dbPTM

TFAP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFAP4_HUMAN
UniProt AC	Q01664
Protein Name	Transcription factor AP-4
Gene Name	TFAP4
Organism	Homo sapiens (Human).
Sequence Length	338
Subcellular Localization	Nucleus.
Protein Description	Transcription factor that activates both viral and cellular genes by binding to the symmetrical DNA sequence 5'-CAGCTG-3'..
Protein Sequence	MEYFMVPTQKVPSLQHFRKTEKEVIGGLCSLANIPLTPETQRDQERRIRREIANSNERRRMQSINAGFQSLKTLIPHTDGEKLSKAAILQQTAEYIFSLEQEKTRLLQQNTQLKRFIQELSGSSPKRRRAEDKDEGIGSPDIWEDEKAEDLRREMIELRQQLDKERSVRMMLEEQVRSLEAHMYPEKLKVIAQQVQLQQQQEQVRLLHQEKLEREQQQLRTQLLPPPAPTHHPTVIVPAPPPPPSHHINVVTMGPSSVINSVSTSRQNLDTIVQAIQHIEGTQEKQELEEEQRRAVIVKPVRSCPEAPTSDTASDSEASDSDAMDQSREEPSGDGELP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MEYFMVPTQK -----CCCCCCCCCC	8.83	20068231
8	Phosphorylation	MEYFMVPTQKVPSLQ CCCCCCCCCCCCCHH	29.61	20068231
10	Ubiquitination	YFMVPTQKVPSLQHF CCCCCCCCCCCHHHH	59.60	-
13	Phosphorylation	VPTQKVPSLQHFRKT CCCCCCCCHHHHHHC	43.58	20068231
13	O-linked_Glycosylation	VPTQKVPSLQHFRKT CCCCCCCCHHHHHHC	43.58	30379171
30	Phosphorylation	EVIGGLCSLANIPLT HHHHHHHHHCCCCCC	35.24	29255136
37	Phosphorylation	SLANIPLTPETQRDQ HHCCCCCCCCCHHHH	17.45	29255136
40	Phosphorylation	NIPLTPETQRDQERR CCCCCCCCHHHHHHH	30.06	29255136
54	Ubiquitination	RIRREIANSNERRRM HHHHHHHCHHHHHHH	51.54	23000965
55	Phosphorylation	IRREIANSNERRRMQ HHHHHHCHHHHHHHH	30.92	30576142
63	Phosphorylation	NERRRMQSINAGFQS HHHHHHHHHHHHHHH	14.41	28555341
70	Phosphorylation	SINAGFQSLKTLIPH HHHHHHHHHHHHCCC	29.58	24719451
78	Phosphorylation	LKTLIPHTDGEKLSK HHHHCCCCCHHHHCH	40.10	29083192
101	Ubiquitination	EYIFSLEQEKTRLLQ HHHHCHHHHHHHHHH	63.88	23000965
103	Ubiquitination	IFSLEQEKTRLLQQN HHCHHHHHHHHHHHH	38.34	29967540
114	Ubiquitination	LQQNTQLKRFIQELS HHHHHHHHHHHHHHH	35.13	23000965
