MIPEP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MIPEP_HUMAN
• UniProt AC: Q99797
• Protein Name: Mitochondrial intermediate peptidase
• Gene Name: MIPEP
• Organism: Homo sapiens (Human).
• Sequence Length: 713
• Subcellular Localization: Mitochondrion matrix.
• Protein Description: Cleaves proteins, imported into the mitochondrion, to their mature size..
• Protein Sequence: MLCVGRLGGLGARAAALPPRRAGRGSLEAGIRARRVSTSWSPVGAAFNVKPQGSRLDLFGERRGLFGVPELSAPEGFHIAQEKALRKTELLVDRACSTPPGPQTVLIFDELSDSLCRVADLADFVKIAHPEPAFREAAEEACRSIGTMVEKLNTNVDLYQSLQKLLADKKLVDSLDPETRRVAELFMFDFEISGIHLDKEKRKRAVDLNVKILDLSSTFLMGTNFPNKIEKHLLPEHIRRNFTSAGDHIIIDGLHAESPDDLVREAAYKIFLYPNAGQLKCLEELLSSRDLLAKLVGYSTFSHRALQGTIAKNPETVMQFLEKLSDKLSERTLKDFEMIRGMKMKLNPQNSEVMPWDPPYYSGVIRAERYNIEPSLYCPFFSLGACMEGLNILLNRLLGISLYAEQPAKGEVWSEDVRKLAVVHESEGLLGYIYCDFFQRADKPHQDCHFTIRGGRLKEDGDYQLPVVVLMLNLPRSSRSSPTLLTPSMMENLFHEMGHAMHSMLGRTRYQHVTGTRCPTDFAEVPSILMEYFANDYRVVNQFARHYQTGQPLPKNMVSRLCESKKVCAAADMQLQVFYATLDQIYHGKHPLRNSTTDILKETQEKFYGLPYVPNTAWQLRFSHLVGYGARYYSYLMSRAVASMVWKECFLQDPFNRAAGERYRREMLAHGGGREPMLMVEGMLQKCPSVDDFVSALVSDLDLDFETFLMDSE

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
50	Malonylation	VGAAFNVKPQGSRLD CCCEEECCCCCCEEE	32.50	26320211
87	Malonylation	AQEKALRKTELLVDR HHHHHHHHCCHHHHC	47.39	26320211
126	Acetylation	ADLADFVKIAHPEPA HHHHHHHHHCCCCHH	33.88	19608861
126	Ubiquitination	ADLADFVKIAHPEPA HHHHHHHHHCCCCHH	33.88	19608861
126	2-Hydroxyisobutyrylation	ADLADFVKIAHPEPA HHHHHHHHHCCCCHH	33.88	-
147	Phosphorylation	EACRSIGTMVEKLNT HHHHHHHHHHHHHCC	19.17	27251275
164	Ubiquitination	DLYQSLQKLLADKKL HHHHHHHHHHHCCHH	51.25	-
216	Phosphorylation	NVKILDLSSTFLMGT CCEEEECCCCEECCC	27.31	28450419
217	Phosphorylation	VKILDLSSTFLMGTN CEEEECCCCEECCCC	30.40	28450419
218	Phosphorylation	KILDLSSTFLMGTNF EEEECCCCEECCCCC	19.88	28450419
223	Phosphorylation	SSTFLMGTNFPNKIE CCCEECCCCCCCHHH	21.52	28450419
231	Acetylation	NFPNKIEKHLLPEHI CCCCHHHHHCCHHHH	42.92	26210075
231	Ubiquitination	NFPNKIEKHLLPEHI CCCCHHHHHCCHHHH	42.92	29967540
272	Ubiquitination	EAAYKIFLYPNAGQL HHHHHHHCCCCHHHH	8.71	24816145
287	Phosphorylation	KCLEELLSSRDLLAK HHHHHHHCCHHHHHH	35.63	24719451
288	Phosphorylation	CLEELLSSRDLLAKL HHHHHHCCHHHHHHH	29.77	24719451
316	Phosphorylation	TIAKNPETVMQFLEK HHCCCHHHHHHHHHH	23.64	25599653
318	Sulfoxidation	AKNPETVMQFLEKLS CCCHHHHHHHHHHHH	2.81	21406390
325	Phosphorylation	MQFLEKLSDKLSERT HHHHHHHHHHHHHHH	43.71	22673903
329	Phosphorylation	EKLSDKLSERTLKDF HHHHHHHHHHHHHHH	30.67	23898821
331	Methylation	LSDKLSERTLKDFEM HHHHHHHHHHHHHHH	41.82	24411419
334	Ubiquitination	KLSERTLKDFEMIRG HHHHHHHHHHHHHHH	60.81	24816145
409	Acetylation	LYAEQPAKGEVWSED CEECCCCCCCCCCHH	63.39	7676599
451	Phosphorylation	PHQDCHFTIRGGRLK CCCCCCEEEECCCCC	6.01	24719451
510	Phosphorylation	SMLGRTRYQHVTGTR HHHCCCCCCCCCCCC	11.45	20068231
514	Phosphorylation	RTRYQHVTGTRCPTD CCCCCCCCCCCCCCC	30.61	20068231
516	Phosphorylation	RYQHVTGTRCPTDFA CCCCCCCCCCCCCHH	21.52	20068231
537	Phosphorylation	MEYFANDYRVVNQFA HHHHCCCHHHHHHHH	12.71	25599653
547	Phosphorylation	VNQFARHYQTGQPLP HHHHHHHHCCCCCCC	11.39	28152594
549	Phosphorylation	QFARHYQTGQPLPKN HHHHHHCCCCCCCHH	30.53	28152594
555	Acetylation	QTGQPLPKNMVSRLC CCCCCCCHHHHHHHH	66.41	26210075
579	Phosphorylation	DMQLQVFYATLDQIY HHHHHHHHHHHHHHH	10.38	-
601	Ubiquitination	NSTTDILKETQEKFY CCHHHHHHHHHHHHH	60.08	-
603	Phosphorylation	TTDILKETQEKFYGL HHHHHHHHHHHHHCC	40.20	30631047
616	Phosphorylation	GLPYVPNTAWQLRFS CCCCCCCCCHHHHHH	24.17	30631047
628	Phosphorylation	RFSHLVGYGARYYSY HHHHHHHCCHHHHHH	10.51	17322306
632	Phosphorylation	LVGYGARYYSYLMSR HHHCCHHHHHHHHHH	9.02	17322306
633	Phosphorylation	VGYGARYYSYLMSRA HHCCHHHHHHHHHHH	5.81	17322306
635	Phosphorylation	YGARYYSYLMSRAVA CCHHHHHHHHHHHHH	7.12	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MIPEP_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 MIPEP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AINX_HUMAN	INA	physical	28514442

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

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND MASS SPECTROMETRY.
PubMed: 19608861