SDA1_HUMAN - dbPTM
SDA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDA1_HUMAN
UniProt AC Q9NVU7
Protein Name Protein SDA1 homolog
Gene Name SDAD1
Organism Homo sapiens (Human).
Sequence Length 687
Subcellular Localization Nucleus, nucleolus .
Protein Description Required for 60S pre-ribosomal subunits export to the cytoplasm..
Protein Sequence MSNRNNNKLPSNLPQLQNLIKRDPPAYIEEFLQQYNHYKSNVEIFKLQPNKPSKELAELVMFMAQISHCYPEYLSNFPQEVKDLLSCNHTVLDPDLRMTFCKALILLRNKNLINPSSLLELFFELFRCHDKLLRKTLYTHIVTDIKNINAKHKNNKVNVVLQNFMYTMLRDSNATAAKMSLDVMIELYRRNIWNDAKTVNVITTACFSKVTKILVAALTFFLGKDEDEKQDSDSESEDDGPTARDLLVQYATGKKSSKNKKKLEKAMKVLKKQKKKKKPEVFNFSAIHLIHDPQDFAEKLLKQLECCKERFEVKMMLMNLISRLVGIHELFLFNFYPFLQRFLQPHQREVTKILLFAAQASHHLVPPEIIQSLLMTVANNFVTDKNSGEVMTVGINAIKEITARCPLAMTEELLQDLAQYKTHKDKNVMMSARTLIHLFRTLNPQMLQKKFRGKPTEASIEARVQEYGELDAKDYIPGAEVLEVEKEENAENDEDGWESTSLSEEEDADGEWIDVQHSSDEEQQEISKKLNSMPMEERKAKAAAISTSRVLTQEDFQKIRMAQMRKELDAAPGKSQKRKYIEIDSDEEPRGELLSLRDIERLHKKPKSDKETRLATAMAGKTDRKEFVRKKTKTNPFSSSTNKEKKKQKNFMMMRYSQNVRSKNKRSFREKQLALRDALLKKRKRMK
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
11PhosphorylationRNNNKLPSNLPQLQN
CCCCCCCCCHHHHHH		62.5320068231
21 (in isoform 1)Ubiquitination-54.6521890473
21UbiquitinationPQLQNLIKRDPPAYI
HHHHHHHHHCCCHHH		54.652189047
136PhosphorylationHDKLLRKTLYTHIVT
CHHHHHHHHHHHHHH		20.6823403867
138PhosphorylationKLLRKTLYTHIVTDI
HHHHHHHHHHHHHCH		11.0823403867
139PhosphorylationLLRKTLYTHIVTDIK
HHHHHHHHHHHHCHH		14.2923403867
143PhosphorylationTLYTHIVTDIKNINA
HHHHHHHHCHHHCCH		31.2523403867
172PhosphorylationMYTMLRDSNATAAKM
HHHHHHCCCHHHHHH		23.17-
175PhosphorylationMLRDSNATAAKMSLD
HHHCCCHHHHHHHHH		31.25-
180PhosphorylationNATAAKMSLDVMIEL
CHHHHHHHHHHHHHH		22.2527470641
188PhosphorylationLDVMIELYRRNIWND
HHHHHHHHHHCCCCC		8.5027470641
208PhosphorylationVITTACFSKVTKILV
HHHHHHHHHHHHHHH		26.54-
209AcetylationITTACFSKVTKILVA
HHHHHHHHHHHHHHH		33.4026051181
229AcetylationLGKDEDEKQDSDSES
HCCCCCCCCCCCCCC		72.2626051181
232PhosphorylationDEDEKQDSDSESEDD
CCCCCCCCCCCCCCC		40.3125159151
234PhosphorylationDEKQDSDSESEDDGP
CCCCCCCCCCCCCCH		47.1525159151
236PhosphorylationKQDSDSESEDDGPTA
CCCCCCCCCCCCHHH		50.7225159151
242PhosphorylationESEDDGPTARDLLVQ
CCCCCCHHHHHHHHH		39.5928985074
252PhosphorylationDLLVQYATGKKSSKN
HHHHHHHHCCCCCCC		44.6028555341
254AcetylationLVQYATGKKSSKNKK
HHHHHHCCCCCCCHH		45.1625953088
2542-HydroxyisobutyrylationLVQYATGKKSSKNKK
HHHHHHCCCCCCCHH		45.16-
256PhosphorylationQYATGKKSSKNKKKL
HHHHCCCCCCCHHHH		50.4530631047
257PhosphorylationYATGKKSSKNKKKLE
HHHCCCCCCCHHHHH		49.4830631047
302AcetylationDFAEKLLKQLECCKE
HHHHHHHHHHHHHHH		64.3725953088
308AcetylationLKQLECCKERFEVKM
HHHHHHHHHHHHHHH		64.6826051181
310DimethylationQLECCKERFEVKMML
HHHHHHHHHHHHHHH		20.65-
310MethylationQLECCKERFEVKMML
HHHHHHHHHHHHHHH		20.6524377515
322PhosphorylationMMLMNLISRLVGIHE
HHHHHHHHHHHHHHH		23.8020860994
341DimethylationNFYPFLQRFLQPHQR
HHHHHHHHHCCHHHH		36.07-
341MethylationNFYPFLQRFLQPHQR
HHHHHHHHHCCHHHH		36.0724377523
431PhosphorylationKDKNVMMSARTLIHL
CCHHHHHHHHHHHHH		9.1220068231
