M1IP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: M1IP1_HUMAN
• UniProt AC: Q9NPA3
• Protein Name: Mid1-interacting protein 1
• Gene Name: MID1IP1
• Organism: Homo sapiens (Human).
• Sequence Length: 183
• Subcellular Localization: Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Associated with microtubules.
• Protein Description: Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity)..
• Protein Sequence: MMQICDTYNQKHSLFNAMNRFIGAVNNMDQTVMVPSLLRDVPLADPGLDNDVGVEVGGSGGCLEERTPPVPDSGSANGSFFAPSRDMYSHYVLLKSIRNDIEWGVLHQPPPPAGSEEGSAWKSKDILVDLGHLEGADAGEEDLEQQFHYHLRGLHTVLSKLTRKANILTNRYKQEIGFGNWGH

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
1	Acetylation	-------MMQICDTY -------CCCCCCCC	3.93	19413330
7	Phosphorylation	-MMQICDTYNQKHSL -CCCCCCCCHHHHHH	21.69	30622161
8	Phosphorylation	MMQICDTYNQKHSLF CCCCCCCCHHHHHHH	11.44	30622161
11	Ubiquitination	ICDTYNQKHSLFNAM CCCCCHHHHHHHHHH	31.36	22505724
59	Phosphorylation	VGVEVGGSGGCLEER CCEECCCCCCCCCCC	26.53	28348404
67	Phosphorylation	GGCLEERTPPVPDSG CCCCCCCCCCCCCCC	34.91	23663014
73	Phosphorylation	RTPPVPDSGSANGSF CCCCCCCCCCCCCCC	28.69	29978859
75	Phosphorylation	PPVPDSGSANGSFFA CCCCCCCCCCCCCCC	23.63	26055452
79	Phosphorylation	DSGSANGSFFAPSRD CCCCCCCCCCCCCHH	19.59	21815630
84	Phosphorylation	NGSFFAPSRDMYSHY CCCCCCCCHHHHHHH	37.17	23186163
89	Phosphorylation	APSRDMYSHYVLLKS CCCHHHHHHHHHHHH	11.16	21712546
91	Phosphorylation	SRDMYSHYVLLKSIR CHHHHHHHHHHHHHH	6.20	27642862
95	Ubiquitination	YSHYVLLKSIRNDIE HHHHHHHHHHHCCCC	39.41	23503661
96	Phosphorylation	SHYVLLKSIRNDIEW HHHHHHHHHHCCCCC	27.10	21712546
115	Phosphorylation	QPPPPAGSEEGSAWK CCCCCCCCCCCCCCC	34.28	29978859
119	Phosphorylation	PAGSEEGSAWKSKDI CCCCCCCCCCCCCCE	33.95	29116813
122	Ubiquitination	SEEGSAWKSKDILVD CCCCCCCCCCCEEEE	47.55	21906983
124	Ubiquitination	EGSAWKSKDILVDLG CCCCCCCCCEEEECC	45.09	22817900
159	Phosphorylation	RGLHTVLSKLTRKAN HHHHHHHHHHHHHHC	22.68	27251275
160	Ubiquitination	GLHTVLSKLTRKANI HHHHHHHHHHHHHCH	50.12	-
164	Ubiquitination	VLSKLTRKANILTNR HHHHHHHHHCHHCHH	40.32	29967540
173	Ubiquitination	NILTNRYKQEIGFGN CHHCHHHHHHCCCCC	37.91	29967540

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

Oops, there are no upstream regulatory protein records of M1IP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of M1IP1_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 M1IP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAD8_HUMAN	AK8	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

Acetylation

"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.
PubMed: 19413330