SP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SP1_HUMAN
• UniProt AC: P08047
• Protein Name: Transcription factor Sp1
• Gene Name: SP1
• Organism: Homo sapiens (Human).
• Sequence Length: 785
• Subcellular Localization: Nucleus. Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.
• 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 an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1. [PubMed: 10391891]
• Protein Sequence: MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF

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	20068231
2	Phosphorylation	------MSDQDHSMD ------CCCCCCCHH	43.93	29255136
7	Phosphorylation	-MSDQDHSMDEMTAV -CCCCCCCHHHEEEE	35.90	29255136
12	Phosphorylation	DHSMDEMTAVVKIEK CCCHHHEEEEEEEEC	17.79	29255136
16	Sumoylation	DEMTAVVKIEKGVGG HHEEEEEEEECCCCC	38.25	-
16	Sumoylation	DEMTAVVKIEKGVGG HHEEEEEEEECCCCC	38.25	28112733
19	Acetylation	TAVVKIEKGVGGNNG EEEEEEECCCCCCCC	63.47	25953088
36	Phosphorylation	GNGGGAFSQARSSST CCCCCCCCCCCCCCC	23.54	26714015
36 (in isoform 3)	Phosphorylation	-	23.54	28634120
40	Phosphorylation	GAFSQARSSSTGSSS CCCCCCCCCCCCCCC	31.49	23401153
40 (in isoform 3)	Phosphorylation	-	31.49	28634120
41	Phosphorylation	AFSQARSSSTGSSSS CCCCCCCCCCCCCCC	26.77	30278072
42	Phosphorylation	FSQARSSSTGSSSST CCCCCCCCCCCCCCC	37.73	30278072
43	Phosphorylation	SQARSSSTGSSSSTG CCCCCCCCCCCCCCC	42.93	30278072
45	Phosphorylation	ARSSSTGSSSSTGGG CCCCCCCCCCCCCCC	27.43	25463755
45 (in isoform 3)	Phosphorylation	-	27.43	28634120
46	Phosphorylation	RSSSTGSSSSTGGGG CCCCCCCCCCCCCCC	29.65	30278072
47	Phosphorylation	SSSTGSSSSTGGGGQ CCCCCCCCCCCCCCC	33.35	30278072
48	Phosphorylation	SSTGSSSSTGGGGQE CCCCCCCCCCCCCCC	32.78	30278072
49	Phosphorylation	STGSSSSTGGGGQES CCCCCCCCCCCCCCC	41.62	30278072
52	Phosphorylation	SSSSTGGGGQESQPS CCCCCCCCCCCCCCC	35.64	32142685
56	Phosphorylation	TGGGGQESQPSPLAL CCCCCCCCCCCHHHH	39.23	17609267
59	Phosphorylation	GGQESQPSPLALLAA CCCCCCCCHHHHHHH	25.55	25159151
67	Phosphorylation	PLALLAATCSRIESP HHHHHHHHHHCCCCC	12.85	30278072
69	Phosphorylation	ALLAATCSRIESPNE HHHHHHHHCCCCCCC	31.75	30278072
71 (in isoform 3)	Phosphorylation	-	3.36	28634120
73	Phosphorylation	ATCSRIESPNENSNN HHHHCCCCCCCCCCC	30.56	20873877
78	Phosphorylation	IESPNENSNNSQGPS CCCCCCCCCCCCCCC	31.07	20873877
81	Phosphorylation	PNENSNNSQGPSQSG CCCCCCCCCCCCCCC	40.54	20873877
85	Phosphorylation	SNNSQGPSQSGGTGE CCCCCCCCCCCCCCC	43.75	26074081
87	Phosphorylation	NSQGPSQSGGTGELD CCCCCCCCCCCCCCC	43.45	26074081
90	Phosphorylation	GPSQSGGTGELDLTA CCCCCCCCCCCCEEE	30.89	26074081
96	Phosphorylation	GTGELDLTATQLSQG CCCCCCEEEEEECCC	27.59	27251275
98	Phosphorylation	GELDLTATQLSQGAN CCCCEEEEEECCCCC	25.47	27251275
101	Phosphorylation	DLTATQLSQGANGWQ CEEEEEECCCCCCEE	19.42	17609267
111	Phosphorylation	ANGWQIISSSSGATP CCCEEEEECCCCCCC	26.29	20873877
112	Phosphorylation	NGWQIISSSSGATPT CCEEEEECCCCCCCC	20.36	20873877
113	Phosphorylation	GWQIISSSSGATPTS CEEEEECCCCCCCCC	26.46	20873877
114	Phosphorylation	WQIISSSSGATPTSK EEEEECCCCCCCCCC	34.10	20873877
117	Phosphorylation	ISSSSGATPTSKEQS EECCCCCCCCCCCCC	30.53	20873877
119	Phosphorylation	SSSGATPTSKEQSGS CCCCCCCCCCCCCCC	48.34	20873877
120	O-linked_Glycosylation	SSGATPTSKEQSGSS CCCCCCCCCCCCCCC	35.08	16027160
120	Phosphorylation	SSGATPTSKEQSGSS CCCCCCCCCCCCCCC	35.08	20873877
126	O-linked_Glycosylation	TSKEQSGSSTNGSNG CCCCCCCCCCCCCCC	38.96	16027160
128	O-linked_Glycosylation	KEQSGSSTNGSNGSE CCCCCCCCCCCCCCC	45.34	16027160
134	O-linked_Glycosylation	STNGSNGSESSKNRT CCCCCCCCCCCCCCE	38.26	16027160
254	O-linked_Glycosylation	SGQTQYVTNVPVALN CCCCEEECCCCEEEC	26.09	16027160
265	O-linked_Glycosylation	VALNGNITLLPVNSV EEECCCEEEEECCCC	26.66	16027160
271	O-linked_Glycosylation	ITLLPVNSVSAATLT EEEEECCCCCEEEEC	20.06	16027160
273	O-linked_Glycosylation	LLPVNSVSAATLTPS EEECCCCCEEEECCC	16.41	16027160
276	O-linked_Glycosylation	VNSVSAATLTPSSQA CCCCCEEEECCCCCC	30.77	16027160
278	Phosphorylation	SVSAATLTPSSQAVT CCCEEEECCCCCCEE	19.44	22817900
312	O-linked_Glycosylation	ISSASLVSSQASSSS ECCHHCCCCCCCCCC	23.25	16027160
375	Phosphorylation	LNIQQNQTSGGSLQA EECCCCCCCCCCCCH	36.57	20068231
