S30BP_HUMAN - dbPTM
S30BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S30BP_HUMAN
UniProt AC Q9UHR5
Protein Name SAP30-binding protein
Gene Name SAP30BP {ECO:0000312|EMBL:AAH07592.1}
Organism Homo sapiens (Human).
Sequence Length 308
Subcellular Localization Nucleus .
Protein Description Induces cell death. May act as a transcriptional corepressor of a gene related to cell survival. May be involved in the regulation of beta-2-microglobulin genes..
Protein Sequence MAGKKNVLSSLAVYAEDSEPESDGEAGIEAVGSAAEEKGGLVSDAYGEDDFSRLGGDEDGYEEEEDENSRQSEDDDSETEKPEADDPKDNTEAEKRDPQELVASFSERVRNMSPDEIKIPPEPPGRCSNHLQDKIQKLYERKIKEGMDMNYIIQRKKEFRNPSIYEKLIQFCAIDELGTNYPKDMFDPHGWSEDSYYEALAKAQKIEMDKLEKAKKERTKIEFVTGTKKGTTTNATSTTTTTASTAVADAQKRKSKWDSAIPVTTIAQPTILTTTATLPAVVTVTTSASGSKTTVISAVGTIVKKAKQ
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
9PhosphorylationAGKKNVLSSLAVYAE
CCCCCHHHHEEEEEC		21.0128176443
10PhosphorylationGKKNVLSSLAVYAED
CCCCHHHHEEEEECC		19.0430278072
14PhosphorylationVLSSLAVYAEDSEPE
HHHHEEEEECCCCCC		9.9225159151
18PhosphorylationLAVYAEDSEPESDGE
EEEEECCCCCCCCCC		46.7026503892
22PhosphorylationAEDSEPESDGEAGIE
ECCCCCCCCCCCCCH		62.7326503892
33PhosphorylationAGIEAVGSAAEEKGG
CCCHHHHHHHHHHCC		20.0820068231
43PhosphorylationEEKGGLVSDAYGEDD
HHHCCCCCCCCCCCC		22.9023927012
46PhosphorylationGGLVSDAYGEDDFSR
CCCCCCCCCCCCHHH		26.4930266825
52PhosphorylationAYGEDDFSRLGGDED
CCCCCCHHHCCCCCC		33.3219664994
61PhosphorylationLGGDEDGYEEEEDEN
CCCCCCCCCCCCCCC		32.2723927012
69PhosphorylationEEEEDENSRQSEDDD
CCCCCCCCCCCCCCC		29.6530278072
72PhosphorylationEDENSRQSEDDDSET
CCCCCCCCCCCCCCC		41.7129255136
77PhosphorylationRQSEDDDSETEKPEA
CCCCCCCCCCCCCCC		54.1129255136
79PhosphorylationSEDDDSETEKPEADD
CCCCCCCCCCCCCCC		53.9429255136
95SumoylationKDNTEAEKRDPQELV
CCCCHHHHCCHHHHH		69.9728112733
104PhosphorylationDPQELVASFSERVRN
CHHHHHHHHHHHHHH		23.0925159151
106PhosphorylationQELVASFSERVRNMS
HHHHHHHHHHHHHCC		23.2320068231
113PhosphorylationSERVRNMSPDEIKIP
HHHHHHCCHHHCCCC		32.5219664994
128 (in isoform 2)Ubiquitination-26.3921890473
128PhosphorylationPEPPGRCSNHLQDKI
CCCCCCCCHHHHHHH		26.3928555341
134AcetylationCSNHLQDKIQKLYER
CCHHHHHHHHHHHHH		33.7925953088
134UbiquitinationCSNHLQDKIQKLYER
CCHHHHHHHHHHHHH		33.79-
137AcetylationHLQDKIQKLYERKIK
HHHHHHHHHHHHHHH		57.4125953088
137UbiquitinationHLQDKIQKLYERKIK
HHHHHHHHHHHHHHH		57.41-
144 (in isoform 1)Ubiquitination-51.7721890473
144UbiquitinationKLYERKIKEGMDMNY
HHHHHHHHHCCCHHH		51.7721890473
144UbiquitinationKLYERKIKEGMDMNY
HHHHHHHHHCCCHHH		51.7721890473
151PhosphorylationKEGMDMNYIIQRKKE
HHCCCHHHHHHHCHH		7.8628674151
157UbiquitinationNYIIQRKKEFRNPSI
HHHHHHCHHHCCHHH		65.36-
163PhosphorylationKKEFRNPSIYEKLIQ
CHHHCCHHHHHHHHH		41.1525849741
165PhosphorylationEFRNPSIYEKLIQFC
HHCCHHHHHHHHHHH		16.0228796482
167UbiquitinationRNPSIYEKLIQFCAI
CCHHHHHHHHHHHHH		33.64-
172GlutathionylationYEKLIQFCAIDELGT
HHHHHHHHHHHCCCC		1.5322555962
186 (in isoform 2)Ubiquitination-22.1621890473
192PhosphorylationMFDPHGWSEDSYYEA
CCCCCCCCHHHHHHH		35.8029978859
195PhosphorylationPHGWSEDSYYEALAK
CCCCCHHHHHHHHHH		26.0928796482
196PhosphorylationHGWSEDSYYEALAKA
CCCCHHHHHHHHHHH		20.0428796482
197PhosphorylationGWSEDSYYEALAKAQ
CCCHHHHHHHHHHHH		9.9328796482
202UbiquitinationSYYEALAKAQKIEMD
HHHHHHHHHHHCCHH		52.802190698
202 (in isoform 1)Ubiquitination-52.8021890473
210UbiquitinationAQKIEMDKLEKAKKE
HHHCCHHHHHHHHHH		58.18-
210AcetylationAQKIEMDKLEKAKKE
HHHCCHHHHHHHHHH		58.1825953088
2102-HydroxyisobutyrylationAQKIEMDKLEKAKKE
HHHCCHHHHHHHHHH		58.18-
213UbiquitinationIEMDKLEKAKKERTK
CCHHHHHHHHHHHCC		75.77-
220UbiquitinationKAKKERTKIEFVTGT
