SAP18_HUMAN - dbPTM
SAP18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAP18_HUMAN
UniProt AC O00422
Protein Name Histone deacetylase complex subunit SAP18
Gene Name SAP18
Organism Homo sapiens (Human).
Sequence Length 153
Subcellular Localization Nucleus . Cytoplasm . Nucleus speckle . Shuttles between the nucleus and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (PubMed:20966198).
Protein Description Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function..
Protein Sequence MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFTDVKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPPSGRMRPY
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------MAVESRVTQ
------CCCCCCCCH		17.4919413330
8PhosphorylationMAVESRVTQEEIKKE
CCCCCCCCHHHHHHC		29.2021815630
13AcetylationRVTQEEIKKEPEKPI
CCCHHHHHHCCCCCC		55.1326051181
13SumoylationRVTQEEIKKEPEKPI
CCCHHHHHHCCCCCC		55.1328112733
13SumoylationRVTQEEIKKEPEKPI
CCCHHHHHHCCCCCC		55.13-
18AcetylationEIKKEPEKPIDREKT
HHHHCCCCCCCHHHC		58.9726051181
24UbiquitinationEKPIDREKTCPLLLR
CCCCCHHHCCCEEEE		57.21-
24AcetylationEKPIDREKTCPLLLR
CCCCCHHHCCCEEEE		57.2125953088
25PhosphorylationKPIDREKTCPLLLRV
CCCCHHHCCCEEEEE		18.0122817900
25UbiquitinationKPIDREKTCPLLLRV
CCCCHHHCCCEEEEE		18.0123000965
26GlutathionylationPIDREKTCPLLLRVF
CCCHHHCCCEEEEEE		3.1122555962
32UbiquitinationTCPLLLRVFTTNNGR
CCCEEEEEEECCCCC		5.1527667366
33UbiquitinationCPLLLRVFTTNNGRH
CCEEEEEEECCCCCE		5.8824816145
35PhosphorylationLLLRVFTTNNGRHHR
EEEEEEECCCCCEEC		18.4122817900
43UbiquitinationNNGRHHRMDEFSRGN
CCCCEECCCCHHCCC		5.1333845483
44PhosphorylationNGRHHRMDEFSRGNV
CCCEECCCCHHCCCC		54.4620068230
47PhosphorylationHHRMDEFSRGNVPSS
EECCCCHHCCCCCHH		36.9122210691
54PhosphorylationSRGNVPSSELQIYTW
HCCCCCHHHHHHHHH		35.9320068230
55UbiquitinationRGNVPSSELQIYTWM
CCCCCHHHHHHHHHH		49.3724816145
60PhosphorylationSSELQIYTWMDATLK
HHHHHHHHHHHHHHH		18.8822210691
65PhosphorylationIYTWMDATLKELTSL
HHHHHHHHHHHHHHH		33.8122210691
742-HydroxyisobutyrylationKELTSLVKEVYPEAR
HHHHHHHHHHCHHHH		46.91-
74AcetylationKELTSLVKEVYPEAR
HHHHHHHHHHCHHHH		46.9126051181
74UbiquitinationKELTSLVKEVYPEAR
HHHHHHHHHHCHHHH		46.9121890473
85PhosphorylationPEARKKGTHFNFAIV
HHHHHHCCCEEEEEE		31.9718491316
89UbiquitinationKKGTHFNFAIVFTDV
HHCCCEEEEEEEECC		4.8629901268
93UbiquitinationHFNFAIVFTDVKRPG
CEEEEEEEECCCCCC		3.8423000965
94PhosphorylationFNFAIVFTDVKRPGY
EEEEEEEECCCCCCE		29.05-
101PhosphorylationTDVKRPGYRVKEIGS
ECCCCCCEEEEEECC		18.2118491316
104PhosphorylationKRPGYRVKEIGSTMS
CCCCEEEEEECCCCC		34.3218491316
104UbiquitinationKRPGYRVKEIGSTMS
CCCCEEEEEECCCCC		34.3221890473
108PhosphorylationYRVKEIGSTMSGRKG
EEEEEECCCCCCCCC		26.9721406692
109PhosphorylationRVKEIGSTMSGRKGT
EEEEECCCCCCCCCC		15.3321406692
111PhosphorylationKEIGSTMSGRKGTDD
EEECCCCCCCCCCCC		35.2221406692
114UbiquitinationGSTMSGRKGTDDSMT
CCCCCCCCCCCCCCE		70.4621890473
114SumoylationGSTMSGRKGTDDSMT
