dbPTM

FHL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FHL2_HUMAN
UniProt AC	Q14192
Protein Name	Four and a half LIM domains protein 2
Gene Name	FHL2
Organism	Homo sapiens (Human).
Sequence Length	279
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line .
Protein Description	May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation. Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes. [PubMed: 28717008]
Protein Sequence	MTERFDCHHCNESLFGKKYILREESPYCVVCFETLFANTCEECGKPIGCDCKDLSYKDRHWHEACFHCSQCRNSLVDKPFAAKEDQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFICHRCQQPIGTKSFIPKDNQNFCVPCYEKQHAMQCVQCKKPITTGGVTYREQPWHKECFVCTACRKQLSGQRFTARDDFAYCLNCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTERFDCHH ------CCCCCCCCC	35.55	19413330
13	Phosphorylation	DCHHCNESLFGKKYI CCCCCCHHHCCCEEE	18.27	29214152
17	Ubiquitination	CNESLFGKKYILREE CCHHHCCCEEEECCC	34.76	-
17	Acetylation	CNESLFGKKYILREE CCHHHCCCEEEECCC	34.76	26051181
27	Phosphorylation	ILREESPYCVVCFET EECCCCCCEEEEEEE	13.73	-
56	Phosphorylation	CDCKDLSYKDRHWHE CCCCCCCCCCCCHHH	24.97	-
57	Acetylation	DCKDLSYKDRHWHEA CCCCCCCCCCCHHHH	44.93	30588785
74	Phosphorylation	HCSQCRNSLVDKPFA HHHHHHHHHCCCCCC	15.49	26657352
78	Acetylation	CRNSLVDKPFAAKED HHHHHCCCCCCCCCC	34.26	26051181
78	Sumoylation	CRNSLVDKPFAAKED HHHHHCCCCCCCCCC	34.26	-
78	Sumoylation	CRNSLVDKPFAAKED HHHHHCCCCCCCCCC	34.26	25218447
78	Ubiquitination	CRNSLVDKPFAAKED HHHHHCCCCCCCCCC	34.26	-
83	Acetylation	VDKPFAAKEDQLLCT CCCCCCCCCCEEEEE	59.39	26051181
83	Malonylation	VDKPFAAKEDQLLCT CCCCCCCCCCEEEEE	59.39	26320211
87 (in isoform 2)	Phosphorylation	-	7.02	23911959
93	Phosphorylation	QLLCTDCYSNEYSSK EEEEECCCCCCCHHH	19.83	20562096
97	Phosphorylation	TDCYSNEYSSKCQEC ECCCCCCCHHHHHHH	23.61	-
100	Ubiquitination	YSNEYSSKCQECKKT CCCCCHHHHHHHHCC	33.72	-
106	Ubiquitination	SKCQECKKTIMPGTR HHHHHHHCCCCCCCC	55.75	-
107	Phosphorylation	KCQECKKTIMPGTRK HHHHHHCCCCCCCCC	14.17	-
109 (in isoform 2)	Phosphorylation	-	2.79	21712546
111 (in isoform 2)	Phosphorylation	-	22.29	21712546
112	Acetylation	KKTIMPGTRKMEYKG HCCCCCCCCCCEECC	22.65	-
112	Phosphorylation	KKTIMPGTRKMEYKG HCCCCCCCCCCEECC	22.65	-
116 (in isoform 2)	Phosphorylation	-	47.32	22199227
118 (in isoform 2)	Phosphorylation	-	38.72	22199227
118	Sumoylation	GTRKMEYKGSSWHET CCCCCEECCCCHHCE	38.72	-
118	Malonylation	GTRKMEYKGSSWHET CCCCCEECCCCHHCE	38.72	26320211
118	Sumoylation	GTRKMEYKGSSWHET CCCCCEECCCCHHCE	38.72	-
120 (in isoform 2)	Phosphorylation	-	26.55	22199227
120	Phosphorylation	RKMEYKGSSWHETCF CCCEECCCCHHCEEE	26.55	27251275
121	Phosphorylation	KMEYKGSSWHETCFI CCEECCCCHHCEEEE	40.91	27251275
121 (in isoform 2)	Phosphorylation	-	40.91	22199227
138	Phosphorylation	RCQQPIGTKSFIPKD CCCCCCCCCCCCCCC	25.00	-
139	Sumoylation	CQQPIGTKSFIPKDN CCCCCCCCCCCCCCC	37.85	-
139	Ubiquitination	CQQPIGTKSFIPKDN CCCCCCCCCCCCCCC	37.85	-
139	Sumoylation	CQQPIGTKSFIPKDN CCCCCCCCCCCCCCC	37.85	-
