MID49_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MID49_HUMAN
• UniProt AC: Q96C03
• Protein Name: Mitochondrial dynamics protein MID49
• Gene Name: MIEF2
• Organism: Homo sapiens (Human).
• Sequence Length: 454
• Subcellular Localization: Mitochondrion outer membrane ; Single-pass membrane protein . Colocalizes with DNM1L at mitochondrial membrane. Forms foci and rings around mitochondria.
• 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..
• Protein Sequence: MAEFSQKRGKRRSDEGLGSMVDFLLANARLVLGVGGAAVLGIATLAVKRFIDRATSPRDEDDTKADSWKELSLLKATPHLQPRPPPAALSQPVLPLAPSSSAPEGPAETDPEVTPQLSSPAPLCLTLQERLLAFERDRVTIPAAQVALAKQLAGDIALELQAYFRSKFPELPFGAFVPGGPLYDGLQAGAADHVRLLVPLVLEPGLWSLVPGVDTVARDPRCWAVRRTQLEFCPRGSSPWDRFLVGGYLSSRVLLELLRKALAASVNWPAIGSLLGCLIRPSMASEELLLEVQHERLELTVAVLVAVPGVDADDRLLLAWPLEGLAGNLWLQDLYPVEAARLRALDDHDAGTRRRLLLLLCAVCRGCSALGQLGRGHLTQVVLRLGEDNVDWTEEALGERFLQALELLIGSLEQASLPCHFNPSVNLFSSLREEEIDDIGYALYSGLQEPEGLL

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
7	Ubiquitination	-MAEFSQKRGKRRSD -CCCHHHHHCCCCCC	63.02	-
13	Phosphorylation	QKRGKRRSDEGLGSM HHHCCCCCCCCHHHH	44.01	18669648
64	Ubiquitination	PRDEDDTKADSWKEL CCCCCCCCCCCHHHH	58.13	23000965
64 (in isoform 2)	Ubiquitination	-	58.13	21890473
64 (in isoform 1)	Ubiquitination	-	58.13	21890473
67	Phosphorylation	EDDTKADSWKELSLL CCCCCCCCHHHHHHH	44.93	26471730
69 (in isoform 2)	Ubiquitination	-	53.37	21890473
69 (in isoform 1)	Ubiquitination	-	53.37	21890473
69	Ubiquitination	DTKADSWKELSLLKA CCCCCCHHHHHHHHC	53.37	23000965
71	Ubiquitination	KADSWKELSLLKATP CCCCHHHHHHHHCCC	3.77	23000965
72	Phosphorylation	ADSWKELSLLKATPH CCCHHHHHHHHCCCC	32.52	24719451
75	Ubiquitination	WKELSLLKATPHLQP HHHHHHHHCCCCCCC	56.35	23000965
76	Ubiquitination	KELSLLKATPHLQPR HHHHHHHCCCCCCCC	26.74	21890473
80	Ubiquitination	LLKATPHLQPRPPPA HHHCCCCCCCCCCCC	8.69	21890473
82	Ubiquitination	KATPHLQPRPPPAAL HCCCCCCCCCCCCHH	58.04	23000965
86	Ubiquitination	HLQPRPPPAALSQPV CCCCCCCCCHHCCCC	32.61	23000965
163	Phosphorylation	IALELQAYFRSKFPE HHHHHHHHHHHHCCC	6.12	21394647
167	Ubiquitination	LQAYFRSKFPELPFG HHHHHHHHCCCCCCC	61.76	-
430	Phosphorylation	PSVNLFSSLREEEID CCCCHHHHCCHHHHC	24.90	24719451

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

Oops, there are no upstream regulatory protein records of MID49_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MID49_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 MID49_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRAF1_HUMAN	RABAC1	physical	19060904

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

"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