dbPTM

FOXJ2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FOXJ2_HUMAN
UniProt AC	Q9P0K8
Protein Name	Forkhead box protein J2
Gene Name	FOXJ2
Organism	Homo sapiens (Human).
Sequence Length	574
Subcellular Localization	Nucleus.
Protein Description	Transcriptional activator. Able to bind to two different type of DNA binding sites. Isoform FOXJ2.L behaves as a more potent transactivator than FOXJ2.S..
Protein Sequence	MASDLESSLTSIDWLPQLTLRATIEKLGSASQAGPPGSSRKCSPGSPTDPNATLSKDEAAVHQDGKPRYSYATLITYAINSSPAKKMTLSEIYRWICDNFPYYKNAGIGWKNSIRHNLSLNKCFRKVPRPRDDPGKGSYWTIDTCPDISRKRRHPPDDDLSQDSPEQEASKSPRGGVAGSGEASLPPEGNPQMSLQSPTSIASYSQGTGSVDGGAVAAGASGRESAEGPPPLYNTNHDFKFSYSEINFQDLSWSFRNLYKSMLEKSSSSSQHGFSSLLGDIPPSNNYYMYQQQQPPPPQQQQQQQQPPQPPPQQSQPQQQQAPAQGPSAVGGAPPLHTPSTDGCTPPGGKQAGAEGYGPPPVMAMHPPPLQHGGYHPHQHHPHSHPAQQPPPPQPQAQGQAPINNTGFAFPSDWCSNIDSLKESFKMVNRLNWSSIEQSQFSELMESLRQAEQKNWTLDQHHIANLCDSLNHFLTQTGHVPPQGGTHRPPAPARIADSCALTSGKQESAMSQVNSYGHPQAPHLYPGPSPMYPIPTQDSAGYNRPAHHMVPRPSVPPPGANEEIPDDFDWDLIT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASDLESSL ------CCCHHHHHC	16.26	20068231
3	Phosphorylation	-----MASDLESSLT -----CCCHHHHHCH	41.24	25159151
7	Phosphorylation	-MASDLESSLTSIDW -CCCHHHHHCHHHHH	37.63	30108239
8	Phosphorylation	MASDLESSLTSIDWL CCCHHHHHCHHHHHH	26.70	30108239
10	Phosphorylation	SDLESSLTSIDWLPQ CHHHHHCHHHHHHHH	26.11	30108239
11	Phosphorylation	DLESSLTSIDWLPQL HHHHHCHHHHHHHHH	24.68	28464451
23	Phosphorylation	PQLTLRATIEKLGSA HHHHHHHHHHHHHCH	24.20	20068231
26	Ubiquitination	TLRATIEKLGSASQA HHHHHHHHHHCHHHC	55.06	29967540
29	Phosphorylation	ATIEKLGSASQAGPP HHHHHHHCHHHCCCC	34.87	20068231
31	Phosphorylation	IEKLGSASQAGPPGS HHHHHCHHHCCCCCC	23.43	20068231
38	Phosphorylation	SQAGPPGSSRKCSPG HHCCCCCCCCCCCCC	32.51	25159151
39	Phosphorylation	QAGPPGSSRKCSPGS HCCCCCCCCCCCCCC	41.49	26074081
43	Phosphorylation	PGSSRKCSPGSPTDP CCCCCCCCCCCCCCC	35.02	23927012
46	Phosphorylation	SRKCSPGSPTDPNAT CCCCCCCCCCCCCCC	28.19	29255136
48	Phosphorylation	KCSPGSPTDPNATLS CCCCCCCCCCCCCCC	66.83	29255136
53	Phosphorylation	SPTDPNATLSKDEAA CCCCCCCCCCHHHHH	37.90	20068231
55	Phosphorylation	TDPNATLSKDEAAVH CCCCCCCCHHHHHHC	33.43	28464451
69	Phosphorylation	HQDGKPRYSYATLIT CCCCCCCCEEEHHHH	17.98	26074081
70	Phosphorylation	QDGKPRYSYATLITY CCCCCCCEEEHHHHH	15.01	26074081
71	Phosphorylation	DGKPRYSYATLITYA CCCCCCEEEHHHHHH	8.48	26074081
73	Phosphorylation	KPRYSYATLITYAIN CCCCEEEHHHHHHHH	15.51	26074081
76	Phosphorylation	YSYATLITYAINSSP CEEEHHHHHHHHCCH	15.26	26074081
77	Phosphorylation	SYATLITYAINSSPA EEEHHHHHHHHCCHH	9.86	26074081
