dbPTM

FIS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FIS1_HUMAN
UniProt AC	Q9Y3D6
Protein Name	Mitochondrial fission 1 protein
Gene Name	FIS1
Organism	Homo sapiens (Human).
Sequence Length	152
Subcellular Localization	Mitochondrion outer membrane Single-pass membrane protein. Peroxisome membrane Single-pass membrane protein.
Protein Description	Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission..
Protein Sequence	MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEAVLNEL -------CHHHHHHH	7.23	25944712
10	Phosphorylation	AVLNELVSVEDLLKF HHHHHHCCHHHHHHH	32.20	27732954
16	Ubiquitination	VSVEDLLKFEKKFQS CCHHHHHHHHHHHCC	59.79	23503661
19	Ubiquitination	EDLLKFEKKFQSEKA HHHHHHHHHHCCCCC	63.12	23503661
20	Ubiquitination	DLLKFEKKFQSEKAA HHHHHHHHHCCCCCC	41.25	32142685
25	2-Hydroxyisobutyrylation	EKKFQSEKAAGSVSK HHHHCCCCCCCCCCC	49.10	-
25	Ubiquitination	EKKFQSEKAAGSVSK HHHHCCCCCCCCCCC	49.10	32142685
31	Phosphorylation	EKAAGSVSKSTQFEY CCCCCCCCCCHHHHH	23.68	-
45	Phosphorylation	YAWCLVRSKYNDDIR HHHHHHHHHCCCHHH	31.82	22817900
46	Ubiquitination	AWCLVRSKYNDDIRK HHHHHHHHCCCHHHH	37.19	-
47	Phosphorylation	WCLVRSKYNDDIRKG HHHHHHHCCCHHHHH	25.68	22817900
53	Ubiquitination	KYNDDIRKGIVLLEE HCCCHHHHHHHHHHH	54.01	32142685
64	Ubiquitination	LLEELLPKGSKEEQR HHHHHCCCCCHHHHH	75.64	32015554
67	Ubiquitination	ELLPKGSKEEQRDYV HHCCCCCHHHHHHHH	74.14	32142685
76	Phosphorylation	EQRDYVFYLAVGNYR HHHHHHEEEEECCHH	5.45	25884760
82	Phosphorylation	FYLAVGNYRLKEYEK EEEEECCHHHHHHHH	16.05	25884760
87	Phosphorylation	GNYRLKEYEKALKYV CCHHHHHHHHHHHHH	22.57	25884760
89	Ubiquitination	YRLKEYEKALKYVRG HHHHHHHHHHHHHHH	59.11	32142685
93	Phosphorylation	EYEKALKYVRGLLQT HHHHHHHHHHHHHCC	9.02	25884760
100	Phosphorylation	YVRGLLQTEPQNNQA HHHHHHCCCCCCHHH	49.99	29083192
108	Ubiquitination	EPQNNQAKELERLID CCCCHHHHHHHHHHH	53.74	24816145
116	Ubiquitination	ELERLIDKAMKKDGL HHHHHHHHHHHHCCC	43.30	29967540

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	MARCHF5	Q9NX47	PMID:16874301

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FIS1_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 FIS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FIS1_HUMAN	FIS1	physical	14705031
DNM1L_HUMAN	DNM1L	physical	12861026
BAP31_HUMAN	BCAP31	physical	21183955
CASP8_HUMAN	CASP8	physical	21183955
TBC15_HUMAN	TBC1D15	physical	23077178
TOM40_HUMAN	TOMM40	physical	22939629
KASH5_HUMAN	CCDC155	physical	25416956

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 FIS1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]