dbPTM

LCMT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LCMT1_HUMAN
UniProt AC	Q9UIC8
Protein Name	Leucine carboxyl methyltransferase 1
Gene Name	LCMT1
Organism	Homo sapiens (Human).
Sequence Length	334
Subcellular Localization
Protein Description	Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues..
Protein Sequence	MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCKRFAVSIGYWHDPYIQHFVRLSKERKAPEINRGYFARVHGVSQLIKAFLRKTECHCQIVNLGAGMDTTFWRLKDEDLLPSKYFEVDFPMIVTRKLHSIKCKPPLSSPILELHSEDTLQMDGHILDSKRYAVIGADLRDLSELEEKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSFERAMFINYEQVNMGDRFGQIMIENLRRRQCDLAGVETCKSLESQKERLLSNGWETASAVDMMELYNRLPRAEVSRIESLEFLDEMELLEQLMRHYCLCWATKGGNELGLKEITY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MATRQRESSITSCCS CCCCCCCCCCCCCCC	29.27	28985074
9	Phosphorylation	ATRQRESSITSCCST CCCCCCCCCCCCCCC	25.73	26657352
11	Phosphorylation	RQRESSITSCCSTSS CCCCCCCCCCCCCCC	20.05	29978859
12	Phosphorylation	QRESSITSCCSTSSC CCCCCCCCCCCCCCC	16.08	28348404
15	Phosphorylation	SSITSCCSTSSCDAD CCCCCCCCCCCCCCC	35.33	27251275
16	Phosphorylation	SITSCCSTSSCDADD CCCCCCCCCCCCCCC	15.67	27251275
17	Phosphorylation	ITSCCSTSSCDADDE CCCCCCCCCCCCCCC	16.81	28348404
18	Phosphorylation	TSCCSTSSCDADDEG CCCCCCCCCCCCCCC	18.99	27251275
37	2-Hydroxyisobutyrylation	CEDASLCKRFAVSIG HHCHHHHHHCCCEEC	56.71	-
82	Ubiquitination	HGVSQLIKAFLRKTE HCHHHHHHHHHHCCC	41.50	-
105 (in isoform 2)	Ubiquitination	-	3.77	-
109	Ubiquitination	DTTFWRLKDEDLLPS CCEEEEECCCCCCCC	50.96	29967540
116	Phosphorylation	KDEDLLPSKYFEVDF CCCCCCCCCCEEECC	39.70	24719451
118	Phosphorylation	EDLLPSKYFEVDFPM CCCCCCCCEEECCCE	14.87	18083107
142	Phosphorylation	KCKPPLSSPILELHS CCCCCCCCCEEEECC	24.52	24719451
159	Ubiquitination	TLQMDGHILDSKRYA CCCCCCEECCCCCEE	5.82	24816145
162	Phosphorylation	MDGHILDSKRYAVIG CCCEECCCCCEEEEC	18.65	24719451
176	Phosphorylation	GADLRDLSELEEKLK CCCHHCHHHHHHHHH	44.41	30624053
181	Acetylation	DLSELEEKLKKCNMN CHHHHHHHHHHCCCC	57.12	19608861
181	Ubiquitination	DLSELEEKLKKCNMN CHHHHHHHHHHCCCC	57.12	32142685
183	Acetylation	SELEEKLKKCNMNTQ HHHHHHHHHCCCCCC	67.36	25953088
204	Ubiquitination	AECVLVYMTPEQSAN HHEEEEECCHHHHHH	3.82	24816145
227	Ubiquitination	FERAMFINYEQVNMG HHHHHCCCHHHCCCC	24.03	24816145
241	Sulfoxidation	GDRFGQIMIENLRRR CHHHHHHHHHHHHHC	2.12	21406390
259	Ubiquitination	LAGVETCKSLESQKE CCCHHHHHCHHHHHH	66.55	24816145
270	Phosphorylation	SQKERLLSNGWETAS HHHHHHHHCCCHHHH	37.58	20068231
275	Ubiquitination	LLSNGWETASAVDMM HHHCCCHHHHHHHHH	21.28	29967540
277	Phosphorylation	SNGWETASAVDMMEL HCCCHHHHHHHHHHH	35.92	-
282	Ubiquitination	TASAVDMMELYNRLP HHHHHHHHHHHHHCC	2.51	24816145
330	Ubiquitination	GGNELGLKEITY--- CCCCCCCEECCC---	45.32	2190698
330 (in isoform 1)	Ubiquitination	-	45.32	21906983
353 (in isoform 2)	Ubiquitination	-		21906983

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 LCMT1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LCMT1_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 LCMT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP2AA_HUMAN	PPP2CA	physical	26186194
PP4C_HUMAN	PPP4C	physical	26186194
IF1AX_HUMAN	EIF1AX	physical	26186194
PP4R2_HUMAN	PPP4R2	physical	26186194
NECP1_HUMAN	NECAP1	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
PP2AA_HUMAN	PPP2CA	physical	28514442
PP4R2_HUMAN	PPP4R2	physical	28514442
PP4C_HUMAN	PPP4C	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
DB00149	L-Leucine

Regulatory Network of LCMT1_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-181, AND MASS SPECTROMETRY.	19608861 [Abstract]