376	Phosphorylation	NIQQNQTSGGSLQAG ECCCCCCCCCCCCHH	31.24	20068231
379	Phosphorylation	QNQTSGGSLQAGQQK CCCCCCCCCCHHCCC	22.34	20068231
394	O-linked_Glycosylation	EGEQNQQTQQQQILI CCCCCHHHHHHHHHH	20.69	16027160
421	O-linked_Glycosylation	ALQAAPLSGQTFTTQ HHHHCCCCCCEECCC	28.00	16027160
424	O-linked_Glycosylation	AAPLSGQTFTTQAIS HCCCCCCEECCCCCC	26.86	16027160
446	O-linked_Glycosylation	QLQAVPNSGPIIIRT CEECCCCCCCEEEEC	39.62	16027160
453	O-linked_Glycosylation	SGPIIIRTPTVGPNG CCCEEEECCCCCCCC	16.95	16027160
453	Phosphorylation	SGPIIIRTPTVGPNG CCCEEEECCCCCCCC	16.95	14744793
455	O-linked_Glycosylation	PIIIRTPTVGPNGQV CEEEECCCCCCCCCE	37.17	16027160
491	O-linked_Glycosylation	LAPMQGVSLGQTSSS EECCCCCCCCCCCCC	33.34	16027160
491	O-linked_Glycosylation	LAPMQGVSLGQTSSS EECCCCCCCCCCCCC	33.34	11371615
507	O-linked_Glycosylation	TTLTPIASAASIPAG CCCCCCCCCCCCCCC	25.70	16027160
510	O-linked_Glycosylation	TPIASAASIPAGTVT CCCCCCCCCCCCEEE	28.90	16027160
517	O-linked_Glycosylation	SIPAGTVTVNAAQLS CCCCCEEEECHHHHH	14.10	16027160
562	Ubiquitination	ANAPGDHGAQLGLHG ECCCCCHHCCEECCC	21.54	24816145
575	Ubiquitination	HGAGGDGIHDDTAGG CCCCCCCCCCCCCCC	3.71	29967540
576	Ubiquitination	GAGGDGIHDDTAGGE CCCCCCCCCCCCCCC	32.21	29967540
579	Phosphorylation	GDGIHDDTAGGEEGE CCCCCCCCCCCCCCC	33.01	9153193
588	Phosphorylation	GGEEGENSPDAQPQA CCCCCCCCCCCCCCC	21.61	26657352
603	Ubiquitination	GRRTRREACTCPYCK CCCCCHHHCCCCCCC	7.66	-
603	Ubiquitination	GRRTRREACTCPYCK CCCCCHHHCCCCCCC	7.66	24816145
610	Ubiquitination	ACTCPYCKDSEGRGS HCCCCCCCCCCCCCC	59.45	24816145
612	O-linked_Glycosylation	TCPYCKDSEGRGSGD CCCCCCCCCCCCCCC	27.69	16027160
612	Phosphorylation	TCPYCKDSEGRGSGD CCCCCCCCCCCCCCC	27.69	16332679
616	Ubiquitination	CKDSEGRGSGDPGKK CCCCCCCCCCCCCCC	47.00	29967540
617	Phosphorylation	KDSEGRGSGDPGKKK CCCCCCCCCCCCCCC	38.37	20068231
617	Ubiquitination	KDSEGRGSGDPGKKK CCCCCCCCCCCCCCC	38.37	29967540
623	Ubiquitination	GSGDPGKKKQHICHI CCCCCCCCCEEEEEE	64.68	29967540
624	Ubiquitination	SGDPGKKKQHICHIQ CCCCCCCCEEEEEEE	51.06	29967540
640	O-linked_Glycosylation	CGKVYGKTSHLRAHL CCCEECCCHHHHHHH	19.60	16027160
640	Phosphorylation	CGKVYGKTSHLRAHL CCCEECCCHHHHHHH	19.60	16332679
641	O-linked_Glycosylation	GKVYGKTSHLRAHLR CCEECCCHHHHHHHH	24.82	16027160
641	Phosphorylation	GKVYGKTSHLRAHLR CCEECCCHHHHHHHH	24.82	16332679
645	Ubiquitination	GKTSHLRAHLRWHTG CCCHHHHHHHHCCCC	16.66	29967540
651	Phosphorylation	RAHLRWHTGERPFMC HHHHHCCCCCCCEEE	33.50	22617229
661	Phosphorylation	RPFMCTWSYCGKRFT CCEEEEEEECCCCCC	7.75	29083192
668	Phosphorylation	SYCGKRFTRSDELQR EECCCCCCCCHHHHH	33.04	18258854
670	Phosphorylation	CGKRFTRSDELQRHK CCCCCCCCHHHHHHH	32.17	25159151
678	Ubiquitination	DELQRHKRTHTGEKK HHHHHHHCCCCCCCC	26.14	-
679	Phosphorylation	ELQRHKRTHTGEKKF HHHHHHCCCCCCCCC	28.70	-
681	Phosphorylation	QRHKRTHTGEKKFAC HHHHCCCCCCCCCCC	46.56	17049555
685	Ubiquitination	RTHTGEKKFACPECP CCCCCCCCCCCCCCC	33.61	-
686	Ubiquitination	THTGEKKFACPECPK CCCCCCCCCCCCCCH	14.50	29967540
693	2-Hydroxyisobutyrylation	FACPECPKRFMRSDH CCCCCCCHHHHCCHH	70.67	-
693	Ubiquitination	FACPECPKRFMRSDH CCCCCCCHHHHCCHH	70.67	29967540
698	O-linked_Glycosylation	CPKRFMRSDHLSKHI CCHHHHCCHHHHHHH	20.00	16027160
698	Phosphorylation	CPKRFMRSDHLSKHI CCHHHHCCHHHHHHH	20.00	16332679
702	O-linked_Glycosylation	FMRSDHLSKHIKTHQ HHCCHHHHHHHHHHC	20.83	16027160
702	Phosphorylation	FMRSDHLSKHIKTHQ HHCCHHHHHHHHHHC	20.83	16332679
703	Acetylation	MRSDHLSKHIKTHQN HCCHHHHHHHHHHCC	56.56	16478997
707	Phosphorylation	HLSKHIKTHQNKKGG HHHHHHHHHCCCCCC	28.26	-
720	Phosphorylation	GGPGVALSVGTLPLD CCCCEEEEEEEEECC	14.57	-
723	Phosphorylation	GVALSVGTLPLDSGA CEEEEEEEEECCCCC	24.05	-
728	Phosphorylation	VGTLPLDSGAGSEGS EEEEECCCCCCCCCC	37.92	18239466
732	Phosphorylation	PLDSGAGSEGSGTAT ECCCCCCCCCCCCCC	37.95	18239466
735	Phosphorylation	SGAGSEGSGTATPSA CCCCCCCCCCCCCCC	28.99	28348404
737	Phosphorylation	AGSEGSGTATPSALI CCCCCCCCCCCCCEE	29.11	27251275
739	Phosphorylation	SEGSGTATPSALITT CCCCCCCCCCCEEEC	20.02	11904305
741	Phosphorylation	GSGTATPSALITTNM CCCCCCCCCEEECCC	31.21	28348404
745	Phosphorylation	ATPSALITTNMVAME CCCCCEEECCCCHHH	16.99	28348404
746	Phosphorylation	TPSALITTNMVAMEA CCCCEEECCCCHHHH	17.83	28348404

