SDS3_HUMAN - dbPTM
SDS3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDS3_HUMAN
UniProt AC Q9H7L9
Protein Name Sin3 histone deacetylase corepressor complex component SDS3
Gene Name SUDS3
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Nucleus .
Protein Description Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes..
Protein Sequence MSAAGLLAPAPAQAGAPPAPEYYPEEDEELESAEDDERSCRGRESDEDTEDASETDLAKHDEEDYVEMKEQMYQDKLASLKRQLQQLQEGTLQEYQKRMKKLDQQYKERIRNAELFLQLETEQVERNYIKEKKAAVKEFEDKKVELKENLIAELEEKKKMIENEKLTMELTGDSMEVKPIMTRKLRRRPNDPVPIPDKRRKPAPAQLNYLLTDEQIMEDLRTLNKLKSPKRPASPSSPEHLPATPAESPAQRFEARIEDGKLYYDKRWYHKSQAIYLESKDNQKLSCVISSVGANEIWVRKTSDSTKMRIYLGQLQRGLFVIRRRSAA
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------MSAAGLLAP
------CCCCCCCCC		27.1621406692
2Phosphorylation------MSAAGLLAP
------CCCCCCCCC		27.1628464451
22PhosphorylationGAPPAPEYYPEEDEE
CCCCCCCCCCCCHHH		24.2220873877
23PhosphorylationAPPAPEYYPEEDEEL
CCCCCCCCCCCHHHH		11.5130108239
30UbiquitinationYPEEDEELESAEDDE
CCCCHHHHHCCCCCC		6.2424816145
32PhosphorylationEEDEELESAEDDERS
CCHHHHHCCCCCCHH		49.9729255136
39PhosphorylationSAEDDERSCRGRESD
CCCCCCHHHCCCCCC		13.2027499020
45PhosphorylationRSCRGRESDEDTEDA
HHHCCCCCCCCCCCC		44.9629255136
49PhosphorylationGRESDEDTEDASETD
CCCCCCCCCCCCCCC		33.4429255136
53PhosphorylationDEDTEDASETDLAKH
CCCCCCCCCCCHHHC		54.0429255136
55PhosphorylationDTEDASETDLAKHDE
CCCCCCCCCHHHCCH		33.5423927012
65PhosphorylationAKHDEEDYVEMKEQM
HHCCHHHHHHHHHHH		11.1128796482
69SumoylationEEDYVEMKEQMYQDK
HHHHHHHHHHHHHHH		31.1528112733
69SumoylationEEDYVEMKEQMYQDK
HHHHHHHHHHHHHHH		31.15-
69UbiquitinationEEDYVEMKEQMYQDK
HHHHHHHHHHHHHHH		31.1532015554
73PhosphorylationVEMKEQMYQDKLASL
HHHHHHHHHHHHHHH		17.1629083192
76AcetylationKEQMYQDKLASLKRQ
HHHHHHHHHHHHHHH		30.3525953088
76UbiquitinationKEQMYQDKLASLKRQ
HHHHHHHHHHHHHHH		30.3529967540
79PhosphorylationMYQDKLASLKRQLQQ
HHHHHHHHHHHHHHH		44.8822912867
79UbiquitinationMYQDKLASLKRQLQQ
HHHHHHHHHHHHHHH		44.8824816145
91PhosphorylationLQQLQEGTLQEYQKR
HHHHHHHHHHHHHHH		25.2325003641
95PhosphorylationQEGTLQEYQKRMKKL
HHHHHHHHHHHHHHH		13.3325003641
97AcetylationGTLQEYQKRMKKLDQ
HHHHHHHHHHHHHHH		54.2626051181
101UbiquitinationEYQKRMKKLDQQYKE
HHHHHHHHHHHHHHH		48.2124816145
157UbiquitinationLIAELEEKKKMIENE
HHHHHHHHHHHHHHC		48.6029967540
167PhosphorylationMIENEKLTMELTGDS
HHHHCCEEEEECCCC		21.48-
171PhosphorylationEKLTMELTGDSMEVK
CCEEEEECCCCCCCH		26.15-
174PhosphorylationTMELTGDSMEVKPIM
EEEECCCCCCCHHHC		20.42-
178SumoylationTGDSMEVKPIMTRKL
CCCCCCCHHHCCCCH		18.6028112733
178AcetylationTGDSMEVKPIMTRKL
CCCCCCCHHHCCCCH		18.6026051181
180UbiquitinationDSMEVKPIMTRKLRR
CCCCCHHHCCCCHHC		3.5024816145
201SumoylationPIPDKRRKPAPAQLN
CCCCCCCCCCCCHHH		49.9528112733
209PhosphorylationPAPAQLNYLLTDEQI
CCCCHHHHHCCHHHH		16.2220230923
222PhosphorylationQIMEDLRTLNKLKSP
HHHHHHHHHHHCCCC		41.8126074081
228PhosphorylationRTLNKLKSPKRPASP
HHHHHCCCCCCCCCC		46.2028464451
234PhosphorylationKSPKRPASPSSPEHL
CCCCCCCCCCCCCCC		28.1829255136
236PhosphorylationPKRPASPSSPEHLPA
CCCCCCCCCCCCCCC		56.9029255136
237PhosphorylationKRPASPSSPEHLPAT
CCCCCCCCCCCCCCC		37.3829255136
244PhosphorylationSPEHLPATPAESPAQ
CCCCCCCCCCCCHHH		22.5329255136
248PhosphorylationLPATPAESPAQRFEA
CCCCCCCCHHHHHEE		27.8625159151
261UbiquitinationEARIEDGKLYYDKRW
EEEEECCCEEECCCC		45.7129967540
263PhosphorylationRIEDGKLYYDKRWYH
EEECCCEEECCCCEE		17.0728152594
264PhosphorylationIEDGKLYYDKRWYHK
EECCCEEECCCCEEH		25.9828152594
276PhosphorylationYHKSQAIYLESKDNQ
EEHHEEEEEECCCCC		13.87-
280UbiquitinationQAIYLESKDNQKLSC
EEEEEECCCCCEEEE		51.8532015554
290PhosphorylationQKLSCVISSVGANEI
CEEEEEEEECCCCEE		9.8923401153
305PhosphorylationWVRKTSDSTKMRIYL
EEEECCCCCCEEEEE		29.69-
311PhosphorylationDSTKMRIYLGQLQRG
CCCCEEEEEEEHHCC		8.40-
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 SDS3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
63KAcetylation

21239494
63Kubiquitylation

21239494
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 SDS3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12724404
HDAC2_HUMANHDAC2physical
12724404
SIN3A_HUMANSIN3Aphysical
12724404
SIN3A_HUMANSIN3Aphysical
11909966
SIN3B_HUMANSIN3Bphysical
11909966
SDS3_HUMANSUDS3physical
11909966
HDAC1_HUMANHDAC1physical
11909966
CUL4B_HUMANCUL4Bphysical
25189618
DDB1_HUMANDDB1physical
25189618
U17L2_HUMANUSP17L2physical
21239494
SIN3A_HUMANSIN3Aphysical
26186194
SIN3B_HUMANSIN3Bphysical
26186194
HDAC1_HUMANHDAC1physical
26186194
SIN3B_HUMANSIN3Bphysical
28514442
SIN3A_HUMANSIN3Aphysical
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 SDS3_HUMAN

loading...

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-234, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-53,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-45; THR-49; SER-53;SER-234; SER-237 AND THR-244, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236 AND THR-244, 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-45; THR-49; THR-55 ANDSER-234, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory