dbPTM

FOS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FOS_HUMAN
UniProt AC	P01100
Protein Name	Proto-oncogene c-Fos
Gene Name	FOS
Organism	Homo sapiens (Human).
Sequence Length	380
Subcellular Localization	Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the
Protein Description	Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum..
Protein Sequence	MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	FSGFNADYEASSSRC CCCCCCCCCCCCCCC	15.81	17160021
30	Phosphorylation	AGDSLSYYHSPADSF CCCCCEECCCCCHHC	7.76	17160021
32	Phosphorylation	DSLSYYHSPADSFSS CCCEECCCCCHHCCC	12.98	22817900
56	O-linked_Glycosylation	FCTDLAVSSANFIPT HHHHHHHHHCCCCCE	20.37	15327282
57	O-linked_Glycosylation	CTDLAVSSANFIPTV HHHHHHHHCCCCCEE	22.19	15327282
83	O-linked_Glycosylation	LVQPALVSSVAPSQT HHCHHHHCCCCCCCC	21.68	15327282
84	O-linked_Glycosylation	VQPALVSSVAPSQTR HCHHHHCCCCCCCCC	18.15	15327282
88	O-linked_Glycosylation	LVSSVAPSQTRAPHP HHCCCCCCCCCCCCC	34.15	15327282
90	O-linked_Glycosylation	SSVAPSQTRAPHPFG CCCCCCCCCCCCCCC	32.89	15327282
102	Phosphorylation	PFGVPAPSAGAYSRA CCCCCCCCCCCCCCC	41.25	28555341
113	Acetylation	YSRAGVVKTMTGGRA CCCCCEEEECCCCCH	30.12	26051181
113	Sumoylation	YSRAGVVKTMTGGRA CCCCCEEEECCCCCH	30.12	28112733
113	Sumoylation	YSRAGVVKTMTGGRA CCCCCEEEECCCCCH	30.12	-
113	Ubiquitination	YSRAGVVKTMTGGRA CCCCCEEEECCCCCH	30.12	17203973
114	Phosphorylation	SRAGVVKTMTGGRAQ CCCCEEEECCCCCHH	14.35	20068231
116	Phosphorylation	AGVVKTMTGGRAQSI CCEEEECCCCCHHHC	41.54	20068231
122	Phosphorylation	MTGGRAQSIGRRGKV CCCCCHHHCCCCCCH	26.48	24719451
128	Sumoylation	QSIGRRGKVEQLSPE HHCCCCCCHHHCCHH	40.56	28112733
128	Sumoylation	QSIGRRGKVEQLSPE HHCCCCCCHHHCCHH	40.56	-
133	Phosphorylation	RGKVEQLSPEEEEKR CCCHHHCCHHHHHHH	29.93	21815630
139	Sumoylation	LSPEEEEKRRIRRER CCHHHHHHHHHHHHH	50.70	-
139	Sumoylation	LSPEEEEKRRIRRER CCHHHHHHHHHHHHH	50.70	-
176	Sumoylation	TDQLEDEKSALQTEI HHHHHHHHHHHHHHH	54.04	-
176	Sumoylation	TDQLEDEKSALQTEI HHHHHHHHHHHHHHH	54.04	-
188	Ubiquitination	TEIANLLKEKEKLEF HHHHHHHHHHHHHHH	70.66	-
232	Phosphorylation	GGLPEVATPESEEAF CCCCCCCCCCCCCCC	32.53	16055710
258	Phosphorylation	PSVEPVKSISSMELK CCCCCCCCCCCCCCC	28.12	23312004
260	Phosphorylation	VEPVKSISSMELKTE CCCCCCCCCCCCCCC	30.62	23312004
261	Phosphorylation	EPVKSISSMELKTEP CCCCCCCCCCCCCCC	18.01	23312004
265	Sumoylation	SISSMELKTEPFDDF CCCCCCCCCCCCCCC	37.22	-
265	Sumoylation	SISSMELKTEPFDDF CCCCCCCCCCCCCCC	37.22	28112733
266	Phosphorylation	ISSMELKTEPFDDFL CCCCCCCCCCCCCCC	62.61	23312004
277	Phosphorylation	DDFLFPASSRPSGSE CCCCCCCCCCCCCCC	27.41	23312004
278	O-linked_Glycosylation	DFLFPASSRPSGSET CCCCCCCCCCCCCCC	50.76	15327282
278	Phosphorylation	DFLFPASSRPSGSET CCCCCCCCCCCCCCC	50.76	21712546
281	Phosphorylation	FPASSRPSGSETARS CCCCCCCCCCCCCCC	54.57	23312004
283	Phosphorylation	ASSRPSGSETARSVP CCCCCCCCCCCCCCC	35.79	23312004
283	O-linked_Glycosylation	ASSRPSGSETARSVP CCCCCCCCCCCCCCC	35.79	15327282
285	Phosphorylation	SRPSGSETARSVPDM CCCCCCCCCCCCCCC	29.12	23312004
308	Phosphorylation	ADWEPLHSGSLGMGP CCCCCCCCCCCCCCC	37.45	19285436
325	Phosphorylation	TELEPLCTPVVTCTP CCCCCCCCCEEEECC	27.14	12134156
331	Phosphorylation	CTPVVTCTPSCTAYT CCCEEEECCCCEEEC	14.63	12134156
362	Phosphorylation	AAAHRKGSSSNEPSS HHHHHCCCCCCCCCC	33.36	21712546
