SP3_HUMAN - dbPTM
SP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP3_HUMAN
UniProt AC Q02447
Protein Name Transcription factor Sp3
Gene Name SP3
Organism Homo sapiens (Human).
Sequence Length 781
Subcellular Localization Nucleus. Nucleus, PML body. Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies.
Protein Description Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping..
Protein Sequence MTAPEKPVKQEEMAALDVDSGGGGGGGGGHGEYLQQQQQHGNGAVAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDEEEAAAAAGAPAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIPQIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKGIHSSSTVLASVEAARDDTLITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME
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
2Phosphorylation------MTAPEKPVK
------CCCCCCCCC		51.4229083192
5 (in isoform 5)Phosphorylation-68.4824532841
52 (in isoform 5)Sumoylation-49.94-
65PhosphorylationPLALLAATCSKIGPP
HHHHHHHHHHHCCCC		16.23-
67PhosphorylationALLAATCSKIGPPSP
HHHHHHHHHCCCCCC		23.9726074081
73PhosphorylationCSKIGPPSPGDDEEE
HHHCCCCCCCCCHHH		44.6529255136
94PhosphorylationAPAAAGATGDLASAQ
CCHHHCCCCCHHHHH		30.2528176443
99PhosphorylationGATGDLASAQLGGAP
CCCCCHHHHHCCCCC		24.6828176443
113PhosphorylationPNRWEVLSATPTTIK
CCCEEEEECCCCEEE		34.9626074081
115PhosphorylationRWEVLSATPTTIKDE
CEEEEECCCCEEECC		20.1421815630
117PhosphorylationEVLSATPTTIKDEAG
EEEECCCCEEECCCC		36.4826074081
118O-linked_GlycosylationVLSATPTTIKDEAGN
EEECCCCEEECCCCC		27.5126431879
118PhosphorylationVLSATPTTIKDEAGN
EEECCCCEEECCCCC		27.5126074081
120SumoylationSATPTTIKDEAGNLV
ECCCCEEECCCCCEE		47.63-
120SumoylationSATPTTIKDEAGNLV
ECCCCEEECCCCCEE		47.6312419227
131O-linked_GlycosylationGNLVQIPSAATSSGQ
CCEEECCCCCCCCCC		31.9726431879
134O-linked_GlycosylationVQIPSAATSSGQYVL
EECCCCCCCCCCEEE		24.1226431879
135O-linked_GlycosylationQIPSAATSSGQYVLP
ECCCCCCCCCCEEEE		27.9526431879
136O-linked_GlycosylationIPSAATSSGQYVLPL
CCCCCCCCCCEEEEC		26.0926431879
231O-linked_GlycosylationIQNLIPQTGQVQVQG
HHHHCCCCCEEEEEE		24.9926431879
291 (in isoform 4)Ubiquitination-30.9421906983
308 (in isoform 3)Ubiquitination-47.9521906983
317PhosphorylationERTGERVSPDINETN
CCCCCCCCCCCCCCC		24.0726074081
375PhosphorylationLQGNYIQSPVSEETQ
CCCCEECCCCCHHHH		20.0826074081
375O-linked_GlycosylationLQGNYIQSPVSEETQ
CCCCEECCCCCHHHH		20.0826431879
378PhosphorylationNYIQSPVSEETQAQN
CEECCCCCHHHHHHC		32.8526074081
381PhosphorylationQSPVSEETQAQNIQV
CCCCCHHHHHHCCEE		25.7526074081
389O-linked_GlycosylationQAQNIQVSTAQPVVQ
HHHCCEECCCHHHHH		11.1426431879
390O-linked_GlycosylationAQNIQVSTAQPVVQH
HHCCEECCCHHHHHH		30.3826431879
407O-linked_GlycosylationLQESQQPTSQAQIVQ
HHCCCCCCCHHHHCC		29.1826431879
408O-linked_GlycosylationQESQQPTSQAQIVQG
HCCCCCCCHHHHCCC		30.1526431879
417O-linked_GlycosylationAQIVQGITPQTIHGV
HHHCCCCCHHHHCCE		19.0326431879
420O-linked_GlycosylationVQGITPQTIHGVQAS
CCCCCHHHHCCEECC		19.0226431879
483 (in isoform 5)Sumoylation-15.72-
495 (in isoform 5)Phosphorylation-1.76-
498 (in isoform 5)Phosphorylation-18.06-
525 (in isoform 5)Ubiquitination-19.8421906983
540 (in isoform 6)Ubiquitination-54.4121906983
544PhosphorylationHPGENADSPADIRIK
CCCCCCCCCCCEEEC		21.4126657352
551SumoylationSPADIRIKEEEPDPE
CCCCEEECCCCCCHH		49.5815554904
551AcetylationSPADIRIKEEEPDPE
CCCCEEECCCCCCHH		49.5815554904
551SumoylationSPADIRIKEEEPDPE
CCCCEEECCCCCCHH		49.58-
551 (in isoform 5)Sumoylation-49.58-
563PhosphorylationDPEEWQLSGDSTLNT
CHHHHCCCCCCCCCC		26.0030266825
566PhosphorylationEWQLSGDSTLNTNDL
HHCCCCCCCCCCCCC		38.0230266825
567PhosphorylationWQLSGDSTLNTNDLT
HCCCCCCCCCCCCCC		28.8530266825
570PhosphorylationSGDSTLNTNDLTHLR
CCCCCCCCCCCCEEE		32.9730266825
574PhosphorylationTLNTNDLTHLRVQVV
CCCCCCCCEEEEEEE		23.0228450419
578 (in isoform 5)Phosphorylation-6.79-
581 (in isoform 2)Ubiquitination-4.2421906983
593UbiquitinationDQQHQEGKRLRRVAC
HHHHHHCCEEEEEEE		47.722190698
593 (in isoform 1)Ubiquitination-47.7221906983
593SumoylationDQQHQEGKRLRRVAC
HHHHHHCCEEEEEEE		47.7228112733
593AcetylationDQQHQEGKRLRRVAC
HHHHHHCCEEEEEEE		47.7225953088
601PhosphorylationRLRRVACTCPNCKEG
EEEEEEEECCCCCCC		22.6622115753
606UbiquitinationACTCPNCKEGGGRGT
EEECCCCCCCCCCCC		67.06-
611MethylationNCKEGGGRGTNLGKK
CCCCCCCCCCCCCCC		52.6254559563
619SumoylationGTNLGKKKQHICHIP
CCCCCCCCCEEEECC		51.06-
635PhosphorylationCGKVYGKTSHLRAHL
CCEEECCCHHHHHHH		19.6016332679
636PhosphorylationGKVYGKTSHLRAHLR
CEEECCCHHHHHHHH		24.8216943418
646PhosphorylationRAHLRWHSGERPFVC
HHHHHHCCCCCCEEE		35.0812297010
663PhosphorylationMYCGKRFTRSDELQR
EEECCCCCCCHHHHH		33.0430108239
665PhosphorylationCGKRFTRSDELQRHR
ECCCCCCCHHHHHHH		32.1729496963
674PhosphorylationELQRHRRTHTGEKKF
HHHHHHHCCCCCCEE		24.60-
676PhosphorylationQRHRRTHTGEKKFVC
HHHHHCCCCCCEEEC		46.56-
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
73SPhosphorylationKinaseMAPK1P28482
GPS
73SPhosphorylationKinaseMAPK3P27361
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
551KAcetylation

