dbPTM

MT1X_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MT1X_HUMAN
UniProt AC	P80297
Protein Name	Metallothionein-1X
Gene Name	MT1X
Organism	Homo sapiens (Human).
Sequence Length	61
Subcellular Localization
Protein Description	Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. May be involved in FAM168A anti-apoptotic signaling. [PubMed: 23251525]
Protein Sequence	MDPNCSCSPVGSCACAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGTSDKCSCCA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDPNCSCS -------CCCCCCCC	20.42	19413330
6	Phosphorylation	--MDPNCSCSPVGSC --CCCCCCCCCCCCC	25.03	23927012
8	Phosphorylation	MDPNCSCSPVGSCAC CCCCCCCCCCCCCCC	13.31	23927012
12	Phosphorylation	CSCSPVGSCACAGSC CCCCCCCCCCCCCCC	9.97	28258704
18	Phosphorylation	GSCACAGSCKCKECK CCCCCCCCCCCCCCC	7.59	28258704
32	Phosphorylation	KCTSCKKSCCSCCPV CCCCCCCCCCCCCCC	13.07	22777824
35	Phosphorylation	SCKKSCCSCCPVGCA CCCCCCCCCCCCCCC	24.07	28258704
43	Ubiquitination	CCPVGCAKCAQGCIC CCCCCCCHHHCCCEE	33.89	-
51	Ubiquitination	CAQGCICKGTSDKCS HHCCCEEECCCCCCC	45.36	-
51	Acetylation	CAQGCICKGTSDKCS HHCCCEEECCCCCCC	45.36	25953088
53	Phosphorylation	QGCICKGTSDKCSCC CCCEEECCCCCCCCC	21.17	24719451
58	Phosphorylation	KGTSDKCSCCA---- ECCCCCCCCCC----	20.26	22798277

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 MT1X_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MT1X_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 MT1X_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MT1X_HUMAN !!

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.

Regulatory Network of MT1X_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-8, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Induction by zinc of specific metallothionein isoforms in humanmonocytes."; Pauwels M., van Weyenbergh J., Soumillion A., Proost P., Ley M.; Eur. J. Biochem. 220:105-110(1994). Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.	8119276 [Abstract]
Phosphorylation
Reference	PubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-8, AND MASS SPECTROMETRY.	19413330 [Abstract]