SMAG2_HUMAN - dbPTM
SMAG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAG2_HUMAN
UniProt AC Q5PRF9
Protein Name Protein Smaug homolog 2
Gene Name SAMD4B
Organism Homo sapiens (Human).
Sequence Length 694
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A..
Protein Sequence MMFRDQVGILAGWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQVPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRERQSVLKSLEKDVLEGGNLRNALQELQQIIITPIKAYSVLQATVAAATTTPTAKDGAPGEPPLPGAEPPLAHPGTDKGTEAKDPPAVENYPPPPAPAPTDGSEPAPAPVADGDIPSQFTRVMGKVCTQLLVSRPDEENITSYLQLIEKCLTHEAFTETQKKRLLSWKQQVLKLLRTFPRKAALEMQNYRQQKGWAFGSNSLPIAGSVGMGVARRTQRQFPMPPRALPPGRMGLLSPSGIGGVSPRHALTSPSLGGQGRQNLWFANPGGSNSMPSQSRSSVQRTHSLPVHSSPQAILMFPPDCPVPGPDLEINPTLESLCLSMTEHALGDGTDKTSTI
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
28PhosphorylationEQTVALLSLLKRVTR
HHHHHHHHHHHHHHH		32.2924719451
127PhosphorylationEESRQLLSYALIHPA
HHHHHHHHHHHHCCC		19.5624260401
128PhosphorylationESRQLLSYALIHPAT
HHHHHHHHHHHCCCC		12.8524260401
165PhosphorylationFRSRPEPSYHSRQGS
CCCCCCCCCCCCCCC		33.5426356563
166PhosphorylationRSRPEPSYHSRQGSD
CCCCCCCCCCCCCCC		17.9626356563
168PhosphorylationRPEPSYHSRQGSDEW
CCCCCCCCCCCCCCC		20.3326356563
172PhosphorylationSYHSRQGSDEWGGPA
CCCCCCCCCCCCCCC		24.8223927012
206PhosphorylationGHVPFHPSSSVPPAI
CCCCCCCHHCCCCCH		27.0322210691
231PhosphorylationLPCQIHPSPLKRSMS
CCCEECCCCCCCCCC		28.8024260401
236PhosphorylationHPSPLKRSMSLIPTS
CCCCCCCCCCCCCCC		15.9025159151
238PhosphorylationSPLKRSMSLIPTSPQ
CCCCCCCCCCCCCCC		25.1325159151
242PhosphorylationRSMSLIPTSPQVPGE
CCCCCCCCCCCCCCC		46.1525159151
243PhosphorylationSMSLIPTSPQVPGEW
CCCCCCCCCCCCCCC		14.1625159151
252PhosphorylationQVPGEWPSPEELGAR
CCCCCCCCHHHHCCC		46.1225159151
263PhosphorylationLGARAAFTTPDHAPL
HCCCCEECCCCCCCC		32.4630278072
264PhosphorylationGARAAFTTPDHAPLS
CCCCEECCCCCCCCC		21.9230278072
271PhosphorylationTPDHAPLSPQSSVAS
CCCCCCCCCCCCCCC		21.6029255136
274PhosphorylationHAPLSPQSSVASSGS
CCCCCCCCCCCCCCC		30.1130266825
275PhosphorylationAPLSPQSSVASSGSE
CCCCCCCCCCCCCCC		19.2230266825
278PhosphorylationSPQSSVASSGSEQTE
CCCCCCCCCCCCCCC		32.8330266825
279PhosphorylationPQSSVASSGSEQTEE
CCCCCCCCCCCCCCC		36.2830266825
281PhosphorylationSSVASSGSEQTEEQG
CCCCCCCCCCCCCCC		28.6030266825
284PhosphorylationASSGSEQTEEQGSSR
CCCCCCCCCCCCCCC		37.1230266825
289PhosphorylationEQTEEQGSSRNTFQE
CCCCCCCCCCCCCCC		26.3125850435
290PhosphorylationQTEEQGSSRNTFQED
CCCCCCCCCCCCCCC		36.0525850435
299PhosphorylationNTFQEDGSGMKDVPS
CCCCCCCCCCCCHHH		48.3025159151
324PhosphorylationAALFSQMSYEEMMTL
HHHHHHCCHHHHHHH		23.0428348404
348MethylationVTKGARHKIALSIQK
CCHHHHHHHHHHHHH		24.91116252857
368UbiquitinationSVLKSLEKDVLEGGN
HHHHHHHHHHHCCCC		59.43-
389PhosphorylationELQQIIITPIKAYSV
HHHHHHHCHHHHHHH		14.4621712546
392UbiquitinationQIIITPIKAYSVLQA
HHHHCHHHHHHHHHH		42.34-
400PhosphorylationAYSVLQATVAAATTT
HHHHHHHHHHHHCCC		9.5626657352
405PhosphorylationQATVAAATTTPTAKD
HHHHHHHCCCCCCCC		26.8621725060
406PhosphorylationATVAAATTTPTAKDG
