SMAG1_HUMAN - dbPTM
SMAG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAG1_HUMAN
UniProt AC Q9UPU9
Protein Name Protein Smaug homolog 1
Gene Name SAMD4A
Organism Homo sapiens (Human).
Sequence Length 718
Subcellular Localization Cytoplasm . Cell projection, dendrite. Cell junction, synapse, synaptosome. Enriched in synaptoneurosomes (By similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes throughout the cytoplasm in granules wit
Protein Description Acts as a translational repressor of SRE-containing messengers..
Protein Sequence MMFRDQVGVLAGWFKGWNECEQTVALLSLLKRVSQTQARFLQLCLEHSLADCAELHVLEREANSPGIINQWQQESKDKVISLLLTHLPLLKPGNLDAKVEYMKLLPKILAHSIEHNQHIEESRQLLSYALIHPATSLEDRSALAMWLNHLEDRTSTSFGGQNRGRSDSVDYGQTHYYHQRQNSDDKLNGWQNSRDSGICINASNWQDKSMGCENGHVPLYSSSSVPTTINTIGTSTSTILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAPLSPQSSVASSGSGGSEHLEDQTTARNTFQEEGSGMKDVPAWLKSLRLHKYAALFSQMTYEEMMALTECQLEAQNVTKGARHKIVISIQKLKERQNLLKSLERDIIEGGSLRIPLQELHQMILTPIKAYSSPSTTPEARRREPQAPRQPSLMGPESQSPDCKDGAAATGATATPSAGASGGLQPHQLSSCDGELAVAPLPEGDLPGQFTRVMGKVCTQLLVSRPDEENISSYLQLIDKCLIHEAFTETQKKRLLSWKQQVQKLFRSFPRKTLLDISGYRQQRNRGFGQSNSLPTAGSVGGGMGRRNPRQYQIPSRNVPSARLGLLGTSGFVSSNQRNTTATPTIMKQGRQNLWFANPGGSNSMPSRTHSSVQRTRSLPVHTSPQNMLMFQQPEFQLPVTEPDINNRLESLCLSMTEHALGDGVDRTSTI
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
28PhosphorylationEQTVALLSLLKRVSQ
HHHHHHHHHHHHHHH		32.2924719451
127PhosphorylationEESRQLLSYALIHPA
HHHHHHHHHHHHCCC		19.5624260401
128PhosphorylationESRQLLSYALIHPAT
HHHHHHHHHHHCCCC		12.8524260401
135PhosphorylationYALIHPATSLEDRSA
HHHHCCCCCHHHHHH		37.9924260401
136PhosphorylationALIHPATSLEDRSAL
HHHCCCCCHHHHHHH		31.6924260401
166PhosphorylationGGQNRGRSDSVDYGQ
CCCCCCCCCCCCHHH		36.7423403867
167PhosphorylationGQNRGRSDSVDYGQT
CCCCCCCCCCCHHHH		51.8524719451
168PhosphorylationQNRGRSDSVDYGQTH
CCCCCCCCCCHHHHC		20.3822617229
171PhosphorylationGRSDSVDYGQTHYYH
CCCCCCCHHHHCCCC		14.6923403867
174PhosphorylationDSVDYGQTHYYHQRQ
CCCCHHHHCCCCCCC		13.9023403867
176PhosphorylationVDYGQTHYYHQRQNS
CCHHHHCCCCCCCCC		13.1623403867
177PhosphorylationDYGQTHYYHQRQNSD
CHHHHCCCCCCCCCC		5.4923403867
182PhosphorylationHYYHQRQNSDDKLNG
CCCCCCCCCCCCCCC		49.9824719451
183PhosphorylationYYHQRQNSDDKLNGW
CCCCCCCCCCCCCCC		38.5627251789
193PhosphorylationKLNGWQNSRDSGICI
CCCCCCCCCCCCCEE		23.5127794612
247PhosphorylationLSGQAHHSPLKRSVS
HCCCCCCCCCCCCCC		23.2824260401
251PhosphorylationAHHSPLKRSVSLTPP
CCCCCCCCCCCCCCC		50.3924719451
252PhosphorylationHHSPLKRSVSLTPPM
CCCCCCCCCCCCCCC		17.9222496350
253PhosphorylationHSPLKRSVSLTPPMN
CCCCCCCCCCCCCCC		6.7124719451
254PhosphorylationSPLKRSVSLTPPMNV
CCCCCCCCCCCCCCC		27.9822496350
256PhosphorylationLKRSVSLTPPMNVPN
CCCCCCCCCCCCCCC		20.1723090842
271PhosphorylationQPLGHGWMSHEDLRA
CCCCCCCCCHHHHHH		3.2924719451
272PhosphorylationPLGHGWMSHEDLRAR
CCCCCCCCHHHHHHH		19.7422496350
286PhosphorylationRGPQCLPSDHAPLSP
HCCCCCCCCCCCCCC		29.1322210691
292PhosphorylationPSDHAPLSPQSSVAS
CCCCCCCCCCCCCCC		21.6029507054
295PhosphorylationHAPLSPQSSVASSGS
CCCCCCCCCCCCCCC		30.1125850435
296PhosphorylationAPLSPQSSVASSGSG
CCCCCCCCCCCCCCC		19.2223090842
299PhosphorylationSPQSSVASSGSGGSE
CCCCCCCCCCCCCCH		32.8323090842
300PhosphorylationPQSSVASSGSGGSEH
CCCCCCCCCCCCCHH		27.5223090842
302PhosphorylationSSVASSGSGGSEHLE
CCCCCCCCCCCHHCC		41.7625850435
317PhosphorylationDQTTARNTFQEEGSG
CCHHHCHHHHHCCCC		22.5722210691