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
42	S	Phosphorylation	Kinase	AKT1	P31749	PSP
56	S	Phosphorylation	Kinase	ATM	Q13315	PSP
59	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
59	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
59	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
59	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
101	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
101	S	Phosphorylation	Kinase	ATR	Q13535	PSP
278	T	Phosphorylation	Kinase	JNK1	P45983	PSP
453	T	Phosphorylation	Kinase	MAPK3	P21708	GPS
453	T	Phosphorylation	Kinase	MK01	P28482	PhosphoELM
453	T	Phosphorylation	Kinase	MAPK1	P63086	GPS
453	T	Phosphorylation	Kinase	MK03	P27361	PhosphoELM
453	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
579	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
579	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
641	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
651	T	Phosphorylation	Kinase	PRKCZ	Q05513	Uniprot
668	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
670	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
679	T	Phosphorylation	Kinase	AKT1	P31749	PSP
681	T	Phosphorylation	Kinase	PKCZ	Q05513	PSP
698	S	Phosphorylation	Kinase	AKT1	P31749	PSP
702	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
720	S	Phosphorylation	Kinase	CDK1	P06493	PSP
723	T	Phosphorylation	Kinase	CDK1	P06493	PSP
728	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
732	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
737	T	Phosphorylation	Kinase	CDK1	P06493	PSP
739	T	Phosphorylation	Kinase	MK03	P27361	PhosphoELM
739	T	Phosphorylation	Kinase	MAPK3	P21708	GPS
739	T	Phosphorylation	Kinase	CDK1	P06493	PSP
739	T	Phosphorylation	Kinase	JNK1	P45983	PSP
739	T	Phosphorylation	Kinase	MAPK1	P63086	GPS
739	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
739	T	Phosphorylation	Kinase	MK01	P28482	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:19372209