81	Phosphorylation	LITYAINSSPAKKMT HHHHHHHCCHHHCCC	31.42	26074081
82	Phosphorylation	ITYAINSSPAKKMTL HHHHHHCCHHHCCCH	25.12	26074081
111	Ubiquitination	KNAGIGWKNSIRHNL HCCCCCHHHHHHHHC	35.29	29967540
119	Phosphorylation	NSIRHNLSLNKCFRK HHHHHHCHHHHHCCC	34.90	21712546
122	Ubiquitination	RHNLSLNKCFRKVPR HHHCHHHHHCCCCCC	39.79	29967540
136	Ubiquitination	RPRDDPGKGSYWTID CCCCCCCCCCEEECC	50.50	29967540
138	Phosphorylation	RDDPGKGSYWTIDTC CCCCCCCCEEECCCC	22.45	20068231
149	Phosphorylation	IDTCPDISRKRRHPP CCCCCCHHHCCCCCC	38.85	20068231
161	Phosphorylation	HPPDDDLSQDSPEQE CCCCCCCCCCCHHHH	38.65	17525332
164	Phosphorylation	DDDLSQDSPEQEASK CCCCCCCCHHHHHHH	23.77	25159151
170	Phosphorylation	DSPEQEASKSPRGGV CCHHHHHHHCCCCCC	32.68	23401153
172	Phosphorylation	PEQEASKSPRGGVAG HHHHHHHCCCCCCCC	19.82	23401153
197	Phosphorylation	NPQMSLQSPTSIASY CCCCCCCCCCCCCCC	35.12	12787665
225	Phosphorylation	AGASGRESAEGPPPL CCCCCCCCCCCCCCC	30.20	28985074
252	Phosphorylation	EINFQDLSWSFRNLY ECCHHHHHHHHHHHH	29.03	27251275
254	Phosphorylation	NFQDLSWSFRNLYKS CHHHHHHHHHHHHHH	15.79	27251275
259	Phosphorylation	SWSFRNLYKSMLEKS HHHHHHHHHHHHHHC	12.45	18669648
260	Ubiquitination	WSFRNLYKSMLEKSS HHHHHHHHHHHHHCC	32.33	-
261	Phosphorylation	SFRNLYKSMLEKSSS HHHHHHHHHHHHCCC	18.29	18669648
434	Phosphorylation	MVNRLNWSSIEQSQF HHHCCCHHHHCHHHH	21.99	23090842
435	Phosphorylation	VNRLNWSSIEQSQFS HHCCCHHHHCHHHHH	23.04	28450419
439	Phosphorylation	NWSSIEQSQFSELME CHHHHCHHHHHHHHH	22.02	23090842
447	Phosphorylation	QFSELMESLRQAEQK HHHHHHHHHHHHHHH	18.19	22673903
498	Phosphorylation	APARIADSCALTSGK CCCCHHHHCCCCCCC	7.71	24719451
503	Phosphorylation	ADSCALTSGKQESAM HHHCCCCCCCHHHHH	44.86	24719451
508 (in isoform 2)	Phosphorylation	-	27.12	24043423
511 (in isoform 2)	Phosphorylation	-	30.60	24043423
514 (in isoform 2)	Phosphorylation	-	23.13	24043423
517 (in isoform 2)	Phosphorylation	-	26.31	24043423

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 FOXJ2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FOXJ2_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 FOXJ2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
EGLN3_HUMAN	EGLN3	physical	25416956
RFX1_HUMAN	RFX1	physical	25609649
QSER1_HUMAN	QSER1	physical	25609649
FOXC1_HUMAN	FOXC1	physical	25609649
HXD13_HUMAN	HOXD13	physical	25609649
CHD4_HUMAN	CHD4	physical	25609649
RFX3_HUMAN	RFX3	physical	25609649
EMSY_HUMAN	C11orf30	physical	25609649
ADNP_HUMAN	ADNP	physical	25609649
KDM5C_HUMAN	KDM5C	physical	25609649
ZMYM3_HUMAN	ZMYM3	physical	25609649
SMCA5_HUMAN	SMARCA5	physical	25609649