413PhosphorylationELHQMILTPIKAYSS
HHHHHHHCCHHHCCC		16.4327067055
418PhosphorylationILTPIKAYSSPSTTP
HHCCHHHCCCCCCCH		12.5123927012
419PhosphorylationLTPIKAYSSPSTTPE
HCCHHHCCCCCCCHH		40.4019664994
420PhosphorylationTPIKAYSSPSTTPEA
CCHHHCCCCCCCHHH		15.3619664994
422PhosphorylationIKAYSSPSTTPEARR
HHHCCCCCCCHHHHH		47.0330266825
423PhosphorylationKAYSSPSTTPEARRR
HHCCCCCCCHHHHHC		50.1630266825
424PhosphorylationAYSSPSTTPEARRRE
HCCCCCCCHHHHHCC		24.3830266825
445PhosphorylationPSLMGPESQSPDCKD
CCCCCCCCCCCCCCC		38.8125850435
447PhosphorylationLMGPESQSPDCKDGA
CCCCCCCCCCCCCCC		31.8021815630
511PhosphorylationVCTQLLVSRPDEENI
HHHHHHHCCCCCCCH		37.7624719451
560PhosphorylationFRSFPRKTLLDISGY
HHHCCCCCEEEHHCH		33.5622210691
565PhosphorylationRKTLLDISGYRQQRN
CCCEEEHHCHHHHCC		29.4628555341
567PhosphorylationTLLDISGYRQQRNRG
CEEEHHCHHHHCCCC		9.84-
573MethylationGYRQQRNRGFGQSNS
CHHHHCCCCCCCCCC		43.9618959297
578PhosphorylationRNRGFGQSNSLPTAG
CCCCCCCCCCCCCCC		28.8530266825
579PhosphorylationNRGFGQSNSLPTAGS
CCCCCCCCCCCCCCC		39.4124719451
580PhosphorylationRGFGQSNSLPTAGSV
CCCCCCCCCCCCCCC		40.7630266825
583PhosphorylationGQSNSLPTAGSVGGG
CCCCCCCCCCCCCCC		49.2830266825
586PhosphorylationNSLPTAGSVGGGMGR
CCCCCCCCCCCCCCC		18.3523403867
599PhosphorylationGRRNPRQYQIPSRNV
CCCCCCCCCCCCCCC		15.0823917254
604MethylationRQYQIPSRNVPSARL
CCCCCCCCCCCHHHE		42.69115493253
616PhosphorylationARLGLLGTSGFVSSN
HHEECCCCCCCCCCC		26.1628857561
617PhosphorylationRLGLLGTSGFVSSNQ
HEECCCCCCCCCCCC		28.5628857561
622PhosphorylationGTSGFVSSNQRNTTA
CCCCCCCCCCCCCCC		31.5128555341
630PhosphorylationNQRNTTATPTIMKQG
CCCCCCCCCCCHHHC		20.9029396449
648PhosphorylationLWFANPGGSNSMPSR
EEECCCCCCCCCCCC		25.5524719451
649PhosphorylationWFANPGGSNSMPSRT
EECCCCCCCCCCCCC		31.4830266825
651PhosphorylationANPGGSNSMPSRTHS
CCCCCCCCCCCCCCC		33.4930266825
654PhosphorylationGGSNSMPSRTHSSVQ
CCCCCCCCCCCCCCC		40.9630266825
663PhosphorylationTHSSVQRTRSLPVHT
CCCCCCCCCCCCCCC		13.9121712546
665PhosphorylationSSVQRTRSLPVHTSP
CCCCCCCCCCCCCCC		36.0926846344
669PhosphorylationRTRSLPVHTSPQNML
CCCCCCCCCCCCCEE		20.7724719451
670PhosphorylationTRSLPVHTSPQNMLM
CCCCCCCCCCCCEEE		42.1926846344
671PhosphorylationRSLPVHTSPQNMLMF
CCCCCCCCCCCEEEE		15.0326846344
716PhosphorylationGDGVDRTSTI-----
CCCCCCCCCC-----		25.62-
717PhosphorylationDGVDRTSTI------
CCCCCCCCC------		30.05-
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 SMAG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMAG1_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 SMAG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUTM1_HUMANNUTM1physical
25416956
SHIP2_HUMANINPPL1physical
28514442
TNIP1_HUMANTNIP1physical
28514442
1433Z_HUMANYWHAZphysical
28514442
1433E_HUMANYWHAEphysical
28514442
1433B_HUMANYWHABphysical
28514442
DDB2_HUMANDDB2physical
28514442
1433F_HUMANYWHAHphysical
28514442
CSDE1_HUMANCSDE1physical
28514442
1433G_HUMANYWHAGphysical
28514442
GAN_HUMANGANphysical
28514442
PDP1_HUMANPDP1physical
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 SMAG1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-420; THR-424 ANDSER-580, AND MASS SPECTROMETRY.
"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-420 AND THR-424, ANDMASS SPECTROMETRY.
"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-418; SER-420 ANDSER-422, AND MASS SPECTROMETRY.

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