SAP30_HUMAN - dbPTM
SAP30_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAP30_HUMAN
UniProt AC O75446
Protein Name Histone deacetylase complex subunit SAP30
Gene Name SAP30 {ECO:0000312|HGNC:HGNC:10532}
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Nucleus.
Protein Description Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones..
Protein Sequence MNGFTPDEMSRGGDAAAAVAAVVAAAAAAASAGNGTGAGTGAEVPGAGAVSAAGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFRSIPVNEKDTLTYFIYSVKNDKNKSDLKVDSGVH
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
5Phosphorylation---MNGFTPDEMSRG
---CCCCCHHHHCCC		31.0923186163
84PhosphorylationGRAAGNASFSKRIQK
CHHCCCHHHHHHHHH		33.7724719451
87SumoylationAGNASFSKRIQKSIS
CCCHHHHHHHHHHHC		52.05-
87SumoylationAGNASFSKRIQKSIS
CCCHHHHHHHHHHHC		52.0528112733
87UbiquitinationAGNASFSKRIQKSIS
CCCHHHHHHHHHHHC		52.0529967540
87AcetylationAGNASFSKRIQKSIS
CCCHHHHHHHHHHHC		52.0525953088
91UbiquitinationSFSKRIQKSISQKKV
HHHHHHHHHHCCCCE		47.5929967540
104UbiquitinationKVKIELDKSARHLYI
CEEEEECCCCCEEEE		59.6519608861
104AcetylationKVKIELDKSARHLYI
CEEEEECCCCCEEEE		59.6519608861
105PhosphorylationVKIELDKSARHLYIC
EEEEECCCCCEEEEC		30.1528857561
131PhosphorylationNRRKRKGSDDDGGDS
HHHHCCCCCCCCCCC		40.6825159151
138PhosphorylationSDDDGGDSPVQDIDT
CCCCCCCCCCCCCCC		30.1925159151
145PhosphorylationSPVQDIDTPEVDLYQ
CCCCCCCCCCEEEEH		22.9824043423
151PhosphorylationDTPEVDLYQLQVNTL
CCCCEEEEHHHHHHH		11.6025022875
157PhosphorylationLYQLQVNTLRRYKRH
EEHHHHHHHHHHHHH		23.8420363803
166AcetylationRRYKRHFKLPTRPGL
HHHHHHCCCCCCCCC		47.6430592123
169PhosphorylationKRHFKLPTRPGLNKA
HHHCCCCCCCCCCHH		60.9919413330
175AcetylationPTRPGLNKAQLVEIV
CCCCCCCHHHHEEEE		42.4230592129
175UbiquitinationPTRPGLNKAQLVEIV
CCCCCCCHHHHEEEE		42.4229967540
194AcetylationRSIPVNEKDTLTYFI
ECCCCCCCCEEEEEE		51.3026051181
194SumoylationRSIPVNEKDTLTYFI
ECCCCCCCCEEEEEE		51.3028112733
194UbiquitinationRSIPVNEKDTLTYFI
ECCCCCCCCEEEEEE		51.30-
196PhosphorylationIPVNEKDTLTYFIYS
CCCCCCCEEEEEEEE		31.87-
198PhosphorylationVNEKDTLTYFIYSVK
CCCCCEEEEEEEEEC		20.6227642862
199PhosphorylationNEKDTLTYFIYSVKN
CCCCEEEEEEEEECC		7.35-
202PhosphorylationDTLTYFIYSVKNDKN
CEEEEEEEEECCCCC		9.4920044836
205SumoylationTYFIYSVKNDKNKSD
EEEEEEECCCCCHHH		54.19-
205SumoylationTYFIYSVKNDKNKSD
EEEEEEECCCCCHHH		54.1928112733
214UbiquitinationDKNKSDLKVDSGVH-
CCCHHHCCCCCCCC-		49.3221963094
214SumoylationDKNKSDLKVDSGVH-
CCCHHHCCCCCCCC-		49.32-
214SumoylationDKNKSDLKVDSGVH-
CCCHHHCCCCCCCC-		49.3228112733
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 SAP30_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAP30_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 SAP30_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYY1_HUMANYY1physical
12788099
HDAC1_HUMANHDAC1physical
12788099
SIN3A_HUMANSIN3Aphysical
9651585
RBBP4_HUMANRBBP4physical
9651585
RBBP7_HUMANRBBP7physical
9651585
HDAC1_HUMANHDAC1physical