363	Phosphorylation	AAHRKGSSSNEPSSD HHHHCCCCCCCCCCC	45.94	28450419
364	Phosphorylation	AHRKGSSSNEPSSDS HHHCCCCCCCCCCCC	47.08	28450419
368	Phosphorylation	GSSSNEPSSDSLSSP CCCCCCCCCCCCCCC	40.37	28450419
369	Phosphorylation	SSSNEPSSDSLSSPT CCCCCCCCCCCCCCC	41.77	28450419
371	Phosphorylation	SNEPSSDSLSSPTLL CCCCCCCCCCCCCEE	31.90	28450419
373	Phosphorylation	EPSSDSLSSPTLLAL CCCCCCCCCCCEECC	37.92	22199227
374	Phosphorylation	PSSDSLSSPTLLAL- CCCCCCCCCCEECC-	27.48	12134156
376	Phosphorylation	SDSLSSPTLLAL--- CCCCCCCCEECC---	36.03	22199227

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
10	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
30	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
32	S	Phosphorylation	Kinase	MAPK7	Q13164	GPS
232	T	Phosphorylation	Kinase	MAPK7	Q13164	GPS
232	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
232	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
308	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
325	T	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
325	T	Phosphorylation	Kinase	MK03	P27361	PhosphoELM
331	T	Phosphorylation	Kinase	MK03	P27361	PhosphoELM
331	T	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
362	S	Phosphorylation	Kinase	RSK2	-	PSP
362	S	Phosphorylation	Kinase	MAPK3	P27361	Uniprot
362	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
362	S	Phosphorylation	Kinase	KS6A3	P51812	PhosphoELM
362	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
362	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
362	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
362	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
374	S	Phosphorylation	Kinase	ERK1	P27361	PSP
374	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
374	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
374	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	KDM2B	Q8NHM5	PMID:26725323

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
232	T	Phosphorylation	-
Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation.
232	T	Phosphorylation	16055710
Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232.
232	T	Sumoylation	-
Phosphorylation on Thr-232, induced by HA-RAS, activates the transcriptional activity and antagonizes sumoylation.
232	T	Sumoylation	16055710
Sumoylation inhibits the AP-1 transcriptional activity and is, itself, inhibited by Ras-activated phosphorylation on Thr-232.
325	T	Phosphorylation	12134156
Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain.
331	T	Phosphorylation	12134156
Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain.
362	S	Phosphorylation	7588633
Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain.
362	S	Phosphorylation	7588633
Phosphorylation on Ser-362 by RSK2 in osteoblasts contributes to osteoblast transformation (By similarity).
362	S	Phosphorylation	7588633
Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation.
374	S	Phosphorylation	7588633
Phosphorylation on Ser-362 and Ser-374 primes further phosphorylations on Thr-325 and Thr-331 through promoting docking of MAPK to the DEF domain.
374	S	Phosphorylation	7588633
Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the major site for protein stabilization on NGF stimulation.