HHHHHHCCCCCCCCC		26.5021725060
407PhosphorylationTVAAATTTPTAKDGA
HHHHHCCCCCCCCCC		17.8125159151
409PhosphorylationAAATTTPTAKDGAPG
HHHCCCCCCCCCCCC		44.2225850435
432PhosphorylationPPLAHPGTDKGTEAK
CCCCCCCCCCCCCCC		38.7028555341
489PhosphorylationVCTQLLVSRPDEENI
HHHHHHHCCCCHHCH		37.7624719451
499PhosphorylationDEENITSYLQLIEKC
CHHCHHHHHHHHHHH		6.9921214269
529UbiquitinationSWKQQVLKLLRTFPR
HHHHHHHHHHHHCCH		46.77-
533PhosphorylationQVLKLLRTFPRKAAL
HHHHHHHHCCHHHHH		37.65-
545PhosphorylationAALEMQNYRQQKGWA
HHHHHHHHHHHCCCC		7.91-
555PhosphorylationQKGWAFGSNSLPIAG
HCCCCCCCCCCCCCC		19.4522617229
557PhosphorylationGWAFGSNSLPIAGSV
CCCCCCCCCCCCCCH		36.9022617229
563PhosphorylationNSLPIAGSVGMGVAR
CCCCCCCCHHHHHHH		13.3822115753
570MethylationSVGMGVARRTQRQFP
CHHHHHHHCCCCCCC		39.5180702769
572PhosphorylationGMGVARRTQRQFPMP
HHHHHHCCCCCCCCC		23.66-
592PhosphorylationPGRMGLLSPSGIGGV
CCCCCCCCCCCCCCC		23.2829255136
594PhosphorylationRMGLLSPSGIGGVSP
CCCCCCCCCCCCCCC		39.4029255136
600PhosphorylationPSGIGGVSPRHALTS
CCCCCCCCCCCCCCC		21.3526055452
602MethylationGIGGVSPRHALTSPS
CCCCCCCCCCCCCCC		21.8724129315
602Asymmetric dimethylarginineGIGGVSPRHALTSPS
CCCCCCCCCCCCCCC		21.87-
606PhosphorylationVSPRHALTSPSLGGQ
CCCCCCCCCCCCCCC		39.1030266825
607PhosphorylationSPRHALTSPSLGGQG
CCCCCCCCCCCCCCC		17.2229255136
609PhosphorylationRHALTSPSLGGQGRQ
CCCCCCCCCCCCCCC		39.1430266825
615DimethylationPSLGGQGRQNLWFAN
CCCCCCCCCCCEECC		17.83-
615MethylationPSLGGQGRQNLWFAN
CCCCCCCCCCCEECC		17.8318967451
626PhosphorylationWFANPGGSNSMPSQS
EECCCCCCCCCCCCC		31.4821712546
628PhosphorylationANPGGSNSMPSQSRS
CCCCCCCCCCCCCCC		33.4921712546
631PhosphorylationGGSNSMPSQSRSSVQ
CCCCCCCCCCCCCCC		31.9523403867
633PhosphorylationSNSMPSQSRSSVQRT
CCCCCCCCCCCCCCC		38.1723403867
634MethylationNSMPSQSRSSVQRTH
CCCCCCCCCCCCCCC		25.88115493261
640PhosphorylationSRSSVQRTHSLPVHS
CCCCCCCCCCCCCCC		9.9528348404
642PhosphorylationSSVQRTHSLPVHSSP
CCCCCCCCCCCCCCC		33.4821725060
647PhosphorylationTHSLPVHSSPQAILM
CCCCCCCCCCCEEEE		43.9028348404
648PhosphorylationHSLPVHSSPQAILMF
CCCCCCCCCCEEEEC		13.2228348404
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 SMAG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMAG2_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 SMAG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAG1_HUMANSAMD4Aphysical
28514442
PDP1_HUMANPDP1physical
28514442
1433G_HUMANYWHAGphysical
28514442
1433E_HUMANYWHAEphysical
28514442
ACTA_HUMANACTA2physical
28514442
1433Z_HUMANYWHAZphysical
28514442
1433B_HUMANYWHABphysical
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 SMAG2_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-592, 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 THR-264; SER-271; SER-592AND SER-600, AND MASS SPECTROMETRY.
"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 THR-606, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, AND MASSSPECTROMETRY.

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