHH		31.3928348404
897AcetylationLLVETQMKKLEIKLR
HHHHHHHHHHHHHHH		44.3725953088
897UbiquitinationLLVETQMKKLEIKLR
HHHHHHHHHHHHHHH		44.3721906983
897 (in isoform 1)Ubiquitination-44.3721890473
898UbiquitinationLVETQMKKLEIKLRH
HHHHHHHHHHHHHHC		46.1121890473
898 (in isoform 1)Ubiquitination-46.1121890473
902UbiquitinationQMKKLEIKLRHFEEL
HHHHHHHHHHCHHHH		30.0521890473
902 (in isoform 1)Ubiquitination-30.0521890473
903 (in isoform 2)Ubiquitination-6.7221890473
905 (in isoform 2)Ubiquitination-44.9321890473
911PhosphorylationRHFEELETIMDRERE
HCHHHHHHHHHHHHH		33.9428857561
916 (in isoform 2)Ubiquitination-51.0821890473
928 (in isoform 2)Ubiquitination-3.9621890473
929 (in isoform 2)Ubiquitination-20.6621890473
931MethylationRQQLLADRQAFHMEQ
HHHHHHHHHHHHHHH		24.91115917197
933 (in isoform 2)Ubiquitination-9.3721890473
940UbiquitinationAFHMEQLKYAEMRAR
HHHHHHHHHHHHHHH		41.9521890473
940 (in isoform 1)Ubiquitination-41.9521890473
941PhosphorylationFHMEQLKYAEMRARQ
HHHHHHHHHHHHHHH		19.1822817900
969PhosphorylationPPALPPGSQPIPPTG
CCCCCCCCCCCCCCC		38.2622817900
971 (in isoform 2)Ubiquitination-42.6321890473
1124 (in isoform 2)Phosphorylation-20.99-
1208PhosphorylationAPSPGTVTPVPPPQ-
CCCCCCCCCCCCCC-		20.5717081983
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
969SPhosphorylationKinaseATMQ13315
PSP
969SPhosphorylationKinaseATRQ13535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRC2_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 SMRC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTB_HUMANACTBphysical
9845365
PB1_HUMANPBRM1physical
19650111
ARI1A_HUMANARID1Aphysical
19650111
SMRC1_HUMANSMARCC1physical
19650111
SNF5_HUMANSMARCB1physical
18809673
SMCE1_HUMANSMARCE1physical
18809673
SMRC1_HUMANSMARCC1physical
18809673
SMCA4_HUMANSMARCA4physical
18809673
REST_HUMANRESTphysical
12192000
RCOR1_HUMANRCOR1physical
12192000
HDAC1_HUMANHDAC1physical
12192000
HDAC2_HUMANHDAC2physical
12192000
CHD7_HUMANCHD7physical
20130577
ACL6A_HUMANACTL6Aphysical
20305087
ARI1A_HUMANARID1Aphysical
20305087
ARI1B_HUMANARID1Bphysical
20305087
ARID2_HUMANARID2physical
20305087
BRD7_HUMANBRD7physical
20305087
REQU_HUMANDPF2physical
20305087
IMA1_HUMANKPNA2physical
20305087
PB1_HUMANPBRM1physical
20305087
PHF10_HUMANPHF10physical
20305087
SMCA2_HUMANSMARCA2physical
20305087
SMCA4_HUMANSMARCA4physical
20305087
SNF5_HUMANSMARCB1physical
20305087
SMRC1_HUMANSMARCC1physical
20305087
SMRD1_HUMANSMARCD1physical
20305087
SMRD2_HUMANSMARCD2physical
20305087
SMRD3_HUMANSMARCD3physical
20305087
SMCE1_HUMANSMARCE1physical
20305087
SMRD1_HUMANSMARCD1physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
SNUT1_HUMANSART1physical
22939629
ACL6A_HUMANACTL6Aphysical
26344197
ARI1A_HUMANARID1Aphysical
26344197
ARI1B_HUMANARID1Bphysical
26344197
REQU_HUMANDPF2physical
26344197
DPF3_HUMANDPF3physical
26344197
MDC1_HUMANMDC1physical
26344197
MESD_HUMANMESDC2physical
26344197
MRE11_HUMANMRE11Aphysical
26344197
SAMD9_HUMANSAMD9physical
26344197
SNF5_HUMANSMARCB1physical
26344197
SMRC1_HUMANSMARCC1physical
26344197
SMRD1_HUMANSMARCD1physical
26344197
SMRD2_HUMANSMARCD2physical
26344197
SMRD3_HUMANSMARCD3physical
26344197
SMCE1_HUMANSMARCE1physical
26344197
SSXT_HUMANSS18physical
26344197
TBL1R_HUMANTBL1XR1physical
26344197
TXLNA_HUMANTXLNAphysical
26344197
TXLNG_HUMANTXLNGphysical
26344197
BRD7_HUMANBRD7physical
28514442
DPF1_HUMANDPF1physical
28514442
ARID2_HUMANARID2physical
28514442
PB1_HUMANPBRM1physical
28514442
ARI1B_HUMANARID1Bphysical
28514442
BCL7B_HUMANBCL7Bphysical
28514442
SMRD3_HUMANSMARCD3physical
28514442
SNF5_HUMANSMARCB1physical
28514442
SMRD2_HUMANSMARCD2physical
28514442
PHF10_HUMANPHF10physical
28514442
SMCA2_HUMANSMARCA2physical
28514442
SMCA4_HUMANSMARCA4physical
28514442
BRD9_HUMANBRD9physical
28514442
SMRC1_HUMANSMARCC1physical
28514442
UBE3A_HUMANUBE3Aphysical
28514442
ACL6B_HUMANACTL6Bphysical
28514442
ARI1A_HUMANARID1Aphysical
28514442
CREST_HUMANSS18L1physical
28514442
SFPQ_HUMANSFPQphysical
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 SMRC2_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-326, 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-283; SER-286; SER-302;SER-304 AND SER-347, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-806, AND MASSSPECTROMETRY.
"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-302; SER-304 ANDSER-347, 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-302 AND SER-304, 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-347, 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-302; SER-304; SER-306AND SER-347, 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-304, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-296 AND THR-322, ANDMASS SPECTROMETRY.

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