dbPTM

TMLH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TMLH_HUMAN
UniProt AC	Q9NVH6
Protein Name	Trimethyllysine dioxygenase, mitochondrial
Gene Name	TMLHE
Organism	Homo sapiens (Human).
Sequence Length	421
Subcellular Localization	Mitochondrion matrix .
Protein Description	Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML). [PubMed: 11431483]
Protein Sequence	MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHFELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTWPDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKFLQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALDRHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHEYIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLTIELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Ubiquitination	SRLQDLLKGGVIYPA HHHHHHHCCCCCCCC	62.00	-
29 (in isoform 8)	Ubiquitination	-	46.41	-
84	Ubiquitination	RDHCRSASCYNSKTH HHHHCCCCCCCCCCC	20.55	21890473
119	Phosphorylation	DETTLFFTWPDGHVT CCCEEEEECCCCCEE	28.84	-
126	Phosphorylation	TWPDGHVTKYDLNWL ECCCCCEEEEEHHHH	20.43	-
135 (in isoform 2)	Ubiquitination	-	37.70	21890473
135 (in isoform 1)	Ubiquitination	-	37.70	21890473
135	Ubiquitination	YDLNWLVKNSYEGQK EEHHHHHHCCCCCCC	37.70	21890473
135	Ubiquitination	YDLNWLVKNSYEGQK EEHHHHHHCCCCCCC	37.70	21890473
135	Ubiquitination	YDLNWLVKNSYEGQK EEHHHHHHCCCCCCC	37.70	22817900
144	Ubiquitination	SYEGQKQKVIQPRIL CCCCCCCEEECCEEE	48.63	29967540
146 (in isoform 8)	Ubiquitination	-	6.34	-
179	Acetylation	ETNEGLKKFLQNFLL HCCHHHHHHHHHHHH	57.24	-
210	Phosphorylation	EKLAERISLIRETIY HHHHHHHHHHHHHHH	24.78	24825855
236	Ubiquitination	RGDTAYTKLALDRHT CCCCCHHHHHHCCCC	21.06	19608861
236	Acetylation	RGDTAYTKLALDRHT CCCCCHHHHHHCCCC	21.06	19608861
247 (in isoform 8)	Ubiquitination	-	12.83	-
294	Ubiquitination	EEFELLSKVPLKHEY HHHHHHHCCCCCCCC	48.09	29967540
395	Phosphorylation	LHGRECFTGYRQLCG ECCCCCCCCHHHHHC	44.99	24719451

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of TMLH_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TMLH_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TMLH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TMLH_HUMAN	TMLHE	physical	11431483

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300872	Epsilon-trimethyllysine hydroxylase deficiency (TMLHED)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00139	Succinic acid
DB00126	Vitamin C

Regulatory Network of TMLH_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-236, AND MASS SPECTROMETRY.	19608861 [Abstract]