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 FOS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JUN_HUMAN	JUN	physical	11053448
BCL3_HUMAN	BCL3	physical	10497212
CSK21_HUMAN	CSNK2A1	physical	9685505
JUN_HUMAN	JUN	physical	9160889
T2EB_HUMAN	GTF2E2	physical	8628277
T2FB_HUMAN	GTF2F2	physical	8628277
T2FA_HUMAN	GTF2F1	physical	8628277
JUN_HUMAN	JUN	physical	8380166
JUN_HUMAN	JUN	physical	9872330
NCOR2_HUMAN	NCOR2	physical	10777532
NCOA1_HUMAN	NCOA1	physical	9642216
JUND_HUMAN	JUND	physical	11431474
MK01_HUMAN	MAPK1	physical	11431474
JUN_HUMAN	JUN	physical	16714286
DDX17_HUMAN	DDX17	physical	17226766
KDM2A_HUMAN	KDM2A	physical	20936779
NCOA1_HUMAN	NCOA1	physical	18511550
NCOA2_HUMAN	NCOA2	physical	18511550
NCOA3_HUMAN	NCOA3	physical	18511550
CARM1_HUMAN	CARM1	physical	18511550
ESR1_HUMAN	ESR1	physical	17317669
JUN_HUMAN	JUN	physical	20410304
UBR1_HUMAN	UBR1	physical	17018293
MAF_HUMAN	MAF	physical	21163924
JUN_HUMAN	JUN	physical	16055710
SMAD3_HUMAN	SMAD3	physical	21829441
RB_HUMAN	RB1	physical	9545246
SRA1_HUMAN	SRA1	physical	20398657
EP300_HUMAN	EP300	physical	19064921
TCL1A_HUMAN	TCL1A	physical	19064921
MAFB_HUMAN	MAFB	physical	23661758
ATF3_HUMAN	ATF3	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
FOS_HUMAN	FOS	physical	23661758
JUNB_HUMAN	JUNB	physical	23661758
ATF2_HUMAN	ATF2	physical	23661758
CEBPA_HUMAN	CEBPA	physical	23661758
JUN_HUMAN	JUN	physical	22719067
TSN2_HUMAN	TSPAN2	physical	21988832
GRHPR_HUMAN	GRHPR	physical	21988832
GAMT_HUMAN	GAMT	physical	21988832
BGAL_HUMAN	GLB1	physical	21988832
JUN_HUMAN	JUN	physical	15994313
JUN_HUMAN	JUN	physical	23602568
ZN133_HUMAN	ZNF133	physical	20195357
ATF2_HUMAN	ATF2	physical	20195357
CLUS_HUMAN	CLU	physical	20195357
A4_HUMAN	APP	physical	20195357
JUND_HUMAN	JUND	physical	20195357
CSN4_HUMAN	COPS4	physical	20195357
JUN_HUMAN	JUN	physical	20195357
MAP1B_HUMAN	MAP1B	physical	20195357
CABP1_HUMAN	CABP1	physical	20195357
AR6P4_HUMAN	ARL6IP4	physical	20195357
MTEF4_HUMAN	MTERF4	physical	20195357
SET_HUMAN	SET	physical	20195357
AN32E_HUMAN	ANP32E	physical	20195357
NFM_HUMAN	NEFM	physical	20195357
ATP5I_HUMAN	ATP5I	physical	20195357
JUN_HUMAN	JUN	physical	16928824
JUN_HUMAN	JUN	physical	16008525
NQO1_HUMAN	NQO1	physical	20498278
JUN_HUMAN	JUN	physical	20498278
GBG11_HUMAN	GNG11	physical	25416956
JUNB_HUMAN	JUNB	physical	25416956
AAPK2_HUMAN	PRKAA2	physical	25416956
PRS8_HUMAN	PSMC5	physical	25416956
USF1_HUMAN	USF1	physical	25416956
USF2_HUMAN	USF2	physical	25416956
CREB5_HUMAN	CREB5	physical	25416956
CYH4_HUMAN	CYTH4	physical	25416956
LUZP4_HUMAN	LUZP4	physical	25416956
ARFG1_HUMAN	ARFGAP1	physical	25416956
LMO3_HUMAN	LMO3	physical	25416956
CENPO_HUMAN	CENPO	physical	25416956
JUN_HUMAN	JUN	physical	18848838
ATF2_HUMAN	ATF2	physical	26186194
ATF7_HUMAN	ATF7	physical	26186194
CREB5_HUMAN	CREB5	physical	26186194
STK40_HUMAN	STK40	physical	26186194
JUN_HUMAN	JUN	physical	26186194
JUNB_HUMAN	JUNB	physical	26186194
JUND_HUMAN	JUND	physical	26186194
SYVC_HUMAN	VARS	physical	26186194
RFWD2_HUMAN	RFWD2	physical	26186194
YETS4_HUMAN	YEATS4	physical	26186194
