SMG7_HUMAN - dbPTM
SMG7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMG7_HUMAN
UniProt AC Q92540
Protein Name Protein SMG7
Gene Name SMG7
Organism Homo sapiens (Human).
Sequence Length 1137
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic, and nuclear. Shuttles between nucleus and cytoplasm.
Protein Description Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation..
Protein Sequence MSLQSAQYLRQAEVLKADMTDSKLGPAEVWTSRQALQDLYQKMLVTDLEYALDKKVEQDLWNHAFKNQITTLQGQAKNRANPNRSEVQANLSLFLEAASGFYTQLLQELCTVFNVDLPCRVKSSQLGIISNKQTHTSAIVKPQSSSCSYICQHCLVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKALESRDEVKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQLVHVTVINLFQLHHLRDFSNETEQHTYSQDEQLCWTQLLALFMSFLGILCKCPLQNESQEESYNAYPLPAVKVSMDWLRLRPRVFQEAVVDERQYIWPWLISLLNSFHPHEEDLSSISATPLPEEFELQGFLALRPSFRNLDFSKGHQGITGDKEGQQRRIRQQRLISIGKWIADNQPRLIQCENEVGKLLFITEIPELILEDPSEAKENLILQETSVIESLAADGSPGLKSVLSTSRNLSNNCDTGEKPVVTFKENIKTREVNRDQGRSFPPKEVRRDYSKGITVTKNDGKKDNNKRKTETKKCTLEKLQETGKQNVAVQVKSQTELRKTPVSEARKTPVTQTPTQASNSQFIPIHHPGAFPPLPSRPGFPPPTYVIPPPVAFSMGSGYTFPAGVSVPGTFLQPTAHSPAGNQVQAGKQSHIPYSQQRPSGPGPMNQGPQQSQPPSQQPLTSLPAQPTAQSTSQLQVQALTQQQQSPTKAVPALGKSPPHHSGFQQYQQADASKQLWNPPQVQGPLGKIMPVKQPYYLQTQDPIKLFEPSLQPPVMQQQPLEKKMKPFPMEPYNHNPSEVKVPEFYWDSSYSMADNRSVMAQQANIDRRGKRSPGVFRPEQDPVPRMPFEKSLLEKPSELMSHSSSFLSLTGFSLNQERYPNNSMFNEVYGKNLTSSSKAELSPSMAPQETSLYSLFEGTPWSPSLPASSDHSTPASQSPHSSNPSSLPSSPPTHNHNSVPFSNFGPIGTPDNRDRRTADRWKTDKPAMGGFGIDYLSATSSSESSWHQASTPSGTWTGHGPSMEDSSAVLMESLKSIWSSSMMHPGPSALEQLLMQQKQKQQRGQGTMNPPH
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------MSLQSAQYL
------CCHHHHHHH		46.5519413330
2 (in isoform 2)Acetylation-46.55-
16UbiquitinationLRQAEVLKADMTDSK
HHHHHHHHCCCCCCC		47.73-
23UbiquitinationKADMTDSKLGPAEVW
HCCCCCCCCCHHHHH		61.34-
24UbiquitinationADMTDSKLGPAEVWT
CCCCCCCCCHHHHHC		13.2321890473
42UbiquitinationALQDLYQKMLVTDLE
HHHHHHHHHHHHHHH		22.20-
46PhosphorylationLYQKMLVTDLEYALD
HHHHHHHHHHHHHHH		30.7929759185
50PhosphorylationMLVTDLEYALDKKVE
HHHHHHHHHHHHHHH		21.5520068231
54UbiquitinationDLEYALDKKVEQDLW
HHHHHHHHHHHHHHH		60.6121906983
54 (in isoform 1)Ubiquitination-60.6121890473
54 (in isoform 2)Ubiquitination-60.6121890473
54 (in isoform 4)Ubiquitination-60.6121890473
55UbiquitinationLEYALDKKVEQDLWN
HHHHHHHHHHHHHHH		51.15-
66UbiquitinationDLWNHAFKNQITTLQ
HHHHHHHHHHHHHHH		49.0421890473
66 (in isoform 1)Ubiquitination-49.0421890473
66 (in isoform 2)Ubiquitination-49.0421890473
77MalonylationTTLQGQAKNRANPNR