HHHHHHCCEEEEECC		46.59-
220SumoylationKAKKERTKIEFVTGT
HHHHHHCCEEEEECC		46.59-
220SumoylationKAKKERTKIEFVTGT
HHHHHHCCEEEEECC		46.5928112733
228UbiquitinationIEFVTGTKKGTTTNA
EEEEECCCCCCEECC		51.02-
228AcetylationIEFVTGTKKGTTTNA
EEEEECCCCCCEECC		51.0224468287
2282-HydroxyisobutyrylationIEFVTGTKKGTTTNA
EEEEECCCCCCEECC		51.02-
231O-linked_GlycosylationVTGTKKGTTTNATST
EECCCCCCEECCCCC		39.0530059200
232O-linked_GlycosylationTGTKKGTTTNATSTT
ECCCCCCEECCCCCC		27.0730059200
233O-linked_GlycosylationGTKKGTTTNATSTTT
CCCCCCEECCCCCCC		23.7730059200
236O-linked_GlycosylationKGTTTNATSTTTTTA
CCCEECCCCCCCCCC		28.7730059200
237O-linked_GlycosylationGTTTNATSTTTTTAS
CCEECCCCCCCCCCH		22.7330059200
237PhosphorylationGTTTNATSTTTTTAS
CCEECCCCCCCCCCH		22.7322210691
238O-linked_GlycosylationTTTNATSTTTTTAST
CEECCCCCCCCCCHH		24.6530059200
239O-linked_GlycosylationTTNATSTTTTTASTA
EECCCCCCCCCCHHH		23.1630059200
240O-linked_GlycosylationTNATSTTTTTASTAV
ECCCCCCCCCCHHHH		23.4130059200
241O-linked_GlycosylationNATSTTTTTASTAVA
CCCCCCCCCCHHHHH		20.4830059200
242O-linked_GlycosylationATSTTTTTASTAVAD
CCCCCCCCCHHHHHH		19.2730059200
242PhosphorylationATSTTTTTASTAVAD
CCCCCCCCCHHHHHH		19.2722210691
244O-linked_GlycosylationSTTTTTASTAVADAQ
CCCCCCCHHHHHHHH		18.1430059200
244PhosphorylationSTTTTTASTAVADAQ
CCCCCCCHHHHHHHH		18.1422210691
245O-linked_GlycosylationTTTTTASTAVADAQK
CCCCCCHHHHHHHHH		23.7630059200
255O-linked_GlycosylationADAQKRKSKWDSAIP
HHHHHHHHCCCCCCC		42.9130059200
259O-linked_GlycosylationKRKSKWDSAIPVTTI
HHHHCCCCCCCCCCC		27.3030059200
264O-linked_GlycosylationWDSAIPVTTIAQPTI
CCCCCCCCCCCCCEE		13.7130059200
265PhosphorylationDSAIPVTTIAQPTIL
CCCCCCCCCCCCEEE		17.9828985074
265O-linked_GlycosylationDSAIPVTTIAQPTIL
CCCCCCCCCCCCEEE		17.9830059200
270O-linked_GlycosylationVTTIAQPTILTTTAT
CCCCCCCEEEEECCC		19.2830059200
273O-linked_GlycosylationIAQPTILTTTATLPA
CCCCEEEEECCCCCE		20.4630059200
274O-linked_GlycosylationAQPTILTTTATLPAV
CCCEEEEECCCCCEE		15.8130059200
275O-linked_GlycosylationQPTILTTTATLPAVV
CCEEEEECCCCCEEE		16.6530059200
277PhosphorylationTILTTTATLPAVVTV
EEEEECCCCCEEEEE		31.0528985074
285PhosphorylationLPAVVTVTTSASGSK
CCEEEEEEECCCCCC		12.9818212344
287PhosphorylationAVVTVTTSASGSKTT
EEEEEEECCCCCCEE		15.8628985074
289PhosphorylationVTVTTSASGSKTTVI
EEEEECCCCCCEEEE		43.2828985074
301PhosphorylationTVISAVGTIVKKAKQ
EEEEEEHHHHHHHHC		18.9218212344
301O-linked_GlycosylationTVISAVGTIVKKAKQ
EEEEEEHHHHHHHHC		18.9230059200
304SumoylationSAVGTIVKKAKQ---
EEEHHHHHHHHC---		43.07-
304SumoylationSAVGTIVKKAKQ---
EEEHHHHHHHHC---		43.0728112733
304AcetylationSAVGTIVKKAKQ---
EEEHHHHHHHHC---		43.0725953088
305SumoylationAVGTIVKKAKQ----
EEHHHHHHHHC----		50.3428112733
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 S30BP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S30BP_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 S30BP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUF60_HUMANPUF60physical
18255255
SPF45_HUMANRBM17physical
22365833
U2AF2_HUMANU2AF2physical
22365833
PUF60_HUMANPUF60physical
22365833
RBM39_HUMANRBM39physical
22365833
DHX8_HUMANDHX8physical
22365833
THOC1_HUMANTHOC1physical
22365833
WDR83_HUMANWDR83physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
MEP50_HUMANWDR77physical
22365833
THAP1_HUMANTHAP1physical
25416956
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 S30BP_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-10; SER-18; SER-22;SER-43; SER-52 AND SER-113, 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-18; SER-22; SER-43 ANDSER-113, AND MASS SPECTROMETRY.

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