dbPTM

TCP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCP4_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	P53999
Protein Name	Activated RNA polymerase II transcriptional coactivator p15
Gene Name	SUB1
Organism	Homo sapiens (Human).
Sequence Length	127
Subcellular Localization	Nucleus.
Protein Description	General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA)..
Protein Sequence	MPKSKELVSSSSSGSDSDSEVDKKLKRKKQVAPEKPVKKQKTGETSRALSSSKQSSSSRDDNMFQIGKMRYVSVRDFKGKVLIDIREYWMDPEGEMKPGRKGISLNPEQWSQLKEQISDIDDAVRKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPKSKELVSSS ----CCCCHHHHCCC	26.03	30108239
5	Acetylation	---MPKSKELVSSSS ---CCCCHHHHCCCC	62.28	21669532
9	Phosphorylation	PKSKELVSSSSSGSD CCCHHHHCCCCCCCC	36.81	23401153
10	Phosphorylation	KSKELVSSSSSGSDS CCHHHHCCCCCCCCC	27.10	22167270
11	Phosphorylation	SKELVSSSSSGSDSD CHHHHCCCCCCCCCH	22.48	22167270
12	Phosphorylation	KELVSSSSSGSDSDS HHHHCCCCCCCCCHH	40.44	22167270
13	Phosphorylation	ELVSSSSSGSDSDSE HHHCCCCCCCCCHHH	44.24	22167270
15	Phosphorylation	VSSSSSGSDSDSEVD HCCCCCCCCCHHHHH	35.57	22167270
17	Phosphorylation	SSSSGSDSDSEVDKK CCCCCCCCHHHHHHH	44.74	22167270
19	Phosphorylation	SSGSDSDSEVDKKLK CCCCCCHHHHHHHHH	43.39	22167270
29	Acetylation	DKKLKRKKQVAPEKP HHHHHHHHCCCCCCC	54.78	7670887
29	Ubiquitination	DKKLKRKKQVAPEKP HHHHHHHHCCCCCCC	54.78	-
35	Acetylation	KKQVAPEKPVKKQKT HHCCCCCCCCCCCCC	54.79	19608861
35	Ubiquitination	KKQVAPEKPVKKQKT HHCCCCCCCCCCCCC	54.79	19608861
38	Succinylation	VAPEKPVKKQKTGET CCCCCCCCCCCCCHH	59.00	23954790
38	Acetylation	VAPEKPVKKQKTGET CCCCCCCCCCCCCHH	59.00	25953088
38	Sumoylation	VAPEKPVKKQKTGET CCCCCCCCCCCCCHH	59.00	-
38	Sumoylation	VAPEKPVKKQKTGET CCCCCCCCCCCCCHH	59.00	-
42	Phosphorylation	KPVKKQKTGETSRAL CCCCCCCCCHHHHHH	37.44	28985074
45	Phosphorylation	KKQKTGETSRALSSS CCCCCCHHHHHHHHC	25.51	28102081
46	Phosphorylation	KQKTGETSRALSSSK CCCCCHHHHHHHHCC	15.97	25159151
50	Phosphorylation	GETSRALSSSKQSSS CHHHHHHHHCCCCCC	31.42	21712546
51	Phosphorylation	ETSRALSSSKQSSSS HHHHHHHHCCCCCCC	42.26	21712546
52	Phosphorylation	TSRALSSSKQSSSSR HHHHHHHCCCCCCCC	31.19	21712546
53	2-Hydroxyisobutyrylation	SRALSSSKQSSSSRD HHHHHHCCCCCCCCC	57.03	-
53	Acetylation	SRALSSSKQSSSSRD HHHHHHCCCCCCCCC	57.03	23954790
53	Ubiquitination	SRALSSSKQSSSSRD HHHHHHCCCCCCCCC	57.03	21906983
55	Phosphorylation	ALSSSKQSSSSRDDN HHHHCCCCCCCCCCC	35.60	23401153
56	Phosphorylation	LSSSKQSSSSRDDNM HHHCCCCCCCCCCCC	29.82	23401153
57	Phosphorylation	SSSKQSSSSRDDNMF HHCCCCCCCCCCCCE	34.34	23401153
58	Phosphorylation	SSKQSSSSRDDNMFQ HCCCCCCCCCCCCEE	41.50	25159151
63	Sulfoxidation	SSSRDDNMFQIGKMR CCCCCCCCEEECCEE	3.17	21406390
68	Ubiquitination	DNMFQIGKMRYVSVR CCCEEECCEEEEEEE	23.10	21890473
68	Acetylation	DNMFQIGKMRYVSVR CCCEEECCEEEEEEE	23.10	19608861
68	Sumoylation	DNMFQIGKMRYVSVR CCCEEECCEEEEEEE	23.10	19608861
68	2-Hydroxyisobutyrylation	DNMFQIGKMRYVSVR CCCEEECCEEEEEEE	23.10	-
80	Ubiquitination	SVRDFKGKVLIDIRE EEECCCCCEEEEEHH	34.16	21890473
80	2-Hydroxyisobutyrylation	SVRDFKGKVLIDIRE EEECCCCCEEEEEHH	34.16	-
80	Malonylation	SVRDFKGKVLIDIRE EEECCCCCEEEEEHH	34.16	26320211
90	Sulfoxidation	IDIREYWMDPEGEMK EEEHHHEECCCCCCC	6.36	30846556
96	Sulfoxidation	WMDPEGEMKPGRKGI EECCCCCCCCCCCCC	10.50	30846556
97	Ubiquitination	MDPEGEMKPGRKGIS ECCCCCCCCCCCCCC	39.76	-
97	Sumoylation	MDPEGEMKPGRKGIS ECCCCCCCCCCCCCC	39.76	-
97	Acetylation	MDPEGEMKPGRKGIS ECCCCCCCCCCCCCC	39.76	23749302
101	Malonylation	GEMKPGRKGISLNPE CCCCCCCCCCCCCHH	67.52	26320211
101	Acetylation	GEMKPGRKGISLNPE CCCCCCCCCCCCCHH	67.52	26051181
101	Ubiquitination	GEMKPGRKGISLNPE CCCCCCCCCCCCCHH	67.52	-
104	Phosphorylation	KPGRKGISLNPEQWS CCCCCCCCCCHHHHH	30.66	25159151
111	Phosphorylation	SLNPEQWSQLKEQIS CCCHHHHHHHHHHHH	25.90	28464451
114	Ubiquitination	PEQWSQLKEQISDID HHHHHHHHHHHHCHH	39.68	2190698
118	Phosphorylation	SQLKEQISDIDDAVR HHHHHHHHCHHHHHH	28.36	19664994
126	Ubiquitination	DIDDAVRKL------ CHHHHHHHC------	52.53	-
126	Sumoylation	DIDDAVRKL------ CHHHHHHHC------	52.53	-

