dbPTM

FRIH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FRIH_HUMAN
UniProt AC	P02794
Protein Name	Ferritin heavy chain
Gene Name	FTH1
Organism	Homo sapiens (Human).
Sequence Length	183
Subcellular Localization
Protein Description	Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity)..
Protein Sequence	MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTTASTSQ -------CCCCCHHH	7.29	22814378
2	Acetylation	------MTTASTSQV ------CCCCCHHHH	30.94	22814378
2	Phosphorylation	------MTTASTSQV ------CCCCCHHHH	30.94	28857561
3	Phosphorylation	-----MTTASTSQVR -----CCCCCHHHHH	19.81	24043423
5	Phosphorylation	---MTTASTSQVRQN ---CCCCCHHHHHHH	26.88	28857561
6	Phosphorylation	--MTTASTSQVRQNY --CCCCCHHHHHHHH	22.25	24043423
7	Phosphorylation	-MTTASTSQVRQNYH -CCCCCHHHHHHHHC	24.96	19651622
13	Phosphorylation	TSQVRQNYHQDSEAA HHHHHHHHCCCCHHH	7.79	-
54	Acetylation	VALKNFAKYFLHQSH HHHHHHHHHHHHCCH	32.19	27452117
54	Ubiquitination	VALKNFAKYFLHQSH HHHHHHHHHHHHCCH	32.19	-
69	Ubiquitination	EEREHAEKLMKLQNQ HHHHHHHHHHHHHHH	55.45	-
72	Sumoylation	EHAEKLMKLQNQRGG HHHHHHHHHHHHHCC	58.31	-
72	2-Hydroxyisobutyrylation	EHAEKLMKLQNQRGG HHHHHHHHHHHHHCC	58.31	-
72	Ubiquitination	EHAEKLMKLQNQRGG HHHHHHHHHHHHHCC	58.31	-
72	Sumoylation	EHAEKLMKLQNQRGG HHHHHHHHHHHHHCC	58.31	-
88	Ubiquitination	IFLQDIKKPDCDDWE EEECCCCCCCCCHHH	46.55	-
96	Phosphorylation	PDCDDWESGLNAMEC CCCCHHHHHHHHHHH	44.31	24275569
103	Glutathionylation	SGLNAMECALHLEKN HHHHHHHHHHHHHHH	2.91	22555962
109	Ubiquitination	ECALHLEKNVNQSLL HHHHHHHHHHCHHHH	72.98	-
114	Phosphorylation	LEKNVNQSLLELHKL HHHHHCHHHHHHHHH	29.71	28192239
120	Ubiquitination	QSLLELHKLATDKND HHHHHHHHHHCCCCC	53.06	-
125	Acetylation	LHKLATDKNDPHLCD HHHHHCCCCCHHHHH	59.92	27452117
125	Ubiquitination	LHKLATDKNDPHLCD HHHHHCCCCCHHHHH	59.92	-
125	Malonylation	LHKLATDKNDPHLCD HHHHHCCCCCHHHHH	59.92	30639696
144	Ubiquitination	HYLNEQVKAIKELGD HCHHHHHHHHHHHHH	44.05	-
147	Ubiquitination	NEQVKAIKELGDHVT HHHHHHHHHHHHHHH	52.31	21890473
158	Ubiquitination	DHVTNLRKMGAPESG HHHHHHHHCCCCCCH	44.87	-
164	Phosphorylation	RKMGAPESGLAEYLF HHCCCCCCHHHHHHH	37.74	23927012
169	Phosphorylation	PESGLAEYLFDKHTL CCCHHHHHHHHHHCC	13.68	23927012
175	Phosphorylation	EYLFDKHTLGDSDNE HHHHHHHCCCCCCCC	37.87	22167270
179	Phosphorylation	DKHTLGDSDNES--- HHHCCCCCCCCC---	40.30	25159151
183	Phosphorylation	LGDSDNES------- CCCCCCCC-------	52.34	22167270