434PhosphorylationNVMMSARTLIHLFRT
HHHHHHHHHHHHHHH		29.7624719451
441PhosphorylationTLIHLFRTLNPQMLQ
HHHHHHHHCCHHHHH		24.4520068231
450UbiquitinationNPQMLQKKFRGKPTE
CHHHHHHHHCCCCCC		27.60-
454UbiquitinationLQKKFRGKPTEASIE
HHHHHCCCCCCCHHH		44.50-
456PhosphorylationKKFRGKPTEASIEAR
HHHCCCCCCCHHHHH		47.9020068231
459PhosphorylationRGKPTEASIEARVQE
CCCCCCCHHHHHHHH		18.0925159151
467PhosphorylationIEARVQEYGELDAKD
HHHHHHHHCCCCHHH		9.9820068231
473SumoylationEYGELDAKDYIPGAE
HHCCCCHHHCCCCCE		51.21-
501PhosphorylationEDGWESTSLSEEEDA
CCCCCCCCCCCCCCC		38.90-
518PhosphorylationEWIDVQHSSDEEQQE
CEEECCCCCHHHHHH		23.5326074081
519PhosphorylationWIDVQHSSDEEQQEI
EEECCCCCHHHHHHH		47.0926074081
532PhosphorylationEISKKLNSMPMEERK
HHHHHHHCCCHHHHH		34.4021815630
539MethylationSMPMEERKAKAAAIS
CCCHHHHHHHHHHHH		58.48-
539"N6,N6-dimethyllysine"SMPMEERKAKAAAIS
CCCHHHHHHHHHHHH		58.48-
541"N6,N6-dimethyllysine"PMEERKAKAAAISTS
CHHHHHHHHHHHHHH		41.41-
541MethylationPMEERKAKAAAISTS
CHHHHHHHHHHHHHH		41.41-
552PhosphorylationISTSRVLTQEDFQKI
HHHHCCCCHHHHHHH		27.3623917254
5582-HydroxyisobutyrylationLTQEDFQKIRMAQMR
CCHHHHHHHHHHHHH		32.07-
558UbiquitinationLTQEDFQKIRMAQMR
CCHHHHHHHHHHHHH		32.07-
558AcetylationLTQEDFQKIRMAQMR
CCHHHHHHHHHHHHH		32.0726051181
574AcetylationELDAAPGKSQKRKYI
HHHCCCCCCCCCCEE		48.9725953088
575PhosphorylationLDAAPGKSQKRKYIE
HHCCCCCCCCCCEEE		47.0126074081
580PhosphorylationGKSQKRKYIEIDSDE
CCCCCCCEEEECCCC		14.0730278072
585PhosphorylationRKYIEIDSDEEPRGE
CCEEEECCCCCCCCC		53.2119664994
595PhosphorylationEPRGELLSLRDIERL
CCCCCCCCHHHHHHH		33.7022167270
616PhosphorylationDKETRLATAMAGKTD
CHHHHHHHHHCCCCC		22.8920860994
634PhosphorylationFVRKKTKTNPFSSST
HHHHHCCCCCCCCCC		54.0423312004
638PhosphorylationKTKTNPFSSSTNKEK
HCCCCCCCCCCCHHH		25.3323312004
639PhosphorylationTKTNPFSSSTNKEKK
CCCCCCCCCCCHHHH		41.3725627689
640PhosphorylationKTNPFSSSTNKEKKK
CCCCCCCCCCHHHHH		34.5025627689
641PhosphorylationTNPFSSSTNKEKKKQ
CCCCCCCCCHHHHHH		52.8623312004
643AcetylationPFSSSTNKEKKKQKN
CCCCCCCHHHHHHHC		71.6320167786
656PhosphorylationKNFMMMRYSQNVRSK
HCHHHHHHHHHHHHC		9.1918491316
657PhosphorylationNFMMMRYSQNVRSKN
CHHHHHHHHHHHHCC		12.6218491316
662PhosphorylationRYSQNVRSKNKRSFR
HHHHHHHHCCCHHHH		35.9818491316
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 SDA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDA1_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 SDA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SDA1_HUMAN !!
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 SDA1_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-585, 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-585, 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-232; SER-234; SER-236AND SER-585, 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-585, 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-585, AND MASSSPECTROMETRY.
"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-459 AND SER-585, 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-585, AND MASSSPECTROMETRY.

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