dbPTM

FOSL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FOSL2_HUMAN
UniProt AC	P15408
Protein Name	Fos-related antigen 2
Gene Name	FOSL2
Organism	Homo sapiens (Human).
Sequence Length	326
Subcellular Localization	Nucleus.
Protein Description	Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts..
Protein Sequence	MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKAQRSVIKPISIAGGFYGEEPLHTPIVVTSTPAVTPGTSNLVFTYPSVLEQESPASPSESCSKAHRRSSSSGDQSSDSLNSPTLLAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MYQDYPGN -------CCCCCCCC	6.47	22814378
2	Phosphorylation	------MYQDYPGNF ------CCCCCCCCC	15.30	23401153
5	Phosphorylation	---MYQDYPGNFDTS ---CCCCCCCCCCCC	9.49	23401153
11	Phosphorylation	DYPGNFDTSSRGSSG CCCCCCCCCCCCCCC	25.19	23401153
12	Phosphorylation	YPGNFDTSSRGSSGS CCCCCCCCCCCCCCC	21.63	23401153
13	Phosphorylation	PGNFDTSSRGSSGSP CCCCCCCCCCCCCCC	42.63	23401153
16	Phosphorylation	FDTSSRGSSGSPAHA CCCCCCCCCCCCCCC	30.34	22167270
17	Phosphorylation	DTSSRGSSGSPAHAE CCCCCCCCCCCCCCC	46.22	22167270
19	Phosphorylation	SSRGSSGSPAHAESY CCCCCCCCCCCCCCC	22.36	22167270
25	Phosphorylation	GSPAHAESYSSGGGG CCCCCCCCCCCCCCC	30.97	22167270
26	Phosphorylation	SPAHAESYSSGGGGQ CCCCCCCCCCCCCCC	9.81	23927012
27	Phosphorylation	PAHAESYSSGGGGQQ CCCCCCCCCCCCCCE	31.61	23403867
28	Phosphorylation	AHAESYSSGGGGQQK CCCCCCCCCCCCCEE	32.97	23403867
35	Ubiquitination	SGGGGQQKFRVDMPG CCCCCCEEEEEECCC	27.53	-
35	Sumoylation	SGGGGQQKFRVDMPG CCCCCCEEEEEECCC	27.53	28112733
55	O-linked_Glycosylation	IPTINAITTSQDLQW ECEEEEEECCCCHHH	20.27	29485866
56	O-linked_Glycosylation	PTINAITTSQDLQWM CEEEEEECCCCHHHH	20.48	29485866
57	O-linked_Glycosylation	TINAITTSQDLQWMV EEEEEECCCCHHHHH	17.04	29485866
67	O-linked_Glycosylation	LQWMVQPTVITSMSN HHHHHCCEEEECCCC	13.88	29485866
79	Phosphorylation	MSNPYPRSHPYSPLP CCCCCCCCCCCCCCC	25.06	27794612
82	Phosphorylation	PYPRSHPYSPLPGLA CCCCCCCCCCCCCCC	19.93	24732914
83	Phosphorylation	YPRSHPYSPLPGLAS CCCCCCCCCCCCCCC	25.14	25159151
90	Phosphorylation	SPLPGLASVPGHMAL CCCCCCCCCCCCCCC	33.61	24732914
104	Ubiquitination	LPRPGVIKTIGTTVG CCCCCCEEECCCHHC	31.51	-
104	Acetylation	LPRPGVIKTIGTTVG CCCCCCEEECCCHHC	31.51	23236377
104	Methylation	LPRPGVIKTIGTTVG CCCCCCEEECCCHHC	31.51	-
104	"N6,N6-dimethyllysine"	LPRPGVIKTIGTTVG CCCCCCEEECCCHHC	31.51	-
104	Sumoylation	LPRPGVIKTIGTTVG CCCCCCEEECCCHHC	31.51	28112733
120	Phosphorylation	RRRDEQLSPEEEEKR CHHCCCCCHHHHHHH	29.93	23401153
151	Acetylation	RRRELTEKLQAETEE HHHHHHHHHHHHHHH	40.44	26051181
151	Ubiquitination	RRRELTEKLQAETEE HHHHHHHHHHHHHHH	40.44	-
163	Acetylation	TEELEEEKSGLQKEI HHHHHHHHHHHHHHH	53.77	26051181
168	Ubiquitination	EEKSGLQKEIAELQK HHHHHHHHHHHHHHH	57.01	-
194	Phosphorylation	HGPVCKISPEERRSP CCCEEECCHHHHCCC	16.26	28355574
200	Phosphorylation	ISPEERRSPPAPGLQ CCHHHHCCCCCCCCC	41.26	29255136
