FUND1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FUND1_HUMAN
• UniProt AC: Q8IVP5
• Protein Name: FUN14 domain-containing protein 1
• Gene Name: FUNDC1
• Organism: Homo sapiens (Human).
• Sequence Length: 155
• Subcellular Localization: Mitochondrion outer membrane ; Multi-pass membrane protein .
• Protein Description: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control..
• Protein Sequence: MATRNPPPQDYESDDDSYEVLDLTEYARRHQWWNRVFGHSSGPMVEKYSVATQIVMGGVTGWCAGFLFQKVGKLAATAVGGGFLLLQIASHSGYVQIDWKRVEKDVNKAKRQIKKRANKAAPEINNLIEEATEFIKQNIVISSGFVGGFLLGLAS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATRNPPPQD -----CCCCCCCCCC	29.67	25072903
11	Phosphorylation	RNPPPQDYESDDDSY CCCCCCCCCCCCCCE	16.46	30175587
13	Phosphorylation	PPPQDYESDDDSYEV CCCCCCCCCCCCEEE	39.86	30175587
17	Phosphorylation	DYESDDDSYEVLDLT CCCCCCCCEEEEHHH	30.13	30175587
18	Phosphorylation	YESDDDSYEVLDLTE CCCCCCCEEEEHHHH	19.63	30183078
24	Phosphorylation	SYEVLDLTEYARRHQ CEEEEHHHHHHHHHH	26.98	29978859
26	Phosphorylation	EVLDLTEYARRHQWW EEEHHHHHHHHHHHH	10.52	29978859
40	Phosphorylation	WNRVFGHSSGPMVEK HHHHHCCCCCCHHHC	37.05	-
41	Phosphorylation	NRVFGHSSGPMVEKY HHHHCCCCCCHHHCC	41.04	-
114	Ubiquitination	NKAKRQIKKRANKAA HHHHHHHHHHHHHHC	28.06	23000965
115	Ubiquitination	KAKRQIKKRANKAAP HHHHHHHHHHHHHCH	59.37	23000965
119	Neddylation	QIKKRANKAAPEINN HHHHHHHHHCHHHHH	44.96	32015554
119	Ubiquitination	QIKKRANKAAPEINN HHHHHHHHHCHHHHH	44.96	23000965
155	Phosphorylation	GFLLGLAS------- HHHHHHCC-------	45.88	28857561

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
13	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
17	S	Phosphorylation	Kinase	ULK1	O75385	PSP
18	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FUND1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FUND1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MARH5_HUMAN	MARCH5	physical	28104734

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-13, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-13, AND MASSSPECTROMETRY.
PubMed: 18669648

"Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-inducedmitophagy in mammalian cells.";
Liu L., Feng D., Chen G., Chen M., Zheng Q., Song P., Ma Q., Zhu C.,Wang R., Qi W., Huang L., Xue P., Li B., Wang X., Jin H., Wang J.,Yang F., Liu P., Zhu Y., Sui S., Chen Q.;
Nat. Cell Biol. 14:177-185(2012).
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,PHOSPHORYLATION AT TYR-18, INTERACTION WITH MAP1LC3A; MAP1LC3B ANDGABARAP, AND MUTAGENESIS OF TYR-18; LEU-21 AND 31-TRP-TRP-32.
PubMed: 22267086