HHHHHHHHCCCCCCH		38.7926320211
77UbiquitinationTTLQGQAKNRANPNR
HHHHHHHHCCCCCCH		38.7921906983
77 (in isoform 1)Ubiquitination-38.7921890473
77 (in isoform 2)Ubiquitination-38.7921890473
77 (in isoform 4)Ubiquitination-38.7921890473
122UbiquitinationVDLPCRVKSSQLGII
CCCCCEEEHHHEEEE		25.66-
216UbiquitinationYCRSIAVKFPFPAAS
HHHHHHHHCCCCCCC		37.99-
228UbiquitinationAASTNLQKALSKALE
CCCHHHHHHHHHHHH		55.23-
232AcetylationNLQKALSKALESRDE
HHHHHHHHHHHCCHH		58.8225953088
232MalonylationNLQKALSKALESRDE
HHHHHHHHHHHCCHH		58.8226320211
232UbiquitinationNLQKALSKALESRDE
HHHHHHHHHHHCCHH		58.82-
243UbiquitinationSRDEVKTKWGVSDFI
CCHHHHHHHCHHHHH		35.91-
264UbiquitinationHGHVYLSKSLEKLSP
HCEEEHHHCHHHHHH		57.37-
268UbiquitinationYLSKSLEKLSPLREK
EHHHCHHHHHHHHHH		60.60-
270PhosphorylationSKSLEKLSPLREKLE
HHCHHHHHHHHHHHH		32.7230278072
275UbiquitinationKLSPLREKLEEQFKR
HHHHHHHHHHHHHHH		55.56-
438UbiquitinationFRNLDFSKGHQGITG
HCCCCCCCCCCCCCC		61.48-
447UbiquitinationHQGITGDKEGQQRRI
CCCCCCCHHHHHHHH		66.15-
464AcetylationQRLISIGKWIADNQP
HHHHHHHHHHHCCCC		33.4825953088
464UbiquitinationQRLISIGKWIADNQP
HHHHHHHHHHHCCCC		33.48-
464 (in isoform 4)Ubiquitination-33.48-
509PhosphorylationENLILQETSVIESLA
HHHHEEEHHHHHHHH		18.4828102081
510PhosphorylationNLILQETSVIESLAA
HHHEEEHHHHHHHHC		21.9825159151
514PhosphorylationQETSVIESLAADGSP
EEHHHHHHHHCCCCC		16.5130257219
520PhosphorylationESLAADGSPGLKSVL
HHHHCCCCCCHHHHH		19.1530278072
520 (in isoform 2)Phosphorylation-19.15-
524UbiquitinationADGSPGLKSVLSTSR
CCCCCCHHHHHHHCC		44.42-
525PhosphorylationDGSPGLKSVLSTSRN
CCCCCHHHHHHHCCC		33.0827251275
528PhosphorylationPGLKSVLSTSRNLSN
CCHHHHHHHCCCCCC		23.3730576142
529PhosphorylationGLKSVLSTSRNLSNN
CHHHHHHHCCCCCCC		27.7829449344
530PhosphorylationLKSVLSTSRNLSNNC
HHHHHHHCCCCCCCC		18.7829449344
534PhosphorylationLSTSRNLSNNCDTGE
HHHCCCCCCCCCCCC		29.5528450419
539PhosphorylationNLSNNCDTGEKPVVT
CCCCCCCCCCCCEEE		49.8225159151
542UbiquitinationNNCDTGEKPVVTFKE
CCCCCCCCCEEEEEH		44.44-
573PhosphorylationPKEVRRDYSKGITVT
CHHHCCCHHCCCEEE		15.5224732914
574PhosphorylationKEVRRDYSKGITVTK
HHHCCCHHCCCEEEC		28.7924732914
578PhosphorylationRDYSKGITVTKNDGK
CCHHCCCEEECCCCC		30.6924732914
578 (in isoform 2)Phosphorylation-30.6925849741
580PhosphorylationYSKGITVTKNDGKKD
HHCCCEEECCCCCCC		18.5824732914
581AcetylationSKGITVTKNDGKKDN
HCCCEEECCCCCCCC		49.0230592521
585AcetylationTVTKNDGKKDNNKRK
EEECCCCCCCCCCCC		60.8730592525
617PhosphorylationNVAVQVKSQTELRKT
CEEEEECCCCHHCCC		43.4023927012
619PhosphorylationAVQVKSQTELRKTPV