121	Phosphorylation	KRFIQELSGSSPKRR HHHHHHHHCCCCCCC	35.56	30266825
123	Phosphorylation	FIQELSGSSPKRRRA HHHHHHCCCCCCCCC	39.84	29255136
124	Phosphorylation	IQELSGSSPKRRRAE HHHHHCCCCCCCCCC	37.66	19664994
126	Ubiquitination	ELSGSSPKRRRAEDK HHHCCCCCCCCCCCC	61.56	29967540
127	Ubiquitination	LSGSSPKRRRAEDKD HHCCCCCCCCCCCCC	36.38	22817900
129	Ubiquitination	GSSPKRRRAEDKDEG CCCCCCCCCCCCCCC	46.49	21890473
133	Ubiquitination	KRRRAEDKDEGIGSP CCCCCCCCCCCCCCC	49.54	29967540
139	Phosphorylation	DKDEGIGSPDIWEDE CCCCCCCCCCCCCHH	19.92	25159151
147	Ubiquitination	PDIWEDEKAEDLRRE CCCCCHHHHHHHHHH	70.20	29967540
147	Sumoylation	PDIWEDEKAEDLRRE CCCCCHHHHHHHHHH	70.20	28112733
174	Ubiquitination	SVRMMLEEQVRSLEA HHHHHHHHHHHHHHH	50.87	22817900
176	Ubiquitination	RMMLEEQVRSLEAHM HHHHHHHHHHHHHHC	5.19	21890473
187	Sumoylation	EAHMYPEKLKVIAQQ HHHCCHHHHHHHHHH	49.45	28112733
187	Acetylation	EAHMYPEKLKVIAQQ HHHCCHHHHHHHHHH	49.45	26051181
187	Ubiquitination	EAHMYPEKLKVIAQQ HHHCCHHHHHHHHHH	49.45	22817900
189	Ubiquitination	HMYPEKLKVIAQQVQ HCCHHHHHHHHHHHH	42.54	22817900
189	Sumoylation	HMYPEKLKVIAQQVQ HCCHHHHHHHHHHHH	42.54	28112733
211	Acetylation	VRLLHQEKLEREQQQ HHHHHHHHHHHHHHH	49.42	26051181
211	Ubiquitination	VRLLHQEKLEREQQQ HHHHHHHHHHHHHHH	49.42	29967540
282	Phosphorylation	AIQHIEGTQEKQELE HHHHHHCCHHHHHHH	22.29	21406692
285	Sumoylation	HIEGTQEKQELEEEQ HHHCCHHHHHHHHHH	38.97	28112733
299	Acetylation	QRRAVIVKPVRSCPE HHHCEEEECCCCCCC	27.03	25953088
299	Ubiquitination	QRRAVIVKPVRSCPE HHHCEEEECCCCCCC	27.03	-
312	Phosphorylation	PEAPTSDTASDSEAS CCCCCCCCCCCCCCC	28.03	28348404
314	Phosphorylation	APTSDTASDSEASDS CCCCCCCCCCCCCCC	43.70	28348404
316	Phosphorylation	TSDTASDSEASDSDA CCCCCCCCCCCCCHH	32.35	28348404
319	Phosphorylation	TASDSEASDSDAMDQ CCCCCCCCCCHHHHH	33.33	28348404
332	Phosphorylation	DQSREEPSGDGELP- HHCCCCCCCCCCCC-	53.44	28985074

