SMG9_HUMAN - dbPTM
SMG9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMG9_HUMAN
UniProt AC Q9H0W8
Protein Name Protein SMG9 {ECO:0000305}
Gene Name SMG9 {ECO:0000312|HGNC:HGNC:25763}
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization
Protein Description Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. [PubMed: 19417104 Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8]
Protein Sequence MSESGHSQPGLYGIERRRRWKEPGSGGPQNLSGPGGRERDYIAPWERERRDASEETSTSVMQKTPIILSKPPAERSKQPPPPTAPAAPPAPAPLEKPIVLMKPREEGKGPVAVTGASTPEGTAPPPPAAPAPPKGEKEGQRPTQPVYQIQNRGMGTAAPAAMDPVVGQAKLLPPERMKHSIKLVDDQMNWCDSAIEYLLDQTDVLVVGVLGLQGTGKSMVMSLLSANTPEEDQRTYVFRAQSAEMKERGGNQTSGIDFFITQERIVFLDTQPILSPSILDHLINNDRKLPPEYNLPHTYVEMQSLQIAAFLFTVCHVVIVVQDWFTDLSLYRFLQTAEMVKPSTPSPSHESSSSSGSDEGTEYYPHLVFLQNKARREDFCPRKLRQMHLMIDQLMAHSHLRYKGTLSMLQCNVFPGLPPDFLDSEVNLFLVPFMDSEAESENPPRAGPGSSPLFSLLPGYRGHPSFQSLVSKLRSQVMSMARPQLSHTILTEKNWFHYAARIWDGVRKSSALAEYSRLLA
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------MSESGHSQP
------CCCCCCCCC		40.2318691976
2Phosphorylation------MSESGHSQP
------CCCCCCCCC		40.2323401153
4Phosphorylation----MSESGHSQPGL
----CCCCCCCCCCC		34.2029255136
7Phosphorylation-MSESGHSQPGLYGI
-CCCCCCCCCCCCCH		41.4129255136
12PhosphorylationGHSQPGLYGIERRRR
CCCCCCCCCHHCCCC		23.2123663014
21MethylationIERRRRWKEPGSGGP
HHCCCCCCCCCCCCC		52.8224129315
25PhosphorylationRRWKEPGSGGPQNLS
CCCCCCCCCCCCCCC		51.8223927012
32PhosphorylationSGGPQNLSGPGGRER
CCCCCCCCCCCCCCC		50.9519664994
41PhosphorylationPGGRERDYIAPWERE
CCCCCCCCCCCHHHH		12.7628796482
53PhosphorylationERERRDASEETSTSV
HHHCCCCCCCCCCHH		40.0123927012
56PhosphorylationRRDASEETSTSVMQK
CCCCCCCCCCHHHHH		33.0023927012
57PhosphorylationRDASEETSTSVMQKT
CCCCCCCCCHHHHHC		23.2023403867
58PhosphorylationDASEETSTSVMQKTP
CCCCCCCCHHHHHCC		32.5323403867
64PhosphorylationSTSVMQKTPIILSKP
CCHHHHHCCEEECCC		11.6522199227
69PhosphorylationQKTPIILSKPPAERS
HHCCEEECCCHHHHC		32.4825003641
70AcetylationKTPIILSKPPAERSK
HCCEEECCCHHHHCC		52.1326051181
114PhosphorylationGKGPVAVTGASTPEG
CCCCEEEECCCCCCC		19.7929255136
117PhosphorylationPVAVTGASTPEGTAP
CEEEECCCCCCCCCC		45.9329255136
118PhosphorylationVAVTGASTPEGTAPP
EEEECCCCCCCCCCC		25.4829255136
122PhosphorylationGASTPEGTAPPPPAA
CCCCCCCCCCCCCCC		34.0429255136
137AcetylationPAPPKGEKEGQRPTQ
CCCCCCCCCCCCCCC		75.6723236377
137UbiquitinationPAPPKGEKEGQRPTQ
CCCCCCCCCCCCCCC		75.67-
143PhosphorylationEKEGQRPTQPVYQIQ
CCCCCCCCCCCEEEE		47.93-
147PhosphorylationQRPTQPVYQIQNRGM
CCCCCCCEEEECCCC		13.4425159151
170UbiquitinationDPVVGQAKLLPPERM
CCCCCCCCCCCHHHH		42.54-
197PhosphorylationWCDSAIEYLLDQTDV
HHHHHHHHHHHCCCE		13.3729759185
202PhosphorylationIEYLLDQTDVLVVGV
HHHHHHCCCEEEEEE		27.9529759185
215PhosphorylationGVLGLQGTGKSMVMS
EEEECCCCCHHHHHH		28.6029759185
218PhosphorylationGLQGTGKSMVMSLLS
ECCCCCHHHHHHHHH		20.2521406692
222PhosphorylationTGKSMVMSLLSANTP
CCHHHHHHHHHCCCC		18.1021406692
225PhosphorylationSMVMSLLSANTPEED
HHHHHHHHCCCCHHH		25.4321406692
228PhosphorylationMSLLSANTPEEDQRT
HHHHHCCCCHHHHCC		31.6221406692
248MethylationQSAEMKERGGNQTSG
CCHHHHHCCCCCCCC		53.45115917277
373UbiquitinationHLVFLQNKARREDFC
EEEEECCHHHCCCCC		30.24-
450PhosphorylationPPRAGPGSSPLFSLL
CCCCCCCCCCHHHHC		31.7329255136
451PhosphorylationPRAGPGSSPLFSLLP
CCCCCCCCCHHHHCC		31.3829255136
455PhosphorylationPGSSPLFSLLPGYRG
CCCCCHHHHCCCCCC		36.3623403867
472UbiquitinationSFQSLVSKLRSQVMS
HHHHHHHHHHHHHHH		40.20-
475PhosphorylationSLVSKLRSQVMSMAR
HHHHHHHHHHHHHHC		37.2522210691
479PhosphorylationKLRSQVMSMARPQLS
HHHHHHHHHHCCCCC		15.5022210691
486PhosphorylationSMARPQLSHTILTEK
HHHCCCCCCEEECCC		17.2126270265
488PhosphorylationARPQLSHTILTEKNW
HCCCCCCEEECCCCH		17.8226270265
491PhosphorylationQLSHTILTEKNWFHY
CCCCEEECCCCHHHH		40.8526270265
508UbiquitinationRIWDGVRKSSALAEY
HHHHCHHHHHHHHHH		46.48-
509PhosphorylationIWDGVRKSSALAEYS
HHHCHHHHHHHHHHH		15.4121406692
510PhosphorylationWDGVRKSSALAEYSR
HHCHHHHHHHHHHHH		30.2721406692
515PhosphorylationKSSALAEYSRLLA--
HHHHHHHHHHHHC--		8.0921406692
516PhosphorylationSSALAEYSRLLA---
HHHHHHHHHHHC---		14.1421406692
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 SMG9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMG9_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 SMG9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMG8_HUMANSMG8physical
19417104
SMG1_HUMANSMG1physical
19417104
DDX11_HUMANDDX11physical
26496610
KPRA_HUMANPRPSAP1physical
26496610
DCAF1_HUMANVPRBPphysical
26496610
SMG1_HUMANSMG1physical
26496610
SMG8_HUMANSMG8physical
26496610
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 SMG9_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-53, AND MASSSPECTROMETRY.
"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-32; SER-53 AND SER-451,AND MASS SPECTROMETRY.
"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-7, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, 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-4 AND SER-7, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASSSPECTROMETRY.

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