TRPS1_HUMAN	TRPS1	physical	25609649
GABPA_HUMAN	GABPA	physical	25609649
QRIC1_HUMAN	QRICH1	physical	25609649
WDHD1_HUMAN	WDHD1	physical	25609649
ZN148_HUMAN	ZNF148	physical	25609649
TF3C3_HUMAN	GTF3C3	physical	25609649
HXC13_HUMAN	HOXC13	physical	25609649
INT12_HUMAN	INTS12	physical	25609649
NACC1_HUMAN	NACC1	physical	25609649
RFX2_HUMAN	RFX2	physical	25609649
SLU7_HUMAN	SLU7	physical	25609649
AKAP8_HUMAN	AKAP8	physical	25609649
CUX1_HUMAN	CUX1	physical	25609649
CASP_HUMAN	CUX1	physical	25609649
DGC14_HUMAN	DGCR14	physical	25609649
P66B_HUMAN	GATAD2B	physical	25609649
TF3C1_HUMAN	GTF3C1	physical	25609649
GTSE1_HUMAN	GTSE1	physical	25609649
HDAC2_HUMAN	HDAC2	physical	25609649
HIC2_HUMAN	HIC2	physical	25609649
LIN54_HUMAN	LIN54	physical	25609649
NCOA2_HUMAN	NCOA2	physical	25609649
NFYC_HUMAN	NFYC	physical	25609649
NRF1_HUMAN	NRF1	physical	25609649
SATB2_HUMAN	SATB2	physical	25609649
SMCA1_HUMAN	SMARCA1	physical	25609649
SMC3_HUMAN	SMC3	physical	25609649
ZN131_HUMAN	ZNF131	physical	25609649
BBX_HUMAN	BBX	physical	25609649
DLX5_HUMAN	DLX5	physical	25609649
TDIF1_HUMAN	DNTTIP1	physical	25609649
EVI1_HUMAN	MECOM	physical	25609649
EYA4_HUMAN	EYA4	physical	25609649
FOXF2_HUMAN	FOXF2	physical	25609649
TF3C4_HUMAN	GTF3C4	physical	25609649
KLF16_HUMAN	KLF16	physical	25609649
LMBL2_HUMAN	L3MBTL2	physical	25609649
MD1L1_HUMAN	MAD1L1	physical	25609649
GCR_HUMAN	NR3C1	physical	25609649
PATZ1_HUMAN	PATZ1	physical	25609649
POGZ_HUMAN	POGZ	physical	25609649
PO2F2_HUMAN	POU2F2	physical	25609649
RBM22_HUMAN	RBM22	physical	25609649
RING2_HUMAN	RNF2	physical	25609649
SALL1_HUMAN	SALL1	physical	25609649
SMC1A_HUMAN	SMC1A	physical	25609649
TBP_HUMAN	TBP	physical	25609649
TCRG1_HUMAN	TCERG1	physical	25609649
TOM40_HUMAN	TOMM40	physical	25609649
TSH1_HUMAN	TSHZ1	physical	25609649
UBR5_HUMAN	UBR5	physical	25609649
USF2_HUMAN	USF2	physical	25609649
WDR55_HUMAN	WDR55	physical	25609649
TYY1_HUMAN	YY1	physical	25609649
ZBT34_HUMAN	ZBTB34	physical	25609649
ZFHX4_HUMAN	ZFHX4	physical	25609649
ZMYM2_HUMAN	ZMYM2	physical	25609649
ZMYM4_HUMAN	ZMYM4	physical	25609649
PKCB1_HUMAN	ZMYND8	physical	25609649
ZN536_HUMAN	ZNF536	physical	25609649
ZN644_HUMAN	ZNF644	physical	25609649

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 FOXJ2_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-172, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.	19413330 [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 TYR-259 AND SER-261, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.	17525332 [Abstract]