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
7	S	Phosphorylation	Phosphorylation on Ser-7 enhances ubiquitination and protein degradation.	14593115
7	S	ubiquitylation	Phosphorylation on Ser-7 enhances ubiquitination and protein degradation.	14593115
59	S	Phosphorylation	Dephosphorylation on Ser-59 leads to increased chromatin association during interphase and increases the transcriptional activity.	14593115
59	S	Phosphorylation	Phosphorylation on Ser-59 enhances proteolytic cleavage.	14593115
59	S	Phosphorylation	Ser-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase.	14593115
101	S	Phosphorylation	Hyperphosphorylation on Ser-101 in response to DNA damage has no effect on transcriptional activity.	14593115
278	T	Phosphorylation	Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	14593115
278	T	ubiquitylation	Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	14593115
453	T	Phosphorylation	MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription.	14593115
641	S	Phosphorylation	Phosphorylation on Ser-641 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107.	14593115
668	T	Phosphorylation	Phosphorylation on Thr-668, Ser-670 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	14593115
670	S	Phosphorylation	Phosphorylation on Thr-668, Ser-670 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	14593115
681	T	Phosphorylation	Phosphorylation on Thr-668, Ser-670 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter.	14593115
681	T	Phosphorylation	Ser-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase.	14593115
739	T	Phosphorylation	Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	14593115
739	T	Phosphorylation	MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription.	14593115
739	T	ubiquitylation	Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway.	14593115