9651585
HDAC2_HUMANHDAC2physical
9651585
SIN3A_HUMANSIN3Aphysical
10444591
SIN3B_HUMANSIN3Bphysical
10444591
MTA2_HUMANMTA2physical
10444591
HDAC1_HUMANHDAC1physical
10444591
HDAC2_HUMANHDAC2physical
10444591
RBBP4_HUMANRBBP4physical
10444591
RBBP7_HUMANRBBP7physical
10444591
HDAC1_HUMANHDAC1physical
15235594
SIN3A_HUMANSIN3Aphysical
11390640
HDAC1_HUMANHDAC1physical
11390640
PHF12_HUMANPHF12physical
11390640
HDAC1_HUMANHDAC1physical
11784859
HDAC2_HUMANHDAC2physical
11784859
RBBP4_HUMANRBBP4physical
11784859
RBBP7_HUMANRBBP7physical
11784859
ING1_HUMANING1physical
11784859
SIN3A_HUMANSIN3Aphysical
11784859
NCOR1_HUMANNCOR1physical
9702189
SIN3A_HUMANSIN3Aphysical
9702189
H2B2E_HUMANHIST2H2BEphysical
19015240
SIN3A_HUMANSIN3Aphysical
16820529
HDAC1_HUMANHDAC1physical
16820529
HDAC2_HUMANHDAC2physical
16820529
HDAC3_HUMANHDAC3physical
16820529
ARI4A_HUMANARID4Aphysical
11283269
RBBP7_HUMANRBBP7physical
11283269
RBBP4_HUMANRBBP4physical
11283269
HDAC1_HUMANHDAC1physical
11283269
HDAC2_HUMANHDAC2physical
11283269
SIN3A_HUMANSIN3Aphysical
11283269
CHD4_HUMANCHD4physical
9790534
SIN3A_HUMANSIN3Aphysical
9790534
UBS3B_HUMANUBASH3Bphysical
9790534
HDAC1_HUMANHDAC1physical
9790534
HDAC2_HUMANHDAC2physical
9790534
RBBP4_HUMANRBBP4physical
9790534
RBBP7_HUMANRBBP7physical
9790534
SAMN1_HUMANSAMSN1physical
20478393
CUL4B_HUMANCUL4Bphysical
25189618
DDB1_HUMANDDB1physical
25189618
BRMS1_HUMANBRMS1physical
14581478
LYST_HUMANLYSTphysical
26496610
HDAC1_HUMANHDAC1physical
26496610
HDAC2_HUMANHDAC2physical
26496610
FOXK2_HUMANFOXK2physical
26496610
ING1_HUMANING1physical
26496610
ING2_HUMANING2physical
26496610
ARI4A_HUMANARID4Aphysical
26496610
RBBP7_HUMANRBBP7physical
26496610
SRA1_HUMANSRA1physical
26496610
EBP_HUMANEBPphysical
26496610
SIN3B_HUMANSIN3Bphysical
26496610
BRMS1_HUMANBRMS1physical
26496610
SIN3A_HUMANSIN3Aphysical
26496610
NO40_HUMANZCCHC17physical
26496610
ARI4B_HUMANARID4Bphysical
26496610
GAR1_HUMANGAR1physical
26496610
BAHC1_HUMANBAHCC1physical
26496610
FA60A_HUMANFAM60Aphysical
26496610
SDS3_HUMANSUDS3physical
26496610
SP130_HUMANSAP130physical
26496610
BRM1L_HUMANBRMS1Lphysical
26496610
TNC18_HUMANTNRC18physical
26496610
CMBL_HUMANCMBLphysical
26496610
FOXK1_HUMANFOXK1physical
26496610
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 SAP30_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, AND MASS SPECTROMETRY.
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-131 AND SER-138, ANDMASS SPECTROMETRY.
"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-131; SER-138 ANDTHR-169, 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-131; SER-138 ANDTHR-145, 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-131 AND SER-138, 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-131 AND SER-138, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, ANDMASS SPECTROMETRY.

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