211	Phosphorylation	PGLQPMRSGGGSVGA CCCCCCCCCCCCEEE	35.22	30266825
215	Phosphorylation	PMRSGGGSVGAVVVK CCCCCCCCEEEEEEE	22.20	23927012
222	Sumoylation	SVGAVVVKQEPLEED CEEEEEEECCCCCCC	37.02	25114211
222	Sumoylation	SVGAVVVKQEPLEED CEEEEEEECCCCCCC	37.02	-
222	Acetylation	SVGAVVVKQEPLEED CEEEEEEECCCCCCC	37.02	23236377
230	Phosphorylation	QEPLEEDSPSSSSAG CCCCCCCCCCCCCCC	29.93	22167270
232	Phosphorylation	PLEEDSPSSSSAGLD CCCCCCCCCCCCCCC	46.97	22167270
233	Phosphorylation	LEEDSPSSSSAGLDK CCCCCCCCCCCCCCH	31.53	22167270
234	Phosphorylation	EEDSPSSSSAGLDKA CCCCCCCCCCCCCHH	28.66	22167270
235	Phosphorylation	EDSPSSSSAGLDKAQ CCCCCCCCCCCCHHH	28.44	22167270
240	Acetylation	SSSAGLDKAQRSVIK CCCCCCCHHHHHCCC	52.00	26051181
240	Ubiquitination	SSSAGLDKAQRSVIK CCCCCCCHHHHHCCC	52.00	-
240	Sumoylation	SSSAGLDKAQRSVIK CCCCCCCHHHHHCCC	52.00	28112733
263	O-linked_Glycosylation	YGEEPLHTPIVVTST CCCCCCCCCEEEECC	23.53	29485866
269	O-linked_Glycosylation	HTPIVVTSTPAVTPG CCCEEEECCCCCCCC	22.30	29485866
270	O-linked_Glycosylation	TPIVVTSTPAVTPGT CCEEEECCCCCCCCC	13.10	29485866
292	Phosphorylation	PSVLEQESPASPSES HHHHCCCCCCCCCHH	26.01	25137130
295	Phosphorylation	LEQESPASPSESCSK HCCCCCCCCCHHHHH	32.13	26657352
307	Phosphorylation	CSKAHRRSSSSGDQS HHHHHHHCCCCCCCC	34.23	30266825
308	Phosphorylation	SKAHRRSSSSGDQSS HHHHHHCCCCCCCCC	27.06	30266825
309	Phosphorylation	KAHRRSSSSGDQSSD HHHHHCCCCCCCCCC	39.32	30266825
310	Phosphorylation	AHRRSSSSGDQSSDS HHHHCCCCCCCCCCC	48.62	30266825
314	Phosphorylation	SSSSGDQSSDSLNSP CCCCCCCCCCCCCCC	40.63	22167270
315	Phosphorylation	SSSGDQSSDSLNSPT CCCCCCCCCCCCCCC	26.11	22167270
317	Phosphorylation	SGDQSSDSLNSPTLL CCCCCCCCCCCCCEE	31.25	30266825
320	Phosphorylation	QSSDSLNSPTLLAL- CCCCCCCCCCEECC-	25.26	30266825
322	Phosphorylation	SDSLNSPTLLAL--- CCCCCCCCEECC---	33.94	30266825

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	MAP3K1	Q13233	PMID:15558021

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FOSL2_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 FOSL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JUN_HUMAN	JUN	physical	9160889
SRA1_HUMAN	SRA1	physical	20398657
JUNB_HUMAN	JUNB	physical	19321746
TRAF1_HUMAN	TRAF1	physical	25416956
DNJA3_HUMAN	DNAJA3	physical	25416956
CREB5_HUMAN	CREB5	physical	25416956
LUZP4_HUMAN	LUZP4	physical	25416956
GOPC_HUMAN	GOPC	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
ATF2_HUMAN	ATF2	physical	26186194
ATF7_HUMAN	ATF7	physical	26186194
CREB5_HUMAN	CREB5	physical	26186194
JUN_HUMAN	JUN	physical	26186194
JUNB_HUMAN	JUNB	physical	26186194
JUND_HUMAN	JUND	physical	26186194
SORL_HUMAN	SORL1	physical	26186194
ZZEF1_HUMAN	ZZEF1	physical	26186194
CARM1_HUMAN	CARM1	physical	26186194
CACO1_HUMAN	CALCOCO1	physical	26186194
SYVC_HUMAN	VARS	physical	26186194
HECD3_HUMAN	HECTD3	physical	26186194
ANKH1_HUMAN	ANKHD1	physical	26186194