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANDR_HUMAN	AR	physical	15661808
CEBPB_HUMAN	CEBPB	physical	12847250
AATF_HUMAN	AATF	physical	12847090
HDAC1_HUMAN	HDAC1	physical	12847090
HDAC2_HUMAN	HDAC2	physical	12151407
SMCA4_HUMAN	SMARCA4	physical	11018012
SMRC2_HUMAN	SMARCC2	physical	11018012
SMRC1_HUMAN	SMARCC1	physical	11018012
HDAC1_HUMAN	HDAC1	physical	11896613
RB_HUMAN	RB1	physical	11896613
HDAC1_HUMAN	HDAC1	physical	12091390
HDAC2_HUMAN	HDAC2	physical	12091390
RBBP4_HUMAN	RBBP4	physical	12091390
HDAC1_HUMAN	HDAC1	physical	12176973
HDAC2_HUMAN	HDAC2	physical	12176973
MSX1_HUMAN	MSX1	physical	10215616
MEF2C_HUMAN	MEF2C	physical	9748305
HD_HUMAN	HTT	physical	11839795
AHR_HUMAN	AHR	physical	10471301
ARNT_HUMAN	ARNT	physical	10471301
MYC_HUMAN	MYC	physical	11274368
PO2F1_HUMAN	POU2F1	physical	8668525
TF65_HUMAN	RELA	physical	12055073
KLF4_HUMAN	KLF4	physical	9651398
TF65_HUMAN	RELA	physical	7933095
NFKB1_HUMAN	NFKB1	physical	7933095
NFKB2_HUMAN	NFKB2	physical	7933095
REL_HUMAN	REL	physical	7933095
PURA_HUMAN	PURA	physical	10457364
KLF10_HUMAN	KLF10	physical	10976766
SRBP2_HUMAN	SREBF2	physical	10976766
ELF1_HUMAN	ELF1	physical	10976766
PO2F1_HUMAN	POU2F1	physical	10976766
HCFC1_HUMAN	HCFC1	physical	10976766
POGZ_HUMAN	POGZ	physical	10976766
GATA1_HUMAN	GATA1	physical	12239153
RBTN2_HUMAN	LMO2	physical	12239153
TAL1_HUMAN	TAL1	physical	12239153
LDB1_HUMAN	LDB1	physical	12239153
SMAD3_HUMAN	SMAD3	physical	11432852
MEF2D_HUMAN	MEF2D	physical	12213324
TAF4_HUMAN	TAF4	physical	9742090
SRF_HUMAN	SRF	physical	10082523
MYOG_HUMAN	MYOG	physical	10082523
MYOD1_HUMAN	MYOD1	physical	10082523
JUN_HUMAN	JUN	physical	10506225
STF1_HUMAN	NR5A1	physical	10919277
PSIP1_HUMAN	PSIP1	physical	9885563
TCP4_HUMAN	SUB1	physical	9885563
E2F1_HUMAN	E2F1	physical	8657141
PRS8_HUMAN	PSMC5	physical	18572193
MECP2_HUMAN	MECP2	physical	15109260
HNF4A_HUMAN	HNF4A	physical	19115260
MCAF1_HUMAN	ATF7IP	physical	19106100
HDAC1_HUMAN	HDAC1	physical	19062177
EP300_HUMAN	EP300	physical	19062177
DNMT1_HUMAN	DNMT1	physical	17124180
ESR1_HUMAN	ESR1	physical	19652226
TBX21_HUMAN	TBX21	physical	17075044
TLX3_HUMAN	TLX3	physical	20211142
HDAC4_HUMAN	HDAC4	physical	18850004
HDAC1_HUMAN	HDAC1	physical	18850004
KPCZ_HUMAN	PRKCZ	physical	16943418
STAT3_HUMAN	STAT3	physical	16931573
BRCA2_HUMAN	BRCA2	physical	18769160
CDK4_HUMAN	CDK4	physical	18769160
RAD51_HUMAN	RAD51	physical	18769160
SKP2_HUMAN	SKP2	physical	18769160
SP3_HUMAN	SP3	physical	16734381
CEBPB_HUMAN	CEBPB	physical	16651265
ESR1_HUMAN	ESR1	physical	16651265
CCNA2_HUMAN	CCNA2	physical	16575904
HDAC4_HUMAN	HDAC4	physical	18632985
EP300_HUMAN	EP300	physical	16478997
HDAC1_HUMAN	HDAC1	physical	16478997
JUN_HUMAN	JUN	physical	16478997
ESR1_HUMAN	ESR1	physical	16439465
ERR1_HUMAN	ESRRA	physical	16439465
ERR2_HUMAN	ESRRB	physical	16439465
ERR3_HUMAN	ESRRG	physical	16439465
RARA_HUMAN	RARA	physical	19401466
MCAF1_HUMAN	ATF7IP	physical	16314315
RTA_EBVB9	BRLF1	physical	16314315
P53_HUMAN	TP53	physical	12665570
HDAC1_HUMAN	HDAC1	physical	12665570
SP3_HUMAN	SP3	physical	12200149
HDAC1_HUMAN	HDAC1	physical	12200149
SMCA4_HUMAN	SMARCA4	physical	12192045
HDAC1_HUMAN	HDAC1	physical	16121030
HS90A_HUMAN	HSP90AA1	physical	16118214
CTBP1_HUMAN	CTBP1	physical	16036112
ESR1_HUMAN	ESR1	physical	15987735
NCOR2_HUMAN	NCOR2	physical	15878880
NCOR1_HUMAN	NCOR1	physical	15878880
BCOR_HUMAN	BCOR	physical	15878880
BC11B_HUMAN	BCL11B	physical	15849318
CBX5_HUMAN	CBX5	physical	15849318
COT1_HUMAN	NR2F1	physical	15849318
HDAC1_HUMAN	HDAC1	physical	15722551
HDAC1_HUMAN	HDAC1	physical	15713621
HDAC2_HUMAN	HDAC2	physical	15713621
P53_HUMAN	TP53	physical	15674334
HNF4A_HUMAN	HNF4A	physical	15651981
GATA3_HUMAN	GATA3	physical	18338249
HDAC1_HUMAN	HDAC1	physical	15557281
ESR1_HUMAN	ESR1	physical	15557281
REST_HUMAN	REST	physical	15528196
HDAC1_HUMAN	HDAC1	physical	15528196
SIN3A_HUMAN	SIN3A	physical	15528196
SP3_HUMAN	SP3	physical	11517158
EP300_HUMAN	EP300	physical	11517158
HDAC1_HUMAN	HDAC1	physical	11517158
RARA_HUMAN	RARA	physical	18270252
RXRA_HUMAN	RXRA	physical	18270252
TF65_HUMAN	RELA	physical	18249093
SMAD4_HUMAN	SMAD4	physical	18215124
EP300_HUMAN	EP300	physical	11030335
HDAC1_HUMAN	HDAC1	physical	15155736
E2F1_HUMAN	E2F1	physical	10409740
ESR1_HUMAN	ESR1	physical	15084343
HDAC2_HUMAN	HDAC2	physical	18059533
HDAC1_HUMAN	HDAC1	physical	18059533
GATA4_HUMAN	GATA4	physical	14988427
GATA6_HUMAN	GATA6	physical	14988427
STAT3_HUMAN	STAT3	physical	17471507
TYY1_HUMAN	YY1	physical	17990281
DCAF6_HUMAN	DCAF6	physical	17984071
ANDR_HUMAN	AR	physical	17984071
PARP1_HUMAN	PARP1	physical	17961220
MYC_HUMAN	MYC	physical	17418410
EP300_HUMAN	EP300	physical	17906698
HDAC1_HUMAN	HDAC1	physical	17906119
ESR1_HUMAN	ESR1	physical	17656465
EP300_HUMAN	EP300	physical	17623675
PML_HUMAN	PML	physical	21360626
ESR1_HUMAN	ESR1	physical	17312152
PHX2A_HUMAN	PHOX2A	physical	17344216
PPARG_HUMAN	PPARG	physical	20360975
NR2E1_HUMAN	NR2E1	physical	20599619
HMGA1_HUMAN	HMGA1	physical	20335021
EGR1_HUMAN	EGR1	physical	20121949