EEEECCCCHHCCCCC		44.0423927012
624O-linked_GlycosylationSQTELRKTPVSEARK
CCCHHCCCCCHHCCC		23.6130059200
624PhosphorylationSQTELRKTPVSEARK
CCCHHCCCCCHHCCC		23.6123401153
627O-linked_GlycosylationELRKTPVSEARKTPV
HHCCCCCHHCCCCCC		27.0930059200
627PhosphorylationELRKTPVSEARKTPV
HHCCCCCHHCCCCCC		27.0923927012
735 (in isoform 2)Phosphorylation-47.36-
735 (in isoform 4)Phosphorylation-47.3624719451
740PhosphorylationPQQSQPPSQQPLTSL
CCCCCCCCCCCCCCC		48.4020068231
740 (in isoform 2)Phosphorylation-48.40-
740 (in isoform 4)Phosphorylation-48.4021406692
765PhosphorylationQLQVQALTQQQQSPT
HHHHHHHHHCCCCCC		27.6126074081
770PhosphorylationALTQQQQSPTKAVPA
HHHHCCCCCCCCCCC		30.1426074081
771 (in isoform 2)Ubiquitination-33.3121890473
772PhosphorylationTQQQQSPTKAVPALG
HHCCCCCCCCCCCCC		36.5626074081
775UbiquitinationQQSPTKAVPALGKSP
CCCCCCCCCCCCCCC		2.8021890473
780UbiquitinationKAVPALGKSPPHHSG
CCCCCCCCCCCCCCC		61.72-
781PhosphorylationAVPALGKSPPHHSGF
CCCCCCCCCCCCCCH		41.6925159151
786PhosphorylationGKSPPHHSGFQQYQQ
CCCCCCCCCHHHHHH		37.9630266825
791PhosphorylationHHSGFQQYQQADASK
CCCCHHHHHHCCHHH		7.5730266825
797PhosphorylationQYQQADASKQLWNPP
HHHHCCHHHHCCCCC		22.8323403867
798UbiquitinationYQQADASKQLWNPPQ
HHHCCHHHHCCCCCC		51.65-
801 (in isoform 2)Ubiquitination-16.8821890473
801 (in isoform 4)Ubiquitination-16.8821890473
812UbiquitinationQVQGPLGKIMPVKQP
CCCCCCCCCCCCCCC		43.44-
817UbiquitinationLGKIMPVKQPYYLQT
CCCCCCCCCCEEECC		39.4221890473
817 (in isoform 1)Ubiquitination-39.4221890473
820PhosphorylationIMPVKQPYYLQTQDP
CCCCCCCEEECCCCC		17.8320090780
847UbiquitinationMQQQPLEKKMKPFPM
CCCCCCCCCCCCCCC		66.8921906983
847 (in isoform 1)Ubiquitination-66.8921890473
851 (in isoform 2)Phosphorylation-34.77-
865UbiquitinationNHNPSEVKVPEFYWD
CCCHHHCCCCCCCCC		48.28-
872 (in isoform 4)Phosphorylation-19.1428674419
876 (in isoform 5)Phosphorylation-14.9428674419
883 (in isoform 2)Phosphorylation-3.13-
892 (in isoform 2)Phosphorylation-45.51-
897PhosphorylationIDRRGKRSPGVFRPE
CCCCCCCCCCCCCCC		29.5025159151
910DimethylationPEQDPVPRMPFEKSL
CCCCCCCCCCCCHHH		45.71-
910MethylationPEQDPVPRMPFEKSL
CCCCCCCCCCCCHHH		45.7130989391
910 (in isoform 2)Ubiquitination-45.7121890473
916PhosphorylationPRMPFEKSLLEKPSE
CCCCCCHHHCCCHHH		30.8724719451
928PhosphorylationPSELMSHSSSFLSLT
HHHHHHCCCCHHHHH		21.99-
929PhosphorylationSELMSHSSSFLSLTG
HHHHHCCCCHHHHHC		21.4924719451
930PhosphorylationELMSHSSSFLSLTGF
HHHHCCCCHHHHHCC		32.9728348404
933PhosphorylationSHSSSFLSLTGFSLN
