SP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SP1_MOUSE
• UniProt AC: O89090
• Protein Name: Transcription factor Sp1
• Gene Name: Sp1
• Organism: Mus musculus (Mouse).
• Sequence Length: 784
• Subcellular Localization: Nucleus . Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location (By similarity)..
• Protein Description: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter Plays an essential role in the regulation of FE65 gene expression (By similarity). Positively regulates the transcription of the core clock component ARNTL/BMAL1. [PubMed: 24030830 Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112]
• Protein Sequence: MSDQDHSMDEVTAVVKIEKDVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGNSTNGSNGSESSKNRTVSGGQYVVAATPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIIPNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAGTISSSGSQESSSQPVTSGTAISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTSSGSSGTSSQGQTPQRVGGLQGSDSLNIQQNQTSGGSLQGSQQKEGEQSQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVQNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHQLPGLPLAIANTPGDHGTQLGLHGSGGDGIHDETAGGEGENSSDLQPQAGRRTRREACTCPYCKDSEGRASGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCNWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVTELQSINISGNGF

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
2	Acetylation	------MSDQDHSMD ------CCCCCCCHH	43.93	17242355
2	Phosphorylation	------MSDQDHSMD ------CCCCCCCHH	43.93	26824392
7	Phosphorylation	-MSDQDHSMDEVTAV -CCCCCCCHHEEEEE	35.90	26824392
12	Phosphorylation	DHSMDEVTAVVKIEK CCCHHEEEEEEEEEE	16.22	25619855
41	Phosphorylation	AAFSQTRSSSTGSSS CCCCCCCCCCCCCCC	31.84	25619855
42	Phosphorylation	AFSQTRSSSTGSSSS CCCCCCCCCCCCCCC	28.73	25619855
43	Phosphorylation	FSQTRSSSTGSSSSS CCCCCCCCCCCCCCC	37.73	25619855
44	Phosphorylation	SQTRSSSTGSSSSSG CCCCCCCCCCCCCCC	42.93	25619855
46	Phosphorylation	TRSSSTGSSSSSGGG CCCCCCCCCCCCCCC	27.43	25619855
47	Phosphorylation	RSSSTGSSSSSGGGG CCCCCCCCCCCCCCC	35.27	25619855
48	Phosphorylation	SSSTGSSSSSGGGGG CCCCCCCCCCCCCCC	30.16	25619855
49	Phosphorylation	SSTGSSSSSGGGGGQ CCCCCCCCCCCCCCC	34.64	25619855
50	Phosphorylation	STGSSSSSGGGGGQE CCCCCCCCCCCCCCC	43.32	25619855
58	Phosphorylation	GGGGGQESQPSPLAL CCCCCCCCCCCHHHH	39.23	25619855
61	Phosphorylation	GGQESQPSPLALLAA CCCCCCCCHHHHHHH	25.55	25521595
69	Phosphorylation	PLALLAATCSRIESP HHHHHHHHHHCCCCC	12.85	25619855
71	Phosphorylation	ALLAATCSRIESPNE HHHHHHHHCCCCCCC	31.75	25619855
103	Phosphorylation	DLTATQLSQGANGWQ CEEEEEECCCCCCEE	19.42	-
280	Phosphorylation	SVSAATLTPSSQAGT CCCEEEECCCCCCCC	19.44	-
309	Phosphorylation	TSGTAISSASLVSSQ CCCCEEECHHHCCCC	18.76	-
320	Phosphorylation	VSSQASSSSFFTNAN CCCCCCCCCCCCCCC	28.77	-
321	Phosphorylation	SSQASSSSFFTNANS CCCCCCCCCCCCCCC	26.74	-
369	Phosphorylation	GGLQGSDSLNIQQNQ CCCCCCCCCCCCCCC	25.64	28285833
377	Phosphorylation	LNIQQNQTSGGSLQG CCCCCCCCCCCCCCC	36.57	28285833
385	Phosphorylation	SGGSLQGSQQKEGEQ CCCCCCCCCHHCCCC	19.24	28973931
455	Phosphorylation	SGPIIIRTPTVGPNG CCCEEEECCCCCCCC	16.95	-
493	O-linked_Glycosylation	LAPMQGVSLGQTSSS EECCCCCCCCCCCCC	33.34	-
613	O-linked_Glycosylation	TCPYCKDSEGRASGD CCCCCCCCCCCCCCC	27.69	20138838
613	Phosphorylation	TCPYCKDSEGRASGD CCCCCCCCCCCCCCC	27.69	-
618	Phosphorylation	KDSEGRASGDPGKKK CCCCCCCCCCCCCCC	42.22	28059163
641	O-linked_Glycosylation	CGKVYGKTSHLRAHL CCCEECCCHHHHHHH	19.60	20138838
641	Phosphorylation	CGKVYGKTSHLRAHL CCCEECCCHHHHHHH	19.60	-
642	O-linked_Glycosylation	GKVYGKTSHLRAHLR CCEECCCHHHHHHHH	24.82	20138838
642	Phosphorylation	GKVYGKTSHLRAHLR CCEECCCHHHHHHHH	24.82	-
652	Phosphorylation	RAHLRWHTGERPFMC HHHHHCCCCCCCCCC	33.50	26643407
669	Phosphorylation	SYCGKRFTRSDELQR HHCCCCCCCCHHHHH	33.04	-
671	Phosphorylation	CGKRFTRSDELQRHK CCCCCCCCHHHHHHH	32.17	29514104
682	Phosphorylation	QRHKRTHTGEKKFAC HHHHCCCCCCCCCCC	46.56	-
699	Phosphorylation	CPKRFMRSDHLSKHI CCHHHHCCHHHHHHH	20.00	28059163
699	O-linked_Glycosylation	CPKRFMRSDHLSKHI CCHHHHCCHHHHHHH	20.00	20138838
703	Phosphorylation	FMRSDHLSKHIKTHQ HHCCHHHHHHHHHHC	20.83	-
703	O-linked_Glycosylation	FMRSDHLSKHIKTHQ HHCCHHHHHHHHHHC	20.83	20138838
704	Acetylation	MRSDHLSKHIKTHQN HCCHHHHHHHHHHCC	56.56	-
738	Phosphorylation	AGSEGTATPSALITT CCCCCCCCCCCEEEC	20.02	-