HDAC1_HUMAN	HDAC1	physical	20072153
TF65_HUMAN	RELA	physical	20861353
GATA4_HUMAN	GATA4	physical	21184844
KLF9_HUMAN	KLF9	physical	17717078
KPCD_HUMAN	PRKCD	physical	21159880
HDAC2_HUMAN	HDAC2	physical	21159880
MYCN_HUMAN	MYCN	physical	21123453
GATA6_HUMAN	GATA6	physical	21076612
SMCA4_HUMAN	SMARCA4	physical	20969766
RNF4_HUMAN	RNF4	physical	21983342
HIF1A_HUMAN	HIF1A	physical	17024177
RB_HUMAN	RB1	physical	10850422
CCND1_HUMAN	CCND1	physical	10850422
NFYA_HUMAN	NFYA	physical	10393239
NFYA_HUMAN	NFYA	physical	10446910
SMAD2_HUMAN	SMAD2	physical	10878024
SMAD3_HUMAN	SMAD3	physical	10878024
SMAD4_HUMAN	SMAD4	physical	10878024
SMAD2_HUMAN	SMAD2	physical	22227581
SMAD3_HUMAN	SMAD3	physical	22227581
CDN2A_HUMAN	CDKN2A	physical	21555589
ARF_HUMAN	CDKN2A	physical	21555589
MEIS2_HUMAN	MEIS2	physical	22028617
TYY1_HUMAN	YY1	physical	21335086
STAT3_HUMAN	STAT3	physical	21184768
PRGR_HUMAN	PGR	physical	21184768
KPCD_HUMAN	PRKCD	physical	22496486
EP300_HUMAN	EP300	physical	22415975
EPAS1_HUMAN	EPAS1	physical	22402494
KLF4_HUMAN	KLF4	physical	22282354
PPARG_HUMAN	PPARG	physical	22282354
CDK1_HUMAN	CDK1	physical	22266860
CCNB1_HUMAN	CCNB1	physical	22266860
ACTG_HUMAN	ACTG1	physical	22266860
ACTBL_HUMAN	ACTBL2	physical	22266860
ACTC_HUMAN	ACTC1	physical	22266860
ANXA2_HUMAN	ANXA2	physical	22266860
CAPZB_HUMAN	CAPZB	physical	22266860
CBP_HUMAN	CREBBP	physical	22266860
CNTLN_HUMAN	CNTLN	physical	22266860
CO3A1_HUMAN	COL3A1	physical	22266860
DESM_HUMAN	DES	physical	22266860
DREB_HUMAN	DBN1	physical	22266860
FKB15_HUMAN	FKBP15	physical	22266860
FGOP2_HUMAN	FGFR1OP2	physical	22266860
GBP1_HUMAN	GBP1	physical	22266860
GRP75_HUMAN	HSPA9	physical	22266860
LMO7_HUMAN	LMO7	physical	22266860
LUZP1_HUMAN	LUZP1	physical	22266860
MAT1_HUMAN	MNAT1	physical	22266860
MRCKB_HUMAN	CDC42BPB	physical	22266860
MYH7B_HUMAN	MYH7B	physical	22266860
MYH9_HUMAN	MYH9	physical	22266860
MYH10_HUMAN	MYH10	physical	22266860
MYH11_HUMAN	MYH11	physical	22266860
MYH14_HUMAN	MYH14	physical	22266860
MYO1B_HUMAN	MYO1B	physical	22266860
MYO1C_HUMAN	MYO1C	physical	22266860
MYO1E_HUMAN	MYO1E	physical	22266860
MYO6_HUMAN	MYO6	physical	22266860
ML12A_HUMAN	MYL12A	physical	22266860
MYL9_HUMAN	MYL9	physical	22266860
MYL6B_HUMAN	MYL6B	physical	22266860
MYL3_HUMAN	MYL3	physical	22266860
NEBU_HUMAN	NEB	physical	22266860
ODFP2_HUMAN	ODF2	physical	22266860
PLEC_HUMAN	PLEC	physical	22266860
POTEE_HUMAN	POTEE	physical	22266860
RSF1_HUMAN	RSF1	physical	22266860
FHL1_HUMAN	FHL1	physical	22266860
SRRT_HUMAN	SRRT	physical	22266860
TBA1B_HUMAN	TUBA1B	physical	22266860
TBB3_HUMAN	TUBB3	physical	22266860
TBB4A_HUMAN	TUBB4A	physical	22266860
TIM_HUMAN	TIMELESS	physical	22266860
TITIN_HUMAN	TTN	physical	22266860
TNR11_HUMAN	TNFRSF11A	physical	22266860
TPM1_HUMAN	TPM1	physical	22266860
TPM2_HUMAN	TPM2	physical	22266860
TPM3_HUMAN	TPM3	physical	22266860
TPM4_HUMAN	TPM4	physical	22266860
VIME_HUMAN	VIM	physical	22266860
PTPA_HUMAN	PPP2R4	physical	22266860
HDAC1_HUMAN	HDAC1	physical	21636851
BRCA1_HUMAN	BRCA1	physical	17766039
HLTF_HUMAN	HLTF	physical	10391891
HS90A_HUMAN	HSP90AA1	physical	19245816
MK08_HUMAN	MAPK8	physical	19245816
P53_HUMAN	TP53	physical	9685344
P53_HUMAN	TP53	physical	15574328
P53_HUMAN	TP53	physical	15710382
TBP_HUMAN	TBP	physical	12753906
SP1_HUMAN	SP1	physical	9343410
TAF4_DROME	Taf4	physical	9343410
ESR2_HUMAN	ESR2	physical	10681512
ESR1_HUMAN	ESR1	physical	10681512
VHL_HUMAN	VHL	physical	9271438
RBL1_HUMAN	RBL1	physical	7565695
DDX3X_HUMAN	DDX3X	physical	16818630
P53_HUMAN	TP53	physical	9492043
HIF1A_HUMAN	HIF1A	physical	12228247
SMAD3_HUMAN	SMAD3	physical	12228247
PO2F1_HUMAN	POU2F1	physical	19070619
MYC_HUMAN	MYC	physical	15780936
HIF1A_HUMAN	HIF1A	physical	15780936
NUP62_HUMAN	NUP62	physical	9407313
SP3_HUMAN	SP3	physical	10825178
SP3_HUMAN	SP3	physical	15247906
AP2A_HUMAN	TFAP2A	physical	15705965
ESR1_HUMAN	ESR1	physical	15705965
FOXM1_HUMAN	FOXM1	physical	23635401
KIF1A_HUMAN	KIF1A	physical	20195357
SNUT2_HUMAN	USP39	physical	20195357
DDX5_HUMAN	DDX5	physical	20195357
NP1L1_HUMAN	NAP1L1	physical	20195357
TPIS_HUMAN	TPI1	physical	20195357
SENP6_HUMAN	SENP6	physical	20195357
NEPRO_HUMAN	C3orf17	physical	20195357
PPIG_HUMAN	PPIG	physical	20195357
RHG21_HUMAN	ARHGAP21	physical	20195357
SP3_HUMAN	SP3	physical	12414801
JUN_HUMAN	JUN	physical	17215518
HIC1_HUMAN	HIC1	physical	23704280
PIN1_HUMAN	PIN1	physical	25398907
CDK1_HUMAN	CDK1	physical	25398907
CCNB1_HUMAN	CCNB1	physical	25398907
PPARG_HUMAN	PPARG	physical	24735796
CBP_HUMAN	CREBBP	physical	25294805
ZBTB2_HUMAN	ZBTB2	physical	25609694
STRAP_HUMAN	STRAP	physical	25483064
AP2A_HUMAN	TFAP2A	physical	22182699
TBP_HUMAN	TBP	physical	25363021
RBBP7_HUMAN	RBBP7	physical	25885317
SENP3_HUMAN	SENP3	physical	26511642
NPM_HUMAN	NPM1	physical	19074833
KPCD_HUMAN	PRKCD	physical	19169273
P53_HUMAN	TP53	physical	19846904
MDM2_HUMAN	MDM2	physical	22378045
TCP4_HUMAN	SUB1	physical	23825960
DEAF1_HUMAN	DEAF1	physical	23825960
SP3_HUMAN	SP3	physical	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.