DET1_HUMAN	DET1	physical	26186194
DHB4_HUMAN	HSD17B4	physical	26496610
JUN_HUMAN	JUN	physical	26496610
JUNB_HUMAN	JUNB	physical	26496610
JUND_HUMAN	JUND	physical	26496610
MED17_HUMAN	MED17	physical	26496610
FBP1L_HUMAN	FNBP1L	physical	26496610
RFWD2_HUMAN	RFWD2	physical	26496610
UTP4_HUMAN	CIRH1A	physical	26496610
JUN_HUMAN	JUN	physical	25609649
JUND_HUMAN	JUND	physical	25609649
JUNB_HUMAN	JUNB	physical	25609649
ATF7_HUMAN	ATF7	physical	25609649
EF1D_HUMAN	EEF1D	physical	25609649
HXD13_HUMAN	HOXD13	physical	25609649
ATF2_HUMAN	ATF2	physical	25609649
SYVC_HUMAN	VARS	physical	25609649
SAHH_HUMAN	AHCY	physical	25609649
ANKH1_HUMAN	ANKHD1	physical	25609649
FP100_HUMAN	C17orf70	physical	25609649
LGUL_HUMAN	GLO1	physical	25609649
RFWD2_HUMAN	RFWD2	physical	25609649
STK40_HUMAN	STK40	physical	25609649
TRIB1_HUMAN	TRIB1	physical	25609649
NFAC1_HUMAN	NFATC1	physical	25609649
SMCE1_HUMAN	SMARCE1	physical	25609649
NFIX_HUMAN	NFIX	physical	25609649
COT1_HUMAN	NR2F1	physical	25609649
NR2F6_HUMAN	NR2F6	physical	25609649
SMRC1_HUMAN	SMARCC1	physical	25609649
SMRC2_HUMAN	SMARCC2	physical	25609649
YETS4_HUMAN	YEATS4	physical	25609649
CHK2_HUMAN	CHEK2	physical	25609649
ANR17_HUMAN	ANKRD17	physical	25609649
MTMR1_HUMAN	MTMR1	physical	25609649
KBTB7_HUMAN	KBTBD7	physical	25609649
MYPT1_HUMAN	PPP1R12A	physical	25609649
SSU72_HUMAN	SSU72	physical	25609649
TPC13_HUMAN	TRAPPC13	physical	25609649
CENPO_HUMAN	CENPO	physical	25609649
FOSB_HUMAN	FOSB	physical	25609649
FUBP2_HUMAN	KHSRP	physical	25609649
MK09_HUMAN	MAPK9	physical	25609649
NF2IP_HUMAN	NFATC2IP	physical	25609649
KDM2B_HUMAN	KDM2B	physical	26725323
CBP_HUMAN	CREBBP	physical	10487758
EP300_HUMAN	EP300	physical	11287611
NFAT5_HUMAN	NFAT5	physical	18056707
JUNB_HUMAN	JUNB	physical	28514442
ATF2_HUMAN	ATF2	physical	28514442
ATF7_HUMAN	ATF7	physical	28514442
JUND_HUMAN	JUND	physical	28514442
CREB5_HUMAN	CREB5	physical	28514442
JUN_HUMAN	JUN	physical	28514442
STK40_HUMAN	STK40	physical	28514442
DET1_HUMAN	DET1	physical	28514442
RFWD2_HUMAN	RFWD2	physical	28514442
SYVC_HUMAN	VARS	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
DB08813	Nadroparin
DB00852	Pseudoephedrine

Regulatory Network of FOS_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Molecular interpretation of ERK signal duration by immediate earlygene products."; Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.; Nat. Cell Biol. 4:556-564(2002). Cited for: PHOSPHORYLATION AT THR-325; THR-331 AND SER-374.	12134156 [Abstract]
"The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation andaugments its transforming activity in NIH 3T3 cells."; Okazaki K., Sagata N.; EMBO J. 14:5048-5059(1995). Cited for: PHOSPHORYLATION AT SER-362 AND SER-374, FUNCTION, AND MUTAGENESIS OFSER-362 AND SER-374.	7588633 [Abstract]
Ubiquitylation
Reference	PubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells."; Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.; J. Proteome Res. 6:298-305(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-113, AND MASSSPECTROMETRY.	17203973 [Abstract]

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