HCCCCHHHHHCCCCC		23.1318452278
938PhosphorylationFLSLTGFSLNQERYP
HHHHHCCCCCCCCCC		27.9618452278
943MethylationGFSLNQERYPNNSMF
CCCCCCCCCCCCHHH		42.31115387879
948O-linked_GlycosylationQERYPNNSMFNEVYG
CCCCCCCHHHHHHHC		31.2430059200
954PhosphorylationNSMFNEVYGKNLTSS
CHHHHHHHCCCCCCC		19.0629978859
956UbiquitinationMFNEVYGKNLTSSSK
HHHHHHCCCCCCCCC		30.972190698
956 (in isoform 1)Ubiquitination-30.9721890473
960 (in isoform 4)Ubiquitination-35.4621890473
967PhosphorylationSSSKAELSPSMAPQE
CCCCCCCCCCCCCCC		13.3626074081
969PhosphorylationSKAELSPSMAPQETS
CCCCCCCCCCCCCCC		24.9726074081
997PhosphorylationLPASSDHSTPASQSP
CCCCCCCCCCCHHCC		40.8726074081
998PhosphorylationPASSDHSTPASQSPH
CCCCCCCCCCHHCCC		21.3226074081
1001PhosphorylationSDHSTPASQSPHSSN
CCCCCCCHHCCCCCC		32.1826074081
1003PhosphorylationHSTPASQSPHSSNPS
CCCCCHHCCCCCCCC		23.2926074081
1006PhosphorylationPASQSPHSSNPSSLP
CCHHCCCCCCCCCCC		34.8826074081
1007PhosphorylationASQSPHSSNPSSLPS
CHHCCCCCCCCCCCC		50.1226074081
1010PhosphorylationSPHSSNPSSLPSSPP
CCCCCCCCCCCCCCC		49.0826074081
1011PhosphorylationPHSSNPSSLPSSPPT
CCCCCCCCCCCCCCC		45.6226074081
1014PhosphorylationSNPSSLPSSPPTHNH
CCCCCCCCCCCCCCC		61.8526074081
1015PhosphorylationNPSSLPSSPPTHNHN
CCCCCCCCCCCCCCC		32.7226074081
1018PhosphorylationSLPSSPPTHNHNSVP
CCCCCCCCCCCCCCC		38.4026074081
1023PhosphorylationPPTHNHNSVPFSNFG
CCCCCCCCCCCCCCC		24.5026074081
1027PhosphorylationNHNSVPFSNFGPIGT
CCCCCCCCCCCCCCC		25.7726074081
1034PhosphorylationSNFGPIGTPDNRDRR
CCCCCCCCCCCCCCC		28.3426074081
1075PhosphorylationESSWHQASTPSGTWT
CCCCCCCCCCCCCCC		33.99-
1076PhosphorylationSSWHQASTPSGTWTG
CCCCCCCCCCCCCCC		25.21-
1078PhosphorylationWHQASTPSGTWTGHG
CCCCCCCCCCCCCCC		49.28-
1123UbiquitinationEQLLMQQKQKQQRGQ
HHHHHHHHHHHHCCC		42.44-
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 SMG7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMG7_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 SMG7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HBB_HUMANHBBphysical
21145460
SMG1_HUMANSMG1physical
16452507
MDM2_HUMANMDM2physical
27462439
P53_HUMANTP53physical
27462439
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 SMG7_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-781, 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-897, 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-520 AND SER-781, ANDMASS 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-781, AND MASSSPECTROMETRY.

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