Related Literatures of Post-Translational Modification

Acetylation

"Sp1 deacetylation induced by phorbol ester recruits p300 to activate12(S)-lipoxygenase gene transcription.";
Hung J.J., Wang Y.T., Chang W.C.;
Mol. Cell. Biol. 26:1770-1785(2006).
Cited for: ACETYLATION AT LYS-703, INTERACTION WITH HDAC1; EP300 AND JUN,FUNCTION, AND MUTAGENESIS OF LYS-703.
PubMed: 16478997

O-linked Glycosylation

"Insulin dynamically regulates calmodulin gene expression bysequential O-glycosylation and phosphorylation of SP1 and itssubcellular compartmentalization in liver cells.";
Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A.,Gerling I.C., Raghow R., Solomon S.;
J. Biol. Chem. 281:3642-3650(2006).
Cited for: GLYCOSYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702,PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATIONBY MASS SPECTROMETRY.
PubMed: 16332679

"O-linkage of N-acetylglucosamine to Sp1 activation domain inhibitsits transcriptional capability.";
Yang X., Su K., Roos M.D., Chang Q., Paterson A.J., Kudlow J.E.;
Proc. Natl. Acad. Sci. U.S.A. 98:6611-6616(2001).
Cited for: GLYCOSYLATION AT SER-491, FUNCTION, AND MUTAGENESIS OF SER-491.
PubMed: 11371615

"O glycosylation of an Sp1-derived peptide blocks known Sp1 proteininteractions.";
Roos M.D., Su K., Baker J.R., Kudlow J.E.;
Mol. Cell. Biol. 17:6472-6480(1997).
Cited for: GLYCOSYLATION AT SER-491, MUTAGENESIS OF SER-491, AND IDENTIFICATIONBY MASS SPECTROMETRY.
PubMed: 9343410

