SP3_MOUSE - dbPTM
SP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP3_MOUSE
UniProt AC O70494
Protein Name Transcription factor Sp3
Gene Name Sp3
Organism Mus musculus (Mouse).
Sequence Length 783
Subcellular Localization Nucleus. Nucleus, PML body. Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies (By similarity)..
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 (By similarity)..
Protein Sequence MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDVNETNADTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTTSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQDSQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGALTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKVIHSSSTVLASVEAGRDDALITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME
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
6Acetylation--MTAPEKPVKQEEM
--CCCCCCCCCHHHC
54.7922902405
72PhosphorylationCSKIGPPSPGDDDEE
HHHCCCCCCCCCHHH
44.6527087446
546PhosphorylationHPGENADSPADIRIK
CCCCCCCCCCCEEEC
21.4121082442
553AcetylationSPADIRIKEEEPDPE
CCCCEEECCCCCCHH
49.5815554904
565PhosphorylationDPEEWQLSGDSTLNT
CHHHHCCCCCCCCCC
26.0021149613
568PhosphorylationEWQLSGDSTLNTNDL
HHCCCCCCCCCCCCC
38.0226643407
569PhosphorylationWQLSGDSTLNTNDLT
HCCCCCCCCCCCCCC
28.8526643407
572PhosphorylationSGDSTLNTNDLTHLR
CCCCCCCCCCCCEEE
32.9726643407
576PhosphorylationTLNTNDLTHLRVQVV
CCCCCCCCEEEEEEE
23.0226643407
595AcetylationDQQHQEGKRLRRVAC
HHHHHHCCEEEEEEE
47.727662983
648PhosphorylationRAHLRWHSGERPFIC
HHHHHHCCCCCCEEE
35.0826643407
667PhosphorylationCGKRFTRSDELQRHR
ECCCCCCCHHHHHHH
32.1729514104
675MethylationDELQRHRRTHTGEKK
HHHHHHHHCCCCCCE
25.4116287701
691MethylationVCPECSKRFMRSDHL
ECCHHHHHHHCHHHH
17.8216287709

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 SP3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
553KAcetylation

-
553KSumoylation

-
553KSumoylation

-
553KSumoylation

-

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REST_MOUSERestphysical
17130167
SIN3A_MOUSESin3aphysical
16109738
HDAC2_MOUSEHdac2physical
16109738

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SP3_MOUSE

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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-553, AND FUNCTION.

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