CCCCCCCCCCCCCCE		70.46-
114AcetylationGSTMSGRKGTDDSMT
CCCCCCCCCCCCCCE		70.4626051181
116PhosphorylationTMSGRKGTDDSMTLQ
CCCCCCCCCCCCEEE		39.40-
119PhosphorylationGRKGTDDSMTLQSQK
CCCCCCCCCEEECCC		19.2421815630
119UbiquitinationGRKGTDDSMTLQSQK
CCCCCCCCCEEECCC		19.2433845483
120PhosphorylationRKGTDDSMTLQSQKF
CCCCCCCCEEECCCE		5.8018491316
121PhosphorylationKGTDDSMTLQSQKFQ
CCCCCCCEEECCCEE		26.12-
123UbiquitinationTDDSMTLQSQKFQIG
CCCCCEEECCCEECC		34.3533845483
126UbiquitinationSMTLQSQKFQIGDYL
CCEEECCCEECCCEE		44.4721890473
132PhosphorylationQKFQIGDYLDIAITP
CCEECCCEEEEEECC		10.8920068231
142MethylationIAITPPNRAPPPSGR
EEECCCCCCCCCCCC		55.00115493297
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 SAP18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAP18_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 SAP18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPN2_HUMANRPN2physical
17353931
OST48_HUMANDDOSTphysical
17353931
RGS10_HUMANRGS10physical
17353931
SYYC_HUMANYARSphysical
17353931
KBP_HUMANKIAA1279physical
17353931
DDX3X_HUMANDDX3Xphysical
17353931
NSF_HUMANNSFphysical
17353931
EIF3E_HUMANEIF3Ephysical
17353931
ATP5L_HUMANATP5Lphysical
17353931
ARMT1_HUMANC6orf211physical
17353931
SIN3A_HUMANSIN3Aphysical
9651585
SIN3A_MOUSESin3aphysical
11960000
SUFU_MOUSESufuphysical
11960000
SUFU_MOUSESufugenetic
11960000
SIN3A_MOUSESin3agenetic
11960000
RNPS1_HUMANRNPS1physical
16537548
ACINU_HUMANACIN1physical
16537548
ACINU_HUMANACIN1physical
22388736
RNPS1_HUMANRNPS1physical
22388736
RNPS1_HUMANRNPS1physical
12665594
ACINU_HUMANACIN1physical
12665594
SMCA5_HUMANSMARCA5physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SRS11_HUMANSRSF11physical
22939629
SRSF1_HUMANSRSF1physical
22939629
SRSF3_HUMANSRSF3physical
22939629
SRSF5_HUMANSRSF5physical
22939629
SRSF7_HUMANSRSF7physical
22939629
SMD2_HUMANSNRPD2physical
22939629
SNUT1_HUMANSART1physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
SMU1_HUMANSMU1physical
22939629
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SRRT_HUMANSRRTphysical
22939629
SSRP1_HUMANSSRP1physical
22939629
SEPT2_HUMANSEPT2physical
22939629
SEPT7_HUMANSEPT7physical
22939629
SERA_HUMANPHGDHphysical
22939629
SRS10_HUMANSRSF10physical
22939629
WDR18_HUMANWDR18physical
22939629
SAP_HUMANPSAPphysical
22939629
TRI55_HUMANTRIM55physical
22939629
TFPI1_HUMANTFPIphysical
22939629
TR150_HUMANTHRAP3physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
SSRG_HUMANSSR3physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
TPR_HUMANTPRphysical
22939629
SURF4_HUMANSURF4physical
22939629
VTNC_HUMANVTNphysical
22939629
RBM39_HUMANRBM39physical
22365833
INCA1_HUMANINCA1physical
25416956
RNPS1_HUMANRNPS1physical
26344197
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 SAP18_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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