MID51_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MID51_HUMAN
• UniProt AC: Q9NQG6
• Protein Name: Mitochondrial dynamics protein MID51
• Gene Name: MIEF1
• Organism: Homo sapiens (Human).
• Sequence Length: 463
• Subcellular Localization: Mitochondrion outer membrane ; Single-pass membrane protein .
• Protein Description: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L..
• Protein Sequence: MAGAGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSPTRLSHSGKRSWEEPNWMGSPRLLNRDMKTGLSRSLQTLPTDSSTFDTDTFCPPRPKPVARKGQVDLKKSRLRMSLQEKLLTYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMPLRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCIPGEDTIMNVPGFFLVRRENPEYFPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPPPEALTLEVQYERDKHLFIDFLPSVTLGDTVLVAKPHRLAQYDNLWRLSLRPAETARLRALDQADSGCRSLCLKILKAICKSTPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLEAGVLPSALNPKVNLFAELTPEEIDELGYTLYCSLSEPEVLLQT

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
55	Phosphorylation	RMYDRAISAPTSPTR HHHHHHHCCCCCCCC	27.49	29255136
58	Phosphorylation	DRAISAPTSPTRLSH HHHHCCCCCCCCCCC	47.24	29255136
59	Phosphorylation	RAISAPTSPTRLSHS HHHCCCCCCCCCCCC	24.18	29255136
61	Phosphorylation	ISAPTSPTRLSHSGK HCCCCCCCCCCCCCC	43.97	29255136
64	Phosphorylation	PTSPTRLSHSGKRSW CCCCCCCCCCCCCCC	16.59	25159151
66	Phosphorylation	SPTRLSHSGKRSWEE CCCCCCCCCCCCCCC	42.51	30576142
68	Ubiquitination	TRLSHSGKRSWEEPN CCCCCCCCCCCCCCC	46.39	-
70	Phosphorylation	LSHSGKRSWEEPNWM CCCCCCCCCCCCCCC	42.18	25159151
79	Phosphorylation	EEPNWMGSPRLLNRD CCCCCCCCHHHCCHH	7.25	23401153
88	Acetylation	RLLNRDMKTGLSRSL HHCCHHHHCCCCHHC	43.67	7822455
88	Ubiquitination	RLLNRDMKTGLSRSL HHCCHHHHCCCCHHC	43.67	-
89	Phosphorylation	LLNRDMKTGLSRSLQ HCCHHHHCCCCHHCC	36.40	23403867
92	Phosphorylation	RDMKTGLSRSLQTLP HHHHCCCCHHCCCCC	22.59	23403867
94 (in isoform 2)	Phosphorylation	-	22.81	-
94	Phosphorylation	MKTGLSRSLQTLPTD HHCCCCHHCCCCCCC	22.81	29255136
97	Phosphorylation	GLSRSLQTLPTDSST CCCHHCCCCCCCCCC	39.74	30266825
100	Phosphorylation	RSLQTLPTDSSTFDT HHCCCCCCCCCCCCC	52.18	30108239
102	Phosphorylation	LQTLPTDSSTFDTDT CCCCCCCCCCCCCCC	33.48	23927012
103	Phosphorylation	QTLPTDSSTFDTDTF CCCCCCCCCCCCCCC	35.58	23927012
104	Phosphorylation	TLPTDSSTFDTDTFC CCCCCCCCCCCCCCC	29.49	22199227
107	Phosphorylation	TDSSTFDTDTFCPPR CCCCCCCCCCCCCCC	32.52	23927012
109	Phosphorylation	SSTFDTDTFCPPRPK CCCCCCCCCCCCCCC	29.27	23927012
258	Phosphorylation	CVVGGYLSPKTVADT CEECCEECHHHHHHH	18.83	24719451
340	Phosphorylation	YDNLWRLSLRPAETA CCCEEECCCCHHHHH	17.48	23532336
365	Ubiquitination	GCRSLCLKILKAICK HHHHHHHHHHHHHHH	45.02	-
365	Acetylation	GCRSLCLKILKAICK HHHHHHHHHHHHHHH	45.02	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MID51_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MID51_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 MID51_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MID51_HUMAN	MIEF1	physical	21701560
DNM1L_HUMAN	DNM1L	physical	21701560
FIS1_HUMAN	FIS1	physical	21701560
ATRAP_HUMAN	AGTRAP	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-58 AND SER-59,AND MASS SPECTROMETRY.
PubMed: 19413330

"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-55 AND SER-59, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
PubMed: 18691976