140	Phosphorylation	QQPIGTKSFIPKDNQ CCCCCCCCCCCCCCC	28.39	-
144	Ubiquitination	GTKSFIPKDNQNFCV CCCCCCCCCCCCEEE	65.58	-
144	Sumoylation	GTKSFIPKDNQNFCV CCCCCCCCCCCCEEE	65.58	-
144	Acetylation	GTKSFIPKDNQNFCV CCCCCCCCCCCCEEE	65.58	26051181
144	Sumoylation	GTKSFIPKDNQNFCV CCCCCCCCCCCCEEE	65.58	-
144	Malonylation	GTKSFIPKDNQNFCV CCCCCCCCCCCCEEE	65.58	26320211
154	Phosphorylation	QNFCVPCYEKQHAMQ CCEEEECCCHHHHEE	21.79	28152594
156	Ubiquitination	FCVPCYEKQHAMQCV EEEECCCHHHHEEHE	22.40	-
156	Acetylation	FCVPCYEKQHAMQCV EEEECCCHHHHEEHE	22.40	26051181
160	Sulfoxidation	CYEKQHAMQCVQCKK CCCHHHHEEHEECCC	2.73	30846556
166	Ubiquitination	AMQCVQCKKPITTGG HEEHEECCCCCCCCC	44.48	-
167	Ubiquitination	MQCVQCKKPITTGGV EEHEECCCCCCCCCC	49.64	-
167	Sumoylation	MQCVQCKKPITTGGV EEHEECCCCCCCCCC	49.64	25218447
167	Malonylation	MQCVQCKKPITTGGV EEHEECCCCCCCCCC	49.64	26320211
167	Sumoylation	MQCVQCKKPITTGGV EEHEECCCCCCCCCC	49.64	-
170	Phosphorylation	VQCKKPITTGGVTYR EECCCCCCCCCCEEC	28.10	21406692
171	Phosphorylation	QCKKPITTGGVTYRE ECCCCCCCCCCEECC	32.43	20068231
175	Phosphorylation	PITTGGVTYREQPWH CCCCCCCEECCCCCC	21.82	20068231
176	Phosphorylation	ITTGGVTYREQPWHK CCCCCCEECCCCCCC	15.11	20068231
183	Acetylation	YREQPWHKECFVCTA ECCCCCCCCEEEEHH	52.92	26051181
183	Malonylation	YREQPWHKECFVCTA ECCCCCCCCEEEEHH	52.92	26320211
189	Phosphorylation	HKECFVCTACRKQLS CCCEEEEHHHHHHHC	24.40	27251275
219	Acetylation	CFCDLYAKKCAGCTN HHHHHHHHHHCCCCC	34.52	26051181
220	Sumoylation	FCDLYAKKCAGCTNP HHHHHHHHHCCCCCC	22.58	25218447
220	Sumoylation	FCDLYAKKCAGCTNP HHHHHHHHHCCCCCC	22.58	-
220	Ubiquitination	FCDLYAKKCAGCTNP HHHHHHHHHCCCCCC	22.58	-
229	Phosphorylation	AGCTNPISGLGGTKY CCCCCCCCCCCCCEE	29.26	28555341
234	Phosphorylation	PISGLGGTKYISFEE CCCCCCCCEEEECCC	20.90	28555341
235	Ubiquitination	ISGLGGTKYISFEER CCCCCCCEEEECCCE	43.81	-
235	Acetylation	ISGLGGTKYISFEER CCCCCCCEEEECCCE	43.81	26051181
236	Phosphorylation	SGLGGTKYISFEERQ CCCCCCEEEECCCEE	11.13	23403867
238	Phosphorylation	LGGTKYISFEERQWH CCCCEEEECCCEECC	24.42	30266825
252	Ubiquitination	HNDCFNCKKCSLSLV CCCCCCCCCCCEEEE	58.90	-
252	Acetylation	HNDCFNCKKCSLSLV CCCCCCCCCCCEEEE	58.90	26051181
253	Ubiquitination	NDCFNCKKCSLSLVG CCCCCCCCCCEEEEC	31.12	-
253	Sumoylation	NDCFNCKKCSLSLVG CCCCCCCCCCEEEEC	31.12	-
253	Sumoylation	NDCFNCKKCSLSLVG CCCCCCCCCCEEEEC	31.12	-
255	Phosphorylation	CFNCKKCSLSLVGRG CCCCCCCCEEEECCC	29.85	21406692
257	Phosphorylation	NCKKCSLSLVGRGFL CCCCCCEEEECCCCC	12.52	21406692
277	Ubiquitination	ILCPDCGKDI----- CCCCCCCCCC-----	59.59	-
277	Acetylation	ILCPDCGKDI----- CCCCCCCCCC-----	59.59	30588779
277	Ubiquitination	ILCPDCGKDI----- CCCCCCCCCC-----	59.59	21890473

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	TRAF6	Q9Y4K3	PMID:18768464

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FHL2_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 FHL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SFPQ_HUMAN	SFPQ	physical	11161712