Phosphorylation

"Phosphorylation by c-Jun NH2-terminal kinase 1 regulates thestability of transcription factor Sp1 during mitosis.";
Chuang J.-Y., Wang Y.-T., Yeh S.-H., Liu Y.-W., Chang W.-C.,Hung J.-J.;
Mol. Biol. Cell 19:1139-1151(2008).
Cited for: PHOSPHORYLATION AT SER-59, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-59; SER-73; THR-117; THR-278 AND THR-739.
PubMed: 18199680

"Angiotensin II-inducible platelet-derived growth factor-Dtranscription requires specific Ser/Thr residues in the second zincfinger region of Sp1.";
Tan N.Y., Midgley V.C., Kavurma M.M., Santiago F.S., Luo X., Peden R.,Fahmy R.G., Berndt M.C., Molloy M.P., Khachigian L.M.;
Circ. Res. 102:38-51(2008).
Cited for: PHOSPHORYLATION AT THR-668; SER-670 AND THR-681, AND MUTAGENESIS OFTHR-668; SER-670 AND THR-681.
PubMed: 18258854

"Identification of phosphorylation sites on transcription factor Sp1in response to DNA damage and its accumulation at damaged sites.";
Iwahori S., Yasui Y., Kudoh A., Sato Y., Nakayama S., Murata T.,Isomura H., Tsurumi T.;
Cell. Signal. 20:1795-1803(2008).
Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-36;SER-56; SER-81; SER-85; THR-98; SER-101; THR-250; SER-281; SER-291;SER-296; SER-313; SER-351; THR-394; THR-427 AND SER-431.
PubMed: 18619531

"Phosphorylation mediates Sp1 coupled activities of proteolyticprocessing, desumoylation and degradation.";
Spengler M.L., Guo L.W., Brattain M.G.;
Cell Cycle 7:623-630(2008).
Cited for: PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16,PROTEOLYTIC PROCESSING, UBIQUITINATION, FUNCTION, AND MUTAGENESIS OFSER-7; SER-59; SER-728 AND SER-732.
PubMed: 18239466

"Phosphorylation of Sp1 in response to DNA damage by ataxiatelangiectasia-mutated kinase.";
Olofsson B.A., Kelly C.M., Kim J., Hornsby S.M., Azizkhan-Clifford J.;
Mol. Cancer Res. 5:1319-1330(2007).
Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-101.
PubMed: 18171990

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY.
PubMed: 16964243

"Phosphatidylinositol 3-kinase/protein kinase Czeta-inducedphosphorylation of Sp1 and p107 repressor release have a critical rolein histone deacetylase inhibitor-mediated derepression oftranscription of the luteinizing hormone receptor gene.";
Zhang Y., Liao M., Dufau M.L.;
Mol. Cell. Biol. 26:6748-6761(2006).
Cited for: PHOSPHORYLATION AT SER-641, FUNCTION, AND MUTAGENESIS OF SER-641.
PubMed: 16943418

"Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.";
Vicart A., Lefebvre T., Imbert J., Fernandez A., Kahn-Perles B.;
J. Mol. Biol. 364:897-908(2006).
Cited for: PHOSPHORYLATION AT SER-59 AND THR-681, DEPHOSPHORYLATION,GLYCOSYLATION, FUNCTION, AND MUTAGENESIS OF SER-59; SER-220; THR-355;THR-453; THR-651; THR-681 AND THR-739.
PubMed: 17049555

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY.
PubMed: 15302935

"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 THR-651, AND MASSSPECTROMETRY.
PubMed: 18669648

"HER-2/neu represses the metastasis suppressor RECK via ERK and Sptranscription factors to promote cell invasion.";
Hsu M.C., Chang H.C., Hung W.C.;
J. Biol. Chem. 281:4718-4725(2006).
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, AND FUNCTION.
PubMed: 16377629

"Fibroblast growth factor-2 represses platelet-derived growth factorreceptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1phosphorylation and an atypical cis-acting element in the proximalPDGFR-alpha promoter.";
Bonello M.R., Khachigian L.M.;
J. Biol. Chem. 279:2377-2382(2004).
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OFTHR-453 AND THR-739.
PubMed: 14593115

"Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelialgrowth factor gene transcription.";
Milanini-Mongiat J., Pouyssegur J., Pages G.;
J. Biol. Chem. 277:20631-20639(2002).
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OFTHR-355; THR-453 AND THR-739.
PubMed: 11904305

Sumoylation

"Phosphorylation mediates Sp1 coupled activities of proteolyticprocessing, desumoylation and degradation.";
Spengler M.L., Guo L.W., Brattain M.G.;
Cell Cycle 7:623-630(2008).
Cited for: PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16,PROTEOLYTIC PROCESSING, UBIQUITINATION, FUNCTION, AND MUTAGENESIS OFSER-7; SER-59; SER-728 AND SER-732.
PubMed: 18239466

"Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatorydomain and inhibits Sp1-dependent transcription.";
Spengler M.L., Brattain M.G.;
J. Biol. Chem. 281:5567-5574(2006).
Cited for: SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OFLYS-16; GLU-18 AND LYS-19.
PubMed: 16407261