TIM14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIM14_HUMAN
• UniProt AC: Q96DA6
• Protein Name: Mitochondrial import inner membrane translocase subunit TIM14
• Gene Name: DNAJC19
• Organism: Homo sapiens (Human).
• Sequence Length: 116
• Subcellular Localization: Mitochondrion inner membrane ; Single-pass membrane protein .
• Protein Description: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity)..
• Protein Sequence: MASTVVAVGLTIAAAGFAGRYVLQAMKHMEPQVKQVFQSLPKSAFSGGYYRGGFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLEGQAKK

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
2	Acetylation	------MASTVVAVG ------CCCHHHHHH	17.57	25944712
3	Phosphorylation	-----MASTVVAVGL -----CCCHHHHHHH	22.04	26307563
4	Phosphorylation	----MASTVVAVGLT ----CCCHHHHHHHH	14.95	26307563
9	Ubiquitination	ASTVVAVGLTIAAAG CCHHHHHHHHHHHHH	13.83	21890473
11	Phosphorylation	TVVAVGLTIAAAGFA HHHHHHHHHHHHHHH	11.57	26307563
17	Ubiquitination	LTIAAAGFAGRYVLQ HHHHHHHHHHHHHHH	5.81	21890473
21	Phosphorylation	AAGFAGRYVLQAMKH HHHHHHHHHHHHHHH	12.47	26307563
34	Ubiquitination	KHMEPQVKQVFQSLP HHCCHHHHHHHHHCC	35.18	21890473
39	Phosphorylation	QVKQVFQSLPKSAFS HHHHHHHHCCHHHHC	34.86	23917254
42	Ubiquitination	QVFQSLPKSAFSGGY HHHHHCCHHHHCCCC	60.76	21890473
51	Methylation	AFSGGYYRGGFEPKM HHCCCCCCCCCCCCC	30.21	-
68	Acetylation	REAALILGVSPTANK HHHHHHHCCCCCCCC	15.74	19608861
70	Phosphorylation	AALILGVSPTANKGK HHHHHCCCCCCCCCC	18.09	23401153
72	Phosphorylation	LILGVSPTANKGKIR HHHCCCCCCCCCCCC	35.04	30266825
75	Malonylation	GVSPTANKGKIRDAH CCCCCCCCCCCCHHH	60.15	26320211
93	Acetylation	MLLNHPDKGGSPYIA HHHCCCCCCCCCCHH	70.40	23954790
93	Malonylation	MLLNHPDKGGSPYIA HHHCCCCCCCCCCHH	70.40	26320211
107	Malonylation	AAKINEAKDLLEGQA HHHHHHHHHHHHHHC	42.61	26320211
107	Acetylation	AAKINEAKDLLEGQA HHHHHHHHHHHHHHC	42.61	26051181

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

Oops, there are no upstream regulatory protein records of TIM14_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TIM14_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 TIM14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIM16_YEAST	PAM16	physical	19564938
TIM16_HUMAN	PAM16	physical	20053669
GRP75_HUMAN	HSPA9	physical	20053669
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

• Kegg Disease
• H00754: 3-Methylglutaconic aciduria (MGCA)
• OMIM Disease
• 610198: 3-methylglutaconic aciduria 5 (MGA5)
• 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 ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-93, AND MASS SPECTROMETRY.
PubMed: 19608861