MK01_HUMAN	MAPK1	physical	14729955
FHL3_HUMAN	FHL3	physical	11046156
FHL2_HUMAN	FHL2	physical	11046156
CREB1_HUMAN	CREB1	physical	11046156
CTNB1_HUMAN	CTNNB1	physical	12466281
ANDR_HUMAN	AR	physical	10654935
TITIN_HUMAN	TTN	physical	12432079
KAD1_HUMAN	AK1	physical	12432079
PFKAM_HUMAN	PFKM	physical	12432079
KCRM_HUMAN	CKM	physical	12432079
FHL1_HUMAN	FHL1	physical	12432079
ITA3_HUMAN	ITGA3	physical	10906324
ITB2_HUMAN	ITGB2	physical	10906324
ITB6_HUMAN	ITGB6	physical	10906324
ITB1_HUMAN	ITGB1	physical	10906324
ZBT16_HUMAN	ZBTB16	physical	12145280
TRAF6_HUMAN	TRAF6	physical	18768464
RUNX1_HUMAN	RUNX1	physical	18768464
RUNX2_HUMAN	RUNX2	physical	16079911
A4_HUMAN	APP	physical	21832049
ATF3_HUMAN	ATF3	physical	18255255
CSK_HUMAN	CSK	physical	18255255
REQU_HUMAN	DPF2	physical	18255255
FHL2_HUMAN	FHL2	physical	18255255
S30BP_HUMAN	SAP30BP	physical	18255255
ID3_HUMAN	ID3	physical	18255255
PUF60_HUMAN	PUF60	physical	18255255
STAT3_HUMAN	STAT3	physical	18255255
ZN331_HUMAN	ZNF331	physical	18255255
ZN408_HUMAN	ZNF408	physical	18255255
ZN626_HUMAN	ZNF626	physical	18255255
IKZF4_HUMAN	IKZF4	physical	18255255
RN111_HUMAN	RNF111	physical	23212909
SMAD2_HUMAN	SMAD2	physical	19139564
SMAD3_HUMAN	SMAD3	physical	19139564
SMAD4_HUMAN	SMAD4	physical	19139564
GBG12_HUMAN	GNG12	physical	21988832
DCTN3_HUMAN	DCTN3	physical	22863883
FOXO1_HUMAN	FOXO1	physical	15692560
PLAK_HUMAN	JUP	physical	25416956
NRF1_HUMAN	NRF1	physical	25416956
REL_HUMAN	REL	physical	25416956
RFX3_HUMAN	RFX3	physical	25416956
SP2_HUMAN	SP2	physical	25416956
ZN131_HUMAN	ZNF131	physical	25416956
GO45_HUMAN	BLZF1	physical	25416956
ZMYM4_HUMAN	ZMYM4	physical	25416956
RAI2_HUMAN	RAI2	physical	25416956
KANK2_HUMAN	KANK2	physical	25416956
BANP_HUMAN	BANP	physical	25416956
ZF64A_HUMAN	ZFP64	physical	25416956
ZF64B_HUMAN	ZFP64	physical	25416956
DCP1A_HUMAN	DCP1A	physical	25416956
GBG12_HUMAN	GNG12	physical	25416956
SKT_HUMAN	KIAA1217	physical	25416956
RHG09_HUMAN	ARHGAP9	physical	25416956
CCD92_HUMAN	CCDC92	physical	25416956
GLYR1_HUMAN	GLYR1	physical	25416956
DTX2_HUMAN	DTX2	physical	25416956
NIBAN_HUMAN	FAM129A	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
SAXO1_HUMAN	FAM154A	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
SRF_HUMAN	SRF	physical	15610731
HIF1A_HUMAN	HIF1A	physical	22219185
E4F1_HUMAN	E4F1	physical	16652157
MYPC1_HUMAN	MYBPC1	physical	16407297
EP300_HUMAN	EP300	physical	15572674
HCK_HUMAN	HCK	physical	21516116
SKT_HUMAN	KIAA1217	physical	21516116
RFX3_HUMAN	RFX3	physical	21516116
ZBT25_HUMAN	ZBTB25	physical	21516116
ZN131_HUMAN	ZNF131	physical	21516116
FHL2_HUMAN	FHL2	physical	10906324
REV1_HUMAN	REV1	physical	10906324
BIN1_HUMAN	BIN1	physical	10906324
IEX1_HUMAN	IER3	physical	26973248

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 FHL2_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-238, AND MASSSPECTROMETRY.	18669648 [Abstract]