ANR17_HUMAN	ANKRD17	physical	26186194
I2BP2_HUMAN	IRF2BP2	physical	26186194
CYH2_HUMAN	CYTH2	physical	26186194
CYH3_HUMAN	CYTH3	physical	26186194
RFWD2_HUMAN	RFWD2	physical	26186194
KBTB7_HUMAN	KBTBD7	physical	26186194
KBTB6_HUMAN	KBTBD6	physical	26186194
TSR3_HUMAN	TSR3	physical	26186194
NBEA_HUMAN	NBEA	physical	26186194
EF1D_HUMAN	EEF1D	physical	26186194
FBX11_HUMAN	FBXO11	physical	26186194
BACH2_HUMAN	BACH2	physical	26186194
YETS4_HUMAN	YEATS4	physical	26186194
STK40_HUMAN	STK40	physical	26186194
RUFY1_HUMAN	RUFY1	physical	26186194
I2BP1_HUMAN	IRF2BP1	physical	26186194
DET1_HUMAN	DET1	physical	26186194
ANM6_HUMAN	PRMT6	physical	26186194
TRIB1_HUMAN	TRIB1	physical	26186194
I2BPL_HUMAN	IRF2BPL	physical	26186194
JUN_HUMAN	JUN	physical	26496610
JUNB_HUMAN	JUNB	physical	26496610
JUND_HUMAN	JUND	physical	26496610
STMN1_HUMAN	STMN1	physical	26496610
RL21_HUMAN	RPL21	physical	26496610
RL30_HUMAN	RPL30	physical	26496610
SPAST_HUMAN	SPAST	physical	26496610
RL14_HUMAN	RPL14	physical	26496610
RECQ5_HUMAN	RECQL5	physical	26496610
MED16_HUMAN	MED16	physical	26496610
ATF7_HUMAN	ATF7	physical	26496610
RFWD2_HUMAN	RFWD2	physical	26496610
MET17_HUMAN	METTL17	physical	26496610
DPY30_HUMAN	DPY30	physical	26496610
LSM11_HUMAN	LSM11	physical	26496610
JUND_HUMAN	JUND	physical	28514442
ATF7_HUMAN	ATF7	physical	28514442
ATF2_HUMAN	ATF2	physical	28514442
CREB5_HUMAN	CREB5	physical	28514442
BACH2_HUMAN	BACH2	physical	28514442
JUN_HUMAN	JUN	physical	28514442
NBEA_HUMAN	NBEA	physical	28514442
I2BPL_HUMAN	IRF2BPL	physical	28514442
I2BP1_HUMAN	IRF2BP1	physical	28514442
TRIB1_HUMAN	TRIB1	physical	28514442
SORL_HUMAN	SORL1	physical	28514442
RFWD2_HUMAN	RFWD2	physical	28514442
KBTB7_HUMAN	KBTBD7	physical	28514442
STK40_HUMAN	STK40	physical	28514442
CYH3_HUMAN	CYTH3	physical	28514442
USF2_HUMAN	USF2	physical	28514442
CYH2_HUMAN	CYTH2	physical	28514442
YETS4_HUMAN	YEATS4	physical	28514442
CACO1_HUMAN	CALCOCO1	physical	28514442
DET1_HUMAN	DET1	physical	28514442
I2BP2_HUMAN	IRF2BP2	physical	28514442
ZZEF1_HUMAN	ZZEF1	physical	28514442
ANKH1_HUMAN	ANKHD1	physical	28514442
TSR3_HUMAN	TSR3	physical	28514442
SYVC_HUMAN	VARS	physical	28514442
ANR17_HUMAN	ANKRD17	physical	28514442
HECD3_HUMAN	HECTD3	physical	28514442
BAHC1_HUMAN	BAHCC1	physical	28514442
RUFY1_HUMAN	RUFY1	physical	28514442
CARM1_HUMAN	CARM1	physical	28514442
FBX11_HUMAN	FBXO11	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 FOSL2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-200; SER-211; SER-215AND SER-230, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	18220336 [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-83; SER-120; SER-200;SER-230; SER-308 AND SER-320, 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-200 AND SER-230, ANDMASS SPECTROMETRY.	15302935 [Abstract]