11812829
551KSumoylation

11812829
551KSumoylation

11812829
551KSumoylation

11812829
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 SP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK19_HUMANSTK19physical
14667819
HDAC2_HUMANHDAC2physical
12151407
RBBP4_HUMANRBBP4physical
12091390
HDAC1_HUMANHDAC1physical
12176973
HDAC2_HUMANHDAC2physical
12176973
PIAS1_HUMANPIAS1physical
12356736
DNMT1_HUMANDNMT1physical
17124180
SP1_HUMANSP1physical
16734381
P53_HUMANTP53physical
12665570
HDAC1_HUMANHDAC1physical
12200149
SP1_HUMANSP1physical
12200149
SP1_HUMANSP1physical
11517158
EP300_HUMANEP300physical
11517158
HDAC1_HUMANHDAC1physical
11517158
HDAC1_HUMANHDAC1physical
17906119
MECP2_HUMANMECP2physical
20385708
TYY1_HUMANYY1physical
21335086
HLTF_HUMANHLTFphysical
10391891
PP1G_HUMANPPP1CCphysical
23401853
PTPA_HUMANPPP2R4physical
23401853
SP1_HUMANSP1physical
23825960
TCP4_HUMANSUB1physical
23825960
DEAF1_HUMANDEAF1physical
23825960
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 SP3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Sp3 is involved in the regulation of SOCS3 gene expression.";
Ehlting C., Haussinger D., Bode J.G.;
Biochem. J. 387:737-745(2005).
Cited for: ACETYLATION AT LYS-551, AND FUNCTION.
"Transcription factor Sp3 is regulated by acetylation.";
Braun H., Koop R., Ertmer A., Nacht S., Suske G.;
Nucleic Acids Res. 29:4994-5000(2001).
Cited for: ACETYLATION AT LYS-551, FUNCTION, AND MUTAGENESIS OF 551-LYS--GLU-557.
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-73, 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-73; SER-563; SER-566 ANDSER-646, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMO-modified Sp3 represses transcription by provoking localheterochromatic gene silencing.";
Stielow B., Sapetschnig A., Wink C., Kraeger I., Suske G.;
EMBO Rep. 9:899-906(2008).
Cited for: SUMOYLATION AT LYS-551, AND FUNCTION OF ISOFORMS.
"The modification of Sp3 isoforms by SUMOylation has differentialeffects on the SRC1A promoter.";
Ellis D.J., Dehm S.M., Bonham K.;
Gene 379:68-78(2006).
Cited for: SUMOYLATION AT LYS-551, FUNCTION OF ISOFORMS, AND MUTAGENESIS OFLYS-551.
"Sumoylation of internally initiated Sp3 isoforms regulatestranscriptional repression via a Trichostatin A-insensitivemechanism.";
Spengler M.L., Kennett S.B., Moorefield K.S., Simmons S.O.,Brattain M.G., Horowitz J.M.;
Cell. Signal. 17:153-166(2005).
Cited for: SUMOYLATION AT LYS-551, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF 551-LYS--GLU-553.
"SUMO-1 modification represses Sp3 transcriptional activation andmodulates its subnuclear localization.";
Ross S., Best J.L., Zon L.I., Gill G.;
Mol. Cell 10:831-842(2002).
Cited for: SUMOYLATION AT LYS-120 AND LYS-551, SUBCELLULAR LOCATION, FUNCTION,AND MUTAGENESIS OF LYS-120 AND LYS-551.

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