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
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24500709

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFAP4_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 TFAP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLOCK_HUMAN	CLOCK	physical	19505873
USF2_HUMAN	USF2	physical	19505873
NFAC2_HUMAN	NFATC2	physical	19505873
TFCP2_HUMAN	TFCP2	physical	19505873
GTF2I_HUMAN	GTF2I	physical	19505873
UBIP1_HUMAN	UBP1	physical	19505873
COT1_HUMAN	NR2F1	physical	19505873
COT2_HUMAN	NR2F2	physical	19505873
NFIC_HUMAN	NFIC	physical	19505873
NR2F6_HUMAN	NR2F6	physical	19505873
PKNX1_HUMAN	PKNOX1	physical	19505873
SP1_HUMAN	SP1	physical	19505873
NFIA_HUMAN	NFIA	physical	19505873
BRCA1_HUMAN	BRCA1	physical	19505873
ZHX3_HUMAN	ZHX3	physical	19505873
ZBT7B_HUMAN	ZBTB7B	physical	19505873
SP3_HUMAN	SP3	physical	19505873
ERR1_HUMAN	ESRRA	physical	19505873
APEX1_HUMAN	APEX1	physical	19505873
TE2IP_HUMAN	TERF2IP	physical	19505873
HMGB3_HUMAN	HMGB3	physical	19505873
TOPB1_HUMAN	TOPBP1	physical	19505873
MDC1_HUMAN	MDC1	physical	19505873
HMGB2_HUMAN	HMGB2	physical	19505873
DPOE2_HUMAN	POLE2	physical	19505873
HMGB1_HUMAN	HMGB1	physical	19505873
PCNA_HUMAN	PCNA	physical	19505873
PARP2_HUMAN	PARP2	physical	19505873
TERF2_HUMAN	TERF2	physical	19505873
RAD50_HUMAN	RAD50	physical	19505873
ZBT7A_HUMAN	ZBTB7A	physical	19505873
CTBP1_HUMAN	CTBP1	physical	19505873
WIZ_HUMAN	WIZ	physical	19505873
CTCF_HUMAN	CTCF	physical	19505873
TF2L1_HUMAN	TFCP2L1	physical	19505873
SIN3B_HUMAN	SIN3B	physical	19505873
MBD2_HUMAN	MBD2	physical	19505873
SNF5_HUMAN	SMARCB1	physical	19505873
ARI1A_HUMAN	ARID1A	physical	19505873
SMRC2_HUMAN	SMARCC2	physical	19505873
SMCE1_HUMAN	SMARCE1	physical	19505873
ARID2_HUMAN	ARID2	physical	19505873
EHMT1_HUMAN	EHMT1	physical	19505873
EHMT2_HUMAN	EHMT2	physical	19505873
SP130_HUMAN	SAP130	physical	19505873
HDAC1_HUMAN	HDAC1	physical	19505873
HDAC2_HUMAN	HDAC2	physical	19505873
TTF2_HUMAN	TTF2	physical	19505873
BTAF1_HUMAN	BTAF1	physical	19505873
TDIF1_HUMAN	DNTTIP1	physical	19505873
VRK1_HUMAN	VRK1	physical	19505873
ZN462_HUMAN	ZNF462	physical	19505873
BRD7_HUMAN	BRD7	physical	19505873
HPF1_HUMAN	C4orf27	physical	19505873
CHRC1_HUMAN	CHRAC1	physical	19505873
YETS2_HUMAN	YEATS2	physical	19505873
ZZZ3_HUMAN	ZZZ3	physical	19505873
S10A8_HUMAN	S100A8	physical	19505873
EMSA1_HUMAN	ELMSAN1	physical	19505873
ZN335_HUMAN	ZNF335	physical	19505873
UHRF2_HUMAN	UHRF2	physical	19505873
PRD16_HUMAN	PRDM16	physical	19505873
IN80E_HUMAN	INO80E	physical	19505873
PP6R3_HUMAN	PPP6R3	physical	19505873
RAN_HUMAN	RAN	physical	19505873
THYN1_HUMAN	THYN1	physical	19505873
CABIN_HUMAN	CABIN1	physical	19505873
CKAP5_HUMAN	CKAP5	physical	19505873
NAV3_HUMAN	NAV3	physical	19505873
NGEF_HUMAN	NGEF	physical	19505873
DX39B_HUMAN	DDX39B	physical	19505873
MTA3_HUMAN	MTA3	physical	19505873
SOGA3_HUMAN	SOGA3	physical	19505873
P53_HUMAN	TP53	physical	19505873
FBW1B_HUMAN	FBXW11	physical	24500709
FBW1A_HUMAN	BTRC	physical	24500709
SKP1_HUMAN	SKP1	physical	24500709
CUL1_HUMAN	CUL1	physical	24500709
TRAF1_HUMAN	TRAF1	physical	25416956
EXOS8_HUMAN	EXOSC8	physical	25416956
U520_HUMAN	SNRNP200	physical	26344197
FBW1A_HUMAN	BTRC	physical	28514442
ATS4_HUMAN	ADAMTS4	physical	28514442
ANGL7_HUMAN	ANGPTL7	physical	28514442
HIRA_HUMAN	HIRA	physical	28514442
FBW1B_HUMAN	FBXW11	physical	28514442
STN1_HUMAN	OBFC1	physical	28514442
CABIN_HUMAN	CABIN1	physical	28514442
UBN2_HUMAN	UBN2	physical	28514442
FOXK2_HUMAN	FOXK2	physical	28514442
TRIB2_HUMAN	TRIB2	physical	28514442
CTC1_HUMAN	CTC1	physical	28514442
FOXK1_HUMAN	FOXK1	physical	28514442
WIPI3_HUMAN	WDR45B	physical	28514442
ARRB2_HUMAN	ARRB2	physical	28514442
KCTD2_HUMAN	KCTD2	physical	28514442
ATF1_HUMAN	ATF1	physical	28514442
SIN3A_HUMAN	SIN3A	physical	28514442
GBB4_HUMAN	GNB4	physical	28514442

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 TFAP4_HUMAN

Related Literatures of Post-Translational Modification

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-124, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.	19369195 [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-124, AND MASSSPECTROMETRY.	18669648 [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-124, AND MASSSPECTROMETRY.	17287340 [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-124 AND SER-139, ANDMASS 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-124, AND MASSSPECTROMETRY.	15302935 [Abstract]