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 FRIH_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FXR2_HUMAN	FXR2	physical	16189514
FRIL_HUMAN	FTL	physical	16189514
BRD7_HUMAN	BRD7	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
UBR1_HUMAN	UBR1	physical	16169070
DAXX_HUMAN	DAXX	physical	21573799
FRIL_HUMAN	FTL	physical	22939629
GRB2_HUMAN	GRB2	physical	21988832
IMA1_HUMAN	KPNA2	physical	21988832
LBP_HUMAN	LBP	physical	21988832
MYL3_HUMAN	MYL3	physical	21988832
SOX5_HUMAN	SOX5	physical	21988832
1433E_HUMAN	YWHAE	physical	21988832
PIAS4_HUMAN	PIAS4	physical	21988832
TCAM2_HUMAN	TICAM2	physical	21988832
MAX_HUMAN	MAX	physical	20195357
FRIH_HUMAN	FTH1	physical	25416956
FRIL_HUMAN	FTL	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
PCBP1_HUMAN	PCBP1	physical	23640898
PCBP2_HUMAN	PCBP2	physical	23640898
PCBP3_HUMAN	PCBP3	physical	23640898
RHG01_HUMAN	ARHGAP1	physical	26344197
FRIL_HUMAN	FTL	physical	21516116
NCOA4_HUMAN	NCOA4	physical	28514442
RET4_HUMAN	RBP4	physical	28514442
RDHE2_HUMAN	SDR16C5	physical	28514442
SEMG2_HUMAN	SEMG2	physical	28514442
FRIL_HUMAN	FTL	physical	28514442
SEMG1_HUMAN	SEMG1	physical	28514442
HUTH_HUMAN	HAL	physical	28514442
KLK5_HUMAN	KLK5	physical	28514442
TREX2_HUMAN	TREX2	physical	28514442
KLK10_HUMAN	KLK10	physical	28514442
SPB7_HUMAN	SERPINB7	physical	28514442
KLK7_HUMAN	KLK7	physical	28514442
SPA12_HUMAN	SERPINA12	physical	28514442
IL1RA_HUMAN	IL1RN	physical	28514442
PPAP_HUMAN	ACPP	physical	28514442
PLBL1_HUMAN	PLBD1	physical	28514442
POF1B_HUMAN	POF1B	physical	28514442
CRNN_HUMAN	CRNN	physical	28514442
SPB4_HUMAN	SERPINB4	physical	28514442
CBPA4_HUMAN	CPA4	physical	28514442
KLK11_HUMAN	KLK11	physical	28514442
CASPE_HUMAN	CASP14	physical	28514442
SPB3_HUMAN	SERPINB3	physical	28514442
TGM5_HUMAN	TGM5	physical	28514442
TGM1_HUMAN	TGM1	physical	28514442
CATL2_HUMAN	CTSV	physical	28514442
CYTN_HUMAN	CST1	physical	28514442
LX12B_HUMAN	ALOX12B	physical	28514442
FILA_HUMAN	FLG	physical	28514442
MAOX_HUMAN	ME1	physical	28514442
INVO_HUMAN	IVL	physical	28514442
IL37_HUMAN	IL37	physical	28514442
CYTM_HUMAN	CST6	physical	28514442
ASAH1_HUMAN	ASAH1	physical	28514442
PEPL_HUMAN	PPL	physical	28514442
CALL3_HUMAN	CALML3	physical	28514442
CPNS2_HUMAN	CAPNS2	physical	28514442
CBPM_HUMAN	CPM	physical	28514442
LC7L2_HUMAN	LUC7L2	physical	28514442
TGM3_HUMAN	TGM3	physical	28514442
CALL5_HUMAN	CALML5	physical	28514442
FBX50_HUMAN	NCCRP1	physical	28514442
CYTS_HUMAN	CST4	physical	28514442
ECM1_HUMAN	ECM1	physical	28514442
SAP3_HUMAN	GM2A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615517	Hemochromatosis 5 (HFE5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00893	Iron Dextran

Regulatory Network of FRIH_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-175 AND SER-179, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-183, ANDMASS SPECTROMETRY.	18318008 [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-179, AND MASSSPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASSSPECTROMETRY.	16964243 [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-179, AND MASSSPECTROMETRY.	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-179, AND MASSSPECTROMETRY.	15302935 [Abstract]