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
11	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
11	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
13	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
15	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
15	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
17	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
17	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
19	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
19	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TCP4_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 TCP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TCP4_HUMAN	SUB1	physical	9360603
PSIP1_HUMAN	PSIP1	physical	9885563
SUB1_YEAST	SUB1	physical	19706510
REST_HUMAN	REST	physical	20080105
RCOR1_HUMAN	RCOR1	physical	20080105
RPB1_HUMAN	POLR2A	physical	10024883
RPB2_HUMAN	POLR2B	physical	10024883
A4_HUMAN	APP	physical	21832049
TCP4_HUMAN	SUB1	physical	25416956
ABCF1_HUMAN	ABCF1	physical	26344197
CHD5_HUMAN	CHD5	physical	26344197
IF1AX_HUMAN	EIF1AX	physical	26344197
IF2B_HUMAN	EIF2S2	physical	26344197
IF2G_HUMAN	EIF2S3	physical	26344197
NACAM_HUMAN	NACA	physical	26344197
NACA_HUMAN	NACA	physical	26344197
NOLC1_HUMAN	NOLC1	physical	26344197
RPC3_HUMAN	POLR3C	physical	26344197
SNUT1_HUMAN	SART1	physical	26344197
SBNO1_HUMAN	SBNO1	physical	26344197
SET_HUMAN	SET	physical	26344197
SRRM2_HUMAN	SRRM2	physical	26344197
SRSF1_HUMAN	SRSF1	physical	26344197
SRSF2_HUMAN	SRSF2	physical	26344197
SRSF6_HUMAN	SRSF6	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
TPM2_HUMAN	TPM2	physical	26344197
TSR1_HUMAN	TSR1	physical	26344197
COPZ1_HUMAN	COPZ1	physical	27173435
SARNP_HUMAN	SARNP	physical	27173435
CHRD1_HUMAN	CHORDC1	physical	27173435
RRP44_HUMAN	DIS3	physical	27173435
SEPT7_HUMAN	SEPT7	physical	27173435
PRCC_HUMAN	PRCC	physical	27173435
CDK5_HUMAN	CDK5	physical	27173435
SHLB1_HUMAN	SH3GLB1	physical	27173435
SCYL2_HUMAN	SCYL2	physical	27173435
DRG1_HUMAN	DRG1	physical	27173435

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 TCP4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-68, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-104 AND SER-118, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-15; SER-17; SER-19 ANDSER-118, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-17 AND SER-19,AND MASS SPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-52; SER-56 ANDSER-58, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Gradual phosphorylation regulates PC4 coactivator function."; Jonker H.R.A., Wechselberger R.W., Pinkse M., Kaptein R.,Folkers G.E.; FEBS J. 273:1430-1444(2006). Cited for: MASS SPECTROMETRY, FUNCTION, DNA-BINDING, AND PHOSPHORYLATION ATSER-11; SER-13; SER-15; SER-17 AND SER-19.	16689930 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-10; SER-11;SER-12; SER-13; SER-15; SER-17 AND SER-19, AND MASS SPECTROMETRY.	17081983 [Abstract]
"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-17 AND SER-19, AND MASSSPECTROMETRY.	15302935 [Abstract]