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
103	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot
280	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
455	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
455	T	Phosphorylation	Kinase	MAPK3	Q63844	Uniprot
642	S	Phosphorylation	Kinase	PRKCZ	Q02956	Uniprot
652	T	Phosphorylation	Kinase	PRKCZ	Q02956	Uniprot
671	S	Phosphorylation	Kinase	PRKCZ	Q02956	Uniprot
682	T	Phosphorylation	Kinase	PRKCZ	Q02956	Uniprot
738	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
738	T	Phosphorylation	Kinase	MAPK3	Q63844	Uniprot
738	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
7	S	Phosphorylation	Phosphorylation on Ser-7 enhances ubiquitination and protein degradation.	-
7	S	ubiquitylation	Phosphorylation on Ser-7 enhances ubiquitination and protein degradation.	-
61	S	Phosphorylation	Dephosphorylation on Ser-61 leads to increased chromatin association during interphase and increases the transcriptional activity.	21183079
61	S	Phosphorylation	Phosphorylation on Ser-61 enhances proteolytic cleavage.	21183079
61	S	Phosphorylation	Ser-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase.	21183079
103	S	Phosphorylation	Hyperphosphorylation on Ser-103 in response to DNA damage has no effect on transcriptional activity.	-
280	T	Phosphorylation	Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	-
280	T	ubiquitylation	Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	-
455	T	Phosphorylation	MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription.	-
642	S	Phosphorylation	Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107.	-
669	T	Phosphorylation	Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	-
671	S	Phosphorylation	Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	-
682	T	Phosphorylation	Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	-
682	T	Phosphorylation	Ser-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase.	-
738	T	Phosphorylation	Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	-
738	T	Phosphorylation	MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription.	-
738	T	ubiquitylation	Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_MOUSE	Hdac1	physical	16484221
HDAC1_MOUSE	Hdac1	physical	10409740
JUN_MOUSE	Jun	physical	21262356
CREB1_MOUSE	Creb1	physical	21262356
TF65_MOUSE	Rela	physical	21262356
BHE41_MOUSE	Bhlhe41	physical	12657651
EGR1_MOUSE	Egr1	physical	12569082
MSX3_MOUSE	Msx3	physical	15663180
PPARG_MOUSE	Pparg	physical	11777901
SP3_MOUSE	Sp3	physical	12054741
MDM2_MOUSE	Mdm2	physical